Molecular mapping of the heparin-binding exosite of thrombin. - Wikidata - wikimedia - TriplyDB

Molecular mapping of the heparin-binding exosite of thrombin.

Molecular mapping of the heparin-binding exosite of thrombin.

http://www.wikidata.org/entity/Q35478768

about

Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor Molecular mapping of the thrombin-heparin cofactor II complex Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycans Hageman factor, platelets and polyphosphates: early history and recent connection Designing Allosteric Regulators of Thrombin. Exosite 2 Features Multiple Subsites That Can Be Targeted by Sulfated Small Molecules for Inducing Inhibition Low anticoagulant heparin blocks thrombin-induced endothelial permeability in a PAR-dependent manner From natural to synthetic multisite thrombin inhibitors.A peptide found by phage display discriminates a specific structure of a trisaccharide in heparin.The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes.Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.Thrombin inhibition by serpins disrupts exosite II Activation of factor XI by products of prothrombin activation Identification of exosite residues of factor Xa involved in recognition of PAR-2 on endothelial cells Targeting exosites on blood coagulation proteases.Structural investigation of the alpha-1-antichymotrypsin: prostate-specific antigen complex by comparative model building Ixolaris binding to factor X reveals a precursor state of factor Xa heparin-binding exosite.Fluorescent reporters of thrombin, heparin cofactor II, and heparin binding in a ternary complex.Characterization of bothrojaracin interaction with human prothrombin.Anticoagulant activity of a unique sulfated pyranosic (1->3)-β-L-arabinan through direct interaction with thrombin The role of thrombin exosites I and II in the activation of human coagulation factor V.Selection of a suppressor mutation that restores affinity of an oligonucleotide inhibitor for thrombin using in vitro genetics.Thrombin.Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor Factor XI anion-binding sites are required for productive interactions with polyphosphate.Recent advances in oral anticoagulation for atrial fibrillation.Looking at the proteases from a simple perspective.Localization of the thrombin-binding domain on prothrombin fragment 2.The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity.A historical perspective of the biophysics of the thrombin-heparin system: an example of nonspecific binding and the consequent parking problem in action.Polyphosphate binds with high affinity to exosite II of thrombin.Antiplatelet and anticoagulant effects of diterpenes isolated from the marine alga, Dictyota menstrualis.Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C.Definition of a factor Va binding site in factor Xa.Heparin enhances the catalytic activity of des-ETW-thrombin.Interaction of the 268-282 region of glycoprotein Ibalpha with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII.Long range communication between exosites 1 and 2 modulates thrombin function.Ixolaris: a factor Xa heparin-binding exosite inhibitor Functional mapping of the surface residues of human thrombin.Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein.Structural glycobiology of heparin dynamics on the exosite 2 of coagulation cascade proteases: Implications for glycosaminoglycans antithrombotic activity.

P2860

Q24598030-20F1AE48-2F48-479C-843C-59F077CDECCE Q28275459-2821145D-953B-4536-8702-AC292A6B293D Q28588197-9B66BFF3-10D7-4D72-A371-E5327895D40B Q28748668-9B7EE813-4CC8-4894-B683-AD0A9D3398E6 Q29040782-C689B613-1915-4FC8-AE73-005A280A168E Q33412967-EBAC99B9-46F6-4B72-A530-7A6D851DCDD7 Q33668993-9C47ED60-9308-446F-9FA2-0B98BE79D854 Q33824892-2546F331-01FE-4E96-8D54-2607F149C2B9 Q33852592-A58F7B7F-281B-4A7F-BEE2-68F9A7A2D542 Q34341165-BBC29A4D-6971-47B0-BE26-8C6FA56C664D Q34352365-D09C4802-7B31-4572-8B21-4A8E2C0B35DE Q35112259-3A229C52-3DD9-4900-AE93-879CA845E27B Q35856975-7148DE39-4228-40AE-AAD9-B7B7F884725C Q36128237-AA254C74-9708-48E9-AF9B-6721D1279E90 Q36279827-A8008661-DC94-4E0A-A1C7-4A13BE90EF86 Q36281976-F4E7A430-004C-494B-A959-66D6DA9AFACB Q36288526-5AC185F8-D1FE-46F1-AB15-19CF381A1D30 Q36476528-EDE04A69-2852-4EC7-8430-4AC5A6B35669 Q36508588-762B2BF3-31AF-4013-8E75-72C3154EDF8B Q36538501-E9D658CF-B471-4AB2-8504-6A4EA7B3F697 Q36690512-08CA59CA-C223-47EE-82A9-9C6AF5AFCF0C Q36800534-D7CACAB8-4E37-415E-92D4-8B1DA2EFE47C Q37125600-9947DB21-0D0F-4861-9C34-07AD199AEC49 Q37398521-399D7E0C-B865-4B20-AD18-AABB009E0627 Q37802084-2E5CD3AC-B4F5-42C3-A2AE-0294DE15826E Q37848282-843A6ACD-5961-4801-ADD9-59535148BB6B Q38337651-C9FC7284-4F61-466F-8C78-EA35544FD00B Q38337743-6861CED7-D357-4D08-A603-907F8DBAAAB2 Q38783050-90764D0E-3E66-46AE-9ED9-6764DA1D32C5 Q40092357-4C3F3305-EA49-463A-BD29-B61F2B181AE9 Q40539395-CC478BA8-F9C5-49B6-9FE0-75EF8AD3F02E Q40810671-B6F92D81-3106-4391-95F1-E91D7DD02B53 Q40841059-3EF3D25D-2EDE-49BB-95A2-DC51CA389FDC Q41868886-CC348841-4A6F-4DFB-80DB-02C82F8D7BE2 Q41934357-92AE0A3A-4061-4448-BD4E-92370F388EC4 Q42030991-FEECFCC4-5E5A-468C-9E93-23D159E385B5 Q42177621-E9142E9A-D317-4DF1-A24F-26D63E55499F Q42679721-D61EC338-8267-4E65-97B6-4739E1D64999 Q44274672-503C122C-760F-4E4E-9439-A5CD236C0645 Q44505808-89C538D5-5CFA-471B-BE45-8F039643B02A

P2860

Molecular mapping of the heparin-binding exosite of thrombin.

http://www.wikidata.org/entity/Q35478768

description

1994 nî lūn-bûn

@nan

1994 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի հունիսին հրատարակված գիտական հոդված

@hy

1994年の論文

@ja

1994年学术文章

@wuu

1994年学术文章

@zh-cn

1994年学术文章

@zh-hans

1994年学术文章

@zh-my

1994年学术文章

@zh-sg

1994年學術文章

@yue

name

Molecular mapping of the heparin-binding exosite of thrombin.

@ast

Molecular mapping of the heparin-binding exosite of thrombin.

@en

type

label

Molecular mapping of the heparin-binding exosite of thrombin.

@ast

Molecular mapping of the heparin-binding exosite of thrombin.

@en

prefLabel

Molecular mapping of the heparin-binding exosite of thrombin.

@ast

Molecular mapping of the heparin-binding exosite of thrombin.

@en

P1433

Q35478768-81F59A05-A7D5-4A6F-B52F-0F46B3F0DEBF

P1476

Q35478768-CF77EA56-5170-4EF5-BC9E-86970B39C82D

P2860

Q35478768-037D6B86-BC9F-4CED-A997-C9E1B57DD02A

Q35478768-0ABE8F5A-645E-40E8-B603-B25D20973750

Q35478768-130796FF-7CCC-4941-B188-94DCAE8D0AF3

Q35478768-19A044F8-F329-48DB-94A1-259CD0794F39

Q35478768-23820103-F8F3-4E7C-ACFC-C618AE7C8F87

Q35478768-29A322C0-75A5-43F9-B790-3BA91C8C5484

Q35478768-324A1DC1-B998-4C5C-A8C5-5E7C9BE9FB76

Q35478768-3A1C627A-A5CC-4550-994D-AC7B2CDACEF6

Q35478768-4E73BF7B-FF30-4E2D-9CD3-7B104ACF7C1D

Q35478768-51888D7F-6CE5-4D84-B27B-ACAC57B53916

P304

Q35478768-F2FF5E76-3559-4224-9255-E9E599969936

P31

Q35478768-FC0B7694-02C4-42BA-BD02-B075A76992AC

P356

Q35478768-78DA02A0-64C4-4E28-BBB8-FD1F488B272F

P407

Q35478768-00F43E7A-757C-4108-A8E4-F43BB20CAEF9

P433

Q35478768-8EB28989-3640-4151-8368-464366EF6635

P478

Q35478768-276867DC-0BE1-4901-AF3C-02ED81CE8127

P50

Q35478768-5B6F518D-DB44-45A1-82F8-5CEF0F937556

Q35478768-CECF1D1F-188B-400B-9B42-4773893BE0D7

P577

Q35478768-EE73DFE2-1CE0-46EF-92C8-91B07F044977

P5875

Q35478768-C028D3FA-CC28-4A0C-B599-2019C040BFD3

P698

Q35478768-87EE131F-1372-400B-BDC6-5F20A88F6047

P932

Q35478768-07FDFF86-A30E-419F-842A-16FE082A69F0

P356

PNAS.91.12.5518

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Molecular mapping of the heparin-binding exosite of thrombin.

@en

P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

The structure of a complex of recombinant hirudin and human alpha-thrombin

Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin

Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement

Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter

Heparin: mechanism of action, pharmacokinetics, dosing considerations, monitoring, efficacy, and safety.

Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake).

The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution.

Thrombin receptor expression in normal and atherosclerotic human arteries.

P304

5518-5522

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

P31

scholarly article

P356

10.1073/PNAS.91.12.5518

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

P407

P433

12

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

P478

91

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

P50

P577

1994-06-01T00:00:00Z

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

P5875

14995787

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

P698

8202520

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

P932

44027

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