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PubMed:14681236 JSONTXT 28 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-183 Sentence denotes Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation.
T2 184-383 Sentence denotes The membrane type (MT)-matrix metalloproteinases (MMPs) constitute a subgroup of membrane-anchored MMPs that are major mediators of pericellular proteolysis and physiological activators of pro-MMP-2.
T3 384-503 Sentence denotes The MT-MMPs also exhibit differential inhibition by members of the tissue inhibitor of metalloproteinase (TIMP) family.
T4 504-601 Sentence denotes Here we investigated the processing, catalytic activity, and TIMP inhibition of MT3-MMP (MMP-16).
T5 602-754 Sentence denotes Inhibitor profile and mutant enzyme studies indicated that MT3-MMP is regulated on the cell surface by autocatalytic processing and ectodomain shedding.
T6 755-932 Sentence denotes Inhibition kinetic studies showed that TIMP-3 is a high affinity inhibitor of MT3-MMP when compared with MT1-MMP (K(i) = 0.008 nm for MT3-MMP versus K(i) = 0.16 nm for MT1-MMP).
T7 933-986 Sentence denotes In contrast, TIMP-2 is a better inhibitor of MT1-MMP.
T8 987-1192 Sentence denotes MT3-MMP requires TIMP-2 to accomplish full pro-MMP-2 activation and this process is enhanced in marimastatpretreated cells, consistent with regulation of active enzyme turnover by synthetic MMP inhibitors.
T9 1193-1272 Sentence denotes TIMP-3 also enhances the activation of pro-MMP-2 by MT3-MMP but not by MT1-MMP.
T10 1273-1349 Sentence denotes TIMP-4, in contrast, cannot support pro-MMP-2 activation with either enzyme.
T11 1350-1609 Sentence denotes Affinity chromatography experiments demonstrated that pro-MMP-2 can assemble trimolecular complexes with a catalytic domain of MT3-MMP and TIMP-2 or TIMP-3 suggesting that pro-MMP-2 activation by MT3-MMP involves ternary complex formation on the cell surface.
T12 1610-1802 Sentence denotes These results demonstrate that TIMP-3 is a major regulator of MT3-MMP activity and further underscores the unique interactions of TIMPs with MT-MMPs in the control of pericellular proteolysis.