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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1988-3-10
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pubmed:databankReference | |
pubmed:abstractText |
We have determined the nucleotide sequence and transforming activity of the human L-myc gene and a processed L-myc pseudogene (L-myc psi). We demonstrate by cotransformation assays that a 10.6-kb EcoRI fragment derived from a human placental library contains a complete and functional L-myc gene including transcriptional regulatory sequences sufficient for expression in rat embryo fibroblasts. Organization of the L-myc gene was determined by comparing its sequence to those of the L-myc psi gene and an L-myc cDNA clone derived from a human small cell lung carcinoma. Our results show that L-myc has a three-exon organization similar to that of the c-myc and N-myc genes. The putative L-myc gene product consists of 364 amino acids and contains five of the seven homology regions highly conserved between c-myc and N-myc. These conserved regions are located along the entire length of the putative L-myc protein and are interspersed among nonconserved regions. While the putative L-myc gene product is of a smaller size when compared to the c- and N-myc proteins, the relative positions of certain conserved residues occur in corresponding locations along the peptide backbone of the three proteins. In addition, comparison of the human and murine L-myc gene sequences indicate that the relatively large 5' and 3' untranslated regions are evolutionarily conserved, but that these sequences are totally divergent between the L-, c-, and N-myc genes. Finally, we demonstrate that, like the N- and c-myc genes, the L-myc gene can cooperate with a mutant Ha-ras gene to cause malignant transformation of rat embryo fibroblasts in culture. Our analyses clearly prove that L-myc represents a functional member of the myc oncogene family and further delineate structural features that may be important for the common and divergent functions of the members of this gene family.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0890-9369
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1311-26
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3322939-Amino Acid Sequence,
pubmed-meshheading:3322939-Animals,
pubmed-meshheading:3322939-Base Sequence,
pubmed-meshheading:3322939-Cell Transformation, Neoplastic,
pubmed-meshheading:3322939-Cells, Cultured,
pubmed-meshheading:3322939-Genes, ras,
pubmed-meshheading:3322939-Humans,
pubmed-meshheading:3322939-Molecular Sequence Data,
pubmed-meshheading:3322939-Multigene Family,
pubmed-meshheading:3322939-Proto-Oncogene Proteins,
pubmed-meshheading:3322939-Proto-Oncogenes,
pubmed-meshheading:3322939-Pseudogenes,
pubmed-meshheading:3322939-Rats
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pubmed:year |
1987
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pubmed:articleTitle |
The human myc gene family: structure and activity of L-myc and an L-myc pseudogene.
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pubmed:affiliation |
Howard Hughes Medical Institute, New York.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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