Linked Life Data

10425395

Source:http://linkedlifedata.com/resource/pubmed/id/10425395

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-9-9
pubmed:abstractText
Knowledge of the PLD superfamily is rapidly expanding and new insights into the mechanism and regulation of the superfamily are rapidly emerging. The recent structural analysis and use of mutant proteins suggest a mechanism that involves two active sites acting in concert. While a number of residues are required for activity, it appears most likely that a histidine is the residue that becomes covalently linked to phosphatidate in catalysis. Evidence for these proposals is covered in this article.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
1439
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
187-97
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
The PLD superfamily: insights into catalysis.
pubmed:affiliation
Department of Biochemistry, Wake Forest University School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA. mwaite@wfubmc.edu
pubmed:publicationType
Journal Article, Review