Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2008-10-20
pubmed:abstractText
Belactosin A is a potent proteasome inhibitor isolated from Streptomyces metabolites. Here we show that a hydrophobic belactosin A derivative, dansyl-KF33955, can covalently, and specifically, affinity label the catalytic subunits of the 26S proteasome, which consists of the 20S protein degrading core particle and the 19S regulatory particles. The labeling of catalytic subunits proceeds faster in intact proteasomes in vivo than in isolated 20S core particles. These data suggest that the 19S regulatory particle may facilitate entry of the inhibitor into the 20S core particle. This cell-permeable chemical probe is an excellent tool with which to study the interactions of this proteasome inhibitor with proteasomes in intact cells.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1464-3405
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5668-71
pubmed:dateRevised
2009-8-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Affinity labeling of the proteasome by a belactosin A derived inhibitor.
pubmed:affiliation
Graduate School of Bioscience, Nagahama Institute of Bio-Science and Technology, Tamura-cho 1266, Nagahama, Shiga 526-0829, Japan. m_hasegawa@nagahama-i-bio.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't