EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
about
Affimer proteins are versatile and renewable affinity reagentsCollagen induces activation of DDR1 through lateral dimer association and phosphorylation between dimersUnderstanding the FRET Signatures of Interacting Membrane Proteins.Piecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.Activation of the EGF Receptor by Ligand Binding and Oncogenic Mutations: The "Rotation Model".EGF and NRG induce phosphorylation of HER3/ERBB3 by EGFR using distinct oligomeric mechanisms.Epidermal Growth Factor Receptor Signaling Disruption by Endocrine and Metabolic Disrupting Chemicals.Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells.Cyclic trans-phosphorylation in a homodimer as the predominant mechanism of EGFRvIII action and regulation.Inhibitor-induced HER2-HER3 heterodimerisation promotes proliferation through a novel dimer interface.Phosphorylated EGFR Dimers Are Not Sufficient to Activate Ras.Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.The architecture of EGFR's basal complexes reveals autoinhibition mechanisms in dimers and oligomersA conformational sensor based on genetic code expansion reveals an autocatalytic component in EGFR activationAutomated single-molecule imaging in living cells
P2860
Q33842511-1D295312-F5C6-4054-A6E6-9EB44D9C4B14Q33848736-33A12594-1EBB-4F0C-92CE-672DB5C1DDD2Q38966553-8CEEB46C-E14E-454A-A05B-7C7FF84563BEQ39089524-93C270D4-F8D3-4379-8053-55348C5D20DDQ39346046-E19D6D28-B843-4800-831A-36604D6C66CCQ42081733-35ABE57D-C560-4699-9F3B-8556CA214C65Q47656937-868FDD7B-392E-424A-AD01-B2BD660A4EE3Q47892855-435C7D5E-B33F-4CE5-BE04-1E4FCF63D67FQ50324498-0C498D9F-BE39-4544-ACF6-71E0D82332E3Q52715470-4960D519-A2DC-4C54-97C7-2A48C6C17044Q54940071-44A09244-CC8B-4782-83F7-3D5E2408421FQ54976599-A2FC5850-44E4-49F8-886D-30C9BD30B58DQ58600328-6124FC1E-764C-475A-BEBB-B25A6679D80DQ58705164-05B697F3-F806-4F40-87A0-3A3A09262CC0Q58802317-E23AD4B8-8A0B-4E4A-AAE1-64EFE207636A
P2860
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
description
2016 nî lūn-bûn
@nan
2016 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@ast
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@en
type
label
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@ast
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@en
prefLabel
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@ast
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@en
P2093
P2860
P50
P356
P1476
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
@en
P2093
Andrew H A Clayton
Anton Arkhipov
David E Shaw
Eric T Kim
Linda J Pike
Martyn D Winn
Michael Hirsch
Michela Perani
Selene K Roberts
Valeria Losasso
P2860
P2888
P356
10.1038/NCOMMS13307
P407
P50
P577
2016-10-31T00:00:00Z
P6179
1013280320