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...

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Publicado: 2018
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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
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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
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