Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family.
about
The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster developmentStructural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activityMatrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP ComplexesHigh resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedThe C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzymeTissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene familyMaintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million YearsTIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix.Progress in matrix metalloproteinase research.The next generation of MMP inhibitors. Design and synthesis.Regulation and involvement of matrix metalloproteinases in vascular diseasesThe tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversityEngineering of tissue inhibitor of metalloproteinases mutants as potential therapeuticsStructural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.An integrin-binding N-terminal peptide region of TIMP-2 retains potent angio-inhibitory and anti-tumorigenic activity in vivo.Tissue inhibitors of metalloproteinases (TIMPs): their biological functions and involvement in oral disease.Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: a new frontier in TIMP engineering.Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif.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.Identification of the extracellular matrix (ECM) binding motifs of tissue inhibitor of metalloproteinases (TIMP)-3 and effective transfer to TIMP-1.Collagenase: a key enzyme in collagen turnover.Comparative analysis of the noncollagenous NC1 domain of type IV collagen: identification of structural features important for assembly, function, and pathogenesis.Involvement of a region near valine-69 of tissue inhibitor of metalloproteinases (TIMP)-1 in the interaction with matrix metalloproteinase 3 (stromelysin 1).The NTR module: domains of netrins, secreted frizzled related proteins, and type I procollagen C-proteinase enhancer protein are homologous with tissue inhibitors of metalloproteasesCrystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme.Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14.Unveiling the surface epitopes that render tissue inhibitor of metalloproteinase-1 inactive against membrane type 1-matrix metalloproteinase.Threonine 98, the pivotal residue of tissue inhibitor of metalloproteinases (TIMP)-1 in metalloproteinase recognition.Delineating the molecular basis of the inactivity of tissue inhibitor of metalloproteinase-2 against tumor necrosis factor-alpha-converting enzyme.Localization of the functional domains of human tissue inhibitor of metalloproteinases-3 and the effects of a Sorsby's fundus dystrophy mutation.Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion bodies.
P2860
Q24530018-488DD7F4-BE3D-4549-8A0D-102AD9A02D8AQ24530532-5E81100D-FF81-44CF-A77A-8B07C64CCAADQ24673456-EFC6EBDE-44D2-4C0C-9B33-E029DA6DA04BQ27680082-76D4872B-CA3A-4D9D-BB5C-D2E18B4DE2C1Q27765120-2F40BF0A-EBE2-4FEE-BECC-FCB70E7E621BQ28142404-B00883F0-0F87-4F11-AED5-D4816998E6A7Q28202274-312B6CE9-D251-45BB-8489-A9ACDD2AEC1AQ28235218-2EBDEB88-1120-4DDF-8D81-2F045A3722F9Q28258413-0C3BD981-90F6-4A10-A106-CACA74A23DA5Q28303305-74D1425C-9A2D-485B-95EA-8F3FF9DFE693Q30385426-DC6D460B-1BB2-4AE2-966B-BEDC90BB677CQ30886270-4BB7ADEE-F737-437E-ADFC-B05D8D8D381AQ33608536-1B0C227F-C83B-4079-9A5E-32D372D7A46BQ33692898-D8ADD6C1-9712-4113-A477-0A52A874EECAQ33773304-81243164-1940-4023-A545-68F68C4E9FCBQ33786342-C685B95D-F394-4EB8-B049-CCB0CCDD6F09Q34731111-448EB26F-78A4-45E6-A33B-2769658871A2Q35187217-03CE74CC-EA6B-4209-8648-B334A41AA228Q35224732-8C0BC232-EC46-459F-A796-49B874EF3587Q36661278-5714734B-8AEB-4817-831A-4B0719E3BF81Q38270327-9B850F1F-E495-4122-911C-2E673BB03A04Q38296241-6CDCE737-E74C-471B-8700-D8C2FD638700Q38326402-7215D581-2A4D-4571-902A-F90908C58D14Q40254634-5CD31905-7B4B-47E6-963D-923095A12E41Q41481774-6FDA3118-7403-4E22-A067-90A149446E1CQ41854234-7E6B6DED-30C9-4710-A5C5-1C30A2A7364FQ41970870-4B19C114-DD4F-466D-A86C-321FAA9C46B0Q42608136-9031065E-B033-49E2-8224-5C1961AA6246Q42653828-5E6D591D-2E21-4175-9311-D053D20C565AQ43002807-FD2104CF-1DDD-418A-8F43-A0E077857D86Q43628870-1DEDA931-578F-431B-B22B-E8A26FE829B9Q44517538-F5F3474B-88F7-432A-9F0F-5F3C58A17184Q44735775-7E663F4B-CE07-4887-AB41-43873B487E9DQ45016679-681F55C3-6A77-4ED7-8140-DE2E810C105EQ47921791-025F0D2C-B3C4-425C-8E31-3CBDA6548F78Q54579031-E18891E6-1B97-4714-ADFE-7AD335ABACBF
P2860
Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family.
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Solution structure of the acti ...... of the OB fold protein family.
@ast
Solution structure of the acti ...... of the OB fold protein family.
@en
type
label
Solution structure of the acti ...... of the OB fold protein family.
@ast
Solution structure of the acti ...... of the OB fold protein family.
@en
prefLabel
Solution structure of the acti ...... of the OB fold protein family.
@ast
Solution structure of the acti ...... of the OB fold protein family.
@en
P2093
P921
P356
P1433
P1476
Solution structure of the acti ...... of the OB fold protein family.
@en
P2093
Docherty AJ
Freedman RB
Martorell G
Williamson RA
P304
11745-11759
P356
10.1021/BI00205A010
P407
P577
1994-10-01T00:00:00Z