Source:http://linkedlifedata.com/resource/pubmed/id/18414490
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2008-4-23
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pubmed:abstractText |
Helicases and nucleic acid translocases are motor proteins that have essential roles in nearly all aspects of nucleic acid metabolism, ranging from DNA replication to chromatin remodelling. Fuelled by the binding and hydrolysis of nucleoside triphosphates, helicases move along nucleic acid filaments and separate double-stranded DNA into their complementary single strands. Recent evidence indicates that the ability to simply translocate along single-stranded DNA is, in many cases, insufficient for helicase activity. For some of these enzymes, self assembly and/or interactions with accessory proteins seem to regulate their translocase and helicase activities.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1471-0080
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
391-401
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pubmed:meshHeading |
pubmed-meshheading:18414490-Adenosine Triphosphatases,
pubmed-meshheading:18414490-Adenosine Triphosphate,
pubmed-meshheading:18414490-DNA, Single-Stranded,
pubmed-meshheading:18414490-DNA Helicases,
pubmed-meshheading:18414490-Nucleic Acid Conformation,
pubmed-meshheading:18414490-Protein Conformation,
pubmed-meshheading:18414490-Transferases
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pubmed:year |
2008
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pubmed:articleTitle |
Non-hexameric DNA helicases and translocases: mechanisms and regulation.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, Missouri 63110, USA. lohman@biochem.wustl.edu
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pubmed:publicationType |
Journal Article,
Review,
Research Support, N.I.H., Extramural
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