Quality control in the endoplasmic reticulum

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

Hammond, C., Braakman, I., & Helenius, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.913 · Cited by 841

Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus.

Hammond, C., & Helenius, A. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.1.41 · Cited by 443

Correcting temperature-sensitive protein folding defects

Brown, C. R., Hong-Brown, L. Q., & Welch, W. J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119302 · Cited by 176

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

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

The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus

Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173

Cell Wall Assembly in Saccharomyces cerevisiae

Lesage, G., & Bussey, H. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00038-05 · Cited by 849

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

Inside, outside, upside down: damage-associated molecular-pattern molecules (DAMPs) and redox

Rubartelli, A., & Lotze, M. T. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.08.004 · Cited by 614

Subunit-Specific NMDA Receptor Trafficking to Synapses

Barria, A., & Malinow, R. (2002) · Neuron · doi:10.1016/s0896-6273(02)00776-6 · Cited by 515

Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation

Nollen, E. A. A., Garcia, S. M., van Haaften, G., Kim, S., Chavez, A., Morimoto, R. I., & Plasterk, R. H. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307697101 · Cited by 416

Metabolic Labeling of Mammalian Organisms with Stable Isotopes for Quantitative Proteomic Analysis

Wu, C. C., MacCoss, M. J., Howell, K. E., Matthews, D. E., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac049208j · Cited by 386

Yeast viral killer toxins: lethality and self-protection

Schmitt, M. J., & Breinig, F. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1347 · Cited by 314

N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

Mitra, N., Sinha, S., Ramya, T. N. C., & Surolia, A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.003 · Cited by 302

Nicotine upregulates its own receptors through enhanced intracellular maturation

Sallette, J., Pons, S., Devillers-Thiery, A., Soudant, M., Prado de Carvalho, L., Changeux, J.-P., & Corringer, P. J. (2005) · Neuron · doi:10.1016/j.neuron.2005.03.029 · Cited by 261

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

Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control

Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., & Helenius, A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00494-5 · Cited by 221

Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors

Scott, D. B., Blanpied, T. A., & Ehlers, M. D. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00250-8 · Cited by 186

Xbp1-based engineering of secretory capacity enhances the productivity of Chinese hamster ovary cells

Tigges, M., & Fussenegger, M. (2006) · Metabolic Engineering · doi:10.1016/j.ymben.2006.01.006 · Cited by 178

Cooperative Assembly and Misfolding of CFTR Domains In Vivo

Du, K., & Lukacs, G. L. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-09-0950 · Cited by 147

Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation

Spear, E. D., & Ng, D. T. W. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200411136 · Cited by 110

Structure-dependent Impairment of Intracellular Apolipoprotein E4 Trafficking and Its Detrimental Effects Are Rescued by Small-molecule Structure Correctors

Brodbeck, J., McGuire, J., Liu, Z., Meyer-Franke, A., Balestra, M. E., Jeong, D.-E., Pleiss, M., McComas, C., Hess, F., Witter, D., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.217380 · Cited by 113

Melanocortin 1 receptor variants: Functional role and pigmentary associations

Dessinioti, C., Antoniou, C., Katsambas, A., & Stratigos, A. J. (2011) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2011.00970.x · Cited by 111

Folding Efficiency Is Rate-limiting in Dopamine D4 Receptor Biogenesis

Van Craenenbroeck, K., Clark, S. D., Cox, M. J., Oak, J. N., Liu, F., & Van Tol, H. H. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414043200 · Cited by 107

Diversity in Tissue Expression, Substrate Binding, and SCF Complex Formation for a Lectin Family of Ubiquitin Ligases

Glenn, K. A., Nelson, R. F., Wen, H. M., Mallinger, A. J., & Paulson, H. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709508200 · Cited by 86

Dissection of Ire1 Functions Reveals Stress Response Mechanisms Uniquely Evolved in Candida glabrata

Miyazaki, T., Nakayama, H., Nagayoshi, Y., Kakeya, H., & Kohno, S. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003160 · Cited by 78

The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding

Mysling, S., Kristensen, K. K., Larsson, M., Kovrov, O., Bensadouen, A., Jørgensen, T. J., Olivecrona, G., Young, S. G., & Ploug, M. (2016) · eLife · doi:10.7554/elife.20958 · Cited by 77

Exocytic trafficking is required for nicotine-induced up-regulation of α4β2 nicotinic acetylcholine receptors

Darsow, T., Booker, T. K., Piña-Crespo, J. C., & Heinemann, S. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501157200 · Cited by 76

Regulation of Angiopoietin-Like Proteins (ANGPTLs) 3 and 8 by Insulin

Nidhina Haridas, P. A., Soronen, J., Sädevirta, S., Mysore, R., Quagliarini, F., Pasternack, A., Metso, J., Perttilä, J., Leivonen, M., Smas, C. M., et al. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-1254 · Cited by 75

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

Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex

Staron, M., Wu, S., Hong, F., Stojanovic, A., Du, X., Bona, R., Liu, B., & Li, Z. (2011) · Blood · doi:10.1182/blood-2011-01-330464 · Cited by 61

Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway

Nassif, M., Matus, S., Castillo, K., & Hetz, C. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2991 · Cited by 60

ERAD ubiquitin ligases: Multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum

Mehnert, M., Sommer, T., & Jarosch, E. (2010) · BioEssays · doi:10.1002/bies.201000046 · Cited by 60

β-cell adaptation in a mouse model of glucocorticoid-induced metabolic syndrome

Fransson, L., Franzén, S., Rosengren, V., Wolbert, P., Sjöholm, Å., & Ortsäter, H. (2013) · Journal of Endocrinology · doi:10.1530/joe-13-0189 · Cited by 59

Boca‐dependent maturation of β‐propeller/EGF modules in low‐density lipoprotein receptor proteins

Culi, J., Springer, T. A., & Mann, R. S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600132 · Cited by 45

Deletion of Aspartate 182 in OPG Causes Juvenile Paget' Disease by Impairing Both Protein Secretion and Binding to RANKL

Middleton-Hardie, C., Zhu, Q., Cundy, H., Lin, J.-M., Callon, K., Tong, P. C., Xu, J., Grey, A., Cornish, J., & Naot, D. (2006) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.051104 · Cited by 41

Lipid remodeling and an altered membrane-associated proteome may drive the differential effects of EPA and DHA treatment on skeletal muscle glucose uptake and protein accretion

Jeromson, S., Mackenzie, I., Doherty, M. K., Whitfield, P. D., Bell, G., Dick, J., Shaw, A., Rao, F. V., Ashcroft, S. P., Philp, A., et al. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00438.2015 · Cited by 40

The effect of chronic ozone exposure on the activation of endoplasmic reticulum stress and apoptosis in rat hippocampus

Rodríguez-Martínez, E., Nava-Ruiz, C., Escamilla-Chimal, E., Borgonio-Perez, G., & Rivas-Arancibia, S. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00245 · Cited by 39

An IMiD-induced SALL4 degron system for selective degradation of target proteins

Yamanaka, S., Shoya, Y., Matsuoka, S., Nishida-Fukuda, H., Shibata, N., & Sawasaki, T. (2020) · Communications Biology · doi:10.1038/s42003-020-01240-5 · Cited by 29

Berberine induces hERG channel deficiency through trafficking inhibition

Zhang, K., Zhi, D., Huang, T., Gong, Y., Yan, M., Liu, C., Wei, T., Dong, Z., Li, B., & Yang, B. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000363034 · Cited by 26

Assorted dysfunctions of endosomal alkali cation/proton exchanger SLC9A6 variants linked to Christianson syndrome

Ilie, A., Boucher, A., Park, J., Berghuis, A. M., McKinney, R. A., & Orlowski, J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012614 · Cited by 24

The fine-tuning of proteolytic pathways in Alzheimer’s disease

Cecarini, V., Bonfili, L., Cuccioloni, M., Mozzicafreddo, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2238-6 · Cited by 21

Site-Directed Disulfide Mapping of Residues Contributing to the Ca2+ and K+ Binding Pocket of the NCKX2 Na+/Ca2+-K+ Exchanger

Kinjo, T. G., Kang, Szerencsei, R. T., Winkfein, R. J., & Schnetkamp, P. P. M. (2005) · Biochemistry · doi:10.1021/bi0502442 · Cited by 20

GPCR Oligomerization: Contribution to Receptor Biogenesis

Van Craenenbroeck, K. (2012) · Subcellular Biochemistry · doi:10.1007/978-94-007-4765-4_3 · Cited by 18

Proteolysis of type I inositol 1,4,5-trisphosphate receptor in WB rat liver cells

KHAN, M. T., & JOSEPH, S. K. (2003) · Biochemical Journal · doi:10.1042/bj20030828 · Cited by 13

Cytosolic and endoplasmic reticulum chaperones inhibit wt-p53 to increase cancer cells' survival by refluxing ER-proteins to the cytosol

Dabsan, S., Zur, G., Abu-Freha, N., Sofer, S., Grossman-Haham, I., Gilad, A., & Igbaria, A. (2025) · eLife · doi:10.7554/elife.102658 · Cited by 10

Membrane Expression Enhances Folding, Multimeric Structure Formation, and Immunogenicity of Viral Capsid Proteins

Cui, J., Yuan, F., Qin, J., Jeon, J. H., Yun, D. S., Wang, T., Xu, R., Cao, H., Tungate, A. A., Netherton, C. L., et al. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5c00067 · Cited by 1