Linked Life Data

1558752

Source:http://linkedlifedata.com/resource/pubmed/id/1558752

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-5-11
pubmed:abstractText
The sequences of a large number of actin-binding proteins have been compared. These findings, together with the results of protein-chemical analysis, peptide synthesis and site-directed and deletion mutagenesis, have led to the assignment of actin-binding sites. Within these segments, small actin-binding motifs have been delineated. Most actin-binding proteins interact with actin subdomain-1 but our analyses reveal neither primary nor secondary structure homology among these proteins, suggesting that actin binding does not follow simple structural principles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0955-0674
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Structural relationships of actin-binding proteins.
pubmed:affiliation
Laboratory of Physiological Chemistry, University of Ghent, Belgium.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't