rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2004-5-10
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pubmed:abstractText |
Riboflavin synthase catalyzes the transformation of 6,7-dimethyl-8-ribityllumazine into riboflavin in the last step of the riboflavin biosynthetic pathway. Gram-negative bacteria and certain yeasts are unable to incorporate riboflavin from the environment and are therefore absolutely dependent on endogenous synthesis of the vitamin. Riboflavin synthase is therefore a potential target for the development of antiinfective drugs.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11278450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11377200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11399071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11404482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11488927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-116904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11856310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-11925213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-12377123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-1466913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-2023259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-2106516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-3986187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-4552986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-4657965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-5417397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-5439976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-5946633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-623648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-6766130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-6786884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-7304986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-7631418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-7947939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-8011629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-8703935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14690539-9022701
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1471-2091
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pubmed:author |
pubmed-author:BacherAdelbertA,
pubmed-author:CushmanMarkM,
pubmed-author:EisenreichWolfgangW,
pubmed-author:FeichtRichardR,
pubmed-author:FischerMarkusM,
pubmed-author:GerhardtStefanS,
pubmed-author:HuberRobertR,
pubmed-author:IllarionovBorisB,
pubmed-author:KemterKristinaK,
pubmed-author:RichterGeraldG,
pubmed-author:SchottAnn-KathrinAK,
pubmed-author:SteinbacherStefanS
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14690539-Amino Acid Sequence,
pubmed-meshheading:14690539-Fluorine,
pubmed-meshheading:14690539-Molecular Sequence Data,
pubmed-meshheading:14690539-Mutation,
pubmed-meshheading:14690539-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:14690539-Pteridines,
pubmed-meshheading:14690539-Riboflavin,
pubmed-meshheading:14690539-Riboflavin Synthase,
pubmed-meshheading:14690539-Schizosaccharomyces,
pubmed-meshheading:14690539-Sequence Homology, Amino Acid
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pubmed:year |
2003
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pubmed:articleTitle |
Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
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pubmed:affiliation |
Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichten-bergstr, 4, D-85747 Garching, Germany. markus.fischer@ch.tum.de
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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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