One step at a time: endoplasmic reticulum-associated degradation

Global analysis of protein expression in yeast

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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β

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Coupling of Stress in the ER to Activation of JNK Protein Kinases by Transmembrane Protein Kinase IRE1

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Macromolecular crowding: obvious but underappreciated

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Quality control in the endoplasmic reticulum

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Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation

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Molecular Chaperones and Protein Quality Control

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IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response

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Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response

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Degradation of CFTR by the ubiquitin-proteasome pathway

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Coupling endoplasmic reticulum stress to the cell death program

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The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol

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An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin

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Mechanism and function of deubiquitinating enzymes

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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing

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Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.

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Activation of Caspase-12, an Endoplastic Reticulum (ER) Resident Caspase, through Tumor Necrosis Factor Receptor-associated Factor 2-dependent Mechanism in Response to the ER Stress

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

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Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins

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ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway

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A membrane protein required for dislocation of misfolded proteins from the ER

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In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases

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Proteasome subunit Rpn13 is a novel ubiquitin receptor

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Protein degradation in the endoplasmic reticulum

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ASK1 Is Essential for JNK/SAPK Activation by TRAF2

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Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.

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Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

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Proteasomal Proteomics: Identification of Nucleotide-sensitive Proteasome-interacting Proteins by Mass Spectrometric Analysis of Affinity-purified Proteasomes

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Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48

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A Series of Ubiquitin Binding Factors Connects CDC48/p97 to Substrate Multiubiquitylation and Proteasomal Targeting

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OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD

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Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins

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Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

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A regulatory link between ER-associated protein degradation and the unfolded-protein response

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CHIP Is Associated with Parkin, a Gene Responsible for Familial Parkinson's Disease, and Enhances Its Ubiquitin Ligase Activity

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Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle

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A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation

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Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation

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Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate

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EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin

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Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control

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Sequential Quality-Control Checkpoints Triage Misfolded Cystic Fibrosis Transmembrane Conductance Regulator

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A Luminal Surveillance Complex that Selects Misfolded Glycoproteins for ER-Associated Degradation

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Role of Cue1p in ubiquitination and degradation at the ER surface.

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Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.

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Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation

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ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER

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Proteasomes: multicatalytic proteinase complexes

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Human HRD1 Is an E3 Ubiquitin Ligase Involved in Degradation of Proteins from the Endoplasmic Reticulum

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Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex

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E3 ubiquitin ligase that recognizes sugar chains

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CHOP (GADD153) and its oncogenic variant, TLS-CHOP, have opposing effects on the induction of G1/S arrest.Preprint

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The Hdj‐2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis

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A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum

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The Unfolded Protein Response Regulates Multiple Aspects of Secretory and Membrane Protein Biogenesis and Endoplasmic Reticulum Quality Control

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Molecular Chaperones in the Yeast Endoplasmic Reticulum Maintain the Solubility of Proteins for Retrotranslocation and Degradation

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ERp57 Functions as a Subunit of Specific Complexes Formed with the ER Lectins Calreticulin and Calnexin

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The Yin and Yang of protein folding

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Folding of VSV G Protein: Sequential Interaction with BiP and Calnexin

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Endoplasmic Reticulum Degradation Requires Lumen to Cytosol Signaling

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Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation

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Getting In and Out from Calnexin/Calreticulin Cycles

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The Recognition and Retrotranslocation of Misfolded Proteins from the Endoplasmic Reticulum

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Ubx2 links the Cdc48 complex to ER-associated protein degradation

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Simian Virus 40 Depends on ER Protein Folding and Quality Control Factors for Entry into Host Cells

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Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins

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A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum

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Cdc48 (p97): a ‘molecular gearbox’ in the ubiquitin pathway?

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Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers.

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Distinct Machinery Is Required in Saccharomyces cerevisiae for the Endoplasmic Reticulum-associated Degradation of a Multispanning Membrane Protein and a Soluble Luminal Protein

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Hsp70 Molecular Chaperone Facilitates Endoplasmic Reticulum-associated Protein Degradation of Cystic Fibrosis Transmembrane Conductance Regulator in Yeast

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Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin

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Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways

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Sodium 4-phenylbutyrate downregulates Hsc70: implications for intracellular trafficking of ΔF508-CFTR

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Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains

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Dissecting the ER-Associated Degradation of a Misfolded Polytopic Membrane Protein

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Intracellular Inclusions Containing Mutant α1-Antitrypsin Z Are Propagated in the Absence of Autophagic Activity

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EDEM3, a Soluble EDEM Homolog, Enhances Glycoprotein Endoplasmic Reticulum-associated Degradation and Mannose Trimming

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The Number and Location of Glycans on Influenza Hemagglutinin Determine Folding and Association with Calnexin and Calreticulin

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Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen

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Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER

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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery

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Gp78 Cooperates with RMA1 in Endoplasmic Reticulum-associated Degradation of CFTRΔF508

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Characterization of an ERAD Pathway for Nonglycosylated BiP Substrates, which Require Herp

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AAA ATPase p97/Valosin-containing Protein Interacts with gp78, a Ubiquitin Ligase for Endoplasmic Reticulum-associated Degradation

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A genomic screen identifies Dsk2p and Rad23p as essential components of ER‐associated degradation

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Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast

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Role of the proteasome in membrane extraction of a short‐lived ER‐transmembrane protein

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Yos9 Protein Is Essential for Degradation of Misfolded Glycoproteins and May Function as Lectin in ERAD

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The Ubiquitin-domain Protein HERP forms a Complex with Components of the Endoplasmic Reticulum Associated Degradation Pathway

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Human XTP3-B Forms an Endoplasmic Reticulum Quality Control Scaffold with the HRD1-SEL1L Ubiquitin Ligase Complex and BiP

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Cholera Toxin Is Exported from Microsomes by the Sec61p Complex

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