Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases - Wikidata - wikimedia - TriplyDB

Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases

Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases

http://www.wikidata.org/entity/Q27660088

about

Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment Transmembrane helix dimerization: beyond the search for sequence motifs The magic of bicelles lights up membrane protein structure Modeling transmembrane domain dimers/trimers of plexin receptors: implications for mechanisms of signal transmission across the membrane Conformational Changes in the Epidermal Growth Factor Receptor: Role of the Transmembrane Domain Investigated by Coarse-Grained MetaDynamics Free Energy Calculations Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane Segment Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments Structure of FGFR3 Transmembrane Domain Dimer: Implications for Signaling and Human Pathologies NMR structures of polytopic integral membrane proteins.Understanding single-pass transmembrane receptor signaling from a structural viewpoint-what are we missing?Structure and dynamic properties of membrane proteins using NMR.Structure elucidation of dimeric transmembrane domains of bitopic proteins Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".Eph/ephrin signaling in epidermal differentiation and disease Prediction, refinement, and persistency of transmembrane helix dimers in lipid bilayers using implicit and explicit solvent/lipid representations: microsecond molecular dynamics simulations of ErbB1/B2 and EphA1.Evolutionary-guided de novo structure prediction of self-associated transmembrane helical proteins with near-atomic accuracy.FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein.Tie2 and Eph receptor tyrosine kinase activation and signaling.Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Physical-chemical principles underlying RTK activation, and their implications for human disease.Structures of the EphA2 Receptor at the Membrane: Role of Lipid Interactions.Lipid rafts: integrated platforms for vascular organization offering therapeutic opportunities.A helix heterodimer in a lipid bilayer: prediction of the structure of an integrin transmembrane domain via multiscale simulations.EphA2 promotes cell adhesion and spreading of monocyte and monocyte/macrophage cell lines on integrin ligand-coated surfaces.Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase.Cancer somatic mutations disrupt functions of the EphA3 receptor tyrosine kinase through multiple mechanisms.Structural insight into the transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles.Dimerization of the EphA1 receptor tyrosine kinase transmembrane domain: Insights into the mechanism of receptor activation.Bicelles at low concentrations Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment.Role of the Lipid Environment in the Dimerization of Transmembrane Domains of Glycophorin A.Primary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations.Multidimensional umbrella sampling and replica-exchange molecular dynamics simulations for structure prediction of transmembrane helix dimers.The influence of fatty acids on the GpA dimer interface by coarse-grained molecular dynamics simulation.The pathogenic A391E mutation in FGFR3 induces a structural change in the transmembrane domain dimer.Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.Mechanism of Allosteric Coupling into and through the Plasma Membrane by EGFR.A novel pH-dependent membrane peptide that binds to EphA2 and inhibits cell migration

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P2860

Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases

http://www.wikidata.org/entity/Q27660088

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年學術文章

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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Left-Handed Dimer of EphA2 Tra ...... mong Receptor Tyrosine Kinases

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J.BPJ.2009.11.008

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Biophysical Journal

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Left-handed dimer of EphA2 tra ...... mong receptor tyrosine kinases

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Alexander S Arseniev

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Eduard V Bocharov

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Elena N Tkach

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Maxim L Mayzel

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Roman G Efremov

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Yaroslav S Ermolyuk

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P2860

Structure of lipid bilayers

Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger

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

Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1

Cell signaling by receptor tyrosine kinases

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

MOLMOL: a program for display and analysis of macromolecular structures

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Mechanisms and functions of Eph and ephrin signalling

Startle syndromes

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10.1016/J.BPJ.2009.11.008

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Konstantin Mineev

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transmembrane protein

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