rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
|
pubmed:dateCreated |
1999-2-2
|
pubmed:databankReference |
|
pubmed:abstractText |
. Mycobacterium tuberculosis is the single most deadly human pathogen and is responsible for nearly three million deaths every year. Recent elucidation of the mode of action of isoniazid, a frontline antimycobacterial drug, suggests that NAD metabolism is extremely critical for this microorganism. M. tuberculosis depends solely on the de novo pathway to meet its NAD demand. Quinolinic acid phosphoribosyltransferase (QAPRTase), a key enzyme in the de novo biosynthesis of NAD, provides an attractive target for designing novel antitubercular drugs.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0969-2126
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
6
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1587-99
|
pubmed:dateRevised |
2010-3-24
|
pubmed:meshHeading |
pubmed-meshheading:9862811-Amino Acid Sequence,
pubmed-meshheading:9862811-Antitubercular Agents,
pubmed-meshheading:9862811-Crystallography, X-Ray,
pubmed-meshheading:9862811-Drug Design,
pubmed-meshheading:9862811-Humans,
pubmed-meshheading:9862811-Molecular Sequence Data,
pubmed-meshheading:9862811-Mycobacterium tuberculosis,
pubmed-meshheading:9862811-Nicotinamide Mononucleotide,
pubmed-meshheading:9862811-Pentosyltransferases,
pubmed-meshheading:9862811-Protein Conformation,
pubmed-meshheading:9862811-Recombinant Proteins,
pubmed-meshheading:9862811-Sequence Homology, Amino Acid
|
pubmed:year |
1998
|
pubmed:articleTitle |
Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target.
|
pubmed:affiliation |
Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|