An MHC-I cytoplasmic domain/HIV-1 Nef fusion protein binds directly to the mu subunit of the AP-1 endosomal coat complex.
about
Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1HIV-1 Nef disrupts intracellular trafficking of major histocompatibility complex class I, CD4, CD8, and CD28 by distinct pathways that share common elementsStructural basis of evasion of cellular adaptive immunity by HIV-1 NefOne protein to rule them all: modulation of cell surface receptors and molecules by HIV Nef.The identification of a small molecule compound that reduces HIV-1 Nef-mediated viral infectivity enhancementOverlapping effector interfaces define the multiple functions of the HIV-1 Nef polyproline helix.Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef actionSelf-association of the Lentivirus protein, NefTetherin/BST-2 antagonism by Nef depends on a direct physical interaction between Nef and tetherin, and on clathrin-mediated endocytosis.Misdirection of membrane trafficking by HIV-1 Vpu and Nef: Keys to viral virulence and persistence.ADP ribosylation factor 1 activity is required to recruit AP-1 to the major histocompatibility complex class I (MHC-I) cytoplasmic tail and disrupt MHC-I trafficking in HIV-1-infected primary T cells.A noncanonical mu-1A-binding motif in the N terminus of HIV-1 Nef determines its ability to downregulate major histocompatibility complex class I in T lymphocytesAn interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I.Human leukocyte antigen (HLA) class I down-regulation by human immunodeficiency virus type 1 negative factor (HIV-1 Nef): what might we learn from natural sequence variants?Mechanisms of HIV-1 Nef function and intracellular signaling.HLA class I molecules partner with integrin β4 to stimulate endothelial cell proliferation and migration.HIV immune evasion disruption of antigen presentation by the HIV Nef protein.HIV-1 Nef: Taking Control of Protein Trafficking.Function of ubiquitin (Ub) specific protease 15 (USP15) in HIV-1 replication and viral protein degradation.Endocytic activity of HIV-1 Vpu: Phosphoserine-dependent interactions with clathrin adaptors.Identification of a highly conserved valine-glycine-phenylalanine amino acid triplet required for HIV-1 Nef function
P2860
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P2860
An MHC-I cytoplasmic domain/HIV-1 Nef fusion protein binds directly to the mu subunit of the AP-1 endosomal coat complex.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@ast
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@en
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@nl
type
label
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@ast
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@en
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@nl
prefLabel
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@ast
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@en
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@nl
P2093
P2860
P1433
P1476
An MHC-I cytoplasmic domain/HI ...... e AP-1 endosomal coat complex.
@en
P2093
Colleen M Noviello
John C Guatelli
Partho Ghosh
Rajendra Kumar Singh
P2860
P356
10.1371/JOURNAL.PONE.0008364
P407
P577
2009-12-18T00:00:00Z