about
Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzymeIdentification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distributionBiochemical characterization of human collagenase-3The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interactionEvaluation of some newer matrix metalloproteinasesADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitorsThe enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPsMembrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2.Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25).Tissue inhibitor of metalloproteinases-3 peptides inhibit angiogenesis and choroidal neovascularization in miceThe recognition of collagen and triple-helical toolkit peptides by MMP-13: sequence specificity for binding and cleavageP2X7 receptor-mediated TG2 externalization: a link to inflammatory arthritis?P2X7 receptor activation regulates rapid unconventional export of transglutaminase-2.Methods for studying activation of matrix metalloproteinases.Cytokine stimulated vascular cell adhesion molecule-1 (VCAM-1) ectodomain release is regulated by TIMP-3.Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13.Modified platelet deposition on matrix metalloproteinase 13 digested collagen I.Different susceptibility of small and large human tenascin-C isoforms to degradation by matrix metalloproteinases.Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP).Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme.TMEFF2 shedding is regulated by oxidative stress and mediated by ADAMs and transmembrane serine proteases implicated in prostate cancer.The Adhesion G Protein-Coupled Receptor GPR56/ADGRG1 Is an Inhibitory Receptor on Human NK Cells.Differential regulation of TROP2 release by PKC isoforms through vesicles and ADAM17.ADAM17-dependent proteolysis of L-selectin promotes early clonal expansion of cytotoxic T cellsMercurial activation of human PMN leucocyte type IV procollagenase (gelatinase)Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluidInactivation of human plasma C1-inhibitor by human PMN leucocyte matrix metalloproteinasesInactivation of human plasma alpha 1-proteinase inhibitor by human PMN leucocyte collagenaseThe recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificityDegradation of cartilage aggrecan by collagenase-3 (MMP-13)Neutrophil procollagenase can be activated by stromelysin-2Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagensAnalysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesisRecognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinasesThe role of exon 5 in fibroblast collagenase (MMP-1) substrate specificity and inhibitor selectivityThe in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3An analysis of two refolding routes for a C-terminally truncated human collagenase-3 expressed in Escherichia coliSpecific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domainCharacterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinasesTNF-alpha converting enzyme (TACE) is inhibited by TIMP-3
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P50
description
onderzoeker
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researcher ORCID ID = 0000-0002-3965-9924
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V Knauper
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P106
P1153
7006018209
P31
P496
0000-0002-3965-9924