Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2
about
Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial originCollagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysisIdentification, regulation and role of tissue inhibitor of metalloproteinases-4 (TIMP-4) in human plateletsTargeting matrix metalloproteinases in heart disease: lessons from endogenous inhibitorsDomain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activationUtilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding theTIMP-2 is required for efficient activation of proMMP-2 in vivoLocalization and expression of tissue inhibitor of metalloproteinase-4 in the immature gonadotropin-stimulated and adult rat ovaryThe plasmin cascade and matrix metalloproteinases in non-small cell lung cancerThe matrix metalloproteinases and their inhibitors in the treatment of pancreatic cancer.Cellular uptake of proMMP-2:TIMP-2 complexes by the endocytic receptor megalin/LRP-2.Matrix metalloproteinases in tumorigenesis: an evolving paradigm.Complex roles of tissue inhibitors of metalloproteinases in cancer.Proteolytic events of wound-healing--coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules.Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeuticsMyocardial remodeling: cellular and extracellular events and targets.Fetal hypoxia and programming of matrix metalloproteinases.Matrix metalloproteinases: influence on smooth muscle cells and atherosclerotic plaque stability.Homocysteine decreases blood flow to the brain due to vascular resistance in carotid artery.Metastasis review: from bench to bedside.Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate.Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2).The hemopexin domain of MMP-9 inhibits angiogenesis and retards the growth of intracranial glioblastoma xenograft in nude mice.Individual Timp deficiencies differentially impact pro-MMP-2 activation.Identification of an initiator-like element essential for the expression of the tissue inhibitor of metalloproteinases-4 (Timp-4) gene.Rac affects invasion of human renal cell carcinomas by up-regulating tissue inhibitor of metalloproteinases (TIMP)-1 and TIMP-2 expression.Characterization of C-terminally truncated human tissue inhibitor of metalloproteinases-4 expressed in Pichia pastoris.Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2.MMP-2, MMP-9, and TIMP-4 and Response to Aspirin in Diabetic and Nondiabetic Patients with Stable Coronary Artery Disease: A Pilot Study.Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP).Incorporation of β-actin loading control into zymography.Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.Plasma profiling determinants of matrix homeostasis in paediatric dilated cardiomyopathyEstrogen improves TIMP-MMP balance and collagen distribution in volume-overloaded hearts of ovariectomized females.MMP-TIMP interaction depends on residue 2 in TIMP-4.Quantitative analysis of mRNA expression of TIMPs in the periprosthetic interface tissue of loose hips by real-time PCR system.Inhibition of adjuvant-induced arthritis by systemic tissue inhibitor of metalloproteinases 4 gene delivery.Inhibition of Wilms' tumor growth by intramuscular administration of tissue inhibitor of metalloproteinases-4 plasmid DNA.Can EGCG Alleviate Symptoms of Down Syndrome by Altering Proteolytic Activity?
P2860
Q24530532-24314303-E84C-4626-BA2E-C60E4A109CF3Q24532807-011B28E5-B282-4F98-B418-9BB87F24B317Q24652849-5297EE51-D700-46D9-A1DC-38357A4F02BFQ24672897-FEABE30C-775C-4530-9335-7BE6AD5F8446Q26830555-D21C62D1-9B7D-44C0-9EAF-B8FB15A3493EQ28138867-1EBF9176-956F-43AF-9882-3281E6ED31ACQ28206603-9B0D9D34-13D0-4E1A-8E2B-078498B6A605Q28512714-DB10EE97-060D-46EB-A9AD-09A56FBC97AFQ28570779-971D2811-6E84-4079-BD5B-D7C9C0A268BCQ33634208-B4F8727D-FD42-412B-B7F2-357F5A2679DDQ33693020-F244A821-E89A-4AFD-AC69-3621E773435AQ33849227-82CB83F0-018C-4F56-8DB1-5283C6692CBBQ34199345-4E877079-9930-409F-AE72-6C428DA3E848Q34596110-E0A103D7-0E6F-45B4-9033-F49315B5692DQ34632691-1245F610-CB6E-4162-B975-3B2705F5C29EQ34731111-434D14BF-1EE8-4616-A675-FE354EBEE420Q35168352-2F89A5C1-8D0E-4A9D-A960-85FF7FB4A26EQ35643324-43EFC63B-DE97-45DB-B778-5CAE77B239C7Q36752100-4199C1B2-684B-44FC-AE9E-D6CA90F04A99Q37347147-C2851F25-EDCA-42A0-BB24-24254AFAB04AQ38237985-914E4BAD-FC81-44C2-8B90-D96F6962A84BQ38326402-A48EBE5C-7DEC-46B1-A11B-B92B97C2D895Q38679451-D807DA79-7AC4-45EB-9B06-3C06CE22EF0AQ39926498-9995EF41-B926-48A9-A6A5-AD83D8DFAD61Q40318346-DC77D1F8-48AA-4BA6-B902-0F27E7275227Q40734591-6879DCAE-132F-4E4B-A160-35679573F46FQ40781214-DA3E4D81-1AA8-451D-85CC-38CC7DA5BCFEQ40786563-15BF94EE-EEAF-4A99-9AB3-B6D78E5274FFQ40853467-F12F9B32-DBD0-4A13-8B80-6FE3EDA3DD48Q41099760-FD8072E5-3D7A-4345-A19D-3FAA7A23C9C4Q42121172-C6431AF8-6ACA-4FE5-BAAA-EF4A0F5BFE3AQ42323035-9BA31147-E876-42FE-97C9-334CDDB95A87Q42653828-B56FC533-1B04-4416-B1FC-68DBA91320D4Q42733370-50CD25E2-EA36-4FCC-B7A6-426D74D846BFQ43053682-83933F59-1245-44D2-B345-EE4A021EC2D2Q43790567-FEE4F513-A5E1-4876-BFB6-23F792309EACQ43824491-0C8B4A9E-8C2B-4615-8CA4-3CEA09935E13Q44250401-0BFB6BE5-2E2A-486D-89E4-12E26B3A8D0BQ45878766-441AF3F4-DB31-403C-9FB7-4E8225E55325Q47558056-92BB5108-FD38-44FC-B5DC-69576B176D6E
P2860
Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@ast
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@en
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@nl
type
label
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@ast
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@en
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@nl
prefLabel
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@ast
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@en
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@nl
P2093
P2860
P356
P1476
Specific, high affinity bindin ...... in a similar manner to TIMP-2
@en
P2093
P2860
P304
P356
10.1074/JBC.272.24.15496
P407
P577
1997-06-13T00:00:00Z