Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2000-5-31
pubmed:abstractText
Werner syndrome (WS) is the hallmark premature aging disorder in which affected humans appear older than their chronological age. The protein WRNp, defective in WS, has helicase function, DNA-dependent ATPase, and exonuclease activity. Although WRNp functions in nucleic acid metabolism, there is little or no information about the pathways or protein interactions in which it participates. Here we identify Ku70 and Ku86 as proteins that interact with WRNp. Although Ku proteins had no effect on ATPase or helicase activity, they strongly stimulated specific exonuclease activity. These results suggest that WRNp and the Ku complex participate in a common DNA metabolic pathway.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10069804, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10215620, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10220139, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10319867, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10325426, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10373438, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10377944, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10397753, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10446247, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10485901, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-10608841, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-1327851, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-2459043, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-6139375, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-7507567, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-7957065, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-8602509, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9229111, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9288107, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9380512, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9390689, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9430651, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9477961, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9697700, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9716395, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9771700, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9789047, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9852073, http://linkedlifedata.com/resource/pubmed/commentcorrection/10783163-9852074
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
907-12
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:10783163-Adenosine Triphosphatases, pubmed-meshheading:10783163-Animals, pubmed-meshheading:10783163-Antigens, Nuclear, pubmed-meshheading:10783163-Base Sequence, pubmed-meshheading:10783163-Blotting, Western, pubmed-meshheading:10783163-Cell Line, pubmed-meshheading:10783163-Cell Nucleus, pubmed-meshheading:10783163-Chromatography, Affinity, pubmed-meshheading:10783163-DNA Helicases, pubmed-meshheading:10783163-DNA-Binding Proteins, pubmed-meshheading:10783163-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10783163-Enzyme Activation, pubmed-meshheading:10783163-Exodeoxyribonucleases, pubmed-meshheading:10783163-Exonucleases, pubmed-meshheading:10783163-Humans, pubmed-meshheading:10783163-Molecular Sequence Data, pubmed-meshheading:10783163-Nuclear Proteins, pubmed-meshheading:10783163-Precipitin Tests, pubmed-meshheading:10783163-Protein Binding, pubmed-meshheading:10783163-RecQ Helicases, pubmed-meshheading:10783163-Spectrometry, Mass, Matrix-Assisted Laser...
pubmed:year
2000
pubmed:articleTitle
Ku complex interacts with and stimulates the Werner protein.
pubmed:affiliation
Laboratory of Molecular Genetics, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't