Features of TAP-independent MHC class I ligands revealed by quantitative mass spectrometry-Reference-Cited by-同舟云学术

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Features of TAP-independent MHC class I ligands revealed by quantitative mass spectrometry

Published:2008-04-29 Issue:6 Volume:38 Page:1503-1510
ISSN:0014-2980
Container-title:European Journal of Immunology
language:en
Short-container-title:Eur. J. Immunol.

Author:

Weinzierl Andreas O.,Rudolf Despina,Hillen Nina,Tenzer Stefan,van Endert Peter,Schild Hansjörg,Rammensee Hans-Georg,Stevanović Stefan

Publisher

Wiley

Subject

Immunology,Immunology and Allergy

Reference26 articles.

1. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation.;Kisselev;J. Biol. Chem.,1999

2. Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation.;York;J. Immunol.,2006

3. A sequential model for peptide binding and transport by the transporters associated with antigen processing.;van Endert;Immunity.,1994

4. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum.;Serwold;Nature,2002

5. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules.;Falk;Nature,1991

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