Source:http://linkedlifedata.com/resource/pubmed/id/11425553
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
2001-6-26
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pubmed:abstractText |
alpha-Ketohydroxamates were synthesized as bioisosteres of alpha-ketoamides. The alpha-ketohydroxamates were generally more potent than the corresponding alpha-ketoamides. The potency of the compounds suggests that hydrogen bonding and steric bulk of substituents on the nitrogen atom of the ketoamide moiety influence calpain inhibition.
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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 |
Jul
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1753-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
2001
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pubmed:articleTitle |
Significance of hydrogen bonding at the S(1)' subsite of calpain I.
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pubmed:affiliation |
Department of Pharmaceutical Sciences, The University of Tennessee, Johnson Bldg. Room 327E, 847Monroe Avenue, TN 38163, Memphis, USA. idonkor@utmem.edu
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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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