Related references
Note: Only part of the references are listed.Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system
Judit Wahlman et al.
CELL (2007)
Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
Fei Sun et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus
Joanna Gilbert et al.
JOURNAL OF VIROLOGY (2006)
Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection
Brendan N. Lilley et al.
JOURNAL OF VIROLOGY (2006)
Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
J. Michael Younger et al.
CELL (2006)
A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
Robert Gauss et al.
NATURE CELL BIOLOGY (2006)
Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
Pedro Carvalho et al.
CELL (2006)
A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
Vladimir Denic et al.
CELL (2006)
Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation
Michele L. Forster et al.
JOURNAL OF CELL BIOLOGY (2006)
EDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol
M Slominska-Wojewodzka et al.
MOLECULAR BIOLOGY OF THE CELL (2006)
Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
Y Oda et al.
JOURNAL OF CELL BIOLOGY (2006)
Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
BN Lilley et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase
A Pirneskoski et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
A membrane protein required for dislocation of misfolded proteins from the ER
BN Lilley et al.
NATURE (2004)
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
YH Ye et al.
NATURE (2004)
Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum
RA Spooner et al.
BIOCHEMICAL JOURNAL (2004)
Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm
Y Fujinaga et al.
MOLECULAR BIOLOGY OF THE CELL (2003)
The intracellular voyage of cholera toxin: going retro
WI Lencer et al.
TRENDS IN BIOCHEMICAL SCIENCES (2003)
Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation
C Rodighiero et al.
EMBO REPORTS (2002)
Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1
M Tsai et al.
JOURNAL OF CELL BIOLOGY (2002)
Cysteine string protein interacts with and modulates the maturation of the cystic fibrosis transmembrane conductance regulator
H Zhang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
M Molinari et al.
JOURNAL OF CELL BIOLOGY (2002)
Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
B Tsai et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2002)
Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
B Tsai et al.
CELL (2001)
Cholera toxin is exported from microsomes by the Sec61p complex
A Schmitz et al.
JOURNAL OF CELL BIOLOGY (2000)
Share Paper
