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Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane
2 of 67 checkable references need attention · checked 2026-07-22
At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.
References needing attention
does not resolve to a known work10.1002/(SICI)1097-0061(19960930)12:12<1229::AID-YEA15>3.0.CO;2-H
does not resolve to a known work10.1002/(SICI)1097-0061(199604)12:5<425::AID-YEA924>3.0.CO;2-B
The 65 checked references that resolve
resolves10.1002/j.1460-2075.1996.tb00560.x
Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin‐proteasome pathway.
resolves10.1126/science.278.5344.1806
Role of Cue1p in Ubiquitination and Degradation at the ER Surface
resolves10.1091/mbc.9.1.209
Der3p/Hrd1p Is Required for Endoplasmic Reticulum-associated Degradation of Misfolded Lumenal and Integral Membrane Proteins
resolves10.1016/S0962-8924(97)01020-9
ER-associated and proteasomemediated protein degradation: how two topologically restricted events came together
resolves10.1006/scdb.1999.0321
ER protein quality control and proteasome-mediated protein degradation
resolves10.1074/jbc.274.6.3453
The Requirement for Molecular Chaperones during Endoplasmic Reticulum-associated Protein Degradation Demonstrates That Protein Export and Import Are Mechanistically Distinct
resolves10.1083/jcb.137.7.1483
The Lumenal Domain of Sec63p Stimulates the ATPase Activity of BiP and Mediates BiP Recruitment to the Translocon in <i>Saccharomyces cerevisiae</i>
resolves10.1038/349806a0
Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
resolves10.1074/jbc.273.16.9734
Ubiquitination Is Required for the Retro-translocation of a Short-lived Luminal Endoplasmic Reticulum Glycoprotein to the Cytosol for Degradation by the Proteasome
resolves10.1016/S0092-8674(00)81115-0
The Cotranslational Integration of Membrane Proteins into the Phospholipid Bilayer Is a Multistep Process
resolves10.1093/emboj/17.21.6144
Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope–ER network in yeast
resolves10.1016/S0021-9258(18)47010-X
SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus.
resolves10.1083/jcb.126.4.935
Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.
resolves10.1002/j.1460-2075.1996.tb00492.x
A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.
resolves10.1016/S0092-8674(00)81403-8
BiP Maintains the Permeability Barrier of the ER Membrane by Sealing the Lumenal End of the Translocon Pore before and Early in Translocation
resolves10.1091/mbc.7.12.2029
Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.
resolves10.1016/S0092-8674(00)81391-4
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
resolves10.1126/science.273.5282.1725
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
resolves10.1242/jcs.111.6.749
Dissection of the translocation and chaperoning functions of yeast BiP/Kar2p in vivo
resolves10.1002/j.1460-2075.1996.tb00723.x
Competition between folding and glycosylation in the endoplasmic reticulum.
resolves10.1016/S1074-7613(00)80514-2
The α Chain of the T Cell Antigen Receptor Is Degraded in the Cytosol
resolves10.1074/jbc.273.18.11183
Involvement of Heat Shock Protein 90 in the Degradation of Mutant Insulin Receptors by the Proteasome
resolves10.1083/jcb.142.5.1223
Degradation of Misfolded Endoplasmic Reticulum Glycoproteins in <i>Saccharomyces cerevisiae</i> Is Determined by a Specific Oligosaccharide Structure
resolves10.1016/0092-8674(95)90241-4
Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
resolves10.1016/0092-8674(95)90313-5
A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
resolves10.1083/jcb.141.4.887
The β Subunit of the Sec61 Complex Facilitates Cotranslational Protein Transport and Interacts with the Signal Peptidase during Translocation
resolves10.1002/j.1460-2075.1996.tb00411.x
Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast.
resolves10.1074/jbc.273.31.19453
Protein Folding Stability Can Determine the Efficiency of Escape from Endoplasmic Reticulum Quality Control
resolves10.1093/emboj/17.23.6879
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
resolves10.1016/S0092-8674(00)81861-9
Binding of Secretory Precursor Polypeptides to a Translocon Subcomplex Is Regulated by BiP
resolves10.1016/S0092-8674(00)80767-9
BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane
resolves10.1093/emboj/17.12.3251
Role of the proteasome in membrane extraction of a short‐lived ER‐transmembrane protein
resolves10.1083/jcb.132.3.291
Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.
resolves10.1016/0092-8674(95)90077-2
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
resolves10.1093/emboj/16.15.4540
Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
resolves10.1091/mbc.9.12.3455
Sec61p Serves Multiple Roles in Secretory Precursor Binding and Translocation into the Endoplasmic Reticulum Membrane
resolves10.1016/S0092-8674(00)81738-9
Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane
resolves10.1038/42276
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
resolves10.1074/jbc.273.49.32848
Endoplasmic Reticulum Degradation of a Mutated ATP-binding Cassette Transporter Pdr5 Proceeds in a Concerted Action of Sec61 and the Proteasome
resolves10.1016/S0014-5793(98)01724-4
Re‐entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species
resolves10.1242/jcs.112.22.4123
Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
resolves10.1016/0092-8674(92)90415-9
Sec61p and BiP directly facilitate polypeptide translocation into the ER
resolves10.1074/jbc.273.34.21526
Peptides Glycosylated in the Endoplasmic Reticulum of Yeast Are Subsequently Deglycosylated by a Soluble Peptide: N-Glycanase Activity
resolves10.1083/jcb.136.3.555
Interactions between Newly Synthesized Glycoproteins, Calnexin and a Network of Resident Chaperones in the Endoplasmic Reticulum
resolves10.1083/jcb.142.2.365
Dislocation of Type I Membrane Proteins from the ER to the Cytosol Is Sensitive to Changes in Redox Potential
resolves10.1083/jcb.115.4.983
Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum.
resolves10.1073/pnas.93.24.13797
Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
resolves10.1016/S0092-8674(00)81054-5
The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol
resolves10.1038/384432a0
Sec6l-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
resolves10.1074/jbc.271.41.25590
Determination of the Transmembrane Topology of Yeast Sec61p, an Essential Component of the Endoplasmic Reticulum Translocation Complex
resolves10.1093/emboj/16.15.4549
Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p
resolves10.1074/jbc.274.5.2616
Evidence That Endoplasmic Reticulum (ER)-associated Degradation of Cystic Fibrosis Transmembrane Conductance Regulator Is Linked to Retrograde Translocation from the ER Membrane
resolves10.1084/jem.187.6.835
Novel Aspects of Degradation of T Cell Receptor Subunits from the Endoplasmic Reticulum (ER) in T Cells: Importance of Oligosaccharide Processing, Ubiquitination, and Proteasome-dependent Removal from ER Membranes
resolves10.1074/jbc.270.46.27687
In Vivo Assembly of the Proteasomal Complexes, Implications for Antigen Processing
resolves10.1016/S0021-9258(19)36586-X
Regulation of selective protein degradation in the endoplasmic reticulum by redox potential.
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