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Prion|May 8, 2009
Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathwaysPeter M Douglas, Daniel W Summers, Douglas M CyrPrion|June 19, 2009
Prion propagation by Hsp40 molecular chaperonesDaniel W Summers, Peter M Douglas, Douglas M CyrMolecular Biology of the Cell|August 7, 2009
Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleusPeter M Douglas, Daniel W Summers, Hong-Yu Ren, et al.The Journal of Biological Chemistry|December 6, 2008
The type I Hsp40 Ydj1 utilizes a farnesyl moiety and zinc finger-like region to suppress prion toxicityDaniel W Summers, Peter M Douglas, Hong-Yu Ren, et al.Trends in Biochemical Sciences|April 11, 2009
Polypeptide transfer from Hsp40 to Hsp70 molecular chaperonesDaniel W Summers, Peter M Douglas, Carlos H I Ramos, et al.Methods (San Diego, Calif.)|December 1, 2010
Use of yeast as a system to study amyloid toxicityDaniel W Summers, Douglas M CyrBiopolymers|September 22, 2009
Interplay between protein homeostasis networks in protein aggregation and proteotoxicityPeter M Douglas, Douglas M CyrPlos One|January 24, 2013
The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic proteinDaniel W Summers, Katie J Wolfe, Hong Yu Ren, et al.Proceedings of the National Academy of Sciences of the United States of America|June 25, 2009
Identification of a consensus motif in substrates bound by a Type I Hsp40Pradeep Kota, Daniel W Summers, Hong-Yu Ren, et al.Pageof 11