Linked Life Data

12781764

Source:http://linkedlifedata.com/resource/pubmed/id/12781764

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-6-3
pubmed:abstractText
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the enzyme assimilating CO2 in biology. Despite serious efforts, using many different methods, a detailed understanding of activity and regulation in Rubisco still eludes us. New results in X-ray crystallography may provide a structural framework on which to base experimental approaches for more detailed analyses of the function of Rubisco at the molecular level. This article gives a critical review of the field and summarizes recent results from structural studies of Rubisco.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
414
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
130-40
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase.
pubmed:affiliation
Department of Molecular Biology, Swedish University of Agricultural Sciences, BMC Box 590, S-751 24, Uppsala, Sweden. inger@xray.bmc.uu.se <inger@xray.bmc.uu.se>
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't