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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6477
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pubmed:dateCreated |
1994-6-14
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pubmed:databankReference |
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pubmed:abstractText |
In the prokaryotic two-component signal transduction systems, recognition of an environmental stimulus by a sensor molecule results in the activation of its histidine kinase domain and phosphorylation of a histidine residue within that domain. This phosphate group is then transferred to an aspartate residue in the receiver domain of a cognate response regulator molecule, resulting in the activation of its output function. Although a few eukaryotic proteins were identified recently that show sequence similarity to the prokaryotic sensors or response regulators, it has not been clear whether they constituted a part of a 'two-component' system. Here we describe a two-component system in Saccharomyces cerevisiae that regulates an osmosensing MAP kinase cascade.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/PTC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/SLN1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase 2C,
http://linkedlifedata.com/resource/pubmed/chemical/protein-histidine kinase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
369
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
242-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8183345-Amino Acid Sequence,
pubmed-meshheading:8183345-Fungal Proteins,
pubmed-meshheading:8183345-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8183345-Molecular Sequence Data,
pubmed-meshheading:8183345-Mutation,
pubmed-meshheading:8183345-Phosphoprotein Phosphatases,
pubmed-meshheading:8183345-Phosphorylation,
pubmed-meshheading:8183345-Protein Kinases,
pubmed-meshheading:8183345-Protein Phosphatase 2,
pubmed-meshheading:8183345-Protein Tyrosine Phosphatases,
pubmed-meshheading:8183345-Saccharomyces cerevisiae,
pubmed-meshheading:8183345-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8183345-Signal Transduction,
pubmed-meshheading:8183345-Suppression, Genetic
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pubmed:year |
1994
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pubmed:articleTitle |
A two-component system that regulates an osmosensing MAP kinase cascade in yeast.
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pubmed:affiliation |
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, Massachusetts.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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