Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases.Hasty K.A., Pourmotabbed T.F., Goldberg G.I., Thompson J.P., Spinella D.G., Stevens R.M., Mainardi C.L.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 314-337; 347-363 AND 424-441TissueNeutrophilCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 265:11421-11424 (1990)Cited in1
No title available.NIEHS SNPs programCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-3; ILE-32; GLU-87; GLU-154; VAL-193; TYR-246; ALA-436 AND THR-460CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JUL-2005)Cited in9
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project TeamView abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]TissueLungCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms.Knaeuper V., Kraemer S., Reinke H., Tschesche H.View abstractCited forPROTEIN SEQUENCE OF 21-140, VARIANT ILE-32TissueNeutrophilCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 189:295-300 (1990)Cited in1Mapped to4
Mercurial activation of human polymorphonuclear leucocyte procollagenase.Blaeser J., Knaeuper V., Osthues A., Reinke H., Tschesche H.View abstractCited forPROTEIN SEQUENCE OF 21-103TissueNeutrophilCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 202:1223-1230 (1991)Cited in1
Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase.Mallya S.K., Mookthiar K.A., Gao Y., Brew K., Dioszegi M., Birkedal-Hansen H., van Wart H.E.View abstractCited forPROTEIN SEQUENCE OF 85-120, CHARACTERIZATIONTissueNeutrophilCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 29:10628-10634 (1990)Cited in1
Partial amino acid sequence of human PMN leukocyte procollagenase.Knaeuper V., Kraemer S., Reinke H., Tschesche H.View abstractCited forPARTIAL PROTEIN SEQUENCECategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiol. Chem. Hoppe-Seyler 371:295-304 (1990)Cited in1
No title available.Knaeuper V., Kraemer S., Reinke H., Tschesche H.Cited forERRATUM OF PUBMED:2169256SourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiol. Chem. Hoppe-Seyler 371:733-733 (1990)Cited in1
Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism.Blaeser J., Triebel S., Reinke H., Tschesche H.View abstractCited forCYSTEINE-SWITCH MECHANISMTissueNeutrophilCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEBS Lett. 313:59-61 (1992)Cited in1
The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.Bode W., Reinemer P., Huber R., Klein T., Schnierer S., Tschesche H.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-262CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 13:1263-1269 (1994)Cited in1
Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study.Reinemer P., Grams F., Huber R., Kleine T., Schnierer S., Piper M., Tschesche H., Bode W.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-262CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEBS Lett. 338:227-233 (1994)Cited in1
Structure of human neutrophil collagenase reveals large S1' specificity pocket.Stams T., Spurlino J.C., Smith D.L., Wahl R.C., Ho T.F., Qoronfleh M.W., Banks T.M., Rubin B.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 100-262CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Biol. 1:119-123 (1994)Cited in1
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.Betz M., Huxley P., Davies S.J., Mushtaq Y., Pieper M., Tschesche H., Bode W., Gomis-Rueth F.-X.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 100-262CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 247:356-363 (1997)Cited in1
Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.Brandstetter H., Engh R.A., von Roedern E.G., Moroder L., Huber R., Bode W., Grams F.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-262CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 7:1303-1309 (1998)Cited in1
Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain.Yang M., Kurkinen M.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ Biol Chem 273:17893-17900 (1998)Mapped to24
Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain.Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ. Biol. Chem. 272:9749-9754 (1997)Cited in2Mapped to24
Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules.Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., Okada Y.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ Biol Chem 272:2446-2451 (1997)Mapped to13
Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein.Chandler S., Cossins J., Lury J., Wells G.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCBiochem Biophys Res Commun 228:421-429 (1996)Mapped to32
Biochemical characterization of human collagenase-3.Knaeuper V., Lopez-Otin C., Smith B., Knight G., Murphy G.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ. Biol. Chem. 271:1544-1550 (1996)Cited in2Mapped to13
Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins.Sanchez-Lopez R., Alexander C.M., Behrendtsen O., Breathnach R., Werb Z.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ Biol Chem 268:7238-7247 (1993)Mapped to24
Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments.Aimes R.T., Quigley J.P.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ Biol Chem 270:5872-5876 (1995)Mapped to7
X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.Grams F., Reinemer P., Powers J.C., Kleine T., Pieper M., Tschesche H., Huber R., Bode W.View abstractCategoriesStructureSourcePDB: 1JAO, PDB: 1JAQ, PDB: 1ZS0, PDB: 1ZVXPubMedEurope PMCEur J Biochem 228:830-841 (1995)Mapped to1
Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor.Grams F., Crimmin M., Hinnes L., Huxley P., Pieper M., Tschesche H., Bode W.View abstractCategoriesStructureSourcePDB: 1MMB, PDB: 1ZP5PubMedEurope PMCBiochemistry 34:14012-14020 (1995)Mapped to1
The collagen substrate specificity of human skin fibroblast collagenase.Welgus H.G., Jeffrey J.J., Eisen A.Z.AnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-1442475PubMedEurope PMCJ Biol Chem 256:9511-9515 (1981)Mapped to11
The adhesion-GPCR ADGRF5 fuels breast cancer progression by suppressing the MMP8-mediated antitumorigenic effects.Wu Y., Liu H., Sun Z., Liu J., Li K., Fan R., Dai F., Tang H., Hou Q.[...], Tang X.View abstractAnnotationThe adhesion-GPCR ADGRF5 fuels breast cancer progression by suppressing the MMP8-mediated antitumorigenic effects.SourceGeneRif: 4317PubMedEurope PMCCell Death Dis 15:455-455 (2024)Mapped to9