Linked Life Data

18488460

Source:http://linkedlifedata.com/resource/pubmed/id/18488460

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-5-19
pubmed:abstractText
UV-induced aggregation of betaL-crystallin, one of the major lens proteins, was studied under its pulse radiation with XeCl laser at a wavelength of 308 nm. Unlike the in vitro tested dipeptides L-carnosine, N-acetyl carnosine, D-panthetine, and particularly their combination, the so-called new chaperon was demonstrated to slow down the rate of photoaggregatin of beta-crystallin. The new chaperon, a mixture of D-pathethine and N-acetyl carnosine was ascertained to protect a mixture of betaL- and alpha-crystallins from UV-induced aggregation to a greater extent than D-pathethine or N-acetyl carnosine used alone. An effective drug based on the new chaperon may be designed for the prevention of cataract in sight.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0042-465X
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6-8
pubmed:meshHeading
pubmed:articleTitle
[Like anticataract agents, the antiaggregants of lens crystallin. Communication 2. Study of the impact of chaperon-like (protective) activity of short-chain peptides on the rate of UV-induced aggregation of betaL-crystallins by eximer laser].
pubmed:publicationType
Journal Article, Comparative Study, English Abstract