I. Thøgersen

发表

Structural and Functional Implications of Human Transforming Growth Factor β-Induced Protein, TGFBIp, in Corneal Dystrophies.

J. Enghild, R. García-Castellanos, N. S. Nielsen, 2017, Structure.

Spider genomes provide insight into composition and evolution of venom and silk

Jun Wang, X. Fang, Jinjie Duan, 2014, Nature Communications.

Purification and characterization of an alpha-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris.

J. Enghild, S. Pizzo, G. Salvesen, 1992, The Biochemical journal.

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

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

Potential clinical importance of the activation peptide of prostate-specific antigen.

J. Enghild, T. Oury, C. Chu, 2009, International journal of clinical and experimental pathology.

Extracellular Superoxide Dismutase (EC-SOD) Binds to Type I Collagen and Protects Against Oxidative Fragmentation*

R. Bowler, J. Crapo, J. Enghild, 2004, Journal of Biological Chemistry.

The Heparin-binding Domain of Extracellular Superoxide Dismutase Is Proteolytically Processed Intracellularly during Biosynthesis*

J. Crapo, J. Enghild, P. Højrup, 1999, The Journal of Biological Chemistry.

The Protein Composition of the Digestive Fluid from the Venus Flytrap Sheds Light on Prey Digestion Mechanisms*

J. Schultz, J. Enghild, P. Højrup, 2012, Molecular & Cellular Proteomics.

Differential expression and processing of transforming growth factor beta induced protein (TGFBIp) in the normal human cornea during postnatal development and aging.

J. Enghild, T. Møller-Pedersen, K. Runager, 2010, Experimental eye research.

Proteolytic Activities of Human ADAMTS-5

J. Enghild, M. Kashiwagi, I. Thøgersen, 2007, Journal of Biological Chemistry.

Degradation of Interleukin 1β by Matrix Metalloproteinases*

Y. Sasaguri, J. Enghild, Y. Itoh, 1996, The Journal of Biological Chemistry.

Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family

J. Enghild, L. Schauser, G. R. Andersen, 2022, Nature Communications.

Characterization of the gila monster (Heloderma suspectum suspectum) venom proteome.

J. Enghild, I. Thøgersen, Tobias Wang, 2015, Journal of proteomics.

Characterization of the gila monster (Heloderma suspectum suspectum) venom proteome

J. Enghild, I. Thøgersen, Tobias Wang, 2015, Data in brief.

Original Article Potential Clinical Importance of the Activation Peptide of Prostate-specific Antigen

J. Enghild, T. Oury, C. Chu, 2009 .

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

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

Alpha-macroglobulin from Limulus polyphemus exhibits proteinase inhibitory activity and participates in a hemolytic system.

J. Enghild, S. Pizzo, G. Salvesen, 1990, Biochemistry.

Evidence against a blood derived origin for transforming growth factor beta induced protein in corneal disorders caused by mutations in the TGFBI gene

J. Enghild, T. Møller-Pedersen, I. Thøgersen, 2007, Molecular vision.

Analysis of Factor D Isoforms in Malpuech–Michels–Mingarelli–Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement

J. Enghild, S. Thiel, A. Hansen, 2017, The Journal of Immunology.

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

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

Differential Regulation of Extracellular Tissue Inhibitor of Metalloproteinases-3 Levels by Cell Membrane-bound and Shed Low Density Lipoprotein Receptor-related Protein 1

J. Enghild, H. Emonard, D. Strickland, 2012, The Journal of Biological Chemistry.

The paradigm that all oxygen-respiring eukaryotes have cytosolic CuZn-superoxide dismutase and that Mn-superoxide dismutase is localized to the mitochondria does not apply to a large group of marine arthropods.

J. Enghild, M. Brouwer, I. Thøgersen, 1997, Biochemistry.

The low-density lipoprotein receptor-related protein 1 (LRP1) interactome in the human cornea.

J. Enghild, I. Thøgersen, E. T. Poulsen, 2022, Experimental eye research.

The Intracellular Proteolytic Processing of Extracellular Superoxide Dismutase (EC-SOD) is a Two-step Event*

R. Bowler, J. Crapo, J. Enghild, 2004, Journal of Biological Chemistry.

The high concentration of Arg213-->Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities.

J. Crapo, J. Enghild, T. Oury, 2005, The Biochemical journal.

The human cornea proteome: bioinformatic analyses indicate import of plasma proteins into the cornea.

J. Enghild, T. Møller-Pedersen, I. Thøgersen, 2006, Molecular vision.

Primary structure and tissue-specific expression of blue crab (Callinectes sapidus) metallothionein isoforms.

J. Enghild, M. Brouwer, I. Thøgersen, 1995, The Biochemical journal.

The dual nature of human extracellular superoxide dismutase: One sequence and two structures

J. Crapo, J. Enghild, P. Højrup, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Furin Proteolytically Processes the Heparin-binding Region of Extracellular Superoxide Dismutase*

R. Bowler, J. Crapo, J. Enghild, 2002, The Journal of Biological Chemistry.

Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins

P. Mak, I. Thøgersen, A. Dubin, 1996, Infection and immunity.

A top-down approach to uncover the hidden ligandome of low-density lipoprotein receptor-related protein 1 in cartilage.

J. Enghild, C. Scavenius, George Bou-Gharios, 2022, Matrix biology : journal of the International Society for Matrix Biology.

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.

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

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

The Compact and Biologically Relevant Structure of Inter-α-inhibitor Is Maintained by the Chondroitin Sulfate Chain and Divalent Cations*

J. Enghild, D. Otzen, C. Scavenius, 2016, The Journal of Biological Chemistry.

Human inter-α-inhibitor is a substrate for factor XIIIa and tissue transglutaminase.

J. Enghild, P. Højrup, O. Jensen, 2011, Biochimica et biophysica acta.

Organization of the inter-alpha-inhibitor heavy chains on the chondroitin sulfate originating from Ser(10) of bikunin: posttranslational modification of IalphaI-derived bikunin.

J. Enghild, P. Roepstorff, H. Rahbek-Nielsen, 1999, Biochemistry.

New member of the trefoil factor family of proteins is an α-macroglobulin protease inhibitor

J. Enghild, S. Pizzo, S. Hammes, 2002 .

The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.

J. Enghild, V. Dive, I. Thøgersen, 2009, Matrix biology : journal of the International Society for Matrix Biology.

The diversity of FtsY-lipid interactions.

J. Enghild, D. Otzen, K. Nielsen, 2010, Biopolymers.

Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor.

J. Enghild, S. Pizzo, G. Salvesen, 1991, The Journal of biological chemistry.

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

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

Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain 2/bikunin.

J. Enghild, S. Pizzo, G. Salvesen, 1993, The Journal of biological chemistry.

Analysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor, pre-alpha-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycan.

J. Enghild, S. Pizzo, G. Salvesen, 1989, The Journal of biological chemistry.

The TSG-6 and IαI Interaction Promotes a Transesterification Cleaving the Protein-Glycosaminoglycan-Protein (PGP) Cross-link*[boxs]

J. Enghild, I. Thøgersen, K. W. Sanggaard, 2005, 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.

Activated Human Plasma Carboxypeptidase B Is Retained in the Blood by Binding to α2-Macroglobulin and Pregnancy Zone Protein*

J. Enghild, S. Pizzo, C. Chu, 1996, The Journal of Biological Chemistry.

The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis.

J. Crapo, J. Enghild, S. Moestrup, 2010, Free radical biology & medicine.

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.

Human Cornea Proteome: Identification and Quantitation of the Proteins of the Three Main Layers Including Epithelium, Stroma, and Endothelium

J. Enghild, H. Vorum, C. Scavenius, 2012, Journal of proteome research.

An examination of the inhibitory mechanism of serpins by analysing the interaction of trypsin and chymotrypsin with alpha 2-antiplasmin.

J. Enghild, S. Pizzo, G. Salvesen, 1993, The Biochemical journal.

Identification of hemoglobin and two serine proteases in acid extracts of calcium containing kidney stones.

I. Thøgersen, T. E. Petersen, S. E. Petersen, 1989, The Journal of urology.

Proteomics of Fuchs’ Endothelial Corneal Dystrophy Support That the Extracellular Matrix of Descemet’s Membrane Is Disordered

J. Enghild, P. Højrup, H. Vorum, 2014, Journal of proteome research.

Proteomic Analysis of the Soluble Fraction from Human Corneal Fibroblasts with Reference to Ocular Transparency*

J. Enghild, T. Møller-Pedersen, I. Thøgersen, 2004, Molecular & Cellular Proteomics.

Composition and proteolytic processing of corneal deposits associated with mutations in the TGFBI gene.

J. Enghild, P. Højrup, K. Runager, 2012, Experimental eye research.

A conserved region in alpha-macroglobulins participates in binding to the mammalian alpha-macroglobulin receptor.

J. Enghild, S. Pizzo, P. Roche, 1989, Biochemistry.

Identification of monomeric α-macroglobulin proteinase inhibitors in birds, reptiles, amphibians and mammals, and purification and characterization of a monomeric α-macroglobulin proteinase inhibitor from the American bullfrog Rana catesbiana

J. Enghild, S. Pizzo, I. Thøgersen, 1993 .

α1‐Microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound

J. Enghild, T. Cedervall, I. Thøgersen, 1999, Protein science : a publication of the Protein Society.

α1-Microglobulin Destroys the Proteinase Inhibitory Activity of α1-Inhibitor-3 by Complex Formation (*)

J. Enghild, S. Pizzo, G. Salvesen, 1995, The Journal of Biological Chemistry.

The Proteome of Seed Development in the Model Legume Lotus japonicus1[C][W]

J. Enghild, S. Besenbacher, S. Tabata, 2009, Plant Physiology.

ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1)

J. Enghild, N. Ito, Y. Itoh, 2015, Molecular biology of the cell.

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.

Additions and Corrections

I. Thøgersen, P. K. Nielsen, 2005 .

Unique Structural Features Facilitate Lizard Tail Autotomy

J. Enghild, N. Nielsen, I. Thøgersen, 2012, PloS one.

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.

Glucagon fibril polymorphism reflects differences in protofilament backbone structure.

Daniel Erik Otzen, Louise C Serpell, J. Enghild, 2010, Journal of molecular biology.

Secreted major Venus flytrap chitinase enables digestion of Arthropod prey.

J. Enghild, R. Hedrich, I. Thøgersen, 2014, Biochimica et biophysica acta.

Characterization of a novel cold-adapted intracellular serine protease from the extremophile Planococcus halocryophilus Or1

J. Enghild, C. Scavenius, I. Thøgersen, 2023, Frontiers in Microbiology.

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.

Enzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid*

J. Enghild, C. Scavenius, I. Thøgersen, 2015, The Journal of Biological 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.

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.

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.

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

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

α1-Microglobulin Is Found Both in Blood and in Most Tissues

J. Enghild, T. Oury, I. Thøgersen, 1998, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

Isolation and characterization of fibronectin-alpha 1-microglobulin complex in rat plasma.

J. Enghild, G. Salvesen, I. Thøgersen, 1994, The Biochemical journal.

Proteinase binding and inhibition by the monomeric alpha-macroglobulin rat alpha 1-inhibitor-3.

J. Enghild, S. Pizzo, G. Salvesen, 1989, The Journal of biological chemistry.

Rapid and Individual-specific Glycoprofiling of the Low Abundance N-Glycosylated Protein Tissue Inhibitor of Metalloproteinases-1*S

H. Nielsen, N. Brünner, J. Enghild, 2007, Molecular & Cellular Proteomics.

Identification of a potential biomarker panel for the intake of the common dietary trans fat elaidic acid (trans∆9-C18:1).

J. Enghild, P. Højrup, V. Thoma, 2012, Journal of proteomics.

ITIH4 acts as a protease inhibitor by a novel inhibitory mechanism

J. Enghild, S. Thiel, A. Hansen, 2021, Science Advances.

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.

TSG-6 Transfers Proteins between Glycosaminoglycans via a Ser28-mediated Covalent Catalytic Mechanism*

J. Enghild, I. Thøgersen, K. W. Sanggaard, 2008, Journal of Biological Chemistry.

The Transfer of Heavy Chains from Bikunin Proteins to Hyaluronan Requires Both TSG-6 and HC2*

J. Enghild, I. Thøgersen, K. W. Sanggaard, 2008, Journal of Biological Chemistry.

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

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

Investigating the biomarker potential of glycoproteins using comparative glycoprofiling - application to tissue inhibitor of metalloproteinases-1.

H. Nielsen, N. Brünner, J. Enghild, 2008, Biochimica et biophysica acta.

Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.

E. H. Olsen, J. Enghild, P. Roepstorff, 1998, Biochemistry.

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

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

Serine protease HtrA1 accumulates in corneal transforming growth factor beta induced protein (TGFBIp) amyloid deposits

J. Enghild, P. Højrup, K. Runager, 2013, Molecular vision.

Uncovering the ligandome of low-density lipoprotein receptor-related protein 1 in cartilage: a top-down approach to identify therapeutic targets

J. Enghild, C. Scavenius, George Bou-Gharios, 2022, bioRxiv.

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.

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.

Atypical asymmetric lattice corneal dystrophy associated with a novel homozygous mutation (Val624Met) in the TGFBI gene

J. Enghild, I. Thøgersen, N. Afshari, 2008, Molecular vision.

Structural and functional analysis of the spontaneous re-formation of the thiol ester bond in human alpha 2-macroglobulin, rat alpha 1-inhibitor-3 and chemically modified derivatives.

J. Enghild, S. Pizzo, I. Thøgersen, 1996, The Biochemical journal.

Disulfide Bond Pattern of Transforming Growth Factor β-Induced Protein.

J. Enghild, C. Scavenius, I. Thøgersen, 2016, Biochemistry.

Human Phenotypically Distinct TGFBI Corneal Dystrophies Are Linked to the Stability of the Fourth FAS1 Domain of TGFBIp*

J. Enghild, D. Otzen, N. Nielsen, 2010, The Journal of Biological Chemistry.

Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas.

J. Enghild, T. Møller-Pedersen, I. Thøgersen, 2004, Biochemistry.

Complexes between serpins and inactive proteinases are not thermodynamically stable but are recognized by serpin receptors.

J. Enghild, S. Pizzo, I. Thøgersen, 1994, Journal of Biological Chemistry.

Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes

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

The TSG-6/HC2-mediated Transfer Is a Dynamic Process Shuffling Heavy Chains between Glycosaminoglycans*

J. Enghild, C. Scavenius, I. Thøgersen, 2010, The Journal of Biological Chemistry.

A Dataset of Human Cornea Proteins Identified by Peptide Mass Fingerprinting and Tandem Mass Spectrometry*S

J. Enghild, T. Møller-Pedersen, I. Thøgersen, 2005, Molecular & Cellular Proteomics.

α2-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester

J. Enghild, N. S. Nielsen, I. Thøgersen, 2020, The Journal of Biological Chemistry.

Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation.

J. Enghild, P. Højrup, I. Thøgersen, 2006, Biochemistry.

Evolutionary conservation of heavy chain protein transfer between glycosaminoglycans.

J. Enghild, C. Scavenius, I. Thøgersen, 2010, Biochimica et biophysica acta.

Evidence for a two-step mechanism involved in the formation of covalent HC x TSG-6 complexes.

Kristian W Sanggaard, Jan J Enghild, J. Enghild, 2006, Biochemistry.

Matrix-degrading protease ADAMTS-5 cleaves inter-α-inhibitor and releases active heavy chain 2 in synovial fluids from arthritic patients

S. Frostick, J. Enghild, C. Scavenius, 2019, The Journal of Biological Chemistry.

The diversity of FtsY-lipid interactions.

J. Enghild, I. Thøgersen, M. E. Reinau, 2010, Biopolymers.

Proteolytic activities of human ADAMTS-5. comparative studies with human ADAMTS-4 [Erratum]

J. Enghild, M. Kashiwagi, I. Thøgersen, 2007 .

Transforming growth factor beta induced protein accumulation in granular corneal dystrophy type III (Reis-Bücklers dystrophy). Identification by mass spectrometry in 15 year old two-dimensional protein gels.

J. Enghild, T. Møller-Pedersen, I. Thøgersen, 2003, Molecular vision.