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Does topology drive fiber polymerization?

Does topology drive fiber polymerization?

http://www.wikidata.org/entity/Q34731611

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Fibrin Formation, Structure and Properties.Fibrin Association at Hybrid Biointerfaces Made of Clot-Binding Peptides and Polythiophene.

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P2860

Does topology drive fiber polymerization?

http://www.wikidata.org/entity/Q34731611

description

2014 nî lūn-bûn

@nan

2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Does topology drive fiber polymerization?

@ast

Does topology drive fiber polymerization?

@en

Does topology drive fiber polymerization?

@nl

type

label

Does topology drive fiber polymerization?

@ast

Does topology drive fiber polymerization?

@en

Does topology drive fiber polymerization?

@nl

prefLabel

Does topology drive fiber polymerization?

@ast

Does topology drive fiber polymerization?

@en

Does topology drive fiber polymerization?

@nl

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Does topology drive fiber polymerization?

@en

P2093

Camilla Powierza

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

Joe Ping-Lin Hsiao

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

Lihong Huang

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

Russell M Taylor

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

Susan T Lord

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

P2860

Impaired Protofibril Formation in Fibrinogen γN308K Is Due to Altered D:D and “A:a” Interactions ,

Software extensions to UCSF chimera for interactive visualization of large molecular assemblies

Fibrinogen and fibrin: scaffold proteins in hemostasis

Polymerization of rod-like macromolecular monomers studied by stopped-flow, multiangle light scattering: set-up, data processing, and application to fibrin formation.

Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled.

Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers.

A two-step fibrinogen--fibrin transition in blood coagulation.

The structure and function of the alpha C domains of fibrinogen.

Twisting of fibrin fibers limits their radial growth

Substitution of the human αC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers

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7824-7834

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scholarly article

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10.1021/BI500986Z

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49

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53

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2014-12-05T00:00:00Z

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268787832

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25419972

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4270379

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