2026-06-14T03:37:51Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/96962024-09-27T22:38:12Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Lopez, Daniel
author
Calero, Olga
author
Jimenez, Mercedes
author
García-Calvo, Margarita
author
Del Val, Margarita
funder
Instituto de Salud Carlos III
funder
Comunidad de Madrid (España)
funder
Ministerio de Educación y Ciencia (España)
2020-04-23T06:59:43Z
2020-04-23T06:59:43Z
2006-10-13
J Biol Chem. 2006 Oct 13;281(41):30315-8. Epub 2006 Jul 21.
10.1074/jbc.M605973200
0021-9258
The Journal of biological chemistry
16861221
http://hdl.handle.net/20.500.12105/9696
Mass spectrometry (MS)-based methods coupled to reverse phase chromatography separation are a useful technology to analyze complex peptide pools that are comprised of different peptides with unrelated sequences. In antigen presentation, proteasomes generate a set of short peptides that are closely related and overlapping and in some instances may even have identical retention times and identical masses. In these situations, micro-liquid chromatography-MS/MS focused on each theoretical parent ion followed by manual interpretation optimizes the identification of generated peptides. The results suggest that the degradation of short antigens by the proteasome occurs by sequential cleavage.
eng
Antigen processing of a short viral antigen by proteasomes
journal article
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URL
https://repisalud.isciii.es/bitstreams/848f734c-452e-4f3d-b901-51b91781130a/download
File
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application/pdf
AntigenProcessingOfA_2006.pdf
URL
https://repisalud.isciii.es/bitstreams/ffdb2381-b0a0-468b-ac7d-c37e2fbf698c/download
File
MD5
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text/plain
AntigenProcessingOfA_2006.pdf.txt