Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1999-1-22
pubmed:abstractText
We report here that the expression of virtually all proposed c-Myc target genes is unchanged in cells containing a homozygous null deletion of c-myc. Two noteworthy exceptions are the gene cad, which has reduced log phase expression and serum induction in c-myc null cells, and the growth arrest gene gadd45, which is derepressed by c-myc knockout. Thus, cad and gadd45 are the only proposed targets of c-Myc that may contribute to the dramatic slow growth phenotype of c-myc null cells. Our results demonstrate that a loss-of-function approach is critical for the evaluation of potential c-Myc target genes.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-1340466, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-1406956, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-1497324, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-1989881, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-2201910, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-2444981, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-2662015, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-3115591, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-3885045, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-6088986, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-762107, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-7667636, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-7739536, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-7862146, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-7905000, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8035827, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8127680, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8139541, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8297793, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8356088, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8386297, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8494784, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8657582, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8700224, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8700517, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8712067, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8756633, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8861962, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-8972190, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9000049, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9111322, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9178906, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9190899, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9192621, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9271375, http://linkedlifedata.com/resource/pubmed/commentcorrection/9869632-9342182
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate Carbamoyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/CAD trifunctional enzyme, http://linkedlifedata.com/resource/pubmed/chemical/Carbamoyl-Phosphate Synthase..., http://linkedlifedata.com/resource/pubmed/chemical/Cdc25a protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Dihydroorotase, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4E, http://linkedlifedata.com/resource/pubmed/chemical/GADD45 protein, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc, http://linkedlifedata.com/resource/pubmed/chemical/cdc25 Phosphatases
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3797-802
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9869632-Animals, pubmed-meshheading:9869632-Proteins, pubmed-meshheading:9869632-Rats, pubmed-meshheading:9869632-Cell Division, pubmed-meshheading:9869632-Homozygote, pubmed-meshheading:9869632-Phenotype, pubmed-meshheading:9869632-Cell Line, pubmed-meshheading:9869632-Cell Cycle, pubmed-meshheading:9869632-Aspartate Carbamoyltransferase, pubmed-meshheading:9869632-Gene Expression Regulation, pubmed-meshheading:9869632-Peptide Initiation Factors, pubmed-meshheading:9869632-Multienzyme Complexes, pubmed-meshheading:9869632-Ornithine Decarboxylase, pubmed-meshheading:9869632-Down-Regulation, pubmed-meshheading:9869632-Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing), pubmed-meshheading:9869632-Dihydroorotase, pubmed-meshheading:9869632-Intracellular Signaling Peptides and Proteins
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