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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-8-16
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pubmed:abstractText |
Spermidine regulation of protein synthesis (stimulation at low concentrations and inhibition at high concentrations) was studied using a mRNA with a GC-rich 5'-untranslated region. It was found that the initiation complex formation of mRNA, Met-tRNAi, and 40 S ribosomal subunits was regulated by spermidine. The inhibition of initiation complex formation at high spermidine concentrations was greater with 80 S ribosomes than with 40S ribosomal subunits. This was partially explained by the spermidine inhibition of initiation factor-dependent RNA helicase activity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosylmethionine Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Met,
http://linkedlifedata.com/resource/pubmed/chemical/Spermidine,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine Kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
223
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
544-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8687432-Actins,
pubmed-meshheading:8687432-Adenosylmethionine Decarboxylase,
pubmed-meshheading:8687432-Animals,
pubmed-meshheading:8687432-Base Composition,
pubmed-meshheading:8687432-Base Sequence,
pubmed-meshheading:8687432-Cell-Free System,
pubmed-meshheading:8687432-Molecular Sequence Data,
pubmed-meshheading:8687432-Oligodeoxyribonucleotides,
pubmed-meshheading:8687432-Open Reading Frames,
pubmed-meshheading:8687432-Ornithine Decarboxylase,
pubmed-meshheading:8687432-Peptide Chain Initiation, Translational,
pubmed-meshheading:8687432-Protein Biosynthesis,
pubmed-meshheading:8687432-RNA, Messenger,
pubmed-meshheading:8687432-RNA, Transfer, Met,
pubmed-meshheading:8687432-Rabbits,
pubmed-meshheading:8687432-Reticulocytes,
pubmed-meshheading:8687432-Ribosomes,
pubmed-meshheading:8687432-Spermidine,
pubmed-meshheading:8687432-Thymidine Kinase
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pubmed:year |
1996
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pubmed:articleTitle |
Spermidine regulation of protein synthesis at the level of initiation complex formation of Met-tRNAi, mRNA and ribosomes.
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pubmed:affiliation |
Faculty of Pharmaceutical Sciences, Chiba University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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