rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
2011-9-15
|
pubmed:abstractText |
The macrophage infectivity potentiator (MIP) protein is a major virulence factor of Legionella pneumophila, the causative agent of Legionnaires' disease. MIP belongs to the FK506-binding proteins (FKBP) and is necessary for optimal intracellular survival and lung tissue dissemination of L. pneumophila. We aimed to identify new small-molecule inhibitors of MIP by starting from known FKBP12 ligands. Computational analysis, synthesis, and biological testing of pipecolic acid derivatives revealed a promising scaffold for new MIP inhibitors.
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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
|
pubmed:month |
Jan
|
pubmed:issn |
1520-4804
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
13
|
pubmed:volume |
54
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
277-83
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pubmed:meshHeading |
pubmed-meshheading:21142106-Animals,
pubmed-meshheading:21142106-Bacterial Proteins,
pubmed-meshheading:21142106-Binding Sites,
pubmed-meshheading:21142106-Cell Line,
pubmed-meshheading:21142106-Colony Count, Microbial,
pubmed-meshheading:21142106-Guinea Pigs,
pubmed-meshheading:21142106-Legionella pneumophila,
pubmed-meshheading:21142106-Legionnaires' Disease,
pubmed-meshheading:21142106-Magnetic Resonance Spectroscopy,
pubmed-meshheading:21142106-Models, Molecular,
pubmed-meshheading:21142106-Peptidylprolyl Isomerase,
pubmed-meshheading:21142106-Pipecolic Acids,
pubmed-meshheading:21142106-Stereoisomerism,
pubmed-meshheading:21142106-Structure-Activity Relationship,
pubmed-meshheading:21142106-Tacrolimus Binding Protein 1A
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pubmed:year |
2011
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pubmed:articleTitle |
Pipecolic acid derivatives as small-molecule inhibitors of the Legionella MIP protein.
|
pubmed:affiliation |
Institute of Pharmacy and Food Chemistry, University of Wu?rzburg, Wu?rzburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|