Source:http://linkedlifedata.com/resource/pubmed/id/11943536
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2002-4-10
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pubmed:abstractText |
This article describes a novel domain, BSD, that is present in basal transcription factors, synapse-associated proteins and several hypothetical proteins. It occurs in a variety of species ranging from primal protozoan to human. The BSD domain is characterized by three predicted alpha helices, which probably form a three-helical bundle, as well as by conserved tryptophan and phenylalanine residues, located at the C terminus of the domain.
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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 |
Apr
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pubmed:issn |
0968-0004
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
168-70
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:11943536-Amino Acid Motifs,
pubmed-meshheading:11943536-Amino Acid Sequence,
pubmed-meshheading:11943536-Animals,
pubmed-meshheading:11943536-Humans,
pubmed-meshheading:11943536-Molecular Sequence Data,
pubmed-meshheading:11943536-Neuropeptides,
pubmed-meshheading:11943536-Sequence Homology, Amino Acid,
pubmed-meshheading:11943536-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
BSD: a novel domain in transcription factors and synapse-associated proteins.
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pubmed:affiliation |
EMBL, 69012 Heidelberg, Meyerhofstr. 1, and Max-Delbrueck-Centrum, Berlin, Germany. doerks@embl.heidelberg.de
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pubmed:publicationType |
Journal Article
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