Linked Life Data

17081106

Source:http://linkedlifedata.com/resource/pubmed/id/17081106

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10-11
pubmed:dateCreated
2006-11-3
pubmed:abstractText
One of the hallmarks of chronic or severe oxidative stress is the accumulation of oxidized proteins, which tend to form high-molecular-weight aggregates. The major proteolytic system responsible for the removal of oxidized cytosolic and nuclear proteins is the proteasome. This complicated proteolytic system contains a core proteasomal form (20S proteasome) and several regulators. All of these components are affected by oxidative stress to various degrees. The ATP-stimulated 26S proteasome is sensitive to oxidative stress, whereas the 20S form seems to be more resistant. The nuclear proteasome selectively degrades oxidatively damaged histones in the nuclei of mammalian cells, where it is activated and regulated by automodified PARP-1 after oxidative challenge. In this brief review we highlight the proteolysis and its regulatory effects during oxidative stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
387
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1351-5
pubmed:meshHeading
pubmed:articleTitle
Protein oxidation and proteolysis.
pubmed:affiliation
Institute of Biological Chemistry and Nutrition, University of Hohenheim, Garbenstrasse 28, D-70593 Stuttgart, Germany.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't