Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames
Cryptic translation of the 'non-coding' genome is increasingly recognised, however its biological significance remains unclear. Laumont et al.employ proteogenomic techniques to map the human immunoproteome, and find that approximately 10% of MHC class I-associated peptides are cryptic.
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2016-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms10238 |
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doaj-8e030826a1744d55a142f5a4d3124d1e2021-05-11T11:10:48ZengNature Publishing GroupNature Communications2041-17232016-01-017111210.1038/ncomms10238Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading framesCéline M. Laumont0Tariq Daouda1Jean-Philippe Laverdure2Éric Bonneil3Olivier Caron-Lizotte4Marie-Pierre Hardy5Diana P. Granados6Chantal Durette7Sébastien Lemieux8Pierre Thibault9Claude Perreault10Institute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalInstitute for Research in Immunology and Cancer, Université de MontréalCryptic translation of the 'non-coding' genome is increasingly recognised, however its biological significance remains unclear. Laumont et al.employ proteogenomic techniques to map the human immunoproteome, and find that approximately 10% of MHC class I-associated peptides are cryptic.https://doi.org/10.1038/ncomms10238 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Céline M. Laumont Tariq Daouda Jean-Philippe Laverdure Éric Bonneil Olivier Caron-Lizotte Marie-Pierre Hardy Diana P. Granados Chantal Durette Sébastien Lemieux Pierre Thibault Claude Perreault |
spellingShingle |
Céline M. Laumont Tariq Daouda Jean-Philippe Laverdure Éric Bonneil Olivier Caron-Lizotte Marie-Pierre Hardy Diana P. Granados Chantal Durette Sébastien Lemieux Pierre Thibault Claude Perreault Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames Nature Communications |
author_facet |
Céline M. Laumont Tariq Daouda Jean-Philippe Laverdure Éric Bonneil Olivier Caron-Lizotte Marie-Pierre Hardy Diana P. Granados Chantal Durette Sébastien Lemieux Pierre Thibault Claude Perreault |
author_sort |
Céline M. Laumont |
title |
Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames |
title_short |
Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames |
title_full |
Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames |
title_fullStr |
Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames |
title_full_unstemmed |
Global proteogenomic analysis of human MHC class I-associated peptides derived from non-canonical reading frames |
title_sort |
global proteogenomic analysis of human mhc class i-associated peptides derived from non-canonical reading frames |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2016-01-01 |
description |
Cryptic translation of the 'non-coding' genome is increasingly recognised, however its biological significance remains unclear. Laumont et al.employ proteogenomic techniques to map the human immunoproteome, and find that approximately 10% of MHC class I-associated peptides are cryptic. |
url |
https://doi.org/10.1038/ncomms10238 |
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