Linked Life Data

9708889

Source:http://linkedlifedata.com/resource/pubmed/id/9708889

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-9-8
pubmed:abstractText
A sequence motif of about 100 amino acids, termed the 'calponin homology domain' has been suggested to confer actin binding to a variety of cytoskeletal and signalling molecules. Here we analyse and compare the sequences of all calponin homology domain-containing proteins identified to date. We propose that single calponin homology domains do not confer actin-binding per se and that the actin-binding motifs of cross-linking proteins, which comprise two disparate calponin homology domains, represent a unique protein module.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
431
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
134-7
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
CH domains revisited.
pubmed:affiliation
Institute of Molecular Biology, Austrian Academy of Sciences, Department of Cell Biology, Salzburg.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't