9033586

Source:http://linkedlifedata.com/resource/pubmed/id/9033586

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0678594, umls-concept:C0920283, umls-concept:C1260969, umls-concept:C1334043
pubmed:issue	2
pubmed:dateCreated	1997-3-20
pubmed:abstractText	The RecA protein forms a hexameric ring that is similar to the core of the F1-ATPase. Several lines of evidence suggest that this hexamer may be a structural homologue of ring helicases.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9421566
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases, http://linkedlifedata.com/resource/pubmed/chemical/Rec A Recombinases
pubmed:status	MEDLINE
pubmed:month	Feb
pubmed:issn	1072-8368
pubmed:author	pubmed-author:EgelmanE HEH, pubmed-author:YuXX
pubmed:issnType	Print
pubmed:volume	4
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	101-4
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:9033586-DNA Helicases, pubmed-meshheading:9033586-Escherichia coli, pubmed-meshheading:9033586-Macromolecular Substances, pubmed-meshheading:9033586-Microscopy, Electron, pubmed-meshheading:9033586-Models, Structural, pubmed-meshheading:9033586-Protein Folding, pubmed-meshheading:9033586-Protein Structure, Secondary, pubmed-meshheading:9033586-Proton-Translocating ATPases, pubmed-meshheading:9033586-Rec A Recombinases, pubmed-meshheading:9033586-Software
pubmed:year	1997
pubmed:articleTitle	The RecA hexamer is a structural homologue of ring helicases.
pubmed:publicationType	Letter, Comparative Study, Research Support, U.S. Gov't, P.H.S.