Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases - Test2 - elhamkhani - TriplyDB

Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases

Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases

http://www.wikidata.org/entity/Q28270556

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An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor.Aurora-A shines on T cell activation through the regulation of Lck.

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Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases

http://www.wikidata.org/entity/Q28270556

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2015 nî lūn-bûn

@nan

2015 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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type

label

Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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Identifying three-dimensional ...... in crystals of protein kinases

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Science Signaling

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Identifying three-dimensional ...... in crystals of protein kinases

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E Joseph Jordan

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Erin Duffy

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Jeffrey R Peterson

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Kimberly L Malecka

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Lauren Fink

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Qifang Xu

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Samuel Kolander

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P2860

Src family kinases negatively regulate platelet-derived growth factor alpha receptor-dependent signaling and disease progression

Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation

Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells

Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction

Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment

Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites

Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases

EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis

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scholarly article

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3159673

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10.1126/SCISIGNAL.AAA6711

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405

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8

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Roland Dunbrack

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2015-12-01T00:00:00Z

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26628682

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4766099

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