Linked Life Data

16108726

Source:http://linkedlifedata.com/resource/pubmed/id/16108726

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2005-8-19
pubmed:abstractText
The guanylate-binding proteins (GBPs) were first identified in the late 1970s, and within a short period of time, investigators were aware that GBPs possessed unique properties, in particular the ability to bind GMP agarose. Since then, much study has gone into understanding their mechanism of induction by interferons (IFNs) and other cytokines, and they have been used extensively as markers for IFN responsiveness in both cells and organisms. In time, we learned that GBPs had the unusual ability to hydrolyze GTP to both GDP and GMP. More recently, we have begun to appreciate their novel structure, one that suggests unique mechanisms of GTP binding and hydrolysis and unique forms of regulation. In addition, we have begun to unravel some of their functions and to separate these function into those functions that do and those that do not require GTPase activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1079-9907
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
435-43
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
The guanylate-binding proteins (GBPs): proinflammatory cytokine-induced members of the dynamin superfamily with unique GTPase activity.
pubmed:affiliation
Department of Biological Sciences, University of Toledo, Toledo, OH 43606, USA. Deborah.Vestal@utoledo.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural