M. Ksiazek

发表

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.

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.

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 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.

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

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

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.

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.

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.

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..

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

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

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.

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.

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.

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.

Anti-CD44 DNA Aptamers Selectively Target Cancer Cells.

G. Dubin, T. Holak, A. Pęcak, 2020, Nucleic acid therapeutics.

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.

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.

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 .

A Novel Mechanism of Latency in Matrix Metalloproteinases*

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

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.

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.

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

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

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.

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

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

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.

Development of a novel, high-affinity ssDNA trypsin inhibitor

P. Grudnik, G. Dubin, A. Pęcak, 2019, Journal of enzyme inhibition and medicinal chemistry.

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.

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

A. Blom, J. Potempa, P. Garred, 2017 .

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.

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.

A Novel Mechanism of Latency in Matrix Metalloproteinases*

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

A pathogenic trace of Tannerella forsythia - shedding of soluble fully active tumor necrosis factor α from the macrophage surface by karilysin.

M. Ksiazek, B. Potempa, A. Karim, 2014, Molecular oral microbiology.

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.

The Structure of the Catalytic Domain of Tannerella Forsythia Karilysin Reveals It Is a Bacterial Xenolog of Animal Matrix Metalloproteinases Nih Public Access Author Manuscript

K. Nguyen, J. Arolas, M. Ksiazek, 2022 .