Directly Activating the Integrin αIIbβ3 Initiates Outside-In Signaling by Causing αIIbβ3 Clustering.

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RGS10 Negatively Regulates Platelet Activation and Thrombogenesis.Integrin αIIbβ3 outside-in signaling.Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.

P2860

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P2860

Directly Activating the Integrin αIIbβ3 Initiates Outside-In Signaling by Causing αIIbβ3 Clustering.

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http://www.wikidata.org/entity/Q36941098

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2016 nî lūn-bûn

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2016年の論文

@ja

2016年論文

@yue

2016年論文

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2016年論文

@zh-hk

2016年論文

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2016年論文

@zh-tw

2016年论文

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2016年论文

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2016年论文

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name

Directly Activating the Integr ...... by Causing αIIbβ3 Clustering.

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type

Item

label

Directly Activating the Integr ...... by Causing αIIbβ3 Clustering.

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prefLabel

Directly Activating the Integr ...... by Causing αIIbβ3 Clustering.

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P1476

Directly Activating the Integr ...... by Causing αIIbβ3 Clustering.

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P2093

David T Moore

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

Hang Yin

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

Hua Zhu

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

Joel S Bennett

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

Karen P Fong

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

Kyungchul Yoon

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

Lisa M Span

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

Ryo Tamura

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P2860

Structural basis of integrin activation by talin

Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton

Src kinase activation by direct interaction with the integrin beta cytoplasmic domain

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

The structure of an integrin/talin complex reveals the basis of inside-out signal transduction.

Structure-Guided Design of a High-Affinity Platelet Integrin IIb 3 Receptor Antagonist That Disrupts Mg2+ Binding to the MIDAS

Structural and biophysical characterization of the Syk activation switch

Novel platelet inhibitors

Integrins: dynamic scaffolds for adhesion and signaling in platelets

RGD-containing peptides inhibit fibrinogen binding to platelet alpha(IIb)beta3 by inducing an allosteric change in the amino-terminal portion of alpha(IIb)

P304

11706-11716

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P31

scholarly article

P356

10.1074/JBC.M116.716613

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English

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

P478

291

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

P50

William DeGrado

P577

2016-04-07T00:00:00Z

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

P698

27056329

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P932

4882439

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

Directly Activating the Integrin αIIbβ3 Initiates Outside-In Signaling by Causing αIIbβ3 Clustering.

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P2860

P2860

Directly Activating the Integrin αIIbβ3 Initiates Outside-In Signaling by Causing αIIbβ3 Clustering.

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932