Quality and quantity control at the endoplasmic reticulum

Signal integration in the endoplasmic reticulum unfolded protein response

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310 · see citing works

Roles of N-Linked Glycans in the Endoplasmic Reticulum

Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037 · see citing works

One step at a time: endoplasmic reticulum-associated degradation

Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299 · see citing works

Regulated Ire1-dependent decay of messenger RNAs in mammalian cells

Hollien, J., Lin, J. H., Li, H., Stevens, N. S., Walter, P., & Weissman, J. S. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903014 · Cited by 1,021 · see citing works

Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response

Bernales, S., McDonald, K. L., & Walter, P. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040423 · Cited by 1,009 · see citing works

IRE1α Kinase Activation Modes Control Alternate Endoribonuclease Outputs to Determine Divergent Cell Fates

Han, D., Lerner, A. G., Walle, L. V., Upton, J.-P., Xu, W., Hagen, A., Backes, B. J., Oakes, S. A., & Papa, F. R. (2009) · Cell · doi:10.1016/j.cell.2009.07.017 · Cited by 816 · see citing works

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

Carvalho, P., Goder, V., & Rapoport, T. A. (2006) · Cell · doi:10.1016/j.cell.2006.05.043 · Cited by 726 · see citing works

Comprehensive Characterization of Genes Required for Protein Folding in the Endoplasmic Reticulum

Jonikas, M. C., Collins, S. R., Denic, V., Oh, E., Toyama, E. Q., Schmid, V., Weibezahn, J., Schwappach, B., Walter, P., Weissman, J. S., et al. (2009) · Science · doi:10.1126/science.1167983 · Cited by 713 · see citing works

Mechanisms of regulated unconventional protein secretion

Nickel, W., & Rabouille, C. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2617 · Cited by 703 · see citing works

A Novel Human WD Protein, h-βTrCP, that Interacts with HIV-1 Vpu Connects CD4 to the ER Degradation Pathway through an F-Box Motif

Margottin-Goguet, F., Bour, S. P., Durand, H., Selig, L., Bénichou, S., Richard, V., Thomas, D., Strebel, K., & Bénarous, R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80056-8 · Cited by 670 · see citing works

Protein quality control in the early secretory pathway

Anelli, T., & Sitia, R. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601974 · Cited by 623 · see citing works

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

Christianson, J. C., Shaler, T. A., Tyler, R. E., & Kopito, R. R. (2008) · Nature Cell Biology · doi:10.1038/ncb1689 · Cited by 509 · see citing works

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

Molinari, M., Calanca, V., Galli, C., Lucca, P., & Paganetti, P. (2003) · Science · doi:10.1126/science.1079474 · Cited by 470 · see citing works

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

Bays, N. W., Gardner, R. G., Seelig, L. P., Joazeiro, C. A. P., & Hampton, R. Y. (2000) · Nature Cell Biology · doi:10.1038/35050524 · Cited by 465 · see citing works

EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin

Oda, Y., Hosokawa, N., Wada, I., & Nagata, K. (2003) · Science · doi:10.1126/science.1079181 · Cited by 453 · see citing works

Unconventional secretion of Acb1 is mediated by autophagosomes

Duran, J. M., Anjard, C., Stefan, C., Loomis, W. F., & Malhotra, V. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911154 · Cited by 433 · see citing works

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

Denic, V., Toyama, E. Q., & Weissman, J. S. (2006) · Cell · doi:10.1016/j.cell.2006.05.045 · Cited by 419 · see citing works

Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG-CoA reductase

DeBose-Boyd, R. A. (2008) · Cell Research · doi:10.1038/cr.2008.61 · Cited by 391 · see citing works

Gp78, a Membrane-Anchored Ubiquitin Ligase, Associates with Insig-1 and Couples Sterol-Regulated Ubiquitination to Degradation of HMG CoA Reductase

Song, B., Sever, N., & DeBose‐Boyd, R. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.009 · Cited by 368 · see citing works

The ubiquitylation machinery of the endoplasmic reticulum

Hirsch, C., Gauss, R., Horn, S. C., Neuber, O., & Sommer, T. (2009) · Nature · doi:10.1038/nature07962 · Cited by 351 · see citing works

The lectin ERGIC-53 is a cargo transport receptor for glycoproteins

Appenzeller‐Herzog, C., Andersson, H. M., Kappeler, F., & Hauri, H. (1999) · Nature Cell Biology · doi:10.1038/14020 · Cited by 337 · see citing works

Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation

Manjithaya, R. R., Anjard, C., Loomis, W. F., & Subramani, S. E. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911149 · Cited by 337 · see citing works

Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane

Lilley, B. N., & Ploegh, H. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505014102 · Cited by 315 · see citing works

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

Schuberth, C. E., & Buchberger, A. (2005) · Nature Cell Biology · doi:10.1038/ncb1299 · Cited by 314 · see citing works

Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane

Ye, Y., Shibata, Y., Kikkert, M., van Voorden, S., Wiertz, E. J. H. J., & Rapoport, T. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505006102 · Cited by 311 · see citing works

Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3

Wang, X., Herr, R. A., Chua, W., Lybarger, L. P., Wiertz, E. J. H. J., & Hansen, T. H. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611063 · Cited by 310 · see citing works

The endoplasmic reticulum as a protein-folding compartment

Helenius, A., Marquardt, T., & Braakman, I. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90309-b · Cited by 301 · see citing works

Ubx2 links the Cdc48 complex to ER-associated protein degradation

Neuber, O., Jarosch, E., Volkwein, C., Walter, J., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb1298 · Cited by 300 · see citing works

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

Schelhaas, M., Malmström, J. A., Pelkmans, L., Haugstetter, J., Ellgaard, L., Grünewald, K., & Helenius, A. (2007) · Cell · doi:10.1016/j.cell.2007.09.038 · Cited by 300 · see citing works

Substrate-Specific Translocational Attenuation during ER Stress Defines a Pre-Emptive Quality Control Pathway

Kang, S., Rane, N. S., Kim, S. J., Garrison, J. L., Taunton, J., & Hegde, R. S. (2006) · Cell · doi:10.1016/j.cell.2006.10.032 · Cited by 290 · see citing works

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

Ploegh, H. L. (2007) · Nature · doi:10.1038/nature06004 · Cited by 286 · see citing works

Ubiquitination, Ubiquitin-like Modifiers, and Deubiquitination in Viral Infection

Isaacson, M. K., & Ploegh, H. L. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.05.012 · Cited by 281 · see citing works

Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol

Song, B., Javitt, N. B., & DeBose‐Boyd, R. A. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.001 · Cited by 279 · see citing works

N-Linked Glycans Direct the Cotranslational Folding Pathway of Influenza Hemagglutinin

Daniels, R., Kurowski, B. G., Johnson, A. E., & Hebert, D. N. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00821-3 · Cited by 276 · see citing works

SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

Mueller, B., Klemm, E. J., Spooner, E., Claessen, J. H. L., & Ploegh, H. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805371105 · Cited by 266 · see citing works

The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags

Hebert, D. N., Garman, S. C., & Molinari, M. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.05.007 · Cited by 265 · see citing works

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

Kamimoto, T., Shoji, S., Hidvegi, T., Mizushima, N., Umebayashi, K., Perlmutter, D. H., & Yoshimori, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509409200 · Cited by 259 · see citing works

Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum

Clerc, S., Hirsch, C., Oggier, D. M., Deprez, P. N., Jakob, C. A., Sommer, T., & Aebi, M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809198 · Cited by 254 · see citing works

Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation

Quan, E. M., Kamiya, Y., Kamiya, D., Denic, V., Weibezahn, J., Kato, K., & Weissman, J. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.017 · Cited by 242 · see citing works

AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery

White, S. R., & Lauring, B. P. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00642.x · Cited by 221 · see citing works

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

Okuda-Shimizu, Y., & Hendershot, L. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.012 · Cited by 215 · see citing works

Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase

Ye, Y. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.01.005 · Cited by 213 · see citing works

Misfolded Membrane Proteins Are Specifically Recognized by the Transmembrane Domain of the Hrd1p Ubiquitin Ligase

Sato, B. K., Schulz, D., Do, P. H., & Hampton, R. Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.010 · Cited by 210 · see citing works

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

Hosokawa, N., Wada, I., Nagasawa, K., Moriyama, T., Okawa, K., & Nagata, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709336200 · Cited by 198 · see citing works

A Novel Quality Control Compartment Derived from the Endoplasmic Reticulum

Kamhi-Nesher, S., Shenkman, M., Tolchinsky, S., Fromm, S. V., Ehrlich, R. L., & Lederkremer, G. Z. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.6.1711 · Cited by 192 · see citing works

Characterization of an ERAD Gene as VPS30/ATG6 Reveals Two Alternative and Functionally Distinct Protein Quality Control Pathways: One for Soluble Z Variant of Human α-1 Proteinase Inhibitor (A1PiZ) and Another for Aggregates of A1PiZ

Kruse, K. B., Brodsky, J. L., & McCracken, A. A. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-09-0779 · Cited by 192 · see citing works

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates

Bernasconi, R., Galli, C., Calanca, V., Nakajima, T., & Molinari, M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200910042 · Cited by 176 · see citing works

Inaugural article : recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane

Ye, Y. (2005) · Medical Entomology and Zoology · Cited by 165 · see citing works

Multilayered Mechanism of CD4 Downregulation by HIV-1 Vpu Involving Distinct ER Retention and ERAD Targeting Steps

Magadán, J. G., Pérez‐Victoria, F. J., Sougrat, R., Ye, Y., Strebel, K., & Bonifacino, J. S. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000869 · Cited by 163 · see citing works

Molecular Basis of Sugar Recognition by the Human L-type Lectins ERGIC-53, VIPL, and VIP36

Kamiya, Y., Kamiya, D., Yamamoto, K., Nyfeler, B., Hauri, H., & Kato, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m709384200 · Cited by 157 · see citing works

The Hrd1p ligase complex forms a linchpin between ER‐lumenal substrate selection and Cdc48p recruitment

Gauss, R., Sommer, T., & Jarosch, E. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601088 · Cited by 154 · see citing works

The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER

Stagg, H. R., Thomas, M., van den Boomen, D. J. H., Wiertz, E. J. H. J., Drabkin, H. A., Gemmill, R. M., & Lehner, P. J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906110 · Cited by 148 · see citing works

IRE1β Inhibits Chylomicron Production by Selectively Degrading MTP mRNA

Iqbal, J., Dai, K., Seimon, T. A., Jungreis, R., Oyadomari, M., Kuriakose, G., Ron, D., Tabas, I. A., & Hussain, M. M. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.03.005 · Cited by 140 · see citing works

Signal peptide peptidase is required for dislocation from the endoplasmic reticulum

Loureiro, J., Lilley, B. N., Spooner, E., Noriega, V. M., Tortorella, D., & Ploegh, H. L. (2006) · Nature · doi:10.1038/nature04830 · Cited by 134 · see citing works

The Role of a Novel p97/Valosin-containing Protein-interacting Motif of gp78 in Endoplasmic Reticulum-associated Degradation

Ballar, P., Shen, Y., Yang, H., & Fang, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603355200 · Cited by 129 · see citing works

Stress Tolerance of Misfolded Carboxypeptidase Y Requires Maintenance of Protein Trafficking and Degradative Pathways

Spear, E. D., & Ng, D. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-11-0717 · Cited by 123 · see citing works

EDEM1 accelerates the trimming of 1,2-linked mannose on the C branch of N-glycans

Hosokawa, N., Tremblay, L. O., Sleno, B., Kamiya, Y., Wada, I., Nagata, K., Kato, K., & Herscovics, A. A. (2010) · Glycobiology · doi:10.1093/glycob/cwq001 · Cited by 123 · see citing works

ERAD substrates: Which way out?

Hebert, D. N., Bernasconi, R., & Molinari, M. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.12.007 · Cited by 120 · see citing works

Selective Processing and Metabolism of Disease-Causing Mutant Prion Proteins

Ashok, A., & Hegde, R. S. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000479 · Cited by 115 · see citing works

Conditions of Endoplasmic Reticulum Stress Favor the Accumulation of Cytosolic Prion Protein

Orsi, A., Fioriti, L., Chiesa, R., & Sitia, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605320200 · Cited by 114 · see citing works

Uncoupling retro‐translocation and degradation in the ER‐associated degradation of a soluble protein

Lee, R. J., Liu, C., Harty, C., McCracken, A. A., Latterich, M., Römisch, K., Demartino, G., Thomas, P., & Brodsky, J. L. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600232 · Cited by 113 · see citing works

Derlin-1 Facilitates the Retro-Translocation of Cholera Toxin

Bernardi, K. M., Forster, M. L., Lencer, W. I., & Tsai, B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-08-0755 · Cited by 112 · see citing works

Unassisted translocation of large polypeptide domains across phospholipid bilayers

Brambillasca, S., Yabal, M., Makarow, M., & Borgese, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608101 · Cited by 109 · see citing works

Protein Unfolding Is Not a Prerequisite for Endoplasmic Reticulum-to-Cytosol Dislocation

Tirosh, B., Furman, M. H., Tortorella, D., & Ploegh, H. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210158200 · Cited by 98 · see citing works

Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum

Binette, J., Dubé, M., Mercier, J., Halawani, D., Latterich, M., & Cohen, É. A. (2007) · Retrovirology · doi:10.1186/1742-4690-4-75 · Cited by 97 · see citing works

Protein Quality Control as a Strategy for Cellular Regulation: Lessons from Ubiquitin-Mediated Regulation of the Sterol Pathway

Hampton, R. Y., & Garza, R. M. (2009) · Chemical Reviews · doi:10.1021/cr800544v · Cited by 92 · see citing works

Lipid‐mediated, reversible misfolding of a sterol‐sensing domain protein

Shearer, A. G., & Hampton, R. Y. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600498 · Cited by 71 · see citing works

The role of MRH domain-containing lectins in ERAD

Hosokawa, N., Kamiya, Y., & Kato, K. (2010) · Glycobiology · doi:10.1093/glycob/cwq013 · Cited by 71 · see citing works

Protein disulphide isomerase is required for signal peptide peptidase‐mediated protein degradation

Lee, S.-O., Cho, K., Cho, S., Kim, I., Oh, C., & Ahn, K. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.359 · Cited by 70 · see citing works

INSIG: a broadly conserved transmembrane chaperone for sterol‐sensing domain proteins

Flury, I., Garza, R. M., Shearer, A. G., Rosen, J., Cronin, S. R., & Hampton, R. Y. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600855 · Cited by 70 · see citing works

The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation

Mikami, K., Yamaguchi, D., Tateno, H., Hu, D., Qin, S.-Y., Kawasaki, N., Yamada, M., Matsumoto, N., Hirabayashi, J., Ito, Y., et al. (2009) · Glycobiology · doi:10.1093/glycob/cwp175 · Cited by 66 · see citing works

A Proteasomal ATPase Contributes to Dislocation of Endoplasmic Reticulum-associated Degradation (ERAD) Substrates

Lipson, C., Alalouf, G., Bajorek, M., Rabinovich, E., Atir-Lande, A., Glickman, M. H., & Bar‐Nun, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705893200 · Cited by 65 · see citing works

Modularity of the Hrd1 ERAD complex underlies its diverse client range

Kanehara, K., Xie, W., & Ng, D. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200907055 · Cited by 63 · see citing works

The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum − a quantitative approach

Weitzmann, A., Baldes, C., Dudek, J., & Zimmermann, R. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06039.x · Cited by 59 · see citing works

The Viral E3 Ubiquitin Ligase mK3 Uses the Derlin/p97 Endoplasmic Reticulum-associated Degradation Pathway to Mediate Down-regulation of Major Histocompatibility Complex Class I Proteins

Wang, X., Ye, Y., Lencer, W. I., & Hansen, T. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513920200 · Cited by 58 · see citing works

Evasion of Endoplasmic Reticulum Surveillance Makes Wsc1p an Obligate Substrate of Golgi Quality Control

Wang, S., & Ng, D. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-10-0910 · Cited by 54 · see citing works

Glycoprotein Tertiary and Quaternary Structures Are Monitored by the Same Quality Control Mechanism

Keith, N., Parodi, A. J., & Caramelo, J. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501710200 · Cited by 41 · see citing works

Lectins of the ER Quality Control Machinery

Jakob, C. A., Chevet, É., Thomas, D. Y., & Bergeron, J. J. M. (2001) · Results and problems in cell differentiation · doi:10.1007/978-3-540-46410-5_1 · Cited by 20 · see citing works

Quality Control in the Endoplasmic Reticulum: Crosstalk between ERAD and UPR pathways

Hwang, J., & Qi, L. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.06.005 · Cited by 596 · see citing works

Endoplasmic Reticulum Stress Responses in Plants

Howell, S. H. (2013) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050312-120053 · Cited by 564 · see citing works

Protein Folding and Quality Control in the ERPreprint

Araki, K., & Nagata, K. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007526 · Cited by 422 · see citing works

Organizing Principles of Mammalian Nonsense-Mediated mRNA Decay

Popp, M. W., & Maquat, L. E. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-111212-133424 · Cited by 371 · see citing works

Membrane Protein Insertion at the Endoplasmic Reticulum

Shao, S., & Hegde, R. S. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154125 · Cited by 287 · see citing works

Identification of Downstream Components of Ubiquitin-Conjugating Enzyme PHOSPHATE2 by Quantitative Membrane Proteomics in Arabidopsis Roots

Huang, T., Han, C., Lin, S.-I., Chen, Y., Tsai, Y.-C., Chen, Y., Chen, J.-W., Lin, W., Chen, P.-M., Liu, T., et al. (2013) · The Plant Cell · doi:10.1105/tpc.113.115998 · Cited by 283 · see citing works

Structure and Assembly Pathway of the Ribosome Quality Control Complex

Shao, S., Brown, A., Santhanam, B., & Hegde, R. S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.015 · Cited by 225 · see citing works

Signaling Pathways from the Endoplasmic Reticulum and Their Roles in Disease

Kadowaki, H., & Nishitoh, H. (2013) · Genes · doi:10.3390/genes4030306 · Cited by 197 · see citing works

Modulation of ER stress and apoptosis by endoplasmic reticulum calcium leak via translocon during unfolded protein response: involvement of GRP78

Hammadi, M., Oulidi, A., Gackière, F., Katsogiannou, M., Slomianny, C., Roudbaraki, M. M., Dewailly, E., Delcourt, P., Lepage, G., Lotteau, S. J., et al. (2013) · The FASEB Journal · doi:10.1096/fj.12-218875 · Cited by 176 · see citing works

Deubiquitinating enzyme OTUB1 promotes cancer cell immunosuppression via preventing ER-associated degradation of immune checkpoint protein PD-L1

Zhu, D., Xu, R., Huang, X., Tang, Z., Tian, Y., Zhang, J., & Zheng, X. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00700-z · Cited by 179 · see citing works

The Rice CK2 Kinase Regulates Trafficking of Phosphate Transporters in Response to Phosphate Levels

Chen, J., Wang, Y., Wang, F., Yang, J., Gao, M., Li, C., Liu, Y., Liu, Y., Yamaji, N., Feng, J. X., et al. (2015) · The Plant Cell · doi:10.1105/tpc.114.135335 · Cited by 175 · see citing works

ER Stress-Induced Clearance of Misfolded GPI-Anchored Proteins via the Secretory Pathway

Satpute‐Krishnan, P., Ajinkya, M., Bhat, S., Itakura, E., Hegde, R. S., & Lippincott‐Schwartz, J. (2014) · Cell · doi:10.1016/j.cell.2014.06.026 · Cited by 171 · see citing works

The VLDL receptor promotes lipotoxicity and increases mortality in mice following an acute myocardial infarction

Perman, J., Boström, P., Lindbom, M., Lidberg, U., Ståhlman, M., Hägg, D. A., Lindskog, H., Täng, M. S., Ömerovic, E., Hultén, L. M., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43068 · Cited by 168 · see citing works

Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation

Bersuker, K., & Olzmann, J. A. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2017.06.006 · Cited by 160 · see citing works

BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol

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