The eukaryotic linear motif resource - 2018 update
Short linear motifs (SLiMs) are protein binding modules that play major roles in almost all cellular processes. SLiMs are short, often highly degenerate, difficult to characterize and hard to detect. The eukaryotic linear motif (ELM) resource (elm.eu.org) is dedicated to SLiMs, consisting of a manua...
Guardado en:
Publicado: |
2018
|
---|---|
Materias: | |
Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03051048_v46_nD1_pD428_Gouw http://hdl.handle.net/20.500.12110/paper_03051048_v46_nD1_pD428_Gouw |
Aporte de: |
id |
paper:paper_03051048_v46_nD1_pD428_Gouw |
---|---|
record_format |
dspace |
spelling |
paper:paper_03051048_v46_nD1_pD428_Gouw2023-06-08T15:30:33Z The eukaryotic linear motif resource - 2018 update protein kinase protein kinase kinome unclassified drug amino acid sequence application programmatic interface Article cell cycle enzyme structure eukaryote eukaryotic linear motif factual database human nonhuman priority journal protein binding protein database protein motif short linear motif Short linear motifs (SLiMs) are protein binding modules that play major roles in almost all cellular processes. SLiMs are short, often highly degenerate, difficult to characterize and hard to detect. The eukaryotic linear motif (ELM) resource (elm.eu.org) is dedicated to SLiMs, consisting of a manually curated database of over 275 motif classes and over 3000 motif instances, and a pipeline to discover candidate SLiMs in protein sequences. For 15 years, ELM has been one of the major resources for motif research. In this database update, we present the latest additions to the database including 32 new motif classes, and new features including Uniprot and Reactome integration. Finally, to help provide cellular context, we present some biological insights about SLiMs in the cell cycle, as targets for bacterial pathogenicity and their functionality in the human kinome. © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03051048_v46_nD1_pD428_Gouw http://hdl.handle.net/20.500.12110/paper_03051048_v46_nD1_pD428_Gouw |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
protein kinase protein kinase kinome unclassified drug amino acid sequence application programmatic interface Article cell cycle enzyme structure eukaryote eukaryotic linear motif factual database human nonhuman priority journal protein binding protein database protein motif short linear motif |
spellingShingle |
protein kinase protein kinase kinome unclassified drug amino acid sequence application programmatic interface Article cell cycle enzyme structure eukaryote eukaryotic linear motif factual database human nonhuman priority journal protein binding protein database protein motif short linear motif The eukaryotic linear motif resource - 2018 update |
topic_facet |
protein kinase protein kinase kinome unclassified drug amino acid sequence application programmatic interface Article cell cycle enzyme structure eukaryote eukaryotic linear motif factual database human nonhuman priority journal protein binding protein database protein motif short linear motif |
description |
Short linear motifs (SLiMs) are protein binding modules that play major roles in almost all cellular processes. SLiMs are short, often highly degenerate, difficult to characterize and hard to detect. The eukaryotic linear motif (ELM) resource (elm.eu.org) is dedicated to SLiMs, consisting of a manually curated database of over 275 motif classes and over 3000 motif instances, and a pipeline to discover candidate SLiMs in protein sequences. For 15 years, ELM has been one of the major resources for motif research. In this database update, we present the latest additions to the database including 32 new motif classes, and new features including Uniprot and Reactome integration. Finally, to help provide cellular context, we present some biological insights about SLiMs in the cell cycle, as targets for bacterial pathogenicity and their functionality in the human kinome. © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. |
title |
The eukaryotic linear motif resource - 2018 update |
title_short |
The eukaryotic linear motif resource - 2018 update |
title_full |
The eukaryotic linear motif resource - 2018 update |
title_fullStr |
The eukaryotic linear motif resource - 2018 update |
title_full_unstemmed |
The eukaryotic linear motif resource - 2018 update |
title_sort |
eukaryotic linear motif resource - 2018 update |
publishDate |
2018 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03051048_v46_nD1_pD428_Gouw http://hdl.handle.net/20.500.12110/paper_03051048_v46_nD1_pD428_Gouw |
_version_ |
1768543560922038272 |