Linked Life Data

18211002

Source:http://linkedlifedata.com/resource/pubmed/id/18211002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-12
pubmed:abstractText
External stresses cause certain proteins to lose their regular structure and aggregate. In order to clarify this abnormal aggregation process, a structural evolution of human recombinant alphaB-crystallin under UV irradiation was observed with in situ small-angle neutron scattering. The abnormal aggregation process was identified to fall in three time zones: incubation, aggregation, and saturation. During the incubation time, the size of aggregates was almost unchanged but a deformation in the local structure was developing. After the incubation time, abnormal aggregation proceed. When the volume of the aggregates reached around twice the size as that of the initial aggregates, the aggregation rate slowed down, which marked the onset of saturation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1526-4602
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-4
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Structural evolution of human recombinant alpha B-crystallin under UV irradiation.
pubmed:affiliation
Research Reactor Institute, Kyoto University, Osaka 590-0494, Japan. sugiyama@rri.kyoto-u.ac.jp
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't