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MAP kinase phosphatases
Mitogen-activated protein MAP kinases are key signal-transducing enzymes that are activated by a wide range of extracellular stimuli. They are responsible for the induction of a number of cellular responses, such as changes in gene expression, proliferation, differentiation, cell cycle arrest and ap...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139386/ https://www.ncbi.nlm.nih.gov/pubmed/12184814 |
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author | Theodosiou, Aspasia Ashworth, Alan |
author_facet | Theodosiou, Aspasia Ashworth, Alan |
author_sort | Theodosiou, Aspasia |
collection | PubMed |
description | Mitogen-activated protein MAP kinases are key signal-transducing enzymes that are activated by a wide range of extracellular stimuli. They are responsible for the induction of a number of cellular responses, such as changes in gene expression, proliferation, differentiation, cell cycle arrest and apoptosis. Although regulation of MAP kinases by a phosphorylation cascade has long been recognized as significant, their inactivation through the action of specific phosphatases has been less studied. An emerging family of structurally distinct dual-specificity serine, threonine and tyrosine phosphatases that act on MAP kinases consists of ten members in mammals, and members have been found in animals, plants and yeast. Three subgroups have been identified that differ in exon structure, sequence and substrate specificity. |
format | Text |
id | pubmed-139386 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-1393862003-03-04 MAP kinase phosphatases Theodosiou, Aspasia Ashworth, Alan Genome Biol Protein Family Review Mitogen-activated protein MAP kinases are key signal-transducing enzymes that are activated by a wide range of extracellular stimuli. They are responsible for the induction of a number of cellular responses, such as changes in gene expression, proliferation, differentiation, cell cycle arrest and apoptosis. Although regulation of MAP kinases by a phosphorylation cascade has long been recognized as significant, their inactivation through the action of specific phosphatases has been less studied. An emerging family of structurally distinct dual-specificity serine, threonine and tyrosine phosphatases that act on MAP kinases consists of ten members in mammals, and members have been found in animals, plants and yeast. Three subgroups have been identified that differ in exon structure, sequence and substrate specificity. BioMed Central 2002 2002-06-26 /pmc/articles/PMC139386/ /pubmed/12184814 Text en Copyright © 2002 BioMed Central Ltd |
spellingShingle | Protein Family Review Theodosiou, Aspasia Ashworth, Alan MAP kinase phosphatases |
title | MAP kinase phosphatases |
title_full | MAP kinase phosphatases |
title_fullStr | MAP kinase phosphatases |
title_full_unstemmed | MAP kinase phosphatases |
title_short | MAP kinase phosphatases |
title_sort | map kinase phosphatases |
topic | Protein Family Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139386/ https://www.ncbi.nlm.nih.gov/pubmed/12184814 |
work_keys_str_mv | AT theodosiouaspasia mapkinasephosphatases AT ashworthalan mapkinasephosphatases |