OpenProt 2.0 builds a path to the functional ...
Document type :
Article dans une revue scientifique: Article original
DOI :
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Title :
OpenProt 2.0 builds a path to the functional characterization of alternative proteins.
Author(s) :
Leblanc, S. [Auteur]
Yala, F. [Auteur]
Provencher, N. [Auteur]
Lucier, J. F. [Auteur]
Levesque, M. [Auteur]
Lapointe, X. [Auteur]
Jacques, J. F. [Auteur]
FOURNIER, Isabelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U 1192 [PRISM]
Salzet, Michel [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Ouangraoua, A. [Auteur]
Scott, M. S. [Auteur]
Boisvert, F. M. [Auteur]
Brunet, M. A. [Auteur]
Roucou, X. [Auteur]
Yala, F. [Auteur]
Provencher, N. [Auteur]
Lucier, J. F. [Auteur]
Levesque, M. [Auteur]
Lapointe, X. [Auteur]
Jacques, J. F. [Auteur]
FOURNIER, Isabelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U 1192 [PRISM]
Salzet, Michel [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Ouangraoua, A. [Auteur]
Scott, M. S. [Auteur]
Boisvert, F. M. [Auteur]
Brunet, M. A. [Auteur]
Roucou, X. [Auteur]
Journal title :
Nucleic Acids Research
Abbreviated title :
Nucleic Acids Res
Publication date :
2023-11-17
ISSN :
1362-4962
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
The OpenProt proteogenomic resource (https://www.openprot.org/) provides users with a complete and freely accessible set of non-canonical
or alternative open reading frames (AltORFs) within the transcriptome of various ...
Show more >The OpenProt proteogenomic resource (https://www.openprot.org/) provides users with a complete and freely accessible set of non-canonical or alternative open reading frames (AltORFs) within the transcriptome of various species, as well as functional annotations of the corresponding protein sequences not found in standard databases. Enhancements in this update are largely the result of user feedback and include the prediction of structure, subcellular localization, and intrinsic disorder, using cutting-edge algorithms based on machine learning techniques. The mass spectrometry pipeline now integrates a machine learning-based peptide rescoring method to improve peptide identification. We continue to help users explore this cryptic proteome by providing OpenCustomDB, a tool that enables users to build their own customized protein databases, and OpenVar, a genomic annotator including genetic variants within AltORFs and protein sequences. A new interface improves the visualization of all functional annotations, including a spectral viewer and the prediction of multicoding genes. All data on OpenProt are freely available and downloadable. Overall, OpenProt continues to establish itself as an important resource for the exploration and study of new proteins.Show less >
Show more >The OpenProt proteogenomic resource (https://www.openprot.org/) provides users with a complete and freely accessible set of non-canonical or alternative open reading frames (AltORFs) within the transcriptome of various species, as well as functional annotations of the corresponding protein sequences not found in standard databases. Enhancements in this update are largely the result of user feedback and include the prediction of structure, subcellular localization, and intrinsic disorder, using cutting-edge algorithms based on machine learning techniques. The mass spectrometry pipeline now integrates a machine learning-based peptide rescoring method to improve peptide identification. We continue to help users explore this cryptic proteome by providing OpenCustomDB, a tool that enables users to build their own customized protein databases, and OpenVar, a genomic annotator including genetic variants within AltORFs and protein sequences. A new interface improves the visualization of all functional annotations, including a spectral viewer and the prediction of multicoding genes. All data on OpenProt are freely available and downloadable. Overall, OpenProt continues to establish itself as an important resource for the exploration and study of new proteins.Show less >
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
Inserm
CHU Lille
Inserm
CHU Lille
Submission date :
2023-12-13T03:35:43Z
2024-01-29T11:35:26Z
2024-01-29T11:35:26Z
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