Source:http://linkedlifedata.com/resource/pubmed/id/19888688
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2009-11-5
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| pubmed:abstractText |
The steroidogenic acute regulatory-related lipid transfer (START) domain is found in both eukaryotes and prokaryotes, with putative functions including signal transduction, transcriptional regulation, GTPase activation and thioester hydrolysis. Here we report the near complete (1)H, (15)N and (13)C backbone and side chain NMR resonance assignments for the Bacillus subtilis START domain protein yndB.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1874-270X
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
3
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
191-4
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| pubmed:meshHeading |
pubmed-meshheading:19888688-Amino Acid Sequence,
pubmed-meshheading:19888688-Bacillus subtilis,
pubmed-meshheading:19888688-Bacterial Proteins,
pubmed-meshheading:19888688-Molecular Sequence Data,
pubmed-meshheading:19888688-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:19888688-Protein Structure, Tertiary
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| pubmed:year |
2009
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| pubmed:articleTitle |
(1)H, (13)C, and (15)N NMR assignments for the Bacillus subtilis yndB START domain.
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| pubmed:affiliation |
Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA. mercierka@niehs.nih.gov
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural,
Research Support, N.I.H., Intramural
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