Molecular basis for multimerization in the activation of the epidermal growth factor receptor
about
EGFR oligomerization organizes kinase-active dimers into competent signalling platformsPhotoGate microscopy to track single molecules in crowded environments.Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complexCollagen induces activation of DDR1 through lateral dimer association and phosphorylation between dimersEffects of FGFR2 kinase activation loop dynamics on catalytic activitySuppressor of cytokine signaling (SOCS)5 ameliorates influenza infection via inhibition of EGFR signalingA role of the SAM domain in EphA2 receptor activation.Cardiac GPCR-Mediated EGFR Transactivation: Impact and Therapeutic Implications.Role of N-glycosylation in EGFR ectodomain ligand binding.Understanding 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.Single-molecule fluorescence-based analysis of protein conformation, interaction, and oligomerization in cellular systems.Epidermal growth factor receptors containing a single tyrosine in their C-terminal tail bind different effector molecules and are signaling-competent.TGF-β and IL-6 family signalling crosstalk: an integrated model.Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells.Conformationally constrained peptides target the allosteric kinase dimer interface and inhibit EGFR activation.Quantifying Membrane Protein Oligomerization with Fluorescence Cross-Correlation Spectroscopy.Coupled regulation by the juxtamembrane and sterile α motif (SAM) linker is a hallmark of Ephrin tyrosine kinase evolution.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.Charge and Polarity Preferences for N-Glycosylation: A Genome-Wide In Silico Study and Its Implications Regarding Constitutive Proliferation and Adhesion of Carcinoma Cells.The architecture of EGFR's basal complexes reveals autoinhibition mechanisms in dimers and oligomers
P2860
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P2860
Molecular basis for multimerization in the activation of the epidermal growth factor receptor
description
2016 nî lūn-bûn
@nan
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
2016年论文
@zh
2016年论文
@zh-cn
name
Molecular basis for multimeriz ...... idermal growth factor receptor
@en
type
label
Molecular basis for multimeriz ...... idermal growth factor receptor
@en
prefLabel
Molecular basis for multimeriz ...... idermal growth factor receptor
@en
P2093
P2860
P50
P356
P1433
P1476
Molecular basis for multimeriz ...... idermal growth factor receptor
@en
P2093
Adam W Smith
Megan J Kaliszewski
Morgan Marita
Sean M Peterson
Shashank Bharill
Xiaojun Shi
Yongjian Huang
P2860
P356
10.7554/ELIFE.14107
P407
P577
2016-03-28T00:00:00Z