Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues.
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Modeling transmembrane domain dimers/trimers of plexin receptors: implications for mechanisms of signal transmission across the membraneStructure elucidation of dimeric transmembrane domains of bitopic proteinsGxxxG motifs, phenylalanine, and cholesterol guide the self-association of transmembrane domains of ErbB2 receptorsInteractions between ionizable amino acid side chains at a lipid bilayer-water interface.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.Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Self-association of models of transmembrane domains of ErbB receptors in a lipid bilayerA putative transmembrane leucine zipper of agrobacterium VirB10 is essential for t-pilus biogenesis but not type IV secretion.Polar/Ionizable residues in transmembrane segments: effects on helix-helix packing.A thermodynamic approach to alamethicin pore formation
P2860
Q27310828-7C5C3B1F-108F-481A-B017-25A993FF5D7FQ33977508-15FADCA7-58DD-469D-BA23-1A88869C44DEQ35342149-33D4CDFF-1A74-430B-93FA-F528D762021CQ35560700-63BADCF6-EF7C-47EC-A100-FDC2D2B77F7AQ36569264-7EA8767B-3EBB-43B2-A0D9-0A01F1EA99EFQ37764644-B4522186-93D7-435A-A497-AD1E7E8B4A81Q41151906-7ED21088-2813-4B82-A4C3-05C73CCA2A3CQ41435161-F317E843-6804-41DC-BA2F-40D0543069C2Q41872052-177F0D56-C566-4A0B-9951-FA2268E5D88DQ41898520-8A111D23-C38A-4D56-BD81-DA04236D8F0D
P2860
Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Transmembrane helix associatio ...... g and noninterfacial residues.
@en
Transmembrane helix associatio ...... g and noninterfacial residues.
@nl
type
label
Transmembrane helix associatio ...... g and noninterfacial residues.
@en
Transmembrane helix associatio ...... g and noninterfacial residues.
@nl
prefLabel
Transmembrane helix associatio ...... g and noninterfacial residues.
@en
Transmembrane helix associatio ...... g and noninterfacial residues.
@nl
P2860
P1433
P1476
Transmembrane helix associatio ...... g and noninterfacial residues.
@en
P2093
Jinming Zhang
Themis Lazaridis
P2860
P304
P356
10.1016/J.BPJ.2009.03.008
P407
P577
2009-06-01T00:00:00Z