Linked Life Data

10532860

Source:http://linkedlifedata.com/resource/pubmed/id/10532860

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6252
pubmed:dateCreated
1999-10-19
pubmed:abstractText
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hsp60) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E. coli (groES), and Mg-ATP. Because chaperonins are ubiquitous, a conserved Mg-ATP-dependent mechanism exists that uses the chaperonins to facilitate the folding of some other proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
342
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
884-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:articleTitle
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
pubmed:affiliation
Molecular Biology Division, E.I. Du Pont de Nemours & Co., Wilmington, Delaware 19880-0402, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't