|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5693
|
|
pubmed:dateCreated |
2004-10-1
|
|
pubmed:abstractText |
To identify previously unknown small molecules that inhibit cell cycle machinery, we performed a chemical genetic screen in Xenopus extracts. One class of inhibitors, termed ubistatins, blocked cell cycle progression by inhibiting cyclin B proteolysis and inhibited degradation of ubiquitinated Sic1 by purified proteasomes. Ubistatins blocked the binding of ubiquitinated substrates to the proteasome by targeting the ubiquitin-ubiquitin interface of Lys(48)-linked chains. The same interface is recognized by ubiquitin-chain receptors of the proteasome, indicating that ubistatins act by disrupting a critical protein-protein interaction in the ubiquitin-proteasome system.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Quinolines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SIC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfanilic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex,
http://linkedlifedata.com/resource/pubmed/chemical/ubistatin A,
http://linkedlifedata.com/resource/pubmed/chemical/ubistatin B
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
1095-9203
|
|
pubmed:author |
pubmed-author:CoffinoPhilipP,
pubmed-author:D'OnofrioMariapinaM,
pubmed-author:DeshaiesRaymond JRJ,
pubmed-author:FushmanDavidD,
pubmed-author:KingRandall WRW,
pubmed-author:PetersNoel RNR,
pubmed-author:SakamotoKathleen MKM,
pubmed-author:TochtropGregory PGP,
pubmed-author:VaradanRanjaniR,
pubmed-author:VermaRatiR,
pubmed-author:ZhangMingshengM
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
1
|
|
pubmed:volume |
306
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
117-20
|
|
pubmed:dateRevised |
2010-10-22
|
|
pubmed:meshHeading |
pubmed-meshheading:15459393-Animals,
pubmed-meshheading:15459393-Cell Extracts,
pubmed-meshheading:15459393-Cyclin B,
pubmed-meshheading:15459393-Cyclin-Dependent Kinase Inhibitor Proteins,
pubmed-meshheading:15459393-Cysteine Endopeptidases,
pubmed-meshheading:15459393-Drug Evaluation, Preclinical,
pubmed-meshheading:15459393-Interphase,
pubmed-meshheading:15459393-Mitosis,
pubmed-meshheading:15459393-Molecular Structure,
pubmed-meshheading:15459393-Multienzyme Complexes,
pubmed-meshheading:15459393-Ornithine Decarboxylase,
pubmed-meshheading:15459393-Proteasome Endopeptidase Complex,
pubmed-meshheading:15459393-Protein Binding,
pubmed-meshheading:15459393-Proteins,
pubmed-meshheading:15459393-Quinolines,
pubmed-meshheading:15459393-Recombinant Fusion Proteins,
pubmed-meshheading:15459393-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15459393-Sulfanilic Acids,
pubmed-meshheading:15459393-Ubiquitin,
pubmed-meshheading:15459393-Ubiquitin-Protein Ligase Complexes,
pubmed-meshheading:15459393-Xenopus laevis
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain.
|
|
pubmed:affiliation |
Department of Biology, Howard Hughes Medical Institute (HHMI), California Institute of Technology, Pasadena, CA 91125, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
