On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different.

On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different.

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http://www.wikidata.org/entity/Q34477404
Heparan sulfate and heparin interactions with proteinsTargeting the GPIbα binding site of thrombin to simultaneously induce dual anticoagulant and antiplatelet effectsA Simple Method for Discovering Druggable, Specific Glycosaminoglycan-Protein Systems. Elucidation of Key Principles from Heparin/Heparan Sulfate-Binding ProteinsThe Good the Bad and the Ugly of Glycosaminoglycans in Tissue Engineering ApplicationsDesigning allosteric inhibitors of factor XIa. Lessons from the interactions of sulfated pentagalloylglucopyranosides.Discovery of allosteric modulators of factor XIa by targeting hydrophobic domains adjacent to its heparin-binding site.Toward a robust computational screening strategy for identifying glycosaminoglycan sequences that display high specificity for target proteins.Investigation of the heparin-thrombin interaction by dynamic force spectroscopyNatural variation in the heparan sulfate binding domain of the eastern equine encephalitis virus E2 glycoprotein alters interactions with cell surfaces and virulence in miceEmerging sulfated flavonoids and other polyphenols as drugs: nature as an inspiration.Estimating glycosaminoglycan-protein interaction affinity: water dominates the specific antithrombin-heparin interaction.Heparin/Heparan sulfate proteoglycans glycomic interactome in angiogenesis: biological implications and therapeutical use.Hepatitis C virus infection propagates through interactions between Syndecan-1 and CD81 and impacts the hepatocyte glycocalyx.Approaches to prevent bleeding associated with anticoagulants: current status and recent developments.The promise of sulfated synthetic small molecules as modulators of glycosaminoglycan function.So you think computational approaches to understanding glycosaminoglycan-protein interactions are too dry and too rigid? Think again!Heparin: role in protein purification and substitution with animal-component free material
P2860

On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different.

Item
http://www.wikidata.org/entity/Q34477404
description
2012 nî lūn-bûn
@nan
2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
On the specificity of heparin/ ...... n are fundamentally different.
@ast
On the specificity of heparin/ ...... n are fundamentally different.
@en
On the specificity of heparin/ ...... n are fundamentally different.
@nl
type
label
On the specificity of heparin/ ...... n are fundamentally different.
@ast
On the specificity of heparin/ ...... n are fundamentally different.
@en
On the specificity of heparin/ ...... n are fundamentally different.
@nl
prefLabel
On the specificity of heparin/ ...... n are fundamentally different.
@ast
On the specificity of heparin/ ...... n are fundamentally different.
@en
On the specificity of heparin/ ...... n are fundamentally different.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
On the specificity of heparin/ ...... n are fundamentally different.
@en
P2093
P2860
P304
P31
P356
10.1371/JOURNAL.PONE.0048632
P407
P433
P478
P50
P577
P5875
P698
P932