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rdf:type |
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|
lifeskim:mentions |
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pubmed:issue |
6195
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pubmed:dateCreated |
1988-12-19
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pubmed:abstractText |
A cascade of protein phosphorylation, initiated by autophosphorylation of the CheA protein, may be important in the signal transduction pathway of bacterial chemotaxis. A proteolytic fragment of CheA cannot autophosphorylate, but can still transfer phosphate to proteins that generate excitation and adaptation signals. The site of CheA phosphorylation is His 48; mutants altered at this position are non-chemotactic. Similar mechanisms of transient protein phosphorylation and phosphoryl group transfer seem to be involved in processing sensory data and in activating specific gene expression.
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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 |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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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 |
10
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pubmed:volume |
336
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
139-43
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3185734-Amino Acid Sequence,
pubmed-meshheading:3185734-Bacterial Proteins,
pubmed-meshheading:3185734-Chemotaxis,
pubmed-meshheading:3185734-Chromatography, High Pressure Liquid,
pubmed-meshheading:3185734-Histidine,
pubmed-meshheading:3185734-Membrane Proteins,
pubmed-meshheading:3185734-Mutation,
pubmed-meshheading:3185734-Phosphates,
pubmed-meshheading:3185734-Phosphorylation,
pubmed-meshheading:3185734-Signal Transduction
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pubmed:year |
1988
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pubmed:articleTitle |
Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis.
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pubmed:affiliation |
Division of Biology, California Institute of Technology, Pasadena 91125.
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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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