Linked Life Data

11839489

Source:http://linkedlifedata.com/resource/pubmed/id/11839489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-2-12
pubmed:abstractText
Many proteins function as multimeric assemblies into which the folded individual promoters organize as higher order structures. An oligomerization mechanism that appears to impose the coordination of events during folding and oligomer assembly is three-dimensional domain swapping. Recent studies have focused on revealing the structural basis of domain swapping and a possible role for domain swapping in the regulation of protein aggregation and activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0959-440X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
48-53
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Protein folding and three-dimensional domain swapping: a strained relationship?
pubmed:affiliation
Departments of Biological Sciences and Chemistry, 202 Life Sciences Building, Louisiana State University, Baton Rouge, LA 70803, USA. newcomer@lsu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review