Year |
Citation |
Score |
2006 |
Betarbet R, Canet-Aviles RM, Sherer TB, Mastroberardino PG, McLendon C, Kim JH, Lund S, Na HM, Taylor G, Bence NF, Kopito R, Seo BB, Yagi T, Yagi A, Klinefelter G, et al. Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system. Neurobiology of Disease. 22: 404-20. PMID 16439141 DOI: 10.1016/J.Nbd.2005.12.003 |
0.549 |
|
2005 |
Bence NF, Bennett EJ, Kopito RR. Application and analysis of the GFPu family of ubiquitin-proteasome system reporters. Methods in Enzymology. 399: 481-90. PMID 16338377 DOI: 10.1016/S0076-6879(05)99033-2 |
0.549 |
|
2005 |
Mukai H, Isagawa T, Goyama E, Tanaka S, Bence NF, Tamura A, Ono Y, Kopito RR. Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells. Proceedings of the National Academy of Sciences of the United States of America. 102: 10887-92. PMID 16040812 DOI: 10.1073/Pnas.0409283102 |
0.664 |
|
2005 |
Bennett EJ, Bence NF, Jayakumar R, Kopito RR. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Molecular Cell. 17: 351-65. PMID 15694337 DOI: 10.1016/J.Molcel.2004.12.021 |
0.697 |
|
2002 |
Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. The Journal of Biological Chemistry. 277: 34150-60. PMID 12091393 DOI: 10.1074/Jbc.M204955200 |
0.59 |
|
2001 |
Rajan RS, Illing ME, Bence NF, Kopito RR. Specificity in intracellular protein aggregation and inclusion body formation. Proceedings of the National Academy of Sciences of the United States of America. 98: 13060-5. PMID 11687604 DOI: 10.1073/Pnas.181479798 |
0.613 |
|
2001 |
Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science (New York, N.Y.). 292: 1552-5. PMID 11375494 DOI: 10.1126/science.292.5521.1552 |
0.696 |
|
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