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The Delicate Balance Between Secreted Protein Folding and Endoplasmic Reticulum-Associated Degradation in Human Physiology
Open accessAbstract
Protein folding is a complex, error-prone process that often results in an irreparable protein by-product. These by-products can be recognized by cellular quality control machineries and targeted for proteasome-dependent degradation. The folding of proteins in the secretory pathway adds another layer to the protein folding “problem,” as the endoplasmic reticulum maintains a unique chemical environment within the cell. In fact, a growing number of diseases are attributed to defects in secretory protein folding, and many of these by-products are targeted for a process known as endoplasmic reticulum-associated degradation (ERAD). Since its discovery, research on the mechanisms underlying the ERAD pathway has provided new insights into how ERAD contributes to human health during both normal and diseases states. Links between ERAD and disease are evidenced from the loss of protein function as a result of degradation, chronic cellular stress when ERAD fails to keep up with misfolded protein production, and the ability of some pathogens to coopt the ERAD pathway. The growing number of ERAD substrates has also illuminated the differences in the machineries used to recognize and degrade a vast array of potential clients for this pathway. Despite all that is known about ERAD, many questions remain, and new paradigms will likely emerge. Clearly, the key to successful disease treatment lies within defining the molecular details of the ERAD pathway and in understanding how this conserved pathway selects and degrades an innumerable cast of substrates.
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Cites
Diagnosis and Classification of Diabetes Mellitus
American Diabetes Association (2011) · Diabetes Care · doi:10.2337/dc11-s062 · Cited by 13,988
Calcium signalling: dynamics, homeostasis and remodelling
Berridge, M. J., Bootman, M. D., & Roderick, H. L. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1155 · Cited by 5,585
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,860
Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
Hotamisligil, G. S. (2010) · Cell · doi:10.1016/j.cell.2010.02.034 · Cited by 2,802
Haberland, M., Montgomery, R. L., & Olson, E. N. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,526
Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., & Goldberg, A. L. (1994) · Cell · doi:10.1016/s0092-8674(94)90462-6 · Cited by 2,524
Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., & Aronin, N. (1997) · Science · doi:10.1126/science.277.5334.1990 · Cited by 2,439
A "Silent" Polymorphism in the MDR 1 Gene Changes Substrate Specificity
Kimchi-Sarfaty, C., Oh, J. M., Kim, I.-W., Sauna, Z. E., Calcagno, A. M., Ambudkar, S. V., & Gottesman, M. M. (2007) · Science · doi:10.1126/science.1135308 · Cited by 2,416
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
Bence, N. F., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,187
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
From endoplasmic-reticulum stress to the inflammatory response
Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010
Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,001
Travers, K. J., Patil, C. K., Wodicka, L., Lockhart, D. J., Weissman, J. S., & Walter, P. (2000) · Cell · doi:10.1016/s0092-8674(00)80835-1 · Cited by 1,992
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979
Diagnosis and classification of diabetes mellitus
American Diabetes Association (2009) · Diabetes Care · doi:10.2337/dc09-s062 · Cited by 1,817
Cheng, S. H., Gregory, R. J., Marshall, J., Paul, S., Souza, D. W., White, G. A., O'Riordan, C. R., & Smith, A. E. (1990) · Cell · doi:10.1016/0092-8674(90)90148-8 · Cited by 1,792
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,716
Saudou, F., Finkbeiner, S., Devys, D., & Greenberg, M. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81782-1 · Cited by 1,595
Molecular Chaperones and Protein Quality Control
Bukau, B., Weissman, J., & Horwich, A. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,557
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
Schubert, U., Antón, L. C., Gibbs, J., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,536
Defining the Human Deubiquitinating Enzyme Interaction Landscape
Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,512
Proteasome inhibitors: valuable new tools for cell biologists.
Lee, D. H., & Goldberg, A. L. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01346-4 · Cited by 1,474
The ubiquitin-proteasome pathway: on protein death and cell life
Ciechanover, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7151 · Cited by 1,426
Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391
IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response
Lin, J. H., Li, H., Yasumura, D., Cohen, H. R., Zhang, C., Panning, B., Shokat, K. M., LaVail, M. M., & Walter, P. (2007) · Science · doi:10.1126/science.1146361 · Cited by 1,370
FDA Approval Summary: Vorinostat for Treatment of Advanced Primary Cutaneous T-Cell Lymphoma
Mann, B. S., Johnson, J. R., Cohen, M. H., Justice, R., & Pazdur, R. (2007) · The Oncologist · doi:10.1634/theoncologist.12-10-1247 · Cited by 1,365
Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A., & Ichijo, H. (2002) · Genes & Development · doi:10.1101/gad.992302 · Cited by 1,338
Kozutsumi, Y., Segal, M., Normington, K., Gething, M.-J., & Sambrook, J. (1988) · Nature · doi:10.1038/332462a0 · Cited by 1,321
Glutamine Repeats and Neurodegeneration
Zoghbi, H. Y., & Orr, H. T. (2000) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.23.1.217 · Cited by 1,309
Degradation of CFTR by the ubiquitin-proteasome pathway
Ward, C. L., Omura, S., & Kopito, R. R. (1995) · Cell · doi:10.1016/0092-8674(95)90240-6 · Cited by 1,304
The human ATP-binding cassette (ABC) transporter superfamily
Dean, M., Hamon, Y., & Chimini, G. (2001) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31588-1 · Cited by 1,302
Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
Denning, G. M., Anderson, M. P., Amara, J. F., Marshall, J., Smith, A. E., & Welsh, M. J. (1992) · Nature · doi:10.1038/358761a0 · Cited by 1,234
Cox, J. S., Shamu, C. E., & Walter, P. (1993) · Cell · doi:10.1016/0092-8674(93)90648-a · Cited by 1,231
Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator, VX-770
Van Goor, F., Hadida, S., Grootenhuis, P. D. J., Burton, B., Cao, D., Neuberger, T., Turnbull, A., Singh, A., Joubran, J., Hazlewood, A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904709106 · Cited by 1,228
Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.092707.153558 · Cited by 1,163
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
Severe acute respiratory syndrome
Peiris, J. S. M., Guan, Y., & Yuen, K. Y. (2004) · Nature Medicine · doi:10.1038/nm1143 · Cited by 1,139
Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., & Peng, J. (2009) · Cell · doi:10.1016/j.cell.2009.01.041 · Cited by 1,136
The Human ATP-Binding Cassette (ABC) Transporter Superfamily
Dean, M. (2001) · Genome Research · doi:10.1101/gr.gr-1649r · Cited by 1,113
Wiertz, E. J. H. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A., & Ploegh, H. L. (1996) · Nature · doi:10.1038/384432a0 · Cited by 1,105
Pathways of chaperone-mediated protein folding in the cytosol
Young, J. C., Agashe, V. R., Siegers, K., & Hartl, F. U. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1492 · Cited by 1,105
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099
Structure of a serpin–protease complex shows inhibition by deformation
Huntington, J. A., Read, R. J., & Carrell, R. W. (2000) · Nature · doi:10.1038/35038119 · Cited by 1,093
Wiertz, E. J. H. J., Jones, T. R., Sun, L., Bogyo, M., Geuze, H. J., & Ploegh, H. L. (1996) · Cell · doi:10.1016/s0092-8674(00)81054-5 · Cited by 1,072
A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly
Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,056
The mechanism of Z α1-antitrypsin accumulation in the liver
Lomas, D. A., LI-Evans, D., Finch, J. T., & Carrell, R. W. (1992) · Nature · doi:10.1038/357605a0 · Cited by 1,053
Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., & Takahashi, R. (2001) · Cell · doi:10.1016/s0092-8674(01)00407-x · Cited by 1,050
Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome
Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075898 · Cited by 1,000
Lithium induces autophagy by inhibiting inositol monophosphatase
Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
Ye, Y., Shibata, Y., Yun, C., Ron, D., & Rapoport, T. A. (2004) · Nature · doi:10.1038/nature02656 · Cited by 963
Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L.-Y., & Patterson, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4535 · Cited by 943
Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
Jensen, T. J., Loo, M. A., Pind, S., Williams, D. B., Goldberg, A. L., & Riordan, J. R. (1995) · Cell · doi:10.1016/0092-8674(95)90241-4 · Cited by 897
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Immunoglobulin heavy chain binding protein
Haas, I. G., & Wabl, M. (1983) · Nature · doi:10.1038/306387a0 · Cited by 845
Calcium signaling: A tale for all seasons
Carafoli, E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032427999 · Cited by 844
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., & Cyr, D. M. (2001) · Nature Cell Biology · doi:10.1038/35050509 · Cited by 839
Morl, K., Ma, W., Gething, M.-J., & Sambrook, J. (1993) · Cell · doi:10.1016/0092-8674(93)90521-q · Cited by 818
Endoplasmic Reticulum Stress in Disease Pathogenesis
Lin, J. H., Walter, P., & Yen, T. S. B. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.151434 · Cited by 807
n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
RIGGS, M. G., WHITTAKER, R. G., NEUMANN, J. R., & INGRAM, V. M. (1977) · Nature · doi:10.1038/268462a0 · Cited by 787
Inositol trisphosphate and calcium signalling mechanisms
Berridge, M. J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.005 · Cited by 777
Imai, Y., Soda, M., & Takahashi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000447200 · Cited by 766
Peptide-binding specificity of the molecular chaperone BiP
Flynn, G. C., Pohl, J., Flocco, M. T., & Rothman, J. E. (1991) · Nature · doi:10.1038/353726a0 · Cited by 765
A Transmembrane Form of the Prion Protein in Neurodegenerative Disease
Hegde, R. S., Mastrianni, J. A., Scott, M. R., DeFea, K. A., Tremblay, P., Torchia, M., DeArmond, S. J., Prusiner, S. B., & Lingappa, V. R. (1998) · Science · doi:10.1126/science.279.5352.827 · Cited by 729
A cryptic protease couples deubiquitination and degradation by the proteasome
Yao, T., & Cohen, R. E. (2002) · Nature · doi:10.1038/nature01071 · Cited by 725
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
Hiller, M. M., Finger, A., Schweiger, M., & Wolf, D. H. (1996) · Science · doi:10.1126/science.273.5282.1725 · Cited by 708
Altered chloride ion channel kinetics associated with the ΔF508 cystic fibrosis mutation
Dalemans, W., Barbry, P., Champigny, G., Jallat, S., Jallat, S., Dott, K., Dreyer, D., Crystal, R. G., Pavirani, A., Lecocq, J.-P., et al. (1991) · Nature · doi:10.1038/354526a0 · Cited by 707
The ABC protein turned chloride channel whose failure causes cystic fibrosis
Gadsby, D. C., Vergani, P., & Csanády, L. (2006) · Nature · doi:10.1038/nature04712 · Cited by 703
Quality control in the endoplasmic reticulum protein factory
Sitia, R., & Braakman, I. (2003) · Nature · doi:10.1038/nature02262 · Cited by 688
Calcium Pumps in Health and Disease
Brini, M., & Carafoli, E. (2009) · Physiological Reviews · doi:10.1152/physrev.00032.2008 · Cited by 676
A membrane protein required for dislocation of misfolded proteins from the ER
Lilley, B. N., & Ploegh, H. L. (2004) · Nature · doi:10.1038/nature02592 · Cited by 674
Margottin, F., Bour, S. P., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., & Benarous, R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80056-8 · Cited by 672
Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation
Hatahet, F., & Ruddock, L. W. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2466 · Cited by 670
Proteasome subunit Rpn13 is a novel ubiquitin receptor
Husnjak, K., Elsasser, S., Zhang, N., Chen, X., Randles, L., Shi, Y., Hofmann, K., Walters, K. J., Finley, D., & Dikic, I. (2008) · Nature · doi:10.1038/nature06926 · Cited by 660
Protein Glucosylation and Its Role in Protein Folding
Parodi, A. J. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.69 · Cited by 658
Blond-Elguindi, S. (1993) · Cell · doi:10.1016/0092-8674(93)90492-9 · Cited by 645
The Signal Recognition Particle
Keenan, R. J., Freymann, D. M., Stroud, R. M., & Walter, P. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.755 · Cited by 633
A common mechanism of action for three mood-stabilizing drugs
Williams, R. S. B., Cheng, L., Mudge, A. W., & Harwood, A. J. (2002) · Nature · doi:10.1038/417292a · Cited by 618
The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, D. T. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 615
Fan, J.-Q., Ishii, S., Asano, N., & Suzuki, Y. (1999) · Nature Medicine · doi:10.1038/4801 · Cited by 614
CFTR Function and Prospects for Therapy
Riordan, J. R. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142532 · Cited by 610
Hidvegi, T., Ewing, M., Hale, P., Dippold, C., Beckett, C., Kemp, C., Maurice, N., Mukherjee, A., Goldbach, C., Watkins, S., et al. (2010) · Science · doi:10.1126/science.1190354 · Cited by 607
Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., Gurkan, C., Kellner, W., Matteson, J., Plutner, H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.043 · Cited by 601
On the mechanism of sensing unfolded protein in the endoplasmic reticulum
Credle, J. J., Finer-Moore, J. S., Papa, F. R., Stroud, R. M., & Walter, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509487102 · Cited by 587
The Sizes of Peptides Generated from Protein by Mammalian 26 and 20 S Proteasomes
Kisselev, A. F., Akopian, T. N., Woo, K. M., & Goldberg, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3363 · Cited by 573
Wang, J., Takeuchi, T., Tanaka, S., Kubo, S.-K., Kayo, T., Lu, D., Takata, K., Koizumi, A., & Izumi, T. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4431 · Cited by 571
Morello, J.-P., Salahpour, A., Laperrière, A., Bernier, V., Arthus, M.-F., Lonergan, M., Petäjä-Repo, U., Angers, S., Morin, D., Bichet, D. G., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8688 · Cited by 565
Curcumin, a Major Constituent of Turmeric, Corrects Cystic Fibrosis Defects
Egan, M. E., Pearson, M., Weiner, S. A., Rajendran, V., Rubin, D., Glöckner-Pagel, J., Canny, S., Du, K., Lukacs, G. L., & Caplan, M. J. (2004) · Science · doi:10.1126/science.1093941 · Cited by 562
Association of folding intermediates of glycoproteins with calnexin during protein maturation
Ou, W.-J., Cameron, P. H., Thomas, D. Y., & Bergeron, J. J. M. (1993) · Nature · doi:10.1038/364771a0 · Cited by 559
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
Plemper, R. K., Böhmler, S., Bordallo, J., Sommer, T., & Wolf, D. H. (1997) · Nature · doi:10.1038/42276 · Cited by 555
Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
Willey, R. L., Maldarelli, F., Martin, M. A., & Strebel, K. (1992) · Journal of Virology · doi:10.1128/jvi.66.12.7193-7200.1992 · Cited by 554
Wandinger, S. K., Richter, K., & Buchner, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800007200 · Cited by 546
Rabinovich, E., Kerem, A., Fröhlich, K.-U., Diamant, N., & Bar-Nun, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.2.626-634.2002 · Cited by 546
Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1
Panaretou, B., Siligardi, G., Meyer, P., Maloney, A., Sullivan, J. K., Singh, S., Millson, S. H., Clarke, P. A., Naaby-Hansen, S., Stein, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00785-2 · Cited by 542
Pedemonte, N. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24898 · Cited by 538
Selective Inhibition of a Regulatory Subunit of Protein Phosphatase 1 Restores Proteostasis
Tsaytler, P., Harding, H. P., Ron, D., & Bertolotti, A. (2011) · Science · doi:10.1126/science.1201396 · Cited by 536
Ubiquitin: Same Molecule, Different Degradation Pathways
Clague, M. J., & Urbé, S. (2010) · Cell · doi:10.1016/j.cell.2010.11.012 · Cited by 533
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
Jarosch, E., Taxis, C., Volkwein, C., Bordallo, J., Finley, D., Wolf, D. H., & Sommer, T. (2002) · Nature Cell Biology · doi:10.1038/ncb746 · Cited by 532
Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523
OKADA, T., YOSHIDA, H., AKAZAWA, R., NEGISHI, M., & MORI, K. (2002) · Biochemical Journal · doi:10.1042/bj20020391 · Cited by 522
Glycerol Reverses the Misfolding Phenotype of the Most Common Cystic Fibrosis Mutation
Sato, S., Ward, C. L., Krouse, M. E., Wine, J. J., & Kopito, R. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.635 · Cited by 519
Van Goor, F., Straley, K. S., Cao, D., González, J., Hadida, S., Hazlewood, A., Joubran, J., Knapp, T., Makings, L. R., Miller, M., et al. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00169.2005 · Cited by 512
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
Sawkar, A. R., Cheng, W.-C., Beutler, E., Wong, C.-H., Balch, W. E., & Kelly, J. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192582899 · Cited by 503
Global changes to the ubiquitin system in Huntington's disease
Bennett, E. J., Shaler, T. A., Woodman, B., Ryu, K.-Y., Zaitseva, T. S., Becker, C. H., Bates, G. P., Schulman, H., & Kopito, R. R. (2007) · Nature · doi:10.1038/nature06022 · Cited by 497
Chloride Conductance Expressed by ΔF508 and Other Mutant CFTRs In Xenopus Oocytes
Drumm, M. L., Wilkinson, D. J., Smit, L. S., Worrell, R. T., Strong, T. V., Frizzell, R. A., Dawson, D. C., & Collins, F. S. (1991) · Science · doi:10.1126/science.1722350 · Cited by 496
Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins
LIPPINCOTTSCHWARTZ, J. (1988) · Cell · doi:10.1016/0092-8674(88)90553-3 · Cited by 493
N-glycan structures: recognition and processing in the ER
Aebi, M., Bernasconi, R., Clerc, S., & Molinari, M. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.10.001 · Cited by 489
The Biological and Chemical Basis for Tissue-Selective Amyloid Disease
Sekijima, Y., Wiseman, R. L., Matteson, J., Hammarström, P., Miller, S. R., Sawkar, A. R., Balch, W. E., & Kelly, J. W. (2005) · Cell · doi:10.1016/j.cell.2005.01.018 · Cited by 488
Neurotoxicity and Neurodegeneration When PrP Accumulates in the Cytosol
Ma, J., Wollmann, R., & Lindquist, S. (2002) · Science · doi:10.1126/science.1073725 · Cited by 487
Ward, C. L., & Kopito, R. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47306-1 · Cited by 486
Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin
Tsai, B., Rodighiero, C., Lencer, W. I., & Rapoport, T. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00289-6 · Cited by 483
The Role of Endoplasmic Reticulum Stress in the Progression of Atherosclerosis
Tabas, I. (2010) · Circulation Research · doi:10.1161/circresaha.110.224766 · Cited by 480
Mechanisms of neurodegeneration in Huntington’s disease
Gil, J. M., & Rego, A. C. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06310.x · Cited by 471
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., & Hampton, R. Y. (2001) · Nature Cell Biology · doi:10.1038/35050524 · Cited by 465
Curcumin as a therapeutic agent: the evidence from in vitro, animal and human studies
Epstein, J., Sanderson, I. R., & MacDonald, T. T. (2010) · British Journal of Nutrition · doi:10.1017/s0007114509993667 · Cited by 464
Werner, E. D., Brodsky, J. L., & McCracken, A. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13797 · Cited by 462
Self-citationFisher, E. A., & Ginsberg, H. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100068200 · Cited by 460
Brusilow, S. W. (2001) · Medical Entomology and Zoology · Cited by 456
Swanson, R., Locher, M., & Hochstrasser, M. (2001) · Genes & Development · doi:10.1101/gad.933301 · Cited by 455
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
Younger, J. M., Chen, L., Ren, H.-Y., Rosser, M. F. N., Turnbull, E. L., Fan, C.-Y., Patterson, C., & Cyr, D. M. (2006) · Cell · doi:10.1016/j.cell.2006.06.041 · Cited by 440
Endoplasmic reticulum stress in health and disease
Zhao, L., & Ackerman, S. L. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.005 · Cited by 440
Protein folding and quality control in the endoplasmic reticulum
Kleizen, B., & Braakman, I. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.06.012 · Cited by 439
Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437
Pincus, D., Chevalier, M. W., Aragón, T., van Anken, E., Vidal, S. E., El-Samad, H., & Walter, P. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000415 · Cited by 431
Celastrols as Inducers of the Heat Shock Response and Cytoprotection
Westerheide, S. D., Bosman, J. D., Mbadugha, B. N. A., Kawahara, T. L. A., Matsumoto, G., Kim, S., Gu, W., Devlin, J. P., Silverman, R. B., & Morimoto, R. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409267200 · Cited by 427
Burrows, J. A. J., Willis, L. K., & Perlmutter, D. H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1796 · Cited by 426
The surprising complexity of signal sequences
Hegde, R. S., & Bernstein, H. D. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.08.004 · Cited by 424
Brown, C. R., Hong-Brown, L. Q., Biwersi, J., Verkman, A. S., & Welch, W. J. (1996) · Cell Stress & Chaperones · doi:10.1379/1466-1268(1996)001<0117:ccctmp>2.3.co;2 · Cited by 417
Melnick, J., Dul, J. L., & Argon, Y. (1994) · Nature · doi:10.1038/370373a0 · Cited by 417
ER-associated degradation in protein quality control and cellular regulation
Hampton, R. Y. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00358-7 · Cited by 415
The human PDI family: Versatility packed into a single fold
Appenzeller-Herzog, C., & Ellgaard, L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.11.010 · Cited by 415
Jones, T. R., Wiertz, E. J., Sun, L., Fish, K. N., Nelson, J. A., & Ploegh, H. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11327 · Cited by 414
Fang, S., Ferrone, M., Yang, C., Jensen, J. P., Tiwari, S., & Weissman, A. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251401598 · Cited by 413
Scheuner, D., Mierde, D. V., Song, B., Flamez, D., Creemers, J. W. M., Tsukamoto, K., Ribick, M., Schuit, F. C., & Kaufman, R. J. (2005) · Nature Medicine · doi:10.1038/nm1259 · Cited by 412
Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.
McCracken, A. A., & Brodsky, J. L. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.3.291 · Cited by 409
Self-citationPeripheral Protein Quality Control Removes Unfolded CFTR from the Plasma Membrane
Okiyoneda, T., Barrière, H., Bagdány, M., Rabeh, W. M., Du, K., Höhfeld, J., Young, J. C., & Lukacs, G. L. (2010) · Science · doi:10.1126/science.1191542 · Cited by 408
Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase
Cadwell, K., & Coscoy, L. (2005) · Science · doi:10.1126/science.1110340 · Cited by 406
Pilon, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4540 · Cited by 404
That which does not kill me makes me stronger: adapting to chronic ER stress
Rutkowski, D. T., & Kaufman, R. J. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.003 · Cited by 398
Lukacs, G. L., Mohamed, A., Kartner, N., Chang, X. B., Riordan, J. R., & Grinstein, S. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06954.x · Cited by 396
PROTEIN TRANSLOCATION BY THE SEC61/SECY CHANNEL
Osborne, A. R., Rapoport, T. A., & van den Berg, B. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.012704.133214 · Cited by 391
Rubenstein, R. C., Egan, M. E., & Zeitlin, P. L. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119788 · Cited by 389
Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384
HERG Channel Dysfunction in Human Long QT Syndrome
Zhou, Z., Gong, Q., Epstein, M. L., & January, C. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.21061 · Cited by 383
Reggiori, F., Monastyrska, I., Verheije, M. H., Calì, T., Ulasli, M., Bianchi, S., Bernasconi, R., de Haan, C. A. M., & Molinari, M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.05.013 · Cited by 383
Serohijos, A. W. R., Hegedűs, T., Aleksandrov, A. A., He, L., Cui, L., Dokholyan, N. V., & Riordan, J. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800254105 · Cited by 381
Waheed, A., Parkkila, S., Zhou, X. Y., Tomatsu, S., Tsuchihashi, Z., Feder, J. N., Schatzman, R. C., Britton, R. S., Bacon, B. R., & Sly, W. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12384 · Cited by 380
Rational design of potent human transthyretin amyloid disease inhibitors.
Sacchettini, J. C., Klabunde, T., Petrassi, H. M., Oza, V. B., Raman, P., & Kelly, J. W. (2000) · Nature Structural Biology · doi:10.1038/74082 · Cited by 379
Mori, K., Sant, A., Kohno, K., Normington, K., Gething, M. J., & Sambrook, J. F. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05323.x · Cited by 374
Zhou, J., Liu, C. Y., Back, S. H., Clark, R. L., Peisach, D., Xu, Z., & Kaufman, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606480103 · Cited by 374
Loo, M. A., Jensen, T. J., Cui, L., Hou, Y.-X., Chang, X.-B., & Riordan, J. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.6879 · Cited by 374
Many Random Sequences Functionally Replace the Secretion Signal Sequence of Yeast Invertase
Kaiser, C. A., Preuss, D., Grisafi, P., & Botstein, D. (1987) · Science · doi:10.1126/science.3541205 · Cited by 367
Qu, D., Teckman, J. H., Omura, S., & Perlmutter, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22791 · Cited by 366
Selkoe, D. J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004457 · Cited by 363
Chemical and Biological Approaches Synergize to Ameliorate Protein-Folding Diseases
Mu, T.-W., Ong, D. S. T., Wang, Y.-J., Balch, W. E., Yates, J. R., Segatori, L., & Kelly, J. W. (2008) · Cell · doi:10.1016/j.cell.2008.06.037 · Cited by 359
Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
Hammarström, P., Jiang, X., Hurshman, A. R., Powers, E. T., & Kelly, J. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202495199 · Cited by 359
Kohno, K., Normington, K., Sambrook, J., Gething, M. J., & Mori, K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.877 · Cited by 358
Pind, S., Riordan, J. R., & Williams, D. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99944-8 · Cited by 357
Du, K., Sharma, M., & Lukacs, G. L. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb882 · Cited by 356
The Three-dimensional Crystal Structure of Cholera Toxin
Zhang, R.-G., Scott, D. L., Westbrook, M. L., Nance, S., Spangler, B. D., Shipley, G. G., & Westbrook, E. M. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0456 · Cited by 352
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 352
Christiansen, H. E., Schwarze, U., Pyott, S. M., AlSwaid, A., Al Balwi, M., Alrasheed, S., Pepin, M. G., Weis, M. A., Eyre, D. R., & Byers, P. H. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.034 · Cited by 352
Bouman, L., Schlierf, A., Lutz, A. K., Shan, J., Deinlein, A., Kast, J., Galehdar, Z., Palmisano, V, Patenge, N., Berg, D., et al. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.142 · Cited by 347
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D., Dikic, I., Walters, K. J., & Groll, M. (2008) · Nature · doi:10.1038/nature06924 · Cited by 343
Fujita, E., Kouroku, Y., Isoai, A., Kumagai, H., Misutani, A., Matsuda, C., Hayashi, Y. K., & Momoi, T. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm002 · Cited by 342
RUBENSTEIN, R. C., & ZEITLIN, P. L. (1998) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.157.2.9706088 · Cited by 340
Yang, Y., Janich, S., Cohn, J. A., & Wilson, J. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9480 · Cited by 337
The Hdj‐2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
Meacham, G. C., Lu, Z., King, S., Sorscher, E., Tousson, A., & Cyr, D. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1492 · Cited by 335
A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
Sommer, T., & Jentsch, S. (1993) · Nature · doi:10.1038/365176a0 · Cited by 333
Bulleid, N. J., & Freedman, R. B. (1988) · Nature · doi:10.1038/335649a0 · Cited by 333
Nishikawa, S.-I., Fewell, S. W., Kato, Y., Brodsky, J. L., & Endo, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.1061 · Cited by 330
Self-citationTamarappoo, B. K., & Verkman, A. S. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2303 · Cited by 329
Human genetics illuminates the paths to metabolic disease
O’Rahilly, S. (2009) · Nature · doi:10.1038/nature08532 · Cited by 324
Role of the Cytosolic Chaperones Hsp70 and Hsp90 in Maturation of the Cardiac Potassium Channel hERG
Ficker, E., Dennis, A. T., Wang, L., & Brown, A. M. (2003) · Circulation Research · doi:10.1161/01.res.0000079028.31393.15 · Cited by 323
Hazes, B., & Read, R. J. (1997) · Biochemistry · doi:10.1021/bi971383p · Cited by 317
Lilley, B. N., & Ploegh, H. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505014102 · Cited by 315
Illing, M. E., Rajan, R. S., Bence, N. F., & Kopito, R. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204955200 · Cited by 313
The many faces of β-TrCP E3 ubiquitin ligases: reflections in the magic mirror of cancer
Fuchs, S. Y., Spiegelman, V. S., & Suresh Kumar, K. G. (2004) · Oncogene · doi:10.1038/sj.onc.1207389 · Cited by 310
Conformational dynamics of the molecular chaperone Hsp90
Krukenberg, K. A., Street, T. O., Lavery, L. A., & Agard, D. A. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000314 · Cited by 308
Glucose stimulates proinsulin biosynthesis by a dose-dependent recruitment of pancreatic beta cells
Schuit, F. C., In't Veld, P. A., & Pipeleers, D. G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.3865 · Cited by 308
Genetic Modifiers of Liver Disease in Cystic Fibrosis
Bartlett, J. R. (2009) · JAMA · doi:10.1001/jama.2009.1295 · Cited by 308
Transmissible and genetic prion diseases share a common pathway of neurodegeneration
Hegde, R. S., Tremblay, P., Groth, D., DeArmond, S. J., Prusiner, S. B., & Lingappa, V. R. (1999) · Nature · doi:10.1038/45574 · Cited by 307
Kim, M., Lee, H.-S., LaForet, G., McIntyre, C., Martin, E. J., Chang, P., Kim, T. W., Williams, M., Reddy, P. H., Tagle, D., et al. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-03-00964.1999 · Cited by 305
A Stress-Responsive System for Mitochondrial Protein Degradation
Heo, J.-M., Livnat-Levanon, N., Taylor, E. B., Jones, K. T., Dephoure, N., Ring, J., Xie, J., Brodsky, J. L., Madeo, F., Gygi, S. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.021 · Cited by 304
Self-citationAckerman, A. L., Giodini, A., & Cresswell, P. (2006) · Immunity · doi:10.1016/j.immuni.2006.08.017 · Cited by 301
Kimata, Y., Ishiwata-Kimata, Y., Ito, T., Hirata, A., Suzuki, T., Oikawa, D., Takeuchi, M., & Kohno, K. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704166 · Cited by 300
Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
Duennwald, M. L., & Lindquist, S. (2008) · Genes & Development · doi:10.1101/gad.1673408 · Cited by 299
Retrotranslocation of a Misfolded Luminal ER Protein by the Ubiquitin-Ligase Hrd1p
Carvalho, P., Stanley, A. M., & Rapoport, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.028 · Cited by 298
Zhou, Z., Gong, Q., & January, C. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31123 · Cited by 298
Wu, Y., Whitman, I., Molmenti, E., Moore, K., Hippenmeyer, P., & Perlmutter, D. H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9014 · Cited by 290
Lehrman, M. A., Schneider, W. J., Brown, M. S., Davis, C. G., Elhammer, A., Russell, D. W., & Goldstein, J. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75941-9 · Cited by 282
Traffic Jam: A Compendium of Human Diseases that Affect Intracellular Transport Processes
Aridor, M., & Hannan, L. A. (2000) · Traffic · doi:10.1034/j.1600-0854.2000.011104.x · Cited by 278
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Howell, S. H. (2013) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050312-120053 · Cited by 560
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Metadata
- Authors
- Guerriero, C. J., & Brodsky, J. L.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2012-04
- Volume
- 92
- Issue
- 2
- Pages
- 537-576
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W1988364921
- Cited by
- 418
- References
- 552
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- green
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.