The identification of a minimal dimerization motif QXXS that enables homo- and hetero-association of transmembrane helices in vivo.
about
Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.Role of transmembrane segment 5 and extracellular loop 3 in the homodimerization of human ABCC1HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.Identifying ionic interactions within a membrane using BLaTM, a genetic tool to measure homo- and heterotypic transmembrane helix-helix interactions.c-Cbl, a ubiquitin E3 ligase that targets active β-catenin: a novel layer of Wnt signaling regulation.The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies.A day in the life of a G protein-coupled receptor: the contribution to function of G protein-coupled receptor dimerization.Interaction and conformational dynamics of membrane-spanning protein helices.T-cell antigen receptor (TCR) transmembrane peptides: A new paradigm for the treatment of autoimmune diseases.Multiple residues in the transmembrane helix and connecting peptide of mouse tapasin stabilize the transporter associated with the antigen-processing TAP2 subunit.SOBIR1 requires the GxxxG dimerization motif in its transmembrane domain to form constitutive complexes with receptor-like proteins.Conserved polar residues stabilize transmembrane domains and promote oligomerization in human nucleoside triphosphate diphosphohydrolase 3Transmembrane helices that form two opposite homodimeric interactions: an asparagine scan study of alphaM and beta2 integrins.Transmembrane region of bacterial chemoreceptor is capable of promoting protein clustering.Critical residues and motifs for homodimerization of the first transmembrane domain of the plasma membrane glycoprotein CD36.Specificity in transmembrane helix-helix interactions mediated by aromatic residues.The HTLV-1 gp21 fusion peptide inhibits antigen specific T-cell activation in-vitro and in mice.
P2860
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P2860
The identification of a minimal dimerization motif QXXS that enables homo- and hetero-association of transmembrane helices in vivo.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
The identification of a minima ...... transmembrane helices in vivo.
@en
The identification of a minima ...... transmembrane helices in vivo.
@nl
type
label
The identification of a minima ...... transmembrane helices in vivo.
@en
The identification of a minima ...... transmembrane helices in vivo.
@nl
prefLabel
The identification of a minima ...... transmembrane helices in vivo.
@en
The identification of a minima ...... transmembrane helices in vivo.
@nl
P2860
P356
P1476
The identification of a minima ...... transmembrane helices in vivo.
@en
P2093
Doron Gerber
Yechiel Shai
P2860
P304
27449-27457
P356
10.1074/JBC.M503095200
P407
P50
P577
2005-05-23T00:00:00Z