rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
11
|
pubmed:dateCreated |
2002-10-22
|
pubmed:abstractText |
Human Rad51 protein (HsRad51) is a homologue of Escherichia coli RecA protein, and involved in homologous recombination. These eukaryotic and bacterial proteins catalyse strand exchange between two homologous DNA molecules, each forming a complex with single-stranded DNA (ssDNA) and ATP as the initial step. Both proteins hydrolyse ATP; however, the role of ATP hydrolysis appears to vary between the two proteins.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
1356-9597
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
7
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1125-34
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
|
pubmed:year |
2002
|
pubmed:articleTitle |
ADP stabilizes the human Rad51-single stranded DNA complex and promotes its DNA annealing activity.
|
pubmed:affiliation |
Department of Physical Chemistry, Chalmers University of Technology, SE 412 96, Gothenburg, Sweden.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|