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
X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.Pavlovsky A.G., Williams M.G., Ye Q.-Z., Ortwine D.F., Purchase C.F. II, White A.D., Dhanaraj V., Roth B.D., Johnson L.L.[...], Blundell T.L.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-267CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 8:1455-1462 (1999)Cited in1Mapped to1
Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor.Li Y.C., Zhang X., Melton R., Ganu V., Gonnella N.C.View abstractCited forSTRUCTURE BY NMR OF 100-272CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 37:14048-14056 (1998)Cited in1
Design and synthesis of conformationally-constrained MMP inhibitors.Natchus M.G., Cheng M., Wahl C.T., Pikul S., Almstead N.G., Bradley R.S., Taiwo Y.O., Mieling G.E., Dunaway C.M.[...], De B.View abstractCategoriesStructureSourcePDB: 1BIWPubMedEurope PMCBioorg Med Chem Lett 8:2077-2080 (1998)Mapped to1
Discovery of potent, achiral matrix metalloproteinase inhibitors.Pikul S., McDow Dunham K.L., Almstead N.G., De B., Natchus M.G., Anastasio M.V., McPhail S.J., Snider C.E., Taiwo Y.O.[...], Mieling G.E.CategoriesStructureSourcePDB: 1BQOPubMedEurope PMCJ Med Chem 41:3568-3571 (1998)Mapped to1
Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.Van Doren S.R., Kurochkin A.V., Hu W., Ye Q.Z., Johnson L.L., Hupe D.J., Zuiderweg E.R.View abstractCategoriesStructureSourcePDB: 1UMS, PDB: 1UMTPubMedEurope PMCProtein Sci 4:2487-2498 (1995)Mapped to1
Engineering of tissue inhibitor of metalloproteinases TIMP-1 for fine discrimination between closely related stromelysins MMP-3 and MMP-10.Raeeszadeh-Sarmazdeh M., Coban M., Mahajan S., Hockla A., Sankaran B., Downey G.P., Radisky D.C., Radisky E.S.View abstractCategoriesStructureSourcePDB: 7S7L, PDB: 7S7MPubMedEurope PMCJ Biol Chem 298:101654-101654 (2022)Mapped to2
Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.Raeeszadeh-Sarmazdeh M., Greene K.A., Sankaran B., Downey G.P., Radisky D.C., Radisky E.S.View abstractCategoriesStructureSourcePDB: 6MAV, PDB: 6N9DPubMedEurope PMCJ Biol Chem 294:9476-9488 (2019)Mapped to2
Cartilage oligomeric protein, matrix metalloproteinase-3, and Coll2-1 as serum biomarkers in knee osteoarthritis: a cross-sectional study.Georgiev T., Ivanova M., Kopchev A., Velikova T., Miloshov A., Kurteva E., Yuzeir K., Penkov M., Kabakchieva P.[...], Stoilov R.View abstractAnnotationHigher serum MMP-3 levels in knee osteoarthritis reflect disease "generalization".CategoriesFunction, StructureSourceGeneRif: 4314PubMedEurope PMCRheumatol Int 38:821-830 (2018)Mapped to11
Structure of matrix metalloproteinase-3 with a platinum-based inhibitor.Belviso B.D., Caliandro R., Siliqi D., Calderone V., Arnesano F., Natile G.View abstractCategoriesStructureSourcePDB: 4DPE, PDB: 4G9L, PDB: 4JA1PubMedEurope PMCChem Commun (Camb) 49:5492-5494 (2013)Mapped to1
Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.Liang X., Arunima A., Zhao Y., Bhaskaran R., Shende A., Byrne T.S., Fleeks J., Palmier M.O., Van Doren S.R.View abstractAnnotationhigher stability of MMP-3 relative to MMP-12 coincides with the former's considerably lower proteolytic activityCategoriesInteraction, StructureSourceGeneRif: 4314PubMedEurope PMCBiophys J 99:273-283 (2010)Mapped to6
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.Alcaraz L.A., Banci L., Bertini I., Cantini F., Donaire A., Gonnelli L.View abstractAnnotationThe adducts of the catalytic domain of matrix metalloproteinase-3 (MMP3) with three different nonpeptidic inhibitors were structurally characterized.CategoriesStructureSourceGeneRif: 4314, PDB: 2JNP, PDB: 2JT5, PDB: 2JT6PubMedEurope PMCJ Biol Inorg Chem 12:1197-1206 (2007)Mapped to3
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453.Kohno T., Hochigai H., Yamashita E., Tsukihara T., Kanaoka M.View abstractCategoriesStructureSourcePDB: 2D1OPubMedEurope PMCBiochem Biophys Res Commun 344:315-322 (2006)Mapped to2
Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings.Arumugam S., Van Doren S.R.View abstractCategoriesInteraction, StructureSourceIntAct: P08254, PDB: 1OO9PubMedEurope PMCBiochemistry 42:7950-7958 (2003)Cited in1Mapped to1
Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3.Arumugam S., Gao G., Patton B.L., Semenchenko V., Brew K., Van Doren S.R.View abstractAnnotationN-TIMP-1 interaction with the catalytic domain of MMP-3 investigation by titration calorimetry and 15N NMRCategoriesStructureSourceGeneRif: 4314PubMedEurope PMCJ Mol Biol 327:719-734 (2003)Mapped to8
Heterocycle-based MMP inhibitors with P2' substituents.Pikul S., Dunham K.M., Almstead N.G., De B., Natchus M.G., Taiwo Y.O., Williams L.E., Hynd B.A., Hsieh L.C.[...], Mieling G.E.View abstractCategoriesStructureSourcePDB: 1D8M, PDB: 1G05PubMedEurope PMCBioorg Med Chem Lett 11:1009-1013 (2001)Mapped to1
X-ray structure of a novel matrix metalloproteinase inhibitor complexed to stromelysin.Dunten P., Kammlott U., Crowther R., Levin W., Foley L.H., Wang P., Palermo R.View abstractCategoriesStructureSourcePDB: 1G4KPubMedEurope PMCProtein Sci 10:923-926 (2001)Mapped to1
Development of new carboxylic acid-based MMP inhibitors derived from functionalized propargylglycines.Natchus M.G., Bookland R.G., Laufersweiler M.J., Pikul S., Almstead N.G., De B., Janusz M.J., Hsieh L.C., Gu F.[...], Mieling G.E.View abstractCategoriesStructureSourcePDB: 1HY7PubMedEurope PMCJ Med Chem 44:1060-1071 (2001)Mapped to1