HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
about
HSP60 as a target of anti-ergotypic regulatory T cellsThe SCHOOL of nature: I. Transmembrane signaling.Novel mechanistic insights into viral modulation of immune receptor signaling.HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferationThe three lives of viral fusion peptidesA novel ligand-independent peptide inhibitor of TREM-1 suppresses tumor growth in human lung cancer xenografts and prolongs survival of mice with lipopolysaccharide-induced septic shock.The SCHOOL of nature: III. From mechanistic understanding to novel therapiesSelected amino acid mutations in HIV-1 B subtype gp41 are associated with specific gp120v₃ signatures in the regulation of co-receptor usage.Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor designHIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.Effect of the HIV-1 fusion peptide on the mechanical properties and leaflet coupling of lipid bilayers.Recent advances in delivery systems for anti-HIV1 therapy.SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in DBA/1J Mice.An immunomodulating motif of the HIV-1 fusion protein is chirality-independent: implications for its mode of action.Protein intrinsic disorder and oligomericity in cell signaling.T-cell antigen receptor (TCR) transmembrane peptides: A new paradigm for the treatment of autoimmune diseases.New therapeutic strategies targeting transmembrane signal transduction in the immune system.A GxxxG-like motif within HIV-1 fusion peptide is critical to its immunosuppressant activity, structure, and interaction with the transmembrane domain of the T-cell receptor.Conserved salt bridge between the N- and C-terminal heptad repeat regions of the human immunodeficiency virus type 1 gp41 core structure is critical for virus entry and inhibition.Cells diversify transmembrane signaling through the controlled chaos of protein disorder.The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.The SCHOOL of nature: IV. Learning from viruses.Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide.Rationally designed ligand-independent peptide inhibitors of TREM-1 ameliorate collagen-induced arthritis.The topology, in model membranes, of the core peptide derived from the T-cell receptor transmembrane domain.The HTLV-1 gp21 fusion peptide inhibits antigen specific T-cell activation in-vitro and in mice.
P2860
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P2860
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@ast
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@en
type
label
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@ast
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@en
prefLabel
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@ast
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@en
P2093
P2860
P356
P1476
HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation
@en
P2093
Doron Gerber
Francisco J Quintana
Irun R Cohen
Sally C Kent
Yechiel Shai
P2860
P304
P356
10.1172/JCI23956
P407
P577
2005-07-07T00:00:00Z