Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-1-19
pubmed:abstractText
Several significant advances in the understanding of the catalytic mechanisms, structures and evolution of glutathione transferases have occurred in the past year. These advances include new mechanistic information concerning the canonical soluble enzymes, the finding that the fosfomycin-specific enzyme, FosA, is a metalloglutathione transferase and a higher resolution projection structure of the microsomal enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
618-23
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Mechanistic imperatives for the evolution of glutathione transferases.
pubmed:affiliation
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA. armstrong@toxicology.mc.vanderbilt.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review