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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1983-10-8
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pubmed:abstractText |
Transglutaminase may be an important intracellular regulator of protein function through its ability to catalyze the calcium-dependent covalent linkage of primary amines to glutamine residues in peptide linkage with the generation of ammonia. This study provides further evidence that a major alteration in tumor cells is the marked decline in the expression of transglutaminase activity. This may alter its known protein cross-linking activity and favor lack of differentiation and proliferation.
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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 |
Aug
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pubmed:issn |
0024-3205
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
555-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6136887-Acyltransferases,
pubmed-meshheading:6136887-Animals,
pubmed-meshheading:6136887-Kinetics,
pubmed-meshheading:6136887-Male,
pubmed-meshheading:6136887-Putrescine,
pubmed-meshheading:6136887-Rats,
pubmed-meshheading:6136887-Rats, Inbred Strains,
pubmed-meshheading:6136887-Sarcoma, Yoshida,
pubmed-meshheading:6136887-Transglutaminases
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pubmed:year |
1983
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pubmed:articleTitle |
Transglutaminase activity in Yoshida ascites tumor cells.
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pubmed:publicationType |
Journal Article
|