X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition - Wikidata - wikimedia - TriplyDB

X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition

X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition

http://www.wikidata.org/entity/Q27734011

about

Structure of tick anticoagulant peptide at 1.6 A resolution complexed with bovine pancreatic trypsin inhibitor Rational approaches to improving selectivity in drug design Structure of human factor VIIa and its implications for the triggering of blood coagulation (R)-3-Amidinophenylalanine-derived inhibitors of factor Xa with a novel active-site binding mode The discovery of (2R,4R)-N-(4-chlorophenyl)-N- (2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl)-4-methoxypyrrolidine-1,2-dicarboxamide (PD 0348292), an orally efficacious factor Xa inhibitor The Tick-Derived Anticoagulant Madanin Is Processed by Thrombin and Factor Xa Structural basis for dual inhibitory role of tamarind Kunitz inhibitor (TKI) against factor Xa and trypsin The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors Structural basis for chemical inhibition of human blood coagulation factor Xa New enzyme lineages by subdomain shuffling Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor-factor VIIa-factor Xa-tissue factor pathway inhibitor Exosite-driven substrate specificity and function in coagulation Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity A unique substrate recognition profile for matrix metalloproteinase-2.Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries Mapping the active site of factor Xa by selective inhibitors: an NMR and MD study.Approaches to selective peptidic inhibitors of factor Xa.Molecular docking screens using comparative models of proteins An anticoagulant RNA aptamer that inhibits proteinase-cofactor interactions within prothrombinase Structural and energetic determinants of the S1-site specificity in serine proteases.Small, noncovalent serine protease inhibitors.Coagulation factor Xa: the prothrombinase complex as an emerging therapeutic target for small molecule inhibitors.Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin.Factor Xa subsite mapping by proteome-derived peptide libraries improved using WebPICS, a resource for proteomic identification of cleavage sites.Structure and dynamics of zymogen human blood coagulation factor X Role of the active-site solvent in the thermodynamics of factor Xa ligand binding.The structure of thrombin, a chameleon-like proteinase.Factor Xa active site substrate specificity with substrate phage display and computational molecular modeling.Deuterium solvent isotope effect and proton-inventory studies of factor Xa-catalyzed reactions Molecular dynamics simulations of Factor Xa: insight into conformational transition of its binding subsites.Cloning and comparison of factor X from rhesus monkey (Macaca mulatta)Activation mechanisms of coagulation factor IX.Developments in factor Xa inhibitors for the treatment of thromboembolic disorders.Directed glycosylation of human coagulation factor X at residue 333. Insight into factor Va-dependent prothrombin catalysis.Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop.Insight into the molecular mechanism of P-glycoprotein mediated drug toxicity induced by bioflavonoids: an integrated computational approach.Protease Inhibitors in View of Peptide Substrate Databases.Trypsin mutants for structure-based drug design: expression, refolding and crystallisation.Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site.

P2860

Q24672310-F8FE9437-3759-43AD-A8F0-7DEA4224578D Q26865357-6165F2E2-B225-40C9-B554-C05B48309626 Q27619263-49FF24D8-A939-4147-BC98-FFF8AD05DE21 Q27639971-2D1E9CD4-DA01-4411-82A5-BF15DD8A15CC Q27646997-F4024857-2DC6-4BCA-BB92-76E62D62C073 Q27679700-1DF604D9-2B8A-4D75-B0FF-B872A8EC90D3 Q27683033-7FB19E3A-4784-4DF7-8EAA-4721FDA0E1A6 Q27741060-7279585C-7C3A-4412-9E45-70A9E75CC351 Q27742255-71B51BB8-FABC-4F04-989C-EB06B2CD8C67 Q27758367-48FF7A01-F351-43C4-84CC-D98481F9ECF2 Q27765134-23B5B745-5547-450C-9C3E-75045E4D06B6 Q28208644-C66022E7-88C9-4CB2-A031-50655AC6C2FF Q28301227-5F68DBA4-8EBD-43AE-944B-C2C9EF9F7657 Q28576643-F993E4AA-D586-4911-B3DA-2219CE999886 Q30761477-4633AEBC-C4F1-4FDA-B3B2-7F18A0538D67 Q30882677-9E4EC435-E2EE-4076-8FE7-C1486C4289AB Q32083062-49B7F191-38B5-4C5D-A854-C0C9B0FABBBE Q33254680-2DFEAA33-4E85-4453-BD94-42A3ECD32C7E Q33511631-90C6048F-E788-46B6-9E1F-5660DD627EFC Q33519836-D0BD341E-67E4-4809-BCA2-43F4009D2498 Q33548213-2464601B-0056-4BC8-A778-4B354A4D1921 Q33585640-A3F35CE3-CBEE-47BD-931A-6C58D73AC53F Q33751572-A619C1FE-A5C2-43F9-A07B-651CB2496864 Q33940534-E4F2EA14-798C-4BBA-9BA4-C4621E8AEC58 Q33993989-B873F74A-9505-42DF-967A-91ECCB26EDD2 Q34177305-C3336EFA-A896-41C5-965D-F80DF5D7C1BA Q34748976-17CD8BFE-F189-4024-81BF-0202D40C078E Q36126935-9AE5F67D-E161-4C0F-B9C1-5CE70BDF1234 Q36727212-55BE0A56-E46E-477F-B8E4-90BDB2465662 Q36874076-D760543C-66C9-4B7C-A1C4-29C1516D2E91 Q37272161-01A8604F-FB5C-4F8E-9497-72C179746A09 Q37408226-F7505DD9-59AE-4371-9954-3C53D49B1F97 Q37441223-0C3C464D-7638-436B-B437-314EA8E72CC4 Q37646551-1FBDD845-BECF-43A3-A3B3-7AEC24CF5F8E Q38308237-501D39E7-67BF-4B07-83B0-47034B77514C Q38360711-3545B0B2-6354-4CB6-8644-974F6EF9B092 Q38780311-95B19D39-767B-40E8-BE23-45884BF239F5 Q39719414-02CDA011-21F1-485C-B38A-A09A116EACC7 Q40621243-932C4D57-84DA-4807-B8A7-9297352C839A Q40714392-1BF55070-EEE2-4903-8A78-D31BE2634706

P2860

X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition

http://www.wikidata.org/entity/Q27734011

description

1996 nî lūn-bûn

@nan

1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

name

X-ray structure of active site ...... sign and substrate recognition

@ast

X-ray structure of active site ...... sign and substrate recognition

@en

X-ray structure of active site ...... sign and substrate recognition

@nl

type

label

X-ray structure of active site ...... sign and substrate recognition

@ast

X-ray structure of active site ...... sign and substrate recognition

@en

X-ray structure of active site ...... sign and substrate recognition

@nl

prefLabel

X-ray structure of active site ...... sign and substrate recognition

@ast

X-ray structure of active site ...... sign and substrate recognition

@en

X-ray structure of active site ...... sign and substrate recognition

@nl

P1433

Q27734011-ECC9B034-A03D-432A-8D1A-B94AD3E3A757

P1476

Q27734011-E0ED46E9-EB12-4140-9993-775B92C60597

P2093

Q27734011-03AD76F5-46B0-4B02-8ABD-9620D47E1FD2

Q27734011-27FA89F6-F3F8-4070-B4A3-A475BEFE420B

Q27734011-2A7E471F-D31A-4AFC-BAC2-23514D7F0FA4

Q27734011-39853050-4946-4301-A042-4E8515EF423A

Q27734011-5D552486-F101-4E2C-9DE5-B31FED7810A4

Q27734011-771BBD0A-AEEB-43F8-B4CF-61B880179EBC

Q27734011-7CA53FAE-7B4B-45D6-BD81-2F46FDC913FB

P2860

Q27734011-0B95F469-5A55-4D6E-AB7F-8CAA5F8FFAB9

Q27734011-0CFD968D-B438-4862-A267-DA451677FE11

Q27734011-107B9FB7-5256-4712-B06A-282D70804AD2

Q27734011-14C6FF4B-41B1-4DE3-AD6E-DEF5FBC11B16

Q27734011-2DA73E9A-BC17-4DCA-80BE-4EAA7F33F9CF

Q27734011-3D2D1325-447F-45A5-857E-F5EF94D31684

Q27734011-488D4812-D9E4-4BF9-AA19-17F20E51EAC8

Q27734011-49BAD92D-38B3-4F2E-95A7-4E7B3555F967

Q27734011-5C5DEEF7-B7AD-4485-9FBC-D0D4136A0E03

Q27734011-672959CA-7384-443E-88AC-C500EC48446C

P304

Q27734011-0B0F9864-33DD-468A-91B7-7811F8DDD179

P31

Q27734011-F3C37A6C-C1D0-448B-A238-A06D17723717

P3181

Q27734011-A6E66A50-6F57-4A8A-9723-E9BECBF10A53

P356

Q27734011-6E0C2943-A130-4B45-9C86-A8EAB6727942

P407

Q27734011-AB7AC08A-7270-4BDC-AEA6-F39C8E323059

P433

Q27734011-5636C334-4D3C-43D2-8E06-0E4B86A87030

P478

Q27734011-4308C01F-D569-493F-A535-A41CE76A18F0

P577

Q27734011-E5BAF39E-F625-4F6F-BFFE-126B44701038

P5875

Q27734011-A406CBBA-782A-4F6A-BE4F-63A7E9EFAA03

P698

Q27734011-CA01B610-9A29-4468-A177-A7524E51B7C6

P3181

P356

JBC.271.47.29988

P1433

Journal of Biological Chemistry

P1476

X-ray structure of active site ...... sign and substrate recognition

@en

P2093

A Kühne

http://www.w3.org/2001/XMLSchema#string

H Brandstetter

http://www.w3.org/2001/XMLSchema#string

K Wirthensohn

http://www.w3.org/2001/XMLSchema#string

R A Engh

http://www.w3.org/2001/XMLSchema#string

R Huber

http://www.w3.org/2001/XMLSchema#string

W Bode

http://www.w3.org/2001/XMLSchema#string

W von der Saal

http://www.w3.org/2001/XMLSchema#string

P2860

X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B

Crystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombin

Structure of human des(1-45) factor Xa at 2.2 A resolution

The coagulation cascade: initiation, maintenance, and regulation

Proteolytic activation of human factors IX and X by recombinant human factor VIIa: effects of calcium, phospholipids, and tissue factor

The interaction of thrombin with fibrinogen. A structural basis for its specificity.

Proteolytic action of thrombin is required for electrical activity-dependent synapse reduction

Intracerebral infusion of thrombin as a cause of brain edema.

Identification and molecular cloning of a p21cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets.

The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0.

P304

29988-92

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1140811

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.271.47.29988

http://www.w3.org/2001/XMLSchema#string

P407

P433

47

http://www.w3.org/2001/XMLSchema#string

P478

271

http://www.w3.org/2001/XMLSchema#string

P577

1996-11-22T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14267138

http://www.w3.org/2001/XMLSchema#string

P698

8939944

http://www.w3.org/2001/XMLSchema#string