Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state - Wikidata - awgldk - TriplyDB

Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state

Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state

http://www.wikidata.org/entity/Q27649487

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Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment Conformational coupling across the plasma membrane in activation of the EGF receptor Transmembrane helix dimerization: beyond the search for sequence motifs The magic of bicelles lights up membrane protein structure Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1 Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases Structural Evidence for Loose Linkage between Ligand Binding and Kinase Activation in the Epidermal Growth Factor Receptor Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane Segment Structure of FGFR3 Transmembrane Domain Dimer: Implications for Signaling and Human Pathologies Optimal Bicelle Size q for Solution NMR Studies of the Protein Transmembrane Partition NMR structures of polytopic integral membrane proteins.Prediction of the structures of helical membrane proteins based on a minimum unfavorable contacts approach.Understanding single-pass transmembrane receptor signaling from a structural viewpoint-what are we missing?Structure and dynamic properties of membrane proteins using NMR.Structural Symmetry in Membrane Proteins.A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activation Structure elucidation of dimeric transmembrane domains of bitopic proteins Nonmicellar systems for solution NMR spectroscopy of membrane proteins Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET.Protein domain-level landscape of cancer-type-specific somatic mutations.Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms.GxxxG motifs, phenylalanine, and cholesterol guide the self-association of transmembrane domains of ErbB2 receptors Regulation of the catalytic activity of the EGF receptor.Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly.A structural perspective on the regulation of the epidermal growth factor receptor.Analysis of the Role of the C-Terminal Tail in the Regulation of the Epidermal Growth Factor Receptor Understanding cytokine and growth factor receptor activation mechanisms.Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.Production of disulfide-stabilized transmembrane peptide complexes for structural studies.VEGFR-2 conformational switch in response to ligand binding.Evolutionary-guided de novo structure prediction of self-associated transmembrane helical proteins with near-atomic accuracy.APP Receptor? To Be or Not To Be.Architecture and membrane interactions of the EGF receptor.FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Protein-protein interactions in the membrane: sequence, structural, and biological motifs.Interaction and conformational dynamics of membrane-spanning protein helices.Novel germline mutation in the transmembrane domain of HER2 in familial lung adenocarcinomas.A frequent, GxxxG-mediated, transmembrane association motif is optimized for the formation of interhelical Cα-H hydrogen bonds.Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics.

P2860

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P2860

Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state

http://www.wikidata.org/entity/Q27649487

description

2008 nî lūn-bûn

@nan

2008 թուականի Մարտին հրատարակուած գիտական յօդուած

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2008 թվականի մարտին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Spatial structure of the dimer ...... g to the receptor active state

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Spatial structure of the dimer ...... g to the receptor active state

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Spatial structure of the dimer ...... g to the receptor active state

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type

label

Spatial structure of the dimer ...... g to the receptor active state

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Spatial structure of the dimer ...... g to the receptor active state

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Spatial structure of the dimer ...... g to the receptor active state

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prefLabel

Spatial structure of the dimer ...... g to the receptor active state

@ast

Spatial structure of the dimer ...... g to the receptor active state

@en

Spatial structure of the dimer ...... g to the receptor active state

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P1433

Journal of Biological Chemistry

P1476

Spatial structure of the dimer ...... g to the receptor active state

@en

P2093

Alexander G Sobol

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

Alexander S Arseniev

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

Eduard V Bocharov

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

Elena N Tkach

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

Konstantin S Mineev

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

Michail P Kirpichnikov

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

Pavel E Volynsky

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

Roman G Efremov

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

Vladimir V Chupin

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

Yaroslav S Ermolyuk

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6950-6

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scholarly article

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2440524

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10.1074/JBC.M709202200

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11

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283

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2008-03-14T00:00:00Z

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18178548

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P921

transmembrane protein