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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-6-30
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pubmed:abstractText |
Netropsin suppressed the increase of intracellular proteolytic activity when added to B. megaterium incubated in a sporulation medium. The inhibited enzyme was a Ca(2+)-dependent serine proteinase. Sporulation and protein turnover in later sporulation phases were inhibited as well. Different concentrations of netropsin affected various aspects of protein catabolism differently.
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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:issn |
0015-5632
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8388845-Bacillus megaterium,
pubmed-meshheading:8388845-Calcium,
pubmed-meshheading:8388845-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8388845-Morphogenesis,
pubmed-meshheading:8388845-Netropsin,
pubmed-meshheading:8388845-Serine Endopeptidases,
pubmed-meshheading:8388845-Spores, Bacterial
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pubmed:year |
1993
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pubmed:articleTitle |
Netropsin inhibits the increase of intracellular Ca(2+)-dependent serine proteinase activity in sporulating Bacillus megaterium.
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pubmed:affiliation |
Department of Cell and Molecular Microbiology, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague.
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pubmed:publicationType |
Journal Article
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