Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.

about

The structural diversity of C-rich DNA aggregates: unusual self-assembly of beetle-like nanostructures.Observation of Ultrafast Vibrational Energy Transfer in Fibrinogen and Fibrin Fibers.

P2860

Q50037264-FA62DE00-28DE-4BDC-8BFF-9E6676CD0C2E Q55052025-BC5A5F01-3F2D-4F95-9169-669C337B457E

P2860

Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.

Item

http://www.wikidata.org/entity/Q50201615

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Morphometric characterization ...... ly and molecular organization.

@en

Morphometric characterization ...... ly and molecular organization.

@nl

type

Item

label

Morphometric characterization ...... ly and molecular organization.

@en

Morphometric characterization ...... ly and molecular organization.

@nl

prefLabel

Morphometric characterization ...... ly and molecular organization.

@en

Morphometric characterization ...... ly and molecular organization.

@nl

P1476

Morphometric characterization ...... ly and molecular organization.

@en

P2093

Chandrasekaran Nagaswami

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

Dennis K Galanakis

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

Dmitry V Klinov

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

John W Weisel

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

Rustem I Litvinov

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

P2860

Crystal structure of human fibrinogen

Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

Fiji: an open-source platform for biological-image analysis.

Cryo-atomic force microscopy of unphosphorylated and thiophosphorylated single smooth muscle myosin molecules.

Mechanism of fibrin(ogen) forced unfolding.

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

Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.

Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains.

α-α Cross-links increase fibrin fiber elasticity and stiffness

Structural origins of fibrin clot rheology

P304

13707-13716

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

P31

scholarly article

P356

10.1039/C7NR04413E

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

P407

English

P433

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

P478

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

P50

Alexander R Mukhitov

Nikolay Barinov

Anna Protopopova

P577

2017-09-08T00:00:00Z

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

P698

28884176

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

P921

self-assembly

P932

6501582

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

Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.

about

P2860

P2860

Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932