MersV1, Main, Exploration, bibRecord, 003C68

Generation, intracellular transport and loading of peptides associated with MHC class I molecules

Identifieur interne : 003C68 ( Main/Exploration ); précédent : 003C67; suivant : 003C69

Generation, intracellular transport and loading of peptides associated with MHC class I molecules

Auteurs : Jens-Oliver Koopmann [Allemagne] ; Günter J. H Mmerling [Allemagne] ; Frank Momburg [Allemagne]

Source :

Current Opinion in Immunology [ 0952-7915 ] ; 1997.

RBID : ISTEX:2D6D6000E443D97F06B2C61E85A00A35314E1B72

English descriptors

Teeft :
- Allelic, Allelic variants, Amino, Amino acids, Antigen presentation, Antigen processing, Antigenic, Antigenic peptides, Calnexin, Calreticulin, Cell surface, Chaperone, Class peptides, Cleavage, Cresswell, Cytosolic, Different species, Endoplasmic, Endoplasmic reticulum, Epitope, Heavy chains, Heavy heterodimers, Herpes simplex virus, Histocompatibility, Human cells, Human class, Human tap1, Immunol, Inhibitor, Koopmann, Ligand, Major histocompatibility, Molecule, Molecules koopmann, Momburg, Mouse class, Neefjes, Ovalbumin, Pathway, Peptide, Peptide aldehydes, Peptide binding, Peptide binding site, Peptide loading, Peptide translocation, Peptide transport, Peptide transporter, Peptide transporters, Personal communication, Ploegh, Point mutation, Proteasome, Proteasomes, Reticulum, Sequence specificity, Sequence stretches, Substrate specificity, Subunit, Tap1, Tap2, Tapasin, Taps, Translocation, Transporter, Viral.

Abstract

Abstract: MHC class I molecules present antigenic peptides that are mostly derived from endogenous cytosolic proteins. Recent studies addressing the function of the proteasome and its activator complexes have advanced our understanding of the cytosolic processing of peptides. Transporters associated with antigen processing (TAPs) translocate these peptides to the endoplasmic reticulum where MHC class I molecules, which are retained in transient complexes with chaperones and TAPs, await them for binding. The sequence specificity and the peptide length preference of TAPs roughly meet the requirements of class I molecules in a range of different species, suggesting evolutionary shaping of the specificity of TAPs.

Url:

https://api.istex.fr/ark:/67375/6H6-5SLZ3JSS-9/fulltext.pdf

DOI: 10.1016/S0952-7915(97)80163-X

Affiliations:

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Le document en format XML

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<term>Antigen presentation</term>
<term>Antigen processing</term>
<term>Antigenic</term>
<term>Antigenic peptides</term>
<term>Calnexin</term>
<term>Calreticulin</term>
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<term>Class peptides</term>
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<term>Different species</term>
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<term>Ligand</term>
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<term>Neefjes</term>
<term>Ovalbumin</term>
<term>Pathway</term>
<term>Peptide</term>
<term>Peptide aldehydes</term>
<term>Peptide binding</term>
<term>Peptide binding site</term>
<term>Peptide loading</term>
<term>Peptide translocation</term>
<term>Peptide transport</term>
<term>Peptide transporter</term>
<term>Peptide transporters</term>
<term>Personal communication</term>
<term>Ploegh</term>
<term>Point mutation</term>
<term>Proteasome</term>
<term>Proteasomes</term>
<term>Reticulum</term>
<term>Sequence specificity</term>
<term>Sequence stretches</term>
<term>Substrate specificity</term>
<term>Subunit</term>
<term>Tap1</term>
<term>Tap2</term>
<term>Tapasin</term>
<term>Taps</term>
<term>Translocation</term>
<term>Transporter</term>
<term>Viral</term>
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<front><div type="abstract" xml:lang="en">Abstract: MHC class I molecules present antigenic peptides that are mostly derived from endogenous cytosolic proteins. Recent studies addressing the function of the proteasome and its activator complexes have advanced our understanding of the cytosolic processing of peptides. Transporters associated with antigen processing (TAPs) translocate these peptides to the endoplasmic reticulum where MHC class I molecules, which are retained in transient complexes with chaperones and TAPs, await them for binding. The sequence specificity and the peptide length preference of TAPs roughly meet the requirements of class I molecules in a range of different species, suggesting evolutionary shaping of the specificity of TAPs.</div>
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Generation, intracellular transport and loading of peptides associated with MHC class I molecules

Generation, intracellular transport and loading of peptides associated with MHC class I molecules

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri