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  1. No Access

    Protocol

    Analysis of CFTR Folding and Degradation in Transiently Transfected Cells

    Misfolding and premature degradation of F508del-CFTR is the major cause of cystic fibrosis. Components of the ubiquitin-proteasome system function on the surface of the endoplasmic reticulum to select misfolde...

    Diane E. Grove, Meredith F.N. Rosser, Richard L. Watkins, Douglas M. Cyr in Cystic Fibrosis (2011)

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    Protocol

    Reconstitution of CHIP E3 Ubiquitin Ligase Activity

    CHIP, the carboxyl-terminus of Hsp70 interacting protein, is both an E3 ubiquitin ligase and an Hsp70 co-chaperone and is implicated in the degradation of cytosolic quality control and numerous disease substra...

    Hong Yu Ren, Cam Patterson, Douglas M. Cyr, Meredith F. N. Rosser in Molecular Chaperones (2011)

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    Chapter

    Do Hsp40s Act as Chaperones or Co-Chaperones?

    The Hsp70 family plays an essential role in cellular protein metabolism by acting as a polypeptide binding and release factor that interacts with nonnative regions of proteins at different stages o...

    Meredith F. N. Rosser, Douglas M. Cyr in Networking of Chaperones by Co-Chaperones (2007)

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    Protocol

    Cystic Fibrosis Transmembrane Conductance Regulator as a Model Substrate to Study Endoplasmic Reticulum Protein Quality Control in Mammalian Cells

    Components of the ubiquitin-proteasome system function on the surface of the endoplasmic reticulum (ER) to select misfolded proteins for degradation. Herein we describe methods that allow for the study of the ...

    J. Michael Younger, Chun-Yang Fan, Liling Chen… in Ubiquitin-Proteasome Protocols (2005)