Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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Fibrin Formation, Structure and Properties.Oxidation of proteins: is it a programmed process?Recombinant fibrinogen reveals the differential roles of α- and γ-chain cross-linking and molecular heterogeneity in fibrin clot strain-stiffening.

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P2860

Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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http://www.wikidata.org/entity/Q43021082

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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name

Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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type

Item

label

Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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prefLabel

Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

@en

Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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P1476

Structural Basis of Interfacial Flexibility in Fibrin Oligomers

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P2093

Anna D Protopopova

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

Artem Zhmurov

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

John W Weisel

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

Pavel Zhukov

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

Rustem I Litvinov

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

Valeri Barsegov

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

P2860

Mechanisms of fibrin polymerization and clinical implications

The Internal Dynamics of Fibrinogen and Its Implications for Coagulation and Adsorption

The crystal structure of modified bovine fibrinogen

2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site

The crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface

Fibrinogen variant B D432A has normal polymerization but does not bind knob"B"

Crystal structure of human fibrinogen

The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro

Crystal structure of fragment double-D from human fibrin with two different bound ligands

Mechanism of fibrin(ogen) forced unfolding.

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1907-1917

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scholarly article

P356

10.1016/J.STR.2016.08.009

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

P478

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

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Alexander R Mukhitov

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2016-09-29T00:00:00Z

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27692965

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5240993

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Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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P2860

P2860

Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

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P31

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P478

P50

P577

P698

P932