User profiles for Douglas Cyr

Doug Cyr

Department of Cell Biology and Physiology, UNC Chapel Hill
Verified email at med.unc.edu
Cited by 14779

The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

…, C Patterson, W Zhang, JM Younger, DM Cyr - Nature cell …, 2001 - nature.com
The folding of both wild-type and mutant forms of the cystic-fibrosis transmembrane-conductance
regulator (CFTR), a plasma-membrane chloride-ion channel, is inefficient 1, 2, 3, 4. …

DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70

DM Cyr, T Langer, MG Douglas - Trends in biochemical sciences, 1994 - cell.com
THE FUNCTION OF Hsp70 proteins as molecular chaperones in mediating the biogenesis
of proteins has been known for quite some time. The basic mechanism of action for these …

[HTML][HTML] CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation

J Jiang, CA Ballinger, Y Wu, Q Dai, DM Cyr… - Journal of Biological …, 2001 - ASBMB
Proper folding of proteins (either newly synthesized or damaged in response to a stressful
event) occurs in a highly regulated fashion. Cytosolic chaperones such as Hsc/Hsp70 are …

From CFTR biology toward combinatorial pharmacotherapy: expanded classification of cystic fibrosis mutations

…, RA Frizzell, DN Sheppard, DM Cyr… - Molecular biology of …, 2016 - Am Soc Cell Biol
More than 2000 mutations in the cystic fibrosis transmembrane conductance regulator (CFTR)
have been described that confer a range of molecular cell biological and functional …

The J‐protein family: modulating protein assembly, disassembly and translocation

P Walsh, D Bursać, YC Law, D Cyr, T Lithgow - EMBO reports, 2004 - embopress.org
DnaJ is a molecular chaperone and the prototypical member of the J‐protein family. J proteins
are defined by the presence of a J domain that can regulate the activity of 70‐kDa heat‐…

[HTML][HTML] Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator

…, EL Turnbull, CY Fan, C Patterson, DM Cyr - Cell, 2006 - cell.com
Cystic fibrosis arises from the misfolding and premature degradation of CFTRΔF508, a Cl −
ion channel with a single amino acid deletion. Yet, the quality-control machinery that selects …

YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism

AJ Caplan, DM Cyr, MG Douglas - Cell, 1992 - cell.com
The role of S. cerevisiae YDJ1 protein (YDJ1p) in polypeptide translocation across membranes
has been examined. A conditional ydj1 mutant strain (ydj1-151 TS ) is defective for …

[HTML][HTML] Mechanisms for regulation of Hsp70 function by Hsp40

CY Fan, S Lee, DM Cyr - Cell stress & chaperones, 2003 - ncbi.nlm.nih.gov
The Hsp70 family members play an essential role in cellular protein metabolism by acting
as polypeptide-binding and release factors that interact with nonnative regions of proteins at …

Protein quality control: U-box-containing E3 ubiquitin ligases join the fold

DM Cyr, J Höhfeld, C Patterson - Trends in biochemical sciences, 2002 - cell.com
Molecular chaperones act with folding co-chaperones to suppress protein aggregation and
refold stress damaged proteins. However, it is not clear how slowly folding or misfolded …

[HTML][HTML] From the cradle to the grave: molecular chaperones that may choose between folding and degradation

J Höhfeld, DM Cyr, C Patterson - EMBO reports, 2001 - embopress.org
Molecular chaperones are known to facilitate cellular protein folding. They bind non‐native
proteins and orchestrate the folding process in conjunction with regulatory cofactors that …