Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.
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Molecular insights into the dynamics of pharmacogenetically important N-terminal variants of the human β2-adrenergic receptorSolid state NMR and protein-protein interactions in membranesCoupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3Oncogenic HER2 fusions in gastric cancer.Juxtamembrane contribution to transmembrane signaling.A single amino acid substitution converts a transmembrane protein activator of the platelet-derived growth factor β receptor into an inhibitor.The Dipole Potential Modifies the Clustering and Ligand Binding Affinity of ErbB Proteins and Their Signaling Efficiency.The EGFR family: not so prototypical receptor tyrosine kinases.Putting together structures of epidermal growth factor receptorsChemical synthesis of transmembrane peptide and its application for research on the transmembrane-juxtamembrane region of membrane protein.Nuclear magnetic resonance (NMR) applied to membrane-protein complexes.The juxtamembrane regions of human receptor tyrosine kinases exhibit conserved interaction sites with anionic lipids.Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Basic motifs target PSGL-1, CD43, and CD44 to plasma membrane sites where HIV-1 assembles.Interactions of the EGFR juxtamembrane domain with PIP2-containing lipid bilayers: Insights from multiscale molecular dynamics simulations.Primary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations.Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.Lipid-Protein Interplay in Dimerization of Juxtamembrane Domains of Epidermal Growth Factor Receptor.
P2860
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P2860
Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@ast
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@en
type
label
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@ast
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@en
prefLabel
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@ast
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@en
P2093
P2860
P356
P1476
Transmembrane helix orientatio ...... main in Neu receptor peptides.
@en
P2093
Chihiro Matsushita
Hiroko Tamagaki
Saburo Aimoto
Steven O Smith
Takeshi Sato
Yudai Miyazawa
P2860
P304
P356
10.1073/PNAS.1215207110
P407
P577
2013-01-14T00:00:00Z