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
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
Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings.Arumugam S., Van Doren S.R.View abstractCategoryInteraction, StructureSourceIntAct: P08254, PDB: 1OO9PubMedEurope PMCBiochemistry 42:7950-7958 (2003)Cited in1Mapped to1