Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2002-7-31
pubmed:abstractText
Temperature sensitive mutations in host cell factor 1 (HCF-1) arrest cells in the middle of the G1 phase of the cycle. We have shown that the highly conserved C-terminal WYF domain of HCF-1 protein interacts with the MYND domain of the PDCD2 protein. This inter-action is conserved between human HCF-1 and HCF-2 and the C. elegans HCF. Overexpression of PDCD2, which interacts with the N-CoR/mSin3A corepressor complexes, suppresses cotransfected HCF-1 complement-ation of a temperature lesion in the endogenous HCF-1 protein. Overexpression of domains of either PDCD2 or HCF-1, which should interfere with interactions between these two proteins, enhances the complementation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HCFC1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Host Cell Factor C1, http://linkedlifedata.com/resource/pubmed/chemical/NCOR1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Co-Repressor 1, http://linkedlifedata.com/resource/pubmed/chemical/PDCD2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/hcf-1 protein, C elegans
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5245-54
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12149646-Amino Acid Sequence, pubmed-meshheading:12149646-Animals, pubmed-meshheading:12149646-Apoptosis Regulatory Proteins, pubmed-meshheading:12149646-Binding Sites, pubmed-meshheading:12149646-Caenorhabditis elegans, pubmed-meshheading:12149646-Caenorhabditis elegans Proteins, pubmed-meshheading:12149646-Cells, Cultured, pubmed-meshheading:12149646-Gene Deletion, pubmed-meshheading:12149646-Genetic Complementation Test, pubmed-meshheading:12149646-Host Cell Factor C1, pubmed-meshheading:12149646-Humans, pubmed-meshheading:12149646-Molecular Sequence Data, pubmed-meshheading:12149646-Nuclear Proteins, pubmed-meshheading:12149646-Nuclear Receptor Co-Repressor 1, pubmed-meshheading:12149646-Precipitin Tests, pubmed-meshheading:12149646-Protein Structure, Tertiary, pubmed-meshheading:12149646-Proteins, pubmed-meshheading:12149646-Repressor Proteins, pubmed-meshheading:12149646-Saccharomyces cerevisiae, pubmed-meshheading:12149646-Sequence Homology, Amino Acid, pubmed-meshheading:12149646-Transcription Factors, pubmed-meshheading:12149646-Two-Hybrid System Techniques
pubmed:year
2002
pubmed:articleTitle
PDCD2 is a negative regulator of HCF-1 (C1).
pubmed:affiliation
Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, MA 02139-4307, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.