J. Potempa

发表

Carbamylated LL-37 as a modulator of the immune response

J. Enghild, Catalin Koro, A. Hellvard, 2016, Innate immunity.

Heparin-dependent Modification of the Reactive Center Arginine of Antithrombin and Consequent Increase in Heparin Binding Affinity*

R. Carrell, J. Potempa, R. Pike, 1997, The Journal of Biological Chemistry.

A structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome

J. Potempa, T. Goulas, F. Gomis-Rüth, 2017, The Journal of Biological Chemistry.

Serpin α1proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy

G. Salvesen, J. Potempa, H. Kołoczek, 1996, Protein science : a publication of the Protein Society.

The use of alpha 2-antiplasmin as a model for the demonstration of complex reversibility in serpins.

J. Potempa, J. Travis, B. Shieh, 1989, The Journal of biological chemistry.

Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites.

J. Potempa, J. Travis, B. Shieh, 1988, Science.

Comparative Cleavage Sites within the Reactive-Site Loop of Native and Oxidized α1-Proteinase Inhibitor by Selected Bacterial Proteinases

M. Rapala-Kozik, J. Potempa, A. Kozik, 1999, Biological chemistry.

Porphyromonas gingivalis in Alzheimer’s disease brains: Evidence for disease causation and treatment with small-molecule inhibitors

D. Raha, M. Dragunow, E. Reynolds, 2019, Science Advances.

Development of loop-mediated isothermal amplification assay for detection of human coronavirus-NL63

K. Pyrć, A. Milewska, J. Potempa, 2011, Journal of Virological Methods.

Human SCCA serpins inhibit staphylococcal cysteine proteases by forming classic "serpin-like" covalent complexes.

J. Potempa, T. Kantyka, 2011, Methods in enzymology.

Proteinases as Virulence Factors in Bacterial Diseases and as Potential Targets for Therapeutic Intervention with Proteinase Inhibitors

J. Potempa, J. Travis, 2000 .

Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitis.

J. Potempa, T. Imamura, R. Pike, 1997, Journal of periodontal research.

Rheumatoid arthritis - treatment 180. Utility of Body Weight Classified Low-Dose Leflunomide in Japanese Rheumatoid Arthritis

Stanley B. Cohen, D. Symmons, M. Dougados, 2011 .

Stability of infectious human coronavirus NL63

K. Pyrć, J. Potempa, Michal Burmistrz, 2014, Journal of Virological Methods.

HexaPrime: A novel method for detection of coronaviruses

K. Pyrć, J. Potempa, W. Gałan, 2012, Journal of Virological Methods.

Novel polymeric inhibitors of HCoV-NL63

B. Bosch, K. Pyrć, A. Milewska, 2012, Antiviral Research.

Use of Sensitive, Broad-Spectrum Molecular Assays and Human Airway Epithelium Cultures for Detection of Respiratory Pathogens

M. Sanak, K. Pyrć, M. Zembala, 2012, PloS one.

Infection with human coronavirus NL63 enhances streptococcal adherence to epithelial cells.

K. Pyrć, E. Kucewicz, M. Zembala, 2011, The Journal of general virology.

KLIKK proteases of Tannerella forsythia: putative virulence factors with a unique domain structure

J. Enghild, J. Potempa, I. Thøgersen, 2015, Front. Microbiol..

A Metalloproteinase Mirolysin of Tannerella forsythia Inhibits All Pathways of the Complement System

A. Blom, K. Riesbeck, J. Potempa, 2015, The Journal of Immunology.

Presence of Porphyromonas gingivalis in esophagus and its association with the clinicopathological characteristics and survival in patients with esophageal cancer

Xiaoshan Feng, R. Lamont, J. Potempa, 2016, Infectious Agents and Cancer.

The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity

G. Dubin, J. Potempa, A. Dubin, 2007, Biological chemistry.

Protease-armed bacteria in the skin

J. Potempa, J. Koziel, 2012, Cell and Tissue Research.

Inhibition of Arginine Gingipains (RgpB and HRgpA) with Benzamidine Inhibitors: Zinc Increases Inhibitory Potency

J. Potempa, J. Powers, J. Travis, 2002, Biological chemistry.

On the Transcriptional Regulation of Methicillin Resistance

J. Potempa, R. García-Castellanos, F. Gomis-Rüth, 2004, Journal of Biological Chemistry.

Staphylococcal cysteine protease staphopain B (SspB) induces rapid engulfment of human neutrophils and monocytes by macrophages

J. Potempa, M. Zarębski, Mateusz Kuzak, 2009, Biological chemistry.

Gingipains of Porphyromonas gingivalis Affect the Stability and Function of Serine Protease Inhibitor of Kazal-type 6 (SPINK6), a Tissue Inhibitor of Human Kallikreins*

J. Potempa, E. Bielecka, A. Kozik, 2016, The Journal of Biological Chemistry.

Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia

J. Potempa, M. Figlerowicz, Anna Philips, 2020, BMC Genomics.

The role and regulation of the extracellular proteases of Staphylococcus aureus.

S. Foster, J. Potempa, L. Shaw, 2004, Microbiology.

Aza-peptide Michael acceptors: a new class of inhibitors specific for caspases and other clan CD cysteine proteases.

J. Dvorak, J. Mikolajczyk, G. Salvesen, 2004, Journal of medicinal chemistry.

α‐1‐Proteinase Inhibitor

J. Potempa, J. Travis, 2002 .

Effects of statins on multispecies oral biofilm identify simvastatin as a drug candidate targeting Porphyromonas gingivalis.

A. Hellvard, N. Delaleu, Veronika Binder, 2018, Journal of periodontology.

Purification and Characterization of a Novel Endopeptidase in Ragweed (Ambrosia artemisiifolia) Pollen*

J. Potempa, D. Bagarozzi, J. Travis, 1996, The Journal of Biological Chemistry.

Adsorption of Components of the Plasma Kinin-Forming System on the Surface of Porphyromonas gingivalis Involves Gingipains as the Major Docking Platforms

H. Herwald, M. Rapala-Kozik, J. Potempa, 2010, Infection and Immunity.

Mechanisms of vascular damage by systemic dissemination of the oral pathogen Porphyromonas gingivalis

C. Murdoch, J. Potempa, R. Wilkinson, 2020, The FEBS journal.

Role of bacterial proteinases in matrix destruction and modulation of host responses.

J. Potempa, J. Travis, A. Banbula, 2000, Periodontology 2000.

Gingipains, the major cysteine proteinases and virulence factors of Porphyromonas gingivalis: structure, function and assembly of multidomain protein complexes.

J. Potempa, T. Imamura, J. Travis, 2003, Current protein & peptide science.

Peptidylarginine deiminase from Porphyromonas gingivalis (PPAD) contributes to infection of gingival fibroblasts and induction of PGE2-signaling pathway

J. Potempa, B., K. Gawron, 2015 .

Peptidylarginine deiminase from Porphyromonas gingivalis contributes to infection of gingival fibroblasts and induction of prostaglandin E2 -signaling pathway.

J. Potempa, A. Buda, K. Gawron, 2014, Molecular oral microbiology.

Lack of cathelicidin processing in Papillon-Lefèvre syndrome patients reveals essential role of LL-37 in periodontal homeostasis

J. Potempa, P. Eickholz, P. Hiemstra, 2014, Orphanet Journal of Rare Diseases.

Periodontal pathogens affect the level of protease inhibitors in gingival crevicular fluid.

J. Potempa, A. Sculean, S. Eick, 2012, Molecular oral microbiology.

Analysis of neutrophil-derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin LL-37 in the innate immune response against periodontogenic bacteria.

J. Potempa, P. Hiemstra, S. Eick, 2008, Oral microbiology and immunology.

The biphasic virulence activities of gingipains: activation and inactivation of host proteins.

J. Potempa, T. Imamura, J. Travis, 2003, Current protein & peptide science.

The lysine-specific gingipain of Porphyromonas gingivalis : importance to pathogenicity and potential strategies for inhibition.

J. Potempa, R. Pike, L. Wijeyewickrema, 2011, Advances in experimental medicine and biology.

An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center.

J. Potempa, J. Travis, A. Dubin, 1988, The Journal of biological chemistry.

Isolation of nine human plasma proteinase inhibitors by sequential affinity chromatography.

J. Potempa, J. Travis, A. Dubin, 1990, Preparative biochemistry.

High Molecular Weight Gingipains from Porphyromonas gingivalis Induce Cytokine Responses from Human Macrophage-Like Cells via a Nonproteolytic Mechanism

J. Potempa, R. Pike, C. Pagel, 2008, Journal of Innate Immunity.

Porphyromonas gingivalis Peptidyl Arginine Deiminase Can Modulate Neutrophil Activity via Infection of Human Dental Stem Cells

B. Kreikemeyer, J. Potempa, B. Müller-Hilke, 2018, Journal of Innate Immunity.

Dual regulation of interleukin-8 production in human oral epithelial cells upon stimulation with gingipains from Porphyromonas gingivalis.

J. Potempa, T. Imamura, M. Naito, 2008, Journal of medical microbiology.

Arginine-Specific Gingipains from Porphyromonas gingivalis Stimulate Production of Hepatocyte Growth Factor (Scatter Factor) through Protease-Activated Receptors in Human Gingival Fibroblasts in Culture1

J. Potempa, T. Imamura, K. Nakayama, 2005, The Journal of Immunology.

Culture Receptors in Human Gingival Fibroblasts in ( Scatter Factor ) through Protease-Activated Production of Hepatocyte Growth Factor Stimulate

J. Potempa, T. Imamura, K. Nakayama, 2005 .

Arginine-Specific Protease fromPorphyromonas gingivalis Activates Protease-Activated Receptors on Human Oral Epithelial Cells and Induces Interleukin-6 Secretion

M. D'Andrea, J. Potempa, R. Pike, 2001, Infection and Immunity.

Thrombin-activable Fibrinolysis Inhibitor (TAFI) Zymogen Is an Active Carboxypeptidase*

J. Enghild, J. Potempa, I. Thøgersen, 2007, Journal of Biological Chemistry.

Are bacterial proteinases pathogenic factors?

J. Potempa, J. Travis, H. Maeda, 1995, Trends in microbiology.

Functional characteristics of antibodies induced by Arg-gingipain (HRgpA) and Lys-gingipain (Kgp) from Porphyromonas gingivalis.

R. Page, J. Potempa, J. Travis, 2001, Oral microbiology and immunology.

Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of the Porphyromonas gingivalis type-IX secretion system

U. Eckhard, J. Potempa, M. Solà, 2021, Proceedings of the National Academy of Sciences.

The Role of Mcl-1 in S. aureus-Induced Cytoprotection of Infected Macrophages

J. Potempa, P. Mydel, Daniela Chmiest, 2013, Mediators of inflammation.

Ribonucleotide reductase class III, an essential enzyme for the anaerobic growth of Staphylococcus aureus, is a virulence determinant in septic arthritis.

Mahmud Masalha, S. Foster, A. Tarkowski, 2007, Microbial pathogenesis.

Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases

J. Potempa, L. Shaw, E. Golonka, 2005, Molecular microbiology.

Staphostatins resemble lipocalins, not cystatins in fold

M. Bochtler, J. Potempa, A. Dubin, 2003, Protein science : a publication of the Protein Society.

Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity.

J. Potempa, R. Pike, J. Travis, 2001, Blood.

Porphyromonas gingivalis: a proteinase/gene accounting audit.

J. Potempa, J. Travis, N. Pavloff, 1995, Trends in microbiology.

Staphylococcal Proteases Aid in Evasion of the Human Complement System

G. Dubin, A. Blom, J. Potempa, 2013 .

A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.

G. Dubin, T. Holak, G. Popowicz, 2003, Biochemistry.

The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases

J. Potempa, F. Gomis-Rüth, K. Nguyen, 2011, Molecular microbiology.

Expression of human and Porphyromonas gingivalis glutaminyl cyclases in periodontitis and rheumatoid arthritis-A pilot study.

J. Potempa, M. Westermann, A. Sculean, 2019, Archives of oral biology.

Cleavage of extracellular matrix in periodontitis: gingipains differentially affect cell adhesion activities of fibronectin and tenascin-C.

M. Chiquet, J. Potempa, S. Eick, 2013, Biochimica et biophysica acta.

Cleavage of IgG1 in gingival crevicular fluid is associated with the presence of Porphyromonas gingivalis.

J. Potempa, M. Abrahamson, S. Eick, 2013, Journal of periodontal research.

Comparison of gingival crevicular fluid sampling methods in patients with severe chronic periodontitis.

J. Potempa, S. Eick, W. Pfister, 2011, Journal of periodontology.

Neutrophils in chronic and aggressive periodontitis in interaction with Porphyromonas gingivalis and Aggregatibacter actinomycetemcomitans.

J. Potempa, S. Eick, W. Pfister, 2009, Journal of periodontal research.

Relationship between past myocardial infarction, periodontal disease and Porphyromonas gingivalis serum antibodies: A case-control study.

A. Pająk, A. Micek, P. Jankowski, 2013, Cardiology journal.

Porphyromonas gingivalis Gingipains Selectively Reduce CD14 Expression, Leading to Macrophage Hyporesponsiveness to Bacterial Infection

J. Potempa, L. Shapira, G. Nussbaum, 2014, Journal of Innate Immunity.

J. Enghild, G. Dubin, C. Overall, 2020, bioRxiv.

J. Enghild, G. Dubin, C. Overall, 2020, International journal of molecular sciences.

Porphyromonas gingivalis enzymes enhance infection with human metapneumovirus in vitro.

K. Pyrć, P. Strzyz, A. Milewska, 2011, The Journal of general virology.

Endotoxin-Induced Sepsis of Function of LL-37 Essential for Prevention Citrullination Alters Immunomodulatory

K. Pyrć, I. Główczyk, J. Potempa, 2014 .

Phosphorylation of major Porphyromonas gingivalis virulence factors is crucial for their processing and secretion.

R. Lamont, J. Potempa, M. Hackett, 2021, Molecular oral microbiology.

Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis.

J. Potempa, J. Travis, A. Polanowski, 1992, The Journal of biological chemistry.

The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain

J. Potempa, R. Pike, J. Travis, 1995, Infection and immunity.

Modulation of interleukin‐8 activity by gingipains from Porphyromonas gingivalis: implications for pathogenicity of periodontal disease

J. Potempa, J. Travis, J. Mikolajczyk-Pawlinska, 1998, FEBS letters.

Salivary Histatin 5 Is an Inhibitor of Both Host and Bacterial Enzymes Implicated in Periodontal Disease

J. Potempa, J. Travis, F. Oppenheim, 2001, Infection and Immunity.

Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function.

N. Rawlings, J. Potempa, T. Kantyka, 2010, Biochimie.

Cytoplasmic Control of Premature Activation of a Secreted Protease Zymogen: Deletion of Staphostatin B (SspC) in Staphylococcus aureus 8325-4 Yields a Profound Pleiotropic Phenotype

S. Foster, J. Potempa, L. Shaw, 2005, Journal of bacteriology.

Citrullination and Proteolytic Processing of Chemokines by Porphyromonas gingivalis

W. Teughels, G. Opdenakker, P. Proost, 2014, Infection and Immunity.

a Potent Cysteine Protease Activator of -Derived Staphopain B, Staphylococcus aureus

G. Dubin, E. Butcher, T. Handel, 2007 .

Development of Chemical Tools to Monitor Human Kallikrein 13 (KLK13) Activity

G. Dubin, A. Pęcak, M. Magoch, 2019, International journal of molecular sciences.

Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis

J. Potempa, R. Pike, W. McGraw, 1996, Journal of bacteriology.

Verification of a topology model of PorT as an integral outer-membrane protein in Porphyromonas gingivalis.

J. Potempa, K. Nguyen, Paweł Szczęsny, 2009, Microbiology.

Molecular Cloning and Structural Characterization of the Arg-gingipain Proteinase of Porphyromonas gingivalis

P. Barr, J. Potempa, R. Pike, 1995, The Journal of Biological Chemistry.

Genetic Variation of Porphyromonas gingivalis Genes Encoding Gingipains, Cysteine Proteinases with Arginine or Lysine Specificity

T. Kordula, J. Potempa, J. Travis, 1998, Biological chemistry.

Molecular Cloning and Characterization of Porphyromonas gingivalis Lysine-specific Gingipain

P. Barr, J. Potempa, R. Pike, 1997, The Journal of Biological Chemistry.

Loss of Clumping Factor B Fibrinogen Binding Activity byStaphylococcus aureus Involves Cessation of Transcription, Shedding and Cleavage by Metalloprotease*

T. Foster, J. Potempa, F. McAleese, 2001, The Journal of Biological Chemistry.

Heightened immune response to autocitrullinated Porphyromonas gingivalis peptidylarginine deiminase: a potential mechanism for breaching immunologic tolerance in rheumatoid arthritis

R. Zubarev, A. Ytterberg, T. Mikuls, 2013, Annals of the rheumatic diseases.

Biosynthesis of α1-Proteinase Inhibitor by Human Lung-derived Epithelial Cells*

J. Potempa, J. Travis, J. Cichy, 1997, The Journal of Biological Chemistry.

Regulation of α1‐antichymortrypsin synthesis in cells of epithelial origin

J. Potempa, J. Travis, J. Cichy, 1995 .

Citrullination in the periodontium—a possible link between periodontitis and rheumatoid arthritis

P. Venables, J. Potempa, A. Sculean, 2016, Clinical Oral Investigations.

Effect of free and vesicle-bound cysteine proteinases of Porphyromonas gingivalis on plasma clot formation: implications for bleeding tendency at periodontitis sites

J. Potempa, M. Barton, J. Moore, 1995, Infection and immunity.

Smoking, Porphyromonas gingivalis and the immune response to citrullinated autoantigens before the clinical onset of rheumatoid arthritis in a Southern European nested case–control study

E. Riboli, P. Vineis, D. Romaguera, 2015, BMC Musculoskeletal Disorders.

Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and α-enolase: implications for autoimmunity in rheumatoid arthritis.

R. Wait, K. Lundberg, A. Kinloch, 2010, Arthritis and rheumatism.

Neuropeptide Release from Dental Pulp Cells by RgpB via Proteinase-Activated Receptor-2 Signaling

M. Torii, I. Maruyama, S. Tancharoen, 2005, The Journal of Immunology.

Antimicrobial photodynamic therapy effectively reduces the infection of Porphyromonas gingivalis within gingival fibroblasts and keratinocytes: an in vitro study.

J. Potempa, K. Gawron, M. Chomyszyn-Gajewska, 2021, Photodiagnosis and Photodynamic Therapy.

The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin.

G. Dubin, M. Schmitt, V. Magdolen, 2008, The Biochemical journal.

Corruption of Innate Immunity by Bacterial Proteases

J. Potempa, R. Pike, 2008, Journal of Innate Immunity.

Porphyromonas gingivalis Outer Membrane Vesicles as the Major Driver of and Explanation for Neuropathogenesis, the Cholinergic Hypothesis, Iron Dyshomeostasis, and Salivary Lactoferrin in Alzheimer’s Disease

M. Penn, W. Griffin, J. Potempa, 2021, Journal of Alzheimer's disease : JAD.

A Novel Mechanism for Bradykinin Production at Inflammatory Sites

Robert B. Moore, M. Rapala-Kozik, J. Potempa, 1998, The Journal of Biological Chemistry.

Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases

J. Potempa, T. Imamura, J. Travis, 2004, Biological chemistry.

Purification and characterization of an arginine-specific peptidase from ragweed (Ambrosia artemisiifolia) pollen.

J. Potempa, D. Bagarozzi, J. Travis, 1998, American journal of respiratory cell and molecular biology.

The Janus Face of a-Toxin: A Potent Mediator of Cytoprotection in Staphylococci-Infected Macrophages

J. Potempa, Daniela Chmiest, L. Shaw, 2014, Journal of Innate Immunity.

Proteolysis of CD14 on Human Gingival Fibroblasts by Arginine-Specific Cysteine Proteinases from Porphyromonas gingivalis Leading to Down-Regulation of Lipopolysaccharide-Induced Interleukin-8 Production

E. Nemoto, H. Shimauchi, J. Potempa, 2002, Infection and Immunity.

Analysis of mutations in the SOS-1 gene in two Polish families with hereditary gingival fibromatosis.

J. Potempa, K. Gawron, R. Górska, 2017, Oral diseases.

Site-specific O -glycosylation on the MUC2 mucin inhibits cleavage by the Porphyromonas gingivalis secreted cysteine protease (RgpB)

E. Bennett, M. Bäckström, J. Potempa, 2013 .

Relationships of Clinical Isolates of Polymorphism and Genetic Variable-Number Tandem Repeat Analysis Strains : Multiple-Locus aureus Staphylococcus New Method for Typing

J. Krzysztoń-Russjan, J. Potempa, W. Hryniewicz, 2003 .

Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?

Natalia Wegner, P. Venables, J. Potempa, 2010, Arthritis research & therapy.

Degradation of elastin by a cysteine proteinase from Staphylococcus aureus.

J. Potempa, J. Travis, A. Dubin, 1988, The Journal of biological chemistry.

Biosynthesis of alpha1-proteinase inhibitor by human lung-derived epithelial cells.

J. Potempa, J. Travis, J. Cichy, 1997, The Journal of biological chemistry.

Cigarette smoke-exposed neutrophils die unconventionally but are rapidly phagocytosed by macrophages

J. Potempa, B. Gajkowska, D. Scott, 2011, Cell Death and Disease.

Host and bacterial factors linking periodontitis and rheumatoid arthritis

J. Potempa, K. Gawron, G. Bereta, 2022, Frontiers in Immunology.

Erratum to: Smoking, Porphyromonas gingivalis and the immune response to citrullinated autoantigens before the clinical onset of rheumatoid arthritis in a Southern European nested case–control study

E. Riboli, P. Vineis, D. Romaguera, 2016, BMC Musculoskeletal Disorders.

Comparative properties of human α‐1‐proteinase inhibitor glycosylation variants

J. Potempa, J. Travis, A. Dubin, 1990 .

Staphylococcus aureus Proteases Degrade Lung Surfactant Protein A Potentially Impairing Innate Immunity of the Lung

K. Pyrć, J. Potempa, M. Ochman, 2012, Journal of Innate Immunity.

Secretory Leukocyte Proteinase Inhibitor-Competent DNA Deposits Are Potent Stimulators of Plasmacytoid Dendritic Cells: Implication for Psoriasis

J. Potempa, A. Wlodarczyk, A. Dubin, 2012, The Journal of Immunology.

Cells: Implication for Psoriasis Potent Stimulators of Plasmacytoid Dendritic Inhibitor-Competent DNA Deposits Are Secretory Leukocyte Proteinase

J. Potempa, A. Wlodarczyk, A. Dubin, 2012 .

Attenuated Kinin Release from Human Neutrophil Elastase-Pretreated Kininogens by Tissue and Plasma Kallikreins

J. Silberring, M. Rapala-Kozik, J. Potempa, 2003, Biological chemistry.

Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase.

S. Tanase, J. Potempa, T. Imamura, 2002, Biochemical and biophysical research communications.

Inactivation of α1-Proteinase Inhibitor as a Broad Screen for Detecting Proteolytic Activities in Unknown Samples

J. Potempa, D. Nelson, J. Travis, 1998 .

The 1.8 A crystal structure of human cathepsin G in complex with Suc‐Val‐Pro‐PheP‐(OPh)2: a Janus‐faced proteinase with two opposite specificities.

R. Huber, W. Bode, J. Potempa, 1996, The EMBO journal.

Effects of elastase and cathepsin G on the levels of membrane and soluble TNFα

P. Mak, J. Potempa, Monika Bzowska, 2005, Biological chemistry.

Host cell-surface proteins as substrates of gingipains, the main proteases of Porphyromonas gingivalis

J. Potempa, B. Turk, K. Hočevar, 2018, Biological chemistry.

Identification of bacterial biofilm and the Staphylococcus aureus derived protease, staphopain, on the skin surface of patients with atopic dermatitis

A. Schmidtchen, J. Potempa, M. Mörgelin, 2017, Scientific Reports.

Friendly fire against neutrophils: proteolytic enzymes confuse the recognition of apoptotic cells by macrophages.

J. Potempa, K. Guzik, 2008, Biochimie.

The functional role of acute phase plasma proteinase inhibitors.

J. Potempa, J. Travis, B. Shieh, 1988, The Tokai journal of experimental and clinical medicine.

Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins.

J. Potempa, R. Pike, W. McGraw, 1994, The Journal of biological chemistry.

Stimulatory effect of inflammatory cytokines on alpha 1-antichymotrypsin expression in human lung-derived epithelial cells.

J. Potempa, J. Travis, J. Cichy, 1995, The Journal of clinical investigation.

The subversion of toll-like receptor signaling by bacterial and viral proteases during the development of infectious diseases.

J. Potempa, J. Kozieł, Izabela Ciaston, 2022, Molecular aspects of medicine.

Down-regulation of human extracellular cysteine protease inhibitors by the secreted staphylococcal cysteine proteases, staphopain A and B

J. Potempa, M. Abrahamson, B. Vincents, 2007, Biological chemistry.

Modification of cystatin C activity by bacterial proteinases and neutrophil elastase in periodontitis.

J. Potempa, M. Abrahamson, M. Wikström, 1997, Molecular pathology : MP.

A New Pathway of Staphylococcal Pathogenesis: Apoptosis-Like Death Induced by Staphopain B in Human Neutrophils and Monocytes

J. Enghild, J. Potempa, I. Thøgersen, 2008, Journal of Innate Immunity.

pH-regulated Secretion of a Glyceraldehyde-3-Phosphate Dehydrogenase from Streptococcus gordonii FSS2: Purification, Characterization, and Cloning of the Gene Encoding this Enzyme

J. Potempa, D. Nelson, D. Harty, 2001, Journal of dental research.

Equine leukocyte elastase inhibitor. Primary structure and identification as a thymosin-binding protein.

J. Enghild, J. Potempa, J. Travis, 1992, The Journal of biological chemistry.

Intracellular Staphylococcus aureus employs the cysteine protease staphopain A to induce host cell death in epithelial cells

M. Fraunholz, T. Rudel, K. Ohlsen, 2020, bioRxiv.

Intramucosally with IL-17-Producing T Cells in Mice Infected-and γ Fimbriae-Specific IFN-Released by Gingipain Induce Kinin Danger Signals Proteolytically

J. Scharfstein, J. Potempa, K. Nguyen, 2009 .

Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37

J. Enghild, J. Potempa, I. Thøgersen, 2017, Biological chemistry.

TIMP-1 association with collagen type I overproduction in hereditary gingival fibromatosis.

A. Fertala, J. Potempa, A. Grabiec, 2018, Oral diseases.

Transposition of the Endogenous Insertion Sequence Element IS1126 Modulates Gingipain Expression inPorphyromonas gingivalis

V. Bond, J. Potempa, C. Genco, 1999, Infection and Immunity.

Inter-alpha-trypsin inhibitor. Inhibition spectrum of native and derived forms.

J. Potempa, J. Travis, K. Kwon, 1989, The Journal of biological chemistry.

Conjugate of Enkephalin and Temporin Peptides as a Novel Therapeutic Agent for Sepsis.

M. Wysocka, J. Potempa, M. Lech, 2018, Bioconjugate chemistry.

The IgA Protease of Clostridium ramosum

J. Potempa, K. Poulsen, 2013 .

IgA protease of Clostridium ramosum

J. Potempa, K. Poulsen, 2004 .

Microbial Proteases: Relevance to the Inflammatory Response

J. Potempa, T. Imamura, 2011 .

HUMAN CATHEPSIN G

W. Bode, J. Potempa, A. Banbula, 1997 .

Porphyromonas gingivalis-derived Lysine Gingipain Enhances Osteoclast Differentiation Induced by Tumor Necrosis Factor-α and Interleukin-1β but Suppresses That by Interleukin-17A

K. Mishima, Y. Miyamoto, J. Potempa, 2014, The Journal of Biological Chemistry.

DEGRADATION OF IMPORTANCE OF PROTEOLYTIC Suppresses That by Interleukin-17 A : but β and Interleukin-1 α Factor-Differentiation Induced by Tumor Necrosis Gingipain Enhances Osteoclast-derived Lysine

Toshifumi, K. Mishima, Y. Miyamoto, 2014 .

Porphyromonas gingivalis Gingipains-Mediated Degradation of Plasminogen Activator Inhibitor-1 Leads to Delayed Wound Healing Responses in Human Endothelial Cells

E. Nemoto, J. Potempa, K. Matsushita, 2021, Journal of Innate Immunity.

In vivo sortase A and clumping factor A mRNA expression during Staphylococcus aureus infection.

E. Josefsson, J. Potempa, P. Mydel, 2008, Microbial pathogenesis.

A Potential New Pathway for Staphylococcus aureus Dissemination: The Silent Survival of S. aureus Phagocytosed by Human Monocyte-Derived Macrophages

Timothy Foster, T. Foster, J. Potempa, 2008, PloS one.

Proteolytic Activity-Independent Activation of the Immune Response by Gingipains from Porphyromonas gingivalis

R. Lamont, M. Rapala-Kozik, J. Potempa, 2022, mBio.

The Bactericidal Activity of Temporin Analogues Against Methicillin Resistant Staphylococcus aureus

J. Potempa, A. Lesner, A. Golda, 2019, International journal of molecular sciences.

Chapter 114 – Aureolysin

J. Potempa, 2013 .

Differential Regulation by Toll-Like Receptor Agonists Reveals That MCPIP1 Is the Potent Regulator of Innate Immunity in Bacterial and Viral Infections

J. Potempa, J. Jura, J. Kozieł, 2012, Journal of Innate Immunity.

Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence

J. Enghild, J. Potempa, G. Silverman, 2011, Biological chemistry.

Investigations into σB-Modulated Regulatory Pathways Governing Extracellular Virulence Determinant Production in Staphylococcus aureus

S. Foster, J. Potempa, L. Shaw, 2006, Journal of bacteriology.

Citrullination-Resistant LL-37 Is a Potent Antimicrobial Agent in the Inflammatory Environment High in Arginine Deiminase Activity

J. Potempa, E. Bielecka, P. Svoboda, 2020, International journal of molecular sciences.

Regulation of Chemerin Chemoattractant and Antibacterial Activity by Human Cysteine Cathepsins

E. Butcher, T. Handel, S. Allen, 2011, The Journal of Immunology.

Cysteine Cathepsins and Antibacterial Activity by Human Regulation of Chemerin Chemoattractant

E. Butcher, T. Handel, S. Allen, 2011 .

Uncovering the Oral Dysbiotic Microbiota as Masters of Neutrophil Responses in the Pathobiology of Periodontitis

J. Potempa, M. Sochalska, Zsombor Prucsi, 2021, Frontiers in Microbiology.

Porphyromonas gingivalis genes conferring fitness in a tobacco-rich environment.

R. Lamont, J. Potempa, D. Scott, 2019, Molecular oral microbiology.

Inhibition of GSK3 Abolishes Bacterial-Induced Periodontal Bone Loss in Mice

R. Jotwani, J. Potempa, D. Scott, 2012, Molecular medicine.

A Novel Biological Role for Peptidyl-Arginine Deiminases: Citrullination of Cathelicidin LL-37 Controls the Immunostimulatory Potential of Cell-Free DNA

J. Enghild, P. Thompson, C. Scavenius, 2018, The Journal of Immunology.

Inhibition of Tumor Necrosis Factor-– Induced RANTES Secretion by Alkaline Protease in A 549 Cells

T. Krunkosky, J. Potempa, K. Maruo, 2005 .

Triggering NETosis via protease-activated receptor (PAR)-2 signaling as a mechanism of hijacking neutrophils function for pathogen benefits

J. Potempa, M. Lech, S. Eick, 2019, PLoS pathogens.

Cleavage and activation of proteinase‐activated receptor‐2 on human neutrophils by gingipain‐R from Porphyromonas gingivalis

J. Potempa, R. Pike, E. Mackie, 1998, FEBS letters.

Contents Vol. 6, 2014

V. Nizet, Erliang Zeng, K. Ley, 2014, Journal of Innate Immunity.

Proteolytic Inactivation of LL-37 by Karilysin, a Novel Virulence Mechanism of Tannerella forsythia

M. Rapala-Kozik, J. Potempa, K. Nguyen, 2010, Journal of Innate Immunity.

Apoptotic cell clearance in chronic inflammation of lateral neck cysts

J. Potempa, K. Guzik, W. Dobroś, 2011, European Archives of Oto-Rhino-Laryngology.

Immunomodulatory Molecule IRAK-M Balances Macrophage Polarization and Determines Macrophage Responses during Renal Fibrosis

S. Steiger, J. Potempa, M. Lech, 2017, The Journal of Immunology.

The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolytic rate: reply to a rebuttal

J. Enghild, J. Potempa, Z. Valnickova, 2007, Journal of thrombosis and haemostasis : JTH.

Crystallization and preliminary X‐ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H‐D‐Phe‐Phe‐Arg‐chloromethylketone

W. Bode, J. Potempa, J. Travis, 1998, Protein science : a publication of the Protein Society.

Murine myeloid cell MCPIP1 suppresses autoimmunity by regulating B-cell expansion and differentiation

M. Fu, J. Potempa, M. Lech, 2021, Disease Models & Mechanisms.

Posttranslational Modifications in Innate Immunity

J. Potempa, 2012, Journal of Innate Immunity.

Carbamylation of Integrin αIIbβ3: The Mechanistic Link to Platelet Dysfunction in ESKD

T. Hervig, P. Thompson, Veronika Binder, 2022, Journal of the American Society of Nephrology : JASN.

HmuY Haemophore and Gingipain Proteases Constitute a Unique Syntrophic System of Haem Acquisition by Porphyromonas gingivalis

D. Byrne, T. Olczak, J. Smalley, 2011, PloS one.

Activation of Protein C by Arginine-Specific Cysteine Proteinases (Gingipains-R) from Porphyromonas gingivalis

N. Kitamura, J. Potempa, T. Imamura, 1999, Biological chemistry.

Antithrombin III activity (residual thrombin activity) in plasma from non-medicated or heparinized horses

J. Potempa, J. Moore, J. Travis, 2004, Veterinary Research Communications.

Antithrombin III activity in horses with colic: an analysis of 46 cases.

J. Potempa, J. Moore, J. Travis, 1991, Equine veterinary journal.

A Peptide Domain on Gingipain R Which Confers Immunity against Porphyromonas gingivalis Infection in Mice

J. Potempa, C. Genco, J. Travis, 1998, Infection and Immunity.

A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice.

J. Potempa, C. Genco, J. Travis, 1998, Infection and immunity.

Mammalian-like type II glutaminyl cyclases in Porphyromonas gingivalis and other oral pathogenic bacteria as targets for treatment of periodontitis.

C. Parthier, M. Stubbs, J. Potempa, 2021, The Journal of biological chemistry.

Oncostatin M stimulates the expression and release of the IL-6 receptor in human hepatoma HepG2 cells.

S. Rose-John, J. Potempa, J. Pryjma, 1997, Journal of immunology.

Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution.

R. Huber, W. Bode, J. Potempa, 1998, Structure.

Purification and Characterization of a Novel Cysteine Proteinase (Periodontain) from Porphyromonas gingivalis

T. Kordula, J. Potempa, D. Nelson, 1999, The Journal of Biological Chemistry.

The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine

J. Potempa, Ronan K. Carroll, L. Shaw, 2013, Biological chemistry.

Papain-like proteases of Staphylococcus aureus.

J. Potempa, L. Shaw, T. Kantyka, 2011, Advances in experimental medicine and biology.

Investigations into (cid:2) B -Modulated Regulatory Pathways Governing Extracellular Virulence Determinant Production in Staphylococcus aureus

S. Foster, J. Potempa, L. Shaw, 2006 .

Application of the In Vitro HoxB8 Model System to Characterize the Contributions of Neutrophil–LPS Interaction to Periodontal Disease

J. Potempa, A. Grabiec, T. Kantyka, 2020, Pathogens.

Complement System on the Human Porphyromonas gingivalis Biphasic Effect of Gingipains from

A. Blom, K. Riesbeck, J. Potempa, 2007 .

Noncanonical Activation of β-Catenin by Porphyromonas gingivalis

R. Lamont, J. Potempa, D. Scott, 2015, Infection and Immunity.

Aristolochic acid I determine the phenotype and activation of macrophages in acute and chronic kidney disease

S. Steiger, J. Potempa, M. Lech, 2018, Scientific Reports.

Issue information

Takashi Gojobori, Koji Yamanaka, Stuart Ferguson, 2018, Random Struct. Algorithms.

Interaction of a novel form of Pseudomonas aeruginosa alkaline protease (aeruginolysin) with interleukin-6 and interleukin-8

J. Potempa, J. Travis, N. Matheson, 2006, Biological chemistry.

Isolation and properties of extracellular proteinases of Penicillium marneffei

J. Potempa, L. Shaw, J. Travis, 2006, Biological chemistry.

Induction of vascular leakage through release of bradykinin and a novel kinin by cysteine proteinases from Staphylococcus aureus

S. Tanase, J. Potempa, T. Imamura, 2005, The Journal of experimental medicine.

The C‐terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities

J. Potempa, R. Pike, C. Genco, 2004, Molecular microbiology.

Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) ofPorphyromonas gingivalis

J. Potempa, C. Genco, J. Travis, 2001, Journal of bacteriology.

Porphyromonas gingivalis DPP-7 Represents a Novel Type of Dipeptidylpeptidase*

P. Mak, J. Potempa, J. Travis, 2001, The Journal of Biological Chemistry.

Emerging Family of Proline-Specific Peptidases ofPorphyromonas gingivalis: Purification and Characterization of Serine Dipeptidyl Peptidase, a Structural and Functional Homologue of Mammalian Prolyl Dipeptidyl Peptidase IV

J. Potempa, D. Nelson, J. Travis, 2000, Infection and Immunity.

Rapid and efficient inactivation of IL-6 gingipains, lysine- and arginine-specific proteinases from Porphyromonas gingivalis.

P. Heinrich, J. Potempa, J. Travis, 1999, Biochemical and biophysical research communications.

Prolyl Tripeptidyl Peptidase from Porphyromonas gingivalis

P. Mak, J. Silberring, J. Potempa, 1999, The Journal of Biological Chemistry.

Comparative Properties of Two Cysteine Proteinases (Gingipains R), the Products of Two Related but Individual Genes ofPorphyromonas gingivalis *

J. Enghild, J. Potempa, D. Nelson, 1998, The Journal of Biological Chemistry.

Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire process.

J. Potempa, A. Kozik, J. Travis, 1998, Biochimica et biophysica acta.

Inhibition of Trypsin-Like Cysteine Proteinases (Gingipains) fromPorphyromonas gingivalis by Tetracycline and Its Analogues

J. Potempa, K. Matsushita, T. Imamura, 2001, Antimicrobial Agents and Chemotherapy.

Glutaminyl cyclases as novel targets for the treatment of septic arthritis.

R. Jonsson, A. Hellvard, J. Potempa, 2013, The Journal of infectious diseases.

Neutrophil Proteinases

J. Potempa, J. Travis, A. Dubin, 1991, Annals of the New York Academy of Sciences.

Peptidyl Arginine Deiminase from Porphyromonas gingivalis Abolishes Anaphylatoxin C5a Activity*

J. Enghild, A. Blom, E. Prossnitz, 2014, The Journal of Biological Chemistry.

Titration and Mapping of the Active Site of Cysteine Proteinases from Porphyromonas gingivalis (Gingipains) Using Peptidyl Chloromethanes

J. Potempa, J. Travis, R. Pike, 1997, Biological chemistry.

Zebrafish as a new model to study effects of periodontal pathogens on cardiovascular diseases

C. Murdoch, J. Potempa, S. Tazzyman, 2016, Scientific Reports.

Prevalence of genes encoding extracellular proteases in Staphylococcus aureus - important targets triggering immune response in vivo.

G. Dubin, J. Potempa, S. Eick, 2012, FEMS immunology and medical microbiology.

Proteolysis of ICAM-1 on Human Oral Epithelial Cells by Gingipains

E. Nemoto, H. Shimauchi, J. Potempa, 2003, Journal of dental research.

Carbamylation of immunoglobulin abrogates activation of the classical complement pathway

R. Jonsson, J. Enghild, A. Blom, 2014, European journal of immunology.

Proteolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis

J. Potempa, R. Pike, J. Travis, 1996, Infection and immunity.

Response regulator PorX coordinates oligonucleotide signalling and gene expression to control the secretion of virulence factors

V. Šikšnys, R. Lamont, P. Młynarz, 2022, Nucleic acids research.

Comparison of antiproteolytic activities of alpha-1-proteinase inhibitors from the plasma of some mammalian species.

J. Potempa, A. Dubin, A. Koj, 1986, Comparative biochemistry and physiology. B, Comparative biochemistry.

Plasmin inhibition by bacterial serpin: Implications in gum disease

J. Enghild, J. Potempa, I. Thøgersen, 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Protease-dependent mechanisms of complement evasion by bacterial pathogens

J. Potempa, M. Potempa, 2012, Biological chemistry.

19 Kinins in bacterial infections

H. Herwald, J. Potempa, 2011 .

Bacterial proteinases as targets for the development of second-generation antibiotics.

J. Potempa, J. Travis, 2000, Biochimica et biophysica acta.

Proteolytic inactivation of alpha-1-anti-chymotrypsin. Sites of cleavage and generation of chemotactic activity.

J. Potempa, A. Mast, J. Travis, 1991, The Journal of biological chemistry.

Serpins: structure and mechanism of action.

J. Potempa, J. Travis, W. Wątorek, 1990, Biological Chemistry Hoppe-Seyler.

Inhibition of tumor necrosis factor-alpha-induced RANTES secretion by alkaline protease in A549 cells.

T. Krunkosky, J. Potempa, K. Maruo, 2005, American Journal of Respiratory Cell and Molecular Biology.

Inhibition of TNF alpha-induced RANTES secretion by alkaline protease in A549 cells

T. Krunkosky, J. Potempa, K. Maruo, 2005 .

Biochemical and Structural Characterization of SplD Protease from Staphylococcus aureus

G. Dubin, S. Kędracka-Krok, P. Daugherty, 2013, PloS one.

Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases

J. Potempa, A. Dubin, A. Sabat, 2003, Molecular microbiology.

Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis

J. Potempa, T. Imamura, R. Pike, 1995, Infection and immunity.

Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway.

J. Potempa, T. Imamura, R. Pike, 1994, The Journal of clinical investigation.

Kinin Danger Signals Proteolytically Released by Gingipain Induce Fimbriae-Specific IFN-γ- and IL-17-Producing T Cells in Mice Infected Intramucosally with Porphyromonas gingivalis1

J. Scharfstein, J. Potempa, K. Nguyen, 2009, The Journal of Immunology.

Growth phase-dependent production of a cell wall-associated elastinolytic cysteine proteinase by Staphylococcus epidermidis

M. Bogyo, T. Foster, J. Potempa, 2004, Biological chemistry.

Substrate specificity of Staphylococcus aureus cysteine proteases--Staphopains A, B and C.

M. Bogyo, G. Dubin, P. Daugherty, 2012, Biochimie.

Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus.

Y. Nishimura, J. Potempa, T. Imamura, 2011, Microbiology.

Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis.

S. Tanase, J. Potempa, T. Imamura, 2001, The Biochemical journal.

Apolipoprotein E Triggers Complement Activation in Joint Synovial Fluid of Rheumatoid Arthritis Patients by Binding C1q

J. Enghild, K. Ekdahl, A. Blom, 2020, The Journal of Immunology.

Activation of Blood Coagulation Factor X by Arginine-specific Cysteine Proteinases (Gingipain-Rs) from Porphyromonas gingivalis *

S. Tanase, J. Potempa, T. Imamura, 1997, The Journal of Biological Chemistry.

Cartilage proteoglycan degradation by a mouse transformed macrophage cell line is mediated by macrophage metalloelastase

S. Shapiro, J. Potempa, R. Pike, 1999, Inflammation Research.

Strategies for the inhibition of gingipains for the potential treatment of periodontitis and associated systemic diseases

J. Potempa, I. Olsen, 2014, Journal of oral microbiology.

Selective inhibition of Porphyromonas gingivalis growth by a factor Xa inhibitor, DX-9065a.

M. Torii, I. Maruyama, S. Tancharoen, 2006, Journal of periodontal research.

A natural anti-periodontitis agent, epimedokoreanin B, inhibits virulence activities of gingipains from Porphyromonas gingivalis

J. Potempa, T. Imamura, T. Kariu, 2019, Bioscience, biotechnology, and biochemistry.

Inactivation of Epidermal Growth Factor by Porphyromonas gingivalis as a Potential Mechanism for Periodontal Tissue Damage

J. Enghild, K. Pyrć, A. Milewska, 2012, Infection and Immunity.

Inhibition of gingipains and Porphyromonas gingivalis growth and biofilm formation by prenyl flavonoids

J. Potempa, T. Imamura, T. Kariu, 2017, Journal of periodontal research.

Porphyromonas gingivalis HmuY and HmuR: further characterization of a novel mechanism of heme utilization

T. Olczak, J. Potempa, M. Olczak, 2008, Archives of Microbiology.

Exploring the Sn binding pockets in gingipains by newly developed inhibitors: structure-based design, chemistry, and activity.

J. Otlewski, J. Grembecka, J. Potempa, 2006, Journal of medicinal chemistry.

Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus

G. Dubin, G. Popowicz, J. Potempa, 2014, Protein science : a publication of the Protein Society.

Kallikreins - The melting pot of activity and function.

J. Potempa, T. Kantyka, U. Meyer-Hoffert, 2016, Biochimie.

Identification of an intracellular M17 family leucine aminopeptidase that is required for virulence in Staphylococcus aureus.

J. Potempa, Ronan K. Carroll, L. Shaw, 2012, Microbes and infection.

Serum Complement Activation by C4BP-IgM Fusion Protein Can Restore Susceptibility to Antibiotics in Neisseria gonorrhoeae

M. Unemo, A. Blom, S. Ram, 2021, Frontiers in Immunology.

The inactivation of human plasma alpha 1-proteinase inhibitor by proteinases from Staphylococcus aureus.

J. Potempa, J. Travis, W. Wątorek, 1986, The Journal of biological chemistry.

The role of proteolytic enzymes in the development of pulmonary emphysema and periodontal disease.

J. Potempa, T. Imamura, R. Pike, 1994, American journal of respiratory and critical care medicine.

Antimicrobial and Attractant Roles for Chemerin in the Oral Cavity during Inflammatory Gum Disease

B. Zabel, J. Potempa, S. Eick, 2017, Front. Immunol..

Staphylococcus aureus-Derived Staphopain B, a Potent Cysteine Protease Activator of Plasma Chemerin1

G. Dubin, E. Butcher, T. Handel, 2007, The Journal of Immunology.

Neutrophils alter epithelial response to Porphyromonas gingivalis in a gingival crevice model.

J. Potempa, F. Veillard, J. Bagaitkar, 2013, Molecular oral microbiology.

Roles of the Host Oxidative Immune Response and Bacterial Antioxidant Rubrerythrin during Porphyromonas gingivalis Infection

F. C. Gibson, J. Potempa, P. Mydel, 2006, PLoS pathogens.

Gingipains from Porphyromonas gingivalis W83 Induce Cell Adhesion Molecule Cleavage and Apoptosis in Endothelial Cells

J. Potempa, H. Fletcher, J. Travis, 2005, Infection and Immunity.

Hydrolysis of Epithelial Junctional Proteins by Porphyromonas gingivalis Gingipains

S. Michalek, J. Potempa, D. Balkovetz, 2002, Infection and Immunity.

The serpin superfamily of proteinase inhibitors: structure, function, and regulation.

J. Potempa, E. Korzus, J. Travis, 1994, The Journal of biological chemistry.

The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function

J. Potempa, M. Ksiazek, M. Madej, 2017, Front. Cell. Infect. Microbiol..

The Staphostatin-Staphopain Complex

M. Bochtler, J. Potempa, A. Dubin, 2003, Journal of Biological Chemistry.

Role of OmpA2 surface regions of Porphyromonas gingivalis in host–pathogen interactions with oral epithelial cells

Stuart Hunt, Craig Murdoch, C. Murdoch, 2016, MicrobiologyOpen.

The Link Between Periodontal Disease and Rheumatoid Arthritis: An Updated Review

J. Potempa, P. Mydel, J. Kozieł, 2014, Current Rheumatology Reports.

Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins.

J. Potempa, K. Nguyen, Yonghua Guo, 2010, Periodontology 2000.

Protease-armed bacteria in the skin

J. Potempa, J. Kozieł, 2012, Cell and Tissue Research.

Acriflavine, a clinically approved drug, inhibits SARS-CoV-2 and other betacoronaviruses

Magdalena Pachota, K. Pyrć, G. Dubin, 2021, bioRxiv.

The fluorescence quenching resolved spectra and red-edge excitation fluorescence measurements of human alpha 1-proteinase inhibitor.

Z. Wasylewski, J. Potempa, H. Kołoczek, 1991, Biochimica et biophysica acta.

Breakdown of albumin and haemalbumin by the cysteine protease interpain A, an albuminase of Prevotella intermedia

D. Byrne, J. Smalley, J. Potempa, 2015, BMC Microbiology.

Unique Structure and Stability of HmuY, a Novel Heme-Binding Protein of Porphyromonas gingivalis

T. Olczak, J. Potempa, M. Solà, 2009, PLoS pathogens.

Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis

J. Smalley, J. Potempa, A. Birss, 2008, Biological chemistry.

The HA2 haemagglutinin domain of the lysine-specific gingipain (Kgp) of Porphyromonas gingivalis promotes micro-oxo bishaem formation from monomeric iron(III) protoporphyrin IX.

J. Smalley, J. Potempa, A. Birss, 2006, Microbiology.

Mammalian-like type II glutaminyl cyclases in Porphyromonas gingivalis and other oral pathogenic bacteria as targets for treatment of periodontitis

C. Parthier, M. Stubbs, J. Potempa, 2021, The Journal of biological chemistry.

Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases

W. Shafer, B. Lupa, T. Foster, 2004, Antimicrobial Agents and Chemotherapy.

Three-dimensional Structure of MecI

J. Potempa, R. García-Castellanos, F. Gomis-Rüth, 2003, Journal of Biological Chemistry.

Inhibition of Porphyromonas gingivalis proteinases (gingipains) by chlorhexidine: synergistic effect of Zn(II).

J. Potempa, J. Travis, J. A. Mayo, 2006, Oral microbiology and immunology.

Human Coronavirus NL63 Utilizes Heparan Sulfate Proteoglycans for Attachment to Target Cells

K. Pyrć, A. Milewska, J. Potempa, 2014, Journal of Virology.

Proteolytic effects of gingipains on trefoil factor family peptides

J. Potempa, S. Roytrakul, B. Potempa, 2017, Clinical Oral Investigations.

Gingival fibromatosis: clinical, molecular and therapeutic issues

J. Potempa, K. Gawron, M. Chomyszyn-Gajewska, 2016, Orphanet Journal of Rare Diseases.

Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis

D. M. Kurtz Jr., J. Potempa, J. Travis, 2002, Molecular microbiology.

Metabolomic Status of The Oral Cavity in Chronic Periodontitis

P. Młynarz, J. Potempa, P. Mydel, 2019, In Vivo.

Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

A. Blom, K. Riesbeck, J. Potempa, 2012, PloS one.

Manipulation of Neutrophils by Porphyromonas gingivalis in the Development of Periodontitis

J. Potempa, M. Sochalska, 2017, Front. Cell. Infect. Microbiol..

Periodontal Pathogens and Associated Intrathecal Antibodies in Early Stages of Alzheimer's Disease.

A. Johnen, T. Duning, J. Potempa, 2018, Journal of Alzheimer's disease : JAD.

The Nucleocapsid Protein of Human Coronavirus NL63

K. Pyrć, G. Dubin, S. Kędracka-Krok, 2015, PloS one.

Epigenetic regulation in bacterial infections: targeting histone deacetylases

J. Potempa, A. Grabiec, 2017, Critical reviews in microbiology.

MCPIP-1, Alias Regnase-1, Controls Epithelial Inflammation by Posttranscriptional Regulation of IL-8 Production

J. Potempa, M. Lech, J. Jura, 2016, Journal of Innate Immunity.

MCPIP-1, Alias Regnase-1, Controls Epithelial Inflammation by Posttranscriptional Regulation of IL-8 Production.

J. Potempa, M. Lech, J. Jura, 2016, Journal of innate immunity.

Mapping of DNA methylation-sensitive cellular processes in gingival and periodontal ligament fibroblasts in the context of periodontal tissue homeostasis

J. Potempa, T. Kaczmarzyk, A. Grabiec, 2023, Frontiers in Immunology.

Proteolysis of interleukin-6 receptor (IL-6R) by Porphyromonas gingivalis cysteine proteinases (gingipains) inhibits interleukin-6-mediated cell activation.

J. Potempa, J. Travis, A. Banbula, 2002, Microbial pathogenesis.

Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases

J. Potempa, F. Gomis-Rüth, M. Ksiazek, 2020, IUCrJ.

hTERT-immortalized gingival fibroblasts respond to cytokines but fail to mimic primary cell responses to Porphyromonas gingivalis

J. Potempa, T. Kaczmarzyk, A. Grabiec, 2021, Scientific Reports.

Phagocytosis of Staphylococcus aureus by Macrophages Exerts Cytoprotective Effects Manifested by the Upregulation of Antiapoptotic Factors

Adeline R. Whitney, D. Sturdevant, F. DeLeo, 2009, PloS one.

Genes Contributing to Porphyromonas gingivalis Fitness in Abscess and Epithelial Cell Colonization Environments

R. Lamont, J. Potempa, M. Whiteley, 2017, Front. Cell. Infect. Microbiol..

Citrullination as a plausible link to periodontitis, rheumatoid arthritis, atherosclerosis and Alzheimer’s disease

J. Potempa, I. Olsen, S. Singhrao, 2018, Journal of oral microbiology.

Porphyromonas gingivalis Fimbriae Dampen P2X7-Dependent Interleukin-1β Secretion

J. Scharfstein, D. Ojcius, J. Potempa, 2014, Journal of Innate Immunity.

Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus.

J. Potempa, B. Potužníková, J. Zikán, 1992, Immunology letters.

Inhibition of distant caspase homologues by natural caspase inhibitors.

A. Barrett, G. Salvesen, H. Stennicke, 2001, The Biochemical journal.

Interaction of regulators Mdm2 and Mdmx with transcription factors p53, p63 and p73

G. Dubin, S. Kędracka-Krok, A. Pęcak, 2010, Cell cycle.

Multiple Functions of Neutrophil Proteinases and their Inhibitor Complexes

James Travis, J. Potempa, J. Travis, 1992 .

Complement Activation as a Helping Hand for Inflammophilic Pathogens and Cancer

M. Okrój, J. Potempa, 2019, Front. Immunol..

HDAC3 Regulates Gingival Fibroblast Inflammatory Responses in Periodontitis

J. Potempa, T. Kaczmarzyk, G. Fossati, 2019, Journal of dental research.

BET Bromodomain Inhibitors Suppress Inflammatory Activation of Gingival Fibroblasts and Epithelial Cells From Periodontitis Patients

J. Potempa, A. Grabiec, K. Gawron, 2019, Front. Immunol..

Calcium Regulates the Activity and Structural Stability of Tpr, a Bacterial Calpain-like Peptidase*

J. Enghild, M. Bogyo, J. Potempa, 2015, The Journal of Biological Chemistry.

Dipeptidyl-Peptidase 7 of Porphyromonas gingivalis

J. Potempa, J. Travis, A. Banbula, 2013 .

Host and Porphyromonas gingivalis proteinases in periodontitis : a biochemical model of infection and tissue destruction

J. Potempa, R. Pike, J. Travis, 1995 .

Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.

R. Huber, U. Baumann, W. Bode, 1992, Journal of molecular biology.

MCPIP-1 Restricts Inflammation via Promoting Apoptosis of Neutrophils

J. Potempa, M. Lech, M. Kamińska, 2021, Frontiers in Immunology.

Structural basis for ADP-dependent glucokinase inhibition by 8-bromo–substituted adenosine nucleotide

P. Grudnik, G. Dubin, M. Kamiński, 2018, The Journal of Biological Chemistry.

A Dual Role for P2X7 Receptor during Porphyromonas gingivalis Infection

J. Scharfstein, D. Ojcius, J. Potempa, 2015, Journal of dental research.

Arginine-Specific Cysteine Proteinase from Porphyromonas gingivalis as a Convenient Tool in Protein Chemistry

P. Mak, J. Potempa, M. Smoluch, 2001, Biological chemistry.

The Clostridium ramosum IgA Proteinase Represents a Novel Type of Metalloendopeptidase*

L. K. Rasmussen, J. Potempa, M. Kilian, 2002, The Journal of Biological Chemistry.

Comparison of pathogenic properties between two types of arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis.

J. Potempa, T. Imamura, J. Travis, 2000, Microbial pathogenesis.

NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus.

J. Potempa, L. Shaw, V. Nagarajan, 2011, Microbiology.

Activation of Human Prothrombin by Arginine-specific Cysteine Proteinases (Gingipains R) from Porphyromonas gingivalis *

J. Potempa, T. Imamura, J. Travis, 2001, The Journal of Biological Chemistry.

Proteolysis of Gingival Keratinocyte Cell Surface Proteins by Gingipains Secreted From Porphyromonas gingivalis – Proteomic Insights Into Mechanisms Behind Tissue Damage in the Diseased Gingiva

R. Lamont, J. Potempa, M. Fonović, 2020, Frontiers in Microbiology.

Molecular genetics and nomenclature of proteases of Porphyromonas gingivalis.

M. A. Curtis, H. Kuramitsu, E. Reynolds, 1999, Journal of periodontal research.

Crystal structure of gingipain R: an Arg‐specific bacterial cysteine proteinase with a caspase‐like fold

R. Huber, W. Bode, U. Jacob, 1999, The EMBO journal.

The potential role of alpha 2-macroglobulin in the control of cysteine proteinases (gingipains) from Porphyromonas gingivalis.

J. Enghild, S. Pizzo, J. Potempa, 1997, Journal of periodontal research.

Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis.

J. Potempa, J. Travis, T. Hugli, 1992, The Journal of biological chemistry.

Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis

J. Enghild, N. Ranson, S. Rawson, 2020, Nature Microbiology.

Inactivation of Tumor Necrosis Factor-α by Proteinases (Gingipains) from the Periodontal Pathogen, Porphyromonas gingivalis

J. Potempa, J. Travis, C. C. Calkins, 1998, The Journal of Biological Chemistry.

A Metalloproteinase Karilysin Present in the Majority of Tannerella forsythia Isolates Inhibits All Pathways of the Complement System

A. Blom, K. Riesbeck, J. Potempa, 2012, The Journal of Immunology.

Cleavage of the human C5A receptor by proteinases derived from Porphyromonas gingivalis: cleavage of leukocyte C5a receptor.

J. Potempa, R. Pike, J. Travis, 1996, Advances in experimental medicine and biology.

The Bacteroidetes Q-Rule: Pyroglutamate in Signal Peptidase I Substrates

M. Bochtler, P. Veith, E. Reynolds, 2018, Front. Microbiol..

A new insight into phagocytosis of apoptotic cells: proteolytic enzymes divert the recognition and clearance of polymorphonuclear leukocytes by macrophages

J. Potempa, J. Travis, M. Bzowska, 2007, Cell Death and Differentiation.

Shut-Down of Type IX Protein Secretion Alters the Host Immune Response to Tannerella forsythia and Porphyromonas gingivalis

J. Potempa, C. Grünwald‐Gruber, S. Bloch, 2022, Frontiers in Cellular and Infection Microbiology.

Kallikrein 13 serves as a priming protease during infection by the human coronavirus HKU1

K. Pyrć, A. Milewska, P. Mak, 2020, Science Signaling.

Kallikrein 13: a new player in coronaviral infections

K. Pyrć, A. Milewska, P. Mak, 2020, bioRxiv.

Porphyromonas gingivalis Peptidyl Arginine Deiminase: A Unique Bacterial PAD with Implications for Periodontal Disease and Rheumatoid Arthritis

P. Venables, J. Potempa, K. Gawron, 2017 .

Purification, Characterization, and Sequence Analysis of a Potential Virulence Factor from Porphyromonas gingivalis, Peptidylarginine Deiminase

J. Potempa, W. McGraw, J. Travis, 1999, Infection and Immunity.

Antibodies to Porphyromonas gingivalis Indicate Interaction Between Oral Infection, Smoking, and Risk Genes in Rheumatoid Arthritis Etiology

Lars Alfredsson, Xia Jiang, Patrick J Venables, 2016, Arthritis & rheumatology.

Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia

J. Enghild, K. Zak, P. Grudnik, 2021, Journal of enzyme inhibition and medicinal chemistry.

07.14 Novel polymorphism of peptidylarginine deiminase from p. gingivalis augments bacterial pathogenicity and severity of periodontitis

K. Pyrć, P. Venables, J. Potempa, 2017 .

Miropin, a Novel Bacterial Serpin from the Periodontopathogen Tannerella forsythia, Inhibits a Broad Range of Proteases by Using Different Peptide Bonds within the Reactive Center Loop*

J. Enghild, C. Scavenius, J. Potempa, 2014, The Journal of Biological Chemistry.

Role of gingipains R in the pathogenesis of Porphyromonas gingivalis-mediated periodontal disease.

J. Potempa, C. Genco, J. Travis, 1999, Clinical infectious diseases : an official publication of the Infectious Diseases Society of America.

Mice Infection in Porphyromonas gingivalis Confers Immunity against A Peptide Domain on Gingipain R Which

J. Potempa, C. Genco, J. Travis, 1998 .

Inactivation of Membrane Tumor Necrosis Factor Alpha by Gingipains from Porphyromonas gingivalis

R. Black, N. Jura, J. Potempa, 2005, Infection and Immunity.

Does the Importance of the C-Terminal Residues in the Maturation of RgpB from Porphyromonas gingivalis Reveal a Novel Mechanism for Protein Export in a Subgroup of Gram-Negative Bacteria?

J. Potempa, K. Nguyen, J. Travis, 2006, Journal of bacteriology.

Porphyromonas gingivalis Virulence Factor Gingipain RgpB Shows a Unique Zymogenic Mechanism for Cysteine Peptidases*

J. Potempa, F. Veillard, F. Gomis-Rüth, 2013, The Journal of Biological Chemistry.

Sequential Autolytic Processing Activates the Zymogen of Arg-gingipain*

M. Bogyo, T. Nazif, J. Mikolajczyk, 2003, The Journal of Biological Chemistry.

Concentration of antibodies against Porphyromonas gingivalis is increased before the onset of symptoms of rheumatoid arthritis

S. Rantapää-Dahlqvist, K. Lundberg, J. Potempa, 2016, Arthritis Research & Therapy.

Complementary Tolls in the periodontium: how periodontal bacteria modify complement and Toll-like receptor responses to prevail in the host.

John D Lambris, J. Lambris, J. Potempa, 2010, Periodontology 2000.

The case for periodontitis in the pathogenesis of rheumatoid arthritis

J. Potempa, P. Mydel, J. Kozieł, 2017, Nature Reviews Rheumatology.

Porphyromonas gingivalis Facilitates the Development and Progression of Destructive Arthritis through Its Unique Bacterial Peptidylarginine Deiminase (PAD)

R. Jonsson, K. Pyrć, S. Alzabin, 2013, PLoS pathogens.

Effect of metalloproteinase from Staphylococcus aureus on in vitro stimulation of human lymphocytes.

M. Pospišil, J. Potempa, M. Pospíšil, 1988, Immunology letters.

Effect of serine proteinase from Staphylococcus aureus on in vitro stimulation of human lymphocytes.

J. Potempa, L. Prokešová, Z. Porwit-Bóbr, 1988, Immunology letters.

Citrullinome of Porphyromonas gingivalis Outer Membrane Vesicles: Confident Identification of Citrullinated Peptides.

P. Højrup, J. Potempa, G. Bereta, 2020, Molecular & cellular proteomics : MCP.

Citrullinome of Porphyromonas gingivalis Outer Membrane Vesicles: Confident Identification of Citrullinated Peptides*

P. Højrup, J. Potempa, G. Bereta, 2019, Molecular & Cellular Proteomics.

Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus.

G. Dubin, P. Daugherty, J. Potempa, 2018, Structure.

Staphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of Activation*

G. Dubin, G. Salvesen, G. Popowicz, 2014, The Journal of Biological Chemistry.

Structural and functional characterization of SplA, an exclusively specific protease of Staphylococcus aureus.

J. Enghild, G. Dubin, G. Popowicz, 2009, The Biochemical journal.

Enzymatic activity of the Staphylococcus aureus SplB serine protease is induced by substrates containing the sequence Trp-Glu-Leu-Gln.

J. Enghild, G. Dubin, G. Popowicz, 2008, Journal of molecular biology.

Functional and structural characterization of Spl proteases from Staphylococcus aureus.

G. Dubin, T. Holak, G. Popowicz, 2005, Journal of molecular biology.

Two Allelic Forms of the Aureolysin Gene (aur) within Staphylococcus aureus

B. van den Burg, A. Sękowska, J. Potempa, 2000, Infection and Immunity.

Cleavage of human immunoglobulins by proteinase from Staphylococcus aureus.

J. Potempa, B. Potužníková, J. Zikán, 1995, Advances in experimental medicine and biology.

Effect of calcium binding on conformational changes of staphylococcal metalloproteinase measured by means of intrinsic protein fluorescence.

W. Stryjewski, Z. Wasylewski, J. Potempa, 1986, Biochimica et biophysica acta.

C3-targeted therapy in periodontal disease: moving closer to the clinic.

John D Lambris, E. Ioannidou, B. Nilsson, 2021, Trends in immunology.

Identification and Characterization of σS, a Novel Component of the Staphylococcus aureus Stress and Virulence Responses

G. Stewart, J. Potempa, L. Shaw, 2008, PloS one.

Structural and functional probing of PorZ, an essential bacterial surface component of the type-IX secretion system of human oral-microbiomic Porphyromonas gingivalis.

J. Enghild, J. Potempa, Monika Bzowska, 2016, Scientific Reports.

In Search of Spectroscopic Signatures of Periodontitis: A SERS-Based Magnetomicrofluidic Sensor for Detection of Porphyromonas gingivalis and Aggregatibacter actinomycetemcomitans

J. Potempa, K. Niciński, A. Kamińska, 2021, ACS sensors.

Role of OmpA 2 surface regions of Porphyromonas gingivalis in host – pathogen interactions with oral epithelial cells

C. Murdoch, J. Potempa, C. Douglas, 2016 .

Genome Sequence of Porphyromonas gingivalis Strain HG66 (DSM 28984)

J. Potempa, I. Olsen, K. Nguyen, 2014, Genome Announcements.

Pros and cons of causative association between periodontitis and rheumatoid arthritis.

J. Potempa, J. Kozieł, 2022, Periodontology 2000.

Structure and mechanism of a bacterial host-protein citrullinating virulence factor, Porphyromonas gingivalis peptidylarginine deiminase

Theodoros Goulas, Claudia Millán, Isabel Usón, 2015, Scientific Reports.

Epigenetic regulation of inflammation in periodontitis: cellular mechanisms and therapeutic potential

J. Potempa, A. Grabiec, Krzysztof T. Jurdziński, 2020, Clinical Epigenetics.

Proteolytic processing and activation of gingipain zymogens secreted by T9SS of Porphyromonas gingivalis.

J. Enghild, M. Bogyo, J. Potempa, 2019, Biochimie.

Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitor

J. Potempa, F. Gomis-Rüth, M. Ksiazek, 2019, Scientific Reports.

Impact of Porphyromonas gingivalis Peptidylarginine Deiminase on Bacterial Biofilm Formation, Epithelial Cell Invasion, and Epithelial Cell Transcriptional Landscape

R. Lamont, N. Delaleu, B. Bergum, 2018, Scientific Reports.

FACIN, a Double-Edged Sword of the Emerging Periodontal Pathogen Filifactor alocis: A Metabolic Enzyme Moonlighting as a Complement Inhibitor

A. Blom, K. Riesbeck, J. Potempa, 2016, The Journal of Immunology.

A Metalloproteinase Mirolysin of Tannerella forsythia Inhibits All Pathways of the Complement System

A. Blom, K. Riesbeck, J. Potempa, 2013, The Journal of Immunology.

Complement System Inhibits All Pathways of the forsythia Tannerella A Metalloproteinase Mirolysin of

A. Blom, K. Riesbeck, J. Potempa, 2015 .

Filifactor alocis Infection and Inflammatory Responses in the Mouse Subcutaneous Chamber Model

R. Jotwani, S. Uriarte, R. Lamont, 2013, Infection and Immunity.

A Comparison of Staphostatin B with Standard Mechanism Serine Protease Inhibitors*

M. Bochtler, J. Potempa, R. Filipek, 2005, Journal of Biological Chemistry.

A Novel Mechanism of Latency in Matrix Metalloproteinases*

J. Potempa, F. Gomis-Rüth, M. Lopez-pelegrin, 2015, The Journal of Biological Chemistry.

Evolutionary Adaptations of Serpins and their Use in Designing New Proteinase Inhibitors

J. Potempa, J. Travis, B. Shieh, 1990 .

Site-specific O-Glycosylation on the MUC2 Mucin Protein Inhibits Cleavage by the Porphyromonas gingivalis Secreted Cysteine Protease (RgpB)

E. Bennett, M. Bäckström, J. Potempa, 2013, The Journal of Biological Chemistry.

Inactive Gingipains from P. gingivalis Selectively Skews T Cells toward a Th17 Phenotype in an IL-6 Dependent Manner

R. Lamont, I. Główczyk, J. Potempa, 2017, Front. Cell. Infect. Microbiol..

Biphasic Effect of Gingipains from Porphyromonas gingivalis on the Human Complement System1

A. Blom, K. Riesbeck, J. Potempa, 2007, The Journal of Immunology.

Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis

J. Potempa, M. Abrahamson, S. Eick, 2011, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Unaltered expression of the major protease genes in a non-virulent recA-defective mutant of Porphyromonas gingivalis W83.

J. Potempa, H. Abaibou, H. Fletcher, 2000, Oral microbiology and immunology.

Detection of Porphyromonas gingivalis in gingival exudate by a dipeptide-enhanced trypsin-like activity.

J. Potempa, J. Travis, M. Wikström, 1994, The Journal of Periodontology.

In vivo expression of proteases and protease inhibitor, a serpin, by periodontal pathogens at teeth and implants

J. Potempa, A. Sculean, S. Eick, 2018, Molecular oral microbiology.

Correction: Pyocycanin, a Contributory Factor in Haem Acquisition and Virulence Enhancement of Porphyromonas gingivalis in the Lung

D. Byrne, T. Olczak, J. Smalley, 2016, PloS one.

Pyocycanin, a Contributory Factor in Haem Acquisition and Virulence Enhancement of Porphyromonas gingivalis in the Lung

D. Byrne, T. Olczak, J. Smalley, 2015, PloS one.

Evidence of mutualism between two periodontal pathogens: co-operative haem acquisition by the HmuY haemophore of Porphyromonas gingivalis and the cysteine protease interpain A (InpA) of Prevotella intermedia.

D. Byrne, T. Olczak, J. Smalley, 2013, Molecular oral microbiology.

Correction: HmuY Haemophore and Gingipain Proteases Constitute a Unique Syntrophic System of Haem Acquisition by Porphyromonas gingivalis

D. Byrne, T. Olczak, J. Smalley, 2011, PLoS ONE.

Role of the cysteine protease interpain A of Prevotella intermedia in breakdown and release of haem from haemoglobin.

D. Byrne, J. Smalley, J. Potempa, 2009, The Biochemical journal.

Sequential action of R- and K-specific gingipains of Porphyromonas gingivalis in the generation of the haem-containing pigment from oxyhaemoglobin.

J. Smalley, J. Potempa, A. Birss, 2007, Archives of biochemistry and biophysics.

Purification and Characterization of Gingipains

J. Potempa, K. Nguyen, 2007, Current protocols in protein science.

A relationship between proteinase activity and clinical parameters in the treatment of periodontal disease.

J. Potempa, J. Travis, C. Russell, 1998, Journal of clinical periodontology.

Stimulation of proteinase and amidase activities in Porphyromonas (Bacteroides) gingivalis by amino acids and dipeptides

J. Potempa, J. Travis, M. Wikström, 1991, Infection and immunity.

Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K from Porphyromonas gingivalis, a causative agent of gum disease from the human oral microbiome*

J. Huntington, J. Potempa, F. Veillard, 2017, The Journal of Biological Chemistry.

Structure and Mechanism of Cysteine Peptidase Gingipain K (Kgp), a Major Virulence Factor of Porphyromonas gingivalis in Periodontitis*

J. Huntington, J. Potempa, F. Veillard, 2014, The Journal of Biological Chemistry.

Structure and mechanism of cysteine peptidase Kgp , a major virulence factor of Porphyromonas gingivalis in periodontitis * *

J. Huntington, J. Potempa, F. Veillard, 2014 .

Adhesive protein-mediated cross-talk between Candida albicans and Porphyromonas gingivalis in dual species biofilm protects the anaerobic bacterium in unfavorable oxic environment

J. Potempa, Z. Rajfur, J. Karkowska-Kuleta, 2019, Scientific Reports.

The Role of Gingival Fibroblasts in the Pathogenesis of Periodontitis

J. Potempa, A. Wielento, K. B. Lagosz-Cwik, 2023, Journal of dental research.

The S-layer proteins of Tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein O-glycosylation.

J. Potempa, P. Messner, L. Mach, 2014, Molecular oral microbiology.

Sequence‐independent processing site of the C‐terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis

J. Potempa, Xiaoyan Zhou, Jinlong Gao, 2013, Molecular microbiology.

Chapter 486 – Interpain A

J. Potempa, 2013 .

A Phage Display Selected 7-mer Peptide Inhibitor of the Tannerella forsythia Metalloprotease-Like Enzyme Karilysin can be Truncated to Ser-Trp-Phe-Pro

J. Potempa, P. Skottrup, M. Ksiazek, 2012, PloS one.

Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis.

J. Enghild, J. Potempa, F. Veillard, 2011, Analytical biochemistry.

A New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain A*

J. Enghild, J. Potempa, M. Solà, 2008, Journal of Biological Chemistry.

PorZ, an Essential Component of the Type IX Secretion System of Porphyromonas gingivalis, Delivers Anionic Lipopolysaccharide to the PorU Sortase for Transpeptidase Processing of T9SS Cargo Proteins

J. Enghild, C. Scavenius, J. Potempa, 2021, mBio.

The essential Porphyromonas gingivalis type IX secretion system component PorZ delivers anionic-lipopolysaccharide to the PorU sortase for transpeptidase processing of cargos

J. Enghild, C. Scavenius, J. Potempa, 2020, bioRxiv.

Vaccination with recombinant RgpA peptide protects against Porphyromonas gingivalis‐induced bone loss

J. Potempa, L. Shapira, A. Wilensky, 2017, Journal of periodontal research.

Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis

J. Potempa, F. Veillard, K. Nguyen, 2015, Biological chemistry.

Purification and characterization of a novel cysteine proteinase (periodontain) from Porphyromonas gingivalis. Evidence for a role in the inactivation of human alpha1-proteinase inhibitor.

T. Kordula, J. Potempa, D. Nelson, 1999, The Journal of biological chemistry.

Antibodies to Porphyromonas gingivalis Are Increased in Patients with Severe Periodontitis, and Associate with Presence of Specific Autoantibodies and Myocardial Infarction

E. Svenungsson, K. Lundberg, J. Potempa, 2022, Journal of clinical medicine.

A unique bacterial secretion machinery with multiple secretion centers

E. Cascales, R. Lamont, Chenggang Wu, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis.

J. Potempa, T. Goulas, I. Garcia-Ferrer, 2016, Molecular oral microbiology.

Molecular Diversity of a Putative Virulence Factor: Purification and Characterization of Isoforms of an Extracellular Serine Glutamyl Endopeptidase of Enterococcus faecalis with Different Enzymatic Activities

J. Potempa, B. Murray, J. Travis, 2005, Journal of bacteriology.

New Method for Typing Staphylococcus aureus Strains: Multiple-Locus Variable-Number Tandem Repeat Analysis of Polymorphism and Genetic Relationships of Clinical Isolates

James Travis, J. Krzysztoń-Russjan, J. Potempa, 2003, Journal of Clinical Microbiology.

Subversion of Lipopolysaccharide Signaling in Gingival Keratinocytes via MCPIP-1 Degradation as a Novel Pathogenic Strategy of Inflammophilic Pathobionts

R. Lamont, J. Potempa, J. Jura, 2021, mBio.

Peptidylarginine Deiminase of Porphyromonas gingivalis Modulates the Interactions between Candida albicans Biofilm and Human Plasminogen and High-Molecular-Mass Kininogen

J. Potempa, J. Karkowska-Kuleta, A. Kozik, 2020, International journal of molecular sciences.

Dynamic oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis

J. Enghild, N. Ranson, S. Rawson, 2019, bioRxiv.

Porphyromonas gingivalis induce apoptosis in human gingival epithelial cells through a gingipain-dependent mechanism

J. Potempa, D. Kinane, M. Benakanakere, 2009, BMC Microbiology.

Proteinase-mediated Release of Epithelial Cell-associated CD44

E. Puré, R. Bals, J. Potempa, 2002, The Journal of Biological Chemistry.

Benzamidine derivatives inhibit the virulence of Porphyromonas gingivalis.

J. Potempa, S. Eick, W. Pfister, 2013, Molecular oral microbiology.

The activity of bacterial peptidylarginine deiminase is important during formation of dual‐species biofilm by periodontal pathogen Porphyromonas gingivalis and opportunistic fungus Candida albicans

J. Potempa, Z. Rajfur, J. Karkowska-Kuleta, 2018, Pathogens and disease.

Phage display selection of human single domain antibodies towards karilysin, a metalloproteinase and secreted virulence factor from Tannerella forsythia.

J. Potempa, P. Skottrup, M. Ksiazek, 2023, Journal of immunological methods.

Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease‐activated receptors with Toll‐like receptor and NOD1/2 ligands in human monocytic cells

J. Potempa, T. Imamura, J. Travis, 2008, Cellular microbiology.

PDFlib PLOP: PDF Linearization, Optimization, Protection Page inserted by evaluation version www.pdflib.com – sales@pdflib.com Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease-activated receptors with Toll-like receptor and

J. Potempa, T. Imamura, J. Travis, 2008 .

Association of Distinct Fine Specificities of Anti−Citrullinated Peptide Antibodies With Elevated Immune Responses to Prevotella intermedia in a Subgroup of Patients With Rheumatoid Arthritis and Periodontitis

H. Sayles, R. Fischer, T. Mikuls, 2017, Arthritis & rheumatology.

Meprin β induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage

S. Rose-John, P. Saftig, A. Tholey, 2019, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia

J. Enghild, J. Potempa, I. Thøgersen, 2015, Biological chemistry.

Tethering soluble meprin α in an enzyme complex to the cell surface affects IBD‐associated genes

P. Rosenstiel, R. Häsler, J. Potempa, 2019, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037

J. Enghild, G. Dubin, P. Daugherty, 2010, Biological chemistry.

Lysine-specific gingipain promotes lipopolysaccharide- and active-vitamin D3-induced osteoclast differentiation by degrading osteoprotegerin.

Y. Miyamoto, J. Potempa, R. Kamijo, 2009, The Biochemical journal.

Gingipain enzymes from Porphyromonas gingivalis preferentially bind immobilized extracellular proteins: a mechanism favouring colonization?

J. Potempa, R. Pike, J. Travis, 2009, Journal of Periodontal Research.

Antibodies against Porphyromonas gingivalis in serum and saliva and their association with rheumatoid arthritis and periodontitis. Data from two rheumatoid arthritis cohorts in Sweden

J. Potempa, G. R. Persson, B. Potempa, 2023, Frontiers in Immunology.

Fibroblasts from recurrent fibrotic overgrowths reveal high rate of proliferation in vitro - findings from the study of hereditary and idiopathic gingival fibromatosis

A. Fertala, J. Potempa, K. Gawron, 2018, Connective tissue research.

Gingival Fibromatosis with Significant De Novo Formation of Fibrotic Tissue and a High Rate of Recurrence

A. Fertala, J. Potempa, K. Gawron, 2016, The American journal of case reports.

In vitro testing the potential of a novel chimeric IgG variant for inhibiting collagen fibrils formation in recurrent hereditary gingival fibromatosis: chimeric antibody in a gingival model.

K. Pyrć, J. Potempa, K. Stęplewska, 2014, Journal of physiology and pharmacology : an official journal of the Polish Physiological Society.

Gingipains: Critical Factors in the Development of Aspiration Pneumonia Caused by Porphyromonas gingivalis

K. Pyrć, A. Milewska, N. Delaleu, 2015, Journal of Innate Immunity.

A Unique Mdm2-Binding Mode of the 3-Pyrrolin-2-one- and 2-Furanone-Based Antagonists of the p53-Mdm2 Interaction.

K. Zak, B. Musielak, P. Grudnik, 2016, ACS chemical biology.

Interpain A, a Cysteine Proteinase from Prevotella intermedia, Inhibits Complement by Degrading Complement Factor C3

A. Blom, K. Riesbeck, J. Potempa, 2009, PLoS pathogens.

Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases.

J. Enghild, J. Potempa, F. Veillard, 2013, Biochimica et biophysica acta.

Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage

G. Dubin, Ties Latendorf, J. Potempa, 2009, Biological chemistry.

The gingipains from Porphyromonas gingivalis do not directly induce osteoclast differentiation in primary mouse bone marrow cultures.

J. Potempa, R. Pike, C. Pagel, 2009, Journal of periodontal research.

Binding of Complement Inhibitor C4b-Binding Protein Contributes to Serum Resistance of Porphyromonas gingivalis1

A. Blom, M. Okrój, K. Riesbeck, 2008, The Journal of Immunology.

Complement System Porphyromonas gingivalis on the Human Biphasic Effect of Gingipains from

A. Blom, K. Riesbeck, J. Potempa, 2013 .

Porphyromonas gingivalis Resistance of C 4 b-Binding Protein Contributes to Serum Binding of Complement Inhibitor and

A. Blom, M. Okrój, K. Riesbeck, 2008 .

Gingipain aminopeptidase activities in Porphyromonas gingivalis

J. Potempa, F. Veillard, M. Poręba, 2012, Biological chemistry.

Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition.

M. Bochtler, J. Potempa, A. Sabat, 2004, Biochemistry.

The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain

J. Enghild, G. Dubin, J. Trewhella, 2016, Scientific Reports.

Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB.

P. Rosenstiel, S. Rose-John, P. Dempsey, 2017, Cell reports.

TLR2 Activation by Porphyromonas gingivalis Requires Both PPAD Activity and Fimbriae

R. Lamont, J. Potempa, S. Eick, 2022, Frontiers in Immunology.

The RagA and RagB proteins of Porphyromonas gingivalis.

J. Potempa, D. Scott, M. Madej, 2021, Molecular oral microbiology.

Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola

J. Potempa, K. Ishihara, M. Miyamoto, 2010, Biological chemistry.

Pharmacokinetics of sulbactam and ampicillin intravenously applied in combination to healthy volunteers and patients. Determination of the ratio of the two drugs in serum and in various tissues.

K. Engel, J. Potempa, A. Schilling, 1988, Arzneimittel-Forschung.

[The presence of apoptotic neutrophils in contents of neck lateral cysts].

J. Potempa, K. Guzik, W. Dobroś, 2010, Przeglad lekarski.

Gingipains impair attachment of epithelial cell to dental titanium abutment surfaces.

J. Potempa, A. Sculean, S. Eick, 2019, Journal of biomedical materials research. Part B, Applied biomaterials.

Citrullination in the periodontium—a possible link between periodontitis and rheumatoid arthritis

P. Venables, J. Potempa, A. Sculean, 2016, Clinical Oral Investigations.

Grafting of antibodies inside integrated microfluidic-microoptic devices by means of automated microcontact printing.

J. Potempa, J. Vieillard, B. Hannes, 2009, Sensors and actuators. B, Chemical.

The etching of glass patterned by microcontact printing with application to microfluidics and electrophoresis

J. Potempa, J. Vieillard, R. Mazurczyk, 2008 .

Gingipains from Porphyromonas gingivalis W83 Synergistically Disrupt Endothelial Cell Adhesion and Can Induce Caspase-Independent Apoptosis

J. Potempa, H. Fletcher, J. Travis, 2006, Infection and Immunity.

Chapter 185 – Karilysin

J. Potempa, 2013 .

Mechanisms Mediating Porphyromonas gingivalis Gingipain RgpA-Induced Oral Mucosa Inflammation In Vivo

J. Potempa, I. Rubinstein, J. Travis, 2001, Infection and Immunity.

Functional Analysis of Porphyromonas gingivalis W83 CRISPR-Cas Systems

K. Pyrć, M. Bochtler, J. Potempa, 2015, Journal of bacteriology.

Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes

J. Enghild, M. Bogyo, J. Potempa, 2012, Biological chemistry.

PPAD remains a credible candidate for inducing autoimmunity in rheumatoid arthritis: comment on the article by Konig et al.

T. Mikuls, K. Lundberg, P. Venables, 2015, Annals of the rheumatic diseases.

Inhibits All Pathways of the Complement Isolates Tannerella forsythia Majority of A Metalloproteinase Karilysin Present in the

A. Blom, J. Potempa, P. Garred, 2017 .

Aristolochic acid I determine the phenotype and activation of macrophages in acute and chronic kidney disease

S. Steiger, J. Potempa, M. Lech, 2018, Scientific Reports.

Accessory fimbrial subunits and PPAD are necessary for TLR2 activation by Porphyromonas gingivalis.

Maxim N. Artyomov, M. Artyomov, J. Potempa, 2023, Molecular oral microbiology.

Domain shuffling of a highly mutable ligand‐binding fold drives adhesin generation across the bacterial kingdom

A. Bateman, S. Burston, J. Potempa, 2023, Proteins.

Breakdown of albumin and haemalbumin by the cysteine protease interpain A, an albuminase of Prevotella intermedia

D. Byrne, J. Smalley, J. Potempa, 2015, BMC Microbiology.

Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family

G. Dubin, J. Silberring, J. Potempa, 2004, Biological chemistry.

Highly multiplexed bioactivity screening reveals human and microbiota metabolome-GPCRome interactions

J. Potempa, A. Ring, Noah W. Palm, 2023, Cell.

Gingival Fibromatosis with Significant De Novo Formation of Fibrotic Tissue and a High Rate of Recurrence.

A. Fertala, J. Potempa, K. Gawron, 2016, The American journal of case reports.

A pathogenic trace of Tannerella forsythia - shedding of soluble fully active tumor necrosis factor α from the macrophage surface by karilysin.

J. Potempa, E. Bielecka, M. Ksiazek, 2014, Molecular oral microbiology.

Noncatalytic protein component of elastase from horse leucocytes. A protein with regulatory function.

J. Silberring, J. Potempa, E. Korzus, 1988, The International journal of biochemistry.

Citrullination Alters Immunomodulatory Function of LL-37 Essential for Prevention of Endotoxin-Induced Sepsis

K. Pyrć, I. Główczyk, J. Potempa, 2014, The Journal of Immunology.

Cleavage of the Human C5A Receptor by Protienases Derived from Porphyromonas Gingivalis

J. Potempa, R. Pike, J. Travis, 1996 .

Inhibition of CDK9 as a therapeutic strategy for inflammatory arthritis

A. Kehlen, A. Hellvard, N. Delaleu, 2016, Scientific Reports.

Citrullination of C1-inhibitor as a mechanism of impaired complement regulation in rheumatoid arthritis

J. Enghild, B. Nilsson, K. Ekdahl, 2023, Frontiers in Immunology.

Structure, function, and inhibition of a genomic/clinical variant of Porphyromonas gingivalis peptidylarginine deiminase

J. Potempa, M. Solà, E. Bielecka, 2019, Protein science : a publication of the Protein Society.

Porphyromonas gingivalis peptidylarginine deminase (PPAD) mutant G231N/E232T/N235D in complex with Cl-amidine.

J. Potempa, M. Solà, E. Bielecka, 2019 .

Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR

J. Potempa, X. Liu, C. Genco, 2004, Biological chemistry.

Staphylococcal proteases aid evasion of human complement system

G. Dubin, A. Blom, J. Potempa, 2012 .

Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitor

J. Potempa, F. Gomis-Rüth, M. Ksiazek, 2019, Scientific Reports.

Oral Abstracts 7: RA ClinicalO37. Long-Term Outcomes of Early RA Patients Initiated with Adalimumab Plus Methotrexate Compared with Methotrexate Alone Following a Targeted Treatment Approach

H. L. Wright, R. Moots, T. Spector, 2013 .

Porphyromonas gingivalis Peptidyl Arginine Deiminase (PPAD) in the Context of the Feed-Forward Loop of Inflammation in Periodontitis

J. Potempa, M. Sochalska, Zsombor Prucsi, 2023, International journal of molecular sciences.

Impact of Porphyromonas gingivalis Peptidylarginine Deiminase on Bacterial Biofilm Formation, Epithelial Cell Invasion, and Epithelial Cell Transcriptional Landscape

R. Lamont, B. Bergum, J. Potempa, 2018, Scientific Reports.

Alpha 2-macroglobulin from horse plasma. Purification, properties and interaction with certain serine proteinases.

J. Silberring, J. Potempa, A. Dubin, 1984, Biochemistry International.

Structural and functional characterization of elastases from horse neutrophils.

J. Potempa, J. Travis, A. Dubin, 1994, The Biochemical journal.

Bacterial proteases in disease - role in intracellular survival, evasion of coagulation/ fibrinolysis innate defenses, toxicoses and viral infections.

K. Pyrć, G. Dubin, J. Potempa, 2012, Current pharmaceutical design.

A Novel Mechanism of Latency in Matrix Metalloproteinases*

J. Potempa, F. Gomis-Rüth, M. Lopez-pelegrin, 2015, The Journal of Biological Chemistry.

Porphyromonas gingivalis proteinases in periodontitis, a review.

J. Potempa, J. Travis, 1996, Acta biochimica Polonica.

Cleavage of Host Cytokeratin-6 by Lysine-Specific Gingipain Induces Gingival Inflammation in Periodontitis Patients

Takashi Ito, I. Maruyama, K. Kikuchi, 2015, PloS one.

Inhibition of GSK3 Abolishes Bacterial-Induced Periodontal Bone Loss in Mice

R. Jotwani, J. Potempa, D. Scott, 2012, Molecular medicine.

Filifactor alocis Infection and Inflammatory Responses in the Mouse Subcutaneous Chamber Model

R. Jotwani, S. Uriarte, R. Lamont, 2013, Infection and Immunity.

Verification of a topology model of PorT as an integral outer-membrane protein in Porphyromonas gingivalis.

J. Potempa, K. Nguyen, Paweł Szczęsny, 2009, Microbiology.

Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity.

J. Potempa, R. Pike, J. Travis, 2001, Blood.

An IgY-based immunoassay to evaluate the biomarker potential of the Tannerella forsythia virulence factor karilysin in human saliva.

P. Højrup, V. Baelum, J. Potempa, 2019, Journal of immunological methods.

Dual regulation of interleukin-8 production in human oral epithelial cells upon stimulation with gingipains from Porphyromonas gingivalis.

J. Potempa, T. Imamura, M. Naito, 2008, Journal of medical microbiology.

Bacterial peptidases.

J. Potempa, R. Pike, 2005, Contributions to microbiology.

Role of gingipains R in the pathogenesis of Porphyromonas gingivalis-mediated periodontal disease.

J. Potempa, C. Genco, J. Travis, 1999, Clinical infectious diseases : an official publication of the Infectious Diseases Society of America.

Staphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of Activation*

G. Dubin, G. Salvesen, G. Popowicz, 2014, The Journal of Biological Chemistry.

hTERT-immortalized gingival fibroblasts respond to cytokines but fail to mimic primary cell responses to Porphyromonas gingivalis

S. Gibbs, J. Potempa, T. Kaczmarzyk, 2021, Scientific Reports.

Treatment of severe periodontitis may improve clinical disease activity in otherwise treatment-refractory rheumatoid arthritis patients.

S. Reichenbach, J. Potempa, A. Sculean, 2019, Rheumatology.

Pyocycanin, a Contributory Factor in Haem Acquisition and Virulence Enhancement of Porphyromonas gingivalis in the Lung

D. Byrne, T. Olczak, J. Smalley, 2015, PloS one.

Horse leucocyte proteinase-inhibitor system. Kinetic parameters of the inhibition reaction.

J. Silberring, J. Potempa, A. Dubin, 1985, The International journal of biochemistry.

Chemoattractant activity of Staphylococcus aureus serine proteinase modified human plasma α-1-proteinase inhibitor

J. Potempa, Z. Porwit-Bóbr, M. Gorka, 1989, Antonie van Leeuwenhoek.

Comparative properties of three functionally different but structurally related serpin variants from horse plasma.

J. Potempa, J. Travis, J. Wunderlich, 1991, The Biochemical journal.