The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin.Saus J., Quinones S., Otani Y., Nagase H., Harris E.D. Jr., Kurkinen M.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-24CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 263:6742-6745 (1988)Cited in1
Comparison of human stromelysin and collagenase by cloning and sequence analysis.Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A., Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA]TissueFibroblastCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. J. 240:913-916 (1986)Cited in3
Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells.Wilhelm S.M., Collier I.E., Kronberger A., Eisen A.Z., Marmer B.L., Grant G.A., Bauer E.A., Goldberg G.I.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 84:6725-6729 (1987)Cited in1
Three matrix metalloproteinases on 81kb of P1 insert.Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A., Chung E., Davis K., Federspiel N.[...], Davis R.W.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (DEC-1996)Cited in2
Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H.[...], Sugano S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]TissueSynoviumCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Genet. 36:40-45 (2004)Cited in99+99+
No title available.Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-45TissueSynoviumCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (APR-2005)Cited in99+99+
No title available.SeattleSNPs variation discovery resourceCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-45CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (AUG-2001)Cited in2
No title available.Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H.[...], Venter J.C.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JUL-2005)Cited in99+
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], VARIANT GLU-45TissueLungCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4- aminophenyl)mercuric acetate.Nagase H., Enghild J.J., Suzuki K., Salvesen G.View abstractCited forZYMOGEN ACTIVATION, FUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 29:5783-5789 (1990)Cited in1
Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9.Ogata Y., Enghild J.J., Nagase H.View abstractCited forFUNCTION, CATALYTIC ACTIVITYCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 267:3581-3584 (1992)Cited in2Mapped to5
Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results in reduced gene expression.Ye S., Eriksson P., Hamsten A., Kurkinen M., Humphries S.E., Henney A.M.View abstractCited forINVOLVEMENT IN CHDS6CategoriesDisease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 271:13055-13060 (1996)Cited in1
Prostromelysin-1 (proMMP-3) stimulates plasminogen activation by tissue- type plasminogen activator.Arza B., Hoylaerts M.F., Felez J., Collen D., Lijnen H.R.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 267:6378-6384 (2000)Cited in1
Prediction of the risk of myocardial infarction from polymorphisms in candidate genes.Yamada Y., Izawa H., Ichihara S., Takatsu F., Ishihara H., Hirayama H., Sone T., Tanaka M., Yokota M.View abstractCited forINVOLVEMENT IN CHDS6CategoriesDisease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCN. Engl. J. Med. 347:1916-1923 (2002)Cited in1Mapped to5
Role of matrix metalloproteinase 3-mediated alpha-synuclein cleavage in dopaminergic cell death.Choi D.H., Kim Y.J., Kim Y.G., Joh T.H., Beal M.F., Kim Y.S.View abstractCited forFUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITYCategoriesFunction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 286:14168-14177 (2011)Cited in1Mapped to17
Matrix metalloproteinase-3 is activated by HtrA2/Omi in dopaminergic cells: relevance to Parkinson's disease.Shin E.J., Kim E.M., Lee J.A., Rhim H., Hwang O.View abstractCited forFUNCTION, ACTIVITY REGULATIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNeurochem. Int. 60:249-256 (2012)Cited in1Mapped to8
Matrix metalloproteinase 3 restricts viral infection by enhancing host antiviral immunity.Feng T., Tong H., Ming Z., Deng L., Liu J., Wu J., Chen Z., Yan Y., Dai J.View abstractCited forFUNCTION, SUBCELLULAR LOCATIONCategoriesFunction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAntiviral Res. 0:0-0 (2022)Cited in2Mapped to3
The NMR structure of the inhibited catalytic domain of human stromelysin- 1.Gooley P.R., O'Connell J.F., Marcy A.I., Cuca G.C., Salowe S.P., Bush B.L., Hermes J.D., Esser C.K., Hagmann W.K.[...], Johnson B.A.View abstractCited forSTRUCTURE BY NMR OF CATALYTIC DOMAINCategoriesFamily & Domains, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Biol. 1:111-118 (1994)Cited in11
Solution structures of stromelysin complexed to thiadiazole inhibitors.Stockman B.J., Waldon D.J., Gates J.A., Scahill T.A., Kloosterman D.A., Mizsak S.A., Jacobsen E.J., Belonga K.L., Mitchell M.A.[...], Poorman R.A.View abstractCited forSTRUCTURE BY NMR OF 100-267CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 7:2281-2286 (1998)Cited in1
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M.D., Cameron P.M., Esser C.K., Hagmann W.K.[...], Springer J.P.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-272CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 4:1966-1976 (1995)Cited in1
X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily.Dhanaraj V., Ye Q.-Z., Johnson L.L., Hupe D.J., Otwine D.F., Dunbar J.B. Jr., Rubin J.R., Pavlovsky A., Humblet C., Blundell T.L.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-266CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCStructure 4:375-386 (1996)Cited in1
Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl carboxyalkyl dipeptides.Esser C.K., Bugianesi R.L., Caldwell C.G., Chapman K.T., Durette P.L., Girotra N.N., Kopka I.E., Lanza T.J., Levorse D.A.[...], Hagmann W.K.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 105-264CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Med. Chem. 40:1026-1040 (1997)Cited in1
Mechanism of inhibition of the human matrix metalloproteinase stromelysin- 1 by TIMP-1.Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R., Suzuki K., Yoshida N., Nagase H., Brew K.[...], Bode W.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 100-267 IN COMPLEX WITH TIMP1CategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 389:77-81 (1997)Cited in2
Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.Finzel B.C., Baldwin E.T., Bryant G.L. Jr., Hess G.F., Wilks J.W., Trepod C.M., Mott J.E., Marshall V.P., Petzold G.L.[...], Mitchell M.A.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-264CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 7:2118-2126 (1998)Cited in1
Crystal structure of the stromelysin catalytic domain at 2.0-A resolution: inhibitor-induced conformational changes.Chen L., Rydel T.J., Gu F., Dunaway C.M., Pikul S., Dunham K.M., Barnett B.L.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-272CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 293:545-557 (1999)Cited in1