The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Misfolded proteins partition between two distinct quality control compartments
Open accessAbstract
The accumulation of misfolded proteins in intracellular amyloid inclusions, typical of many neurodegenerative disorders including Huntington's and prion disease, is thought to occur after failure of the cellular protein quality control mechanisms. Here we examine the formation of misfolded protein inclusions in the eukaryotic cytosol of yeast and mammalian cell culture models. We identify two intracellular compartments for the sequestration of misfolded cytosolic proteins. Partition of quality control substrates to either compartment seems to depend on their ubiquitination status and aggregation state. Soluble ubiquitinated misfolded proteins accumulate in a juxtanuclear compartment where proteasomes are concentrated. In contrast, terminally aggregated proteins are sequestered in a perivacuolar inclusion. Notably, disease-associated Huntingtin and prion proteins are preferentially directed to the perivacuolar compartment. Enhancing ubiquitination of a prion protein suffices to promote its delivery to the juxtanuclear inclusion. Our findings provide a framework for understanding the preferential accumulation of amyloidogenic proteins in inclusions linked to human disease.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Having multi-valent binding ability for aberrant proteins, the small HSPs may act to seed and concentrate aggregate material, consistent with findings in vivo (Escusa-Toret et al., 2013; Kaganovich et al., 2008; Specht et al., 2011) and in vitro (Haslbeck et al., 2005; Jiao et al., 2005).”
From Widespread Proteome Remodeling and Aggregation in Aging C. elegans (2015) · cites this paper as Kaganovich et al., 2008
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedProtein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
Jacob, H. (1988) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(88)80052-7 · Cited by 4,911
Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N. G., Palmer, A. E., & Tsien, R. Y. (2004) · Nature Biotechnology · doi:10.1038/nbt1037 · Cited by 4,619
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Functional Characterization of the S. cerevisiae Genome by Gene Deletion and Parallel Analysis
Winzeler, E. A., Shoemaker, D. D., Astromoff, A., Liang, H., Anderson, K., Andre, B., Bangham, R., Benito, R., Boeke, J. D., Bussey, H., et al. (1999) · Science · doi:10.1126/science.285.5429.901 · Cited by 3,953
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209
Self-citationInclusion 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
Cited by
Sorted by citations
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Huntington's disease: from molecular pathogenesis to clinical treatment
Ross, C. A., & Tabrizi, S. J. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70245-3 · Cited by 1,816
The proteostasis network and its decline in ageing
Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642
Molecular Chaperone Functions in Protein Folding and Proteostasis
Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,545
In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,477
Proteasomal and Autophagic Degradation Systems
Đikić, I. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044908 · Cited by 1,217
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
Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,165
Liu, W. J., Ye, L., Huang, W. F., Guo, L. J., Xu, Z. G., Wu, H. L., Yang, C., & Liu, H. F. (2016) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-016-0031-z · Cited by 966
Cellular strategies for controlling protein aggregation
Tyedmers, J., Mogk, A., & Bukau, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2993 · Cited by 921
Pathways of cellular proteostasis in aging and disease
Klaips, C. L., Jayaraj, G. G., & Hartl, F. U. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201709072 · Cited by 835
Johnson, B. S., Snead, D., Lee, J. J., McCaffery, J. M., Shorter, J., & Gitler, A. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010264 · Cited by 812
The N‐end rule pathway and regulation by proteolysis
Varshavsky, A. J. (2011) · Protein Science · doi:10.1002/pro.666 · Cited by 721
Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
Maurer‐Stroh, S., Debulpaep, M., Kuemmerer, N., de la Paz, M. L., Martins, I. C., Reumers, J., Morris, K. L., Copland, A., Serpell, L. C., Serrano, L. G., et al. (2010) · Nature Methods · doi:10.1038/nmeth.1432 · Cited by 700
Protein misfolding in neurodegenerative diseases: Implications and strategies
Sweeney, P., Park, H., Baumann, M., Dunlop, J., Frydman, J., Kopito, R., McCampbell, A., Leblanc, G., Venkateswaran, A., Nurmi, A., et al. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0077-5 · Cited by 675
Self-citationProteostasis impairment in protein-misfolding and -aggregation diseases
Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 683
Widespread protein aggregation as an inherent part of aging in C. elegans
David, D. C., Ollikainen, N., Trinidad, J. C., Cary, M. P., Burlingame, A. L., & Kenyon, C. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000450 · Cited by 627
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Walther, D. M., Kasturi, P., Zheng, M., Pinkert, S., Vecchi, G., Ciryam, P., Morimoto, R. I., Dobson, C. M., Vendruscolo, M., Mann, M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.032 · Cited by 569
Kroschwald, S., Maharana, S., Matějů, D., Malinovska, L., Nüske, E., Poser, I., Richter, D., & Alberti, S. (2015) · eLife · doi:10.7554/elife.06807 · Cited by 545
Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., Martinez, G., Cuervo, A. M., Brown, R. H., & Glimcher, L. H. (2009) · Genes & Development · doi:10.1101/gad.1830709 · Cited by 530
mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding
Delarue, M., Brittingham, G. P., Pfeffer, S., Surovtsev, I. V., Pinglay, S., Kennedy, K. J., Schaffer, M., Gutierrez, J. I., Sang, D., Poterewicz, G., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.042 · Cited by 543
Haigis, M. C., & Yankner, B. A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.002 · Cited by 488
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522
Hartl, F. U. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044518 · Cited by 528
Cellular Strategies of Protein Quality ControlPreprint
Chen, B., Retzlaff, M., Roos, T. R., & Frydman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004374 · Cited by 515
Self-citationAmm, I., Sommer, T., & Wolf, D. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 509
Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 514
Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
Matějů, D., Franzmann, T. M., Patel, A., Kopach, A., Boczek, E. E., Maharana, S., Lee, H. O., Carra, S., Hyman, A. A., & Alberti, S. (2017) · The EMBO Journal · doi:10.15252/embj.201695957 · Cited by 496
Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation
Tamás, M. J., Sharma, S., Ibstedt, S., Jacobson, T., & Christen, P. (2014) · Biomolecules · doi:10.3390/biom4010252 · Cited by 487
The Ubiquitin–Proteasome System of Saccharomyces cerevisiae
Finley, D. J., Ulrich, H. D., Sommer, T., & Kaiser, P. (2012) · Genetics · doi:10.1534/genetics.112.140467 · Cited by 449
Protein Folding in the Cytoplasm and the Heat Shock ResponsePreprint
Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M. K., & Hartl, F. U. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004390 · Cited by 450
Liebman, S. W., & Chernoff, Y. O. (2012) · Genetics · doi:10.1534/genetics.111.137760 · Cited by 389
Sánchez‐Ruiz, J. M. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.02.004 · Cited by 369
Cellular Handling of Protein Aggregates by Disaggregation Machines
Mogk, A., Bukau, B., & Kampinga, H. H. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.004 · Cited by 369
Autophagy and the ubiquitin-proteasome system: Collaborators in neuroprotection
Nedelsky, N. B., Todd, P. K., & Taylor, J. P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.002 · Cited by 351
Lu, K., Psakhye, I., & Jentsch, S. (2014) · Cell · doi:10.1016/j.cell.2014.05.048 · Cited by 346
Mechanisms and functions of nuclear envelope remodelling
Ungricht, R., & Kutay, U. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.153 · Cited by 353
Protein Folding and Mechanisms of Proteostasis
Díaz‐Villanueva, J. F., Díaz-Molina, R. J., & García‐González, V. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160817193 · Cited by 354
Dantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 354
Functional AmyloidsPreprint
Otzen, D. E., & Riek, R. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033860 · Cited by 345
Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy
Tanik, S. A., Schultheiss, C. E., Volpicelli-Daley, L. A., Brunden, K. R., & Lee, V. M. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457408 · Cited by 326
Escusa-Toret, S., Vonk, W. I. M., & Frydman, J. (2013) · Nature Cell Biology · doi:10.1038/ncb2838 · Cited by 321
Self-citationBolognesi, B., Lorenzo-Gotor, N., Dhar, R., Cirillo, D., Baldrighi, M., Tartaglia, G. G., & Lehner, B. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.076 · Cited by 318
Aneuploidy causes proteotoxic stress in yeastPreprint
Oromendia, A. B., Dodgson, S. E., & Amon, A. (2012) · Genes & Development · doi:10.1101/gad.207407.112 · Cited by 307
Oxidative stress, inflamm-aging and immunosenescence
Cannizzo, E. S., Clement, C. C., Sahu, R. K., Follo, C., & Santambrogio, L. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.005 · Cited by 315
Targeting proteins for degradation.
Schrader, E. K., Harstad, K. G., & Matouschek, A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.250 · Cited by 287
Geiler‐Samerotte, K., Dion, M. F., Budnik, B., Wang, S. M., Hartl, D. L., & Drummond, D. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017570108 · Cited by 290
Proteotoxicity and Cardiac Dysfunction — Alzheimer's Disease of the Heart?
Willis, M. S., & Patterson, C. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1106180 · Cited by 284
Compartment‐specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition
Miller, S. B. M., Ho, C., Winkler, J., Khokhrina, M., Neuner, A., Mohamed, M. Y. H., Guilbride, D. L., Richter, K., Lisby, M., Schiebel, E., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201489524 · Cited by 278
Winkler, J., Seybert, A., König, L. M., Pruggnaller, S., Haselmann, U., Sourjik, V., Weiß, M., Frangakis, A. S., Mogk, A., & Bukau, B. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.412 · Cited by 277
The Ribosome as a Hub for Protein Quality Control
Pechmann, S., Willmund, F., & Frydman, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.020 · Cited by 278
Self-citationMechanisms and Functions of Spatial Protein Quality Control
Sontag, E. M., Samant, R. S., & Frydman, J. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014616 · Cited by 276
Self-citationScotter, E. L., Vance, C. A., Nishimura, A. L., Lee, Y., Chen, H.-J., Urwin, H., Sardone, V., Mitchell, J. C., Rogelj, B., Rubinsztein, D. C., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.140087 · Cited by 282
Specht, S., Miller, S. B. M., Mogk, A., & Bukau, B. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201106037 · Cited by 254
Unconventional Secretion Mediates the Trans-cellular Spreading of Tau
Katsinelos, T., Zeitler, M., Dimou, E., Karakatsani, A., Müller, H., Nachman, E., Steringer, J. P., de Almodóvar, C. R., Nickel, W., & Jahn, T. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.056 · Cited by 274
Diversity in the origins of proteostasis networks — a driver for protein function in evolution
Powers, E. T., & Balch, W. E. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3542 · Cited by 249
Differential Scales of Protein Quality Control
Wolff, S., Weissman, J. S., & Dillin, A. G. (2014) · Cell · doi:10.1016/j.cell.2014.03.007 · Cited by 251
Walking the tightrope: proteostasis and neurodegenerative disease
Yerbury, J. J., Ooi, L., Dillin, A. G., Saunders, D. N., Hatters, D. M., Beart, P. M., Cashman, N. R., Wilson, M. R., & Ecroyd, H. W. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13575 · Cited by 251
Brodsky, J. L., & Skach, W. R. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.05.004 · Cited by 250
Aggregation of Therapeutic Proteins
Wang, W., & Roberts, C. J. (2010) · Wiley eBooks · doi:10.1002/9780470769829 · Cited by 235
Proteome complexity and the forces that drive proteome imbalance
Harper, J. W., & Bennett, E. J. (2016) · Nature · doi:10.1038/nature19947 · Cited by 239
Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation
Marshall, R. S., & Vierstra, R. D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00040 · Cited by 243
Oxidative Stress, Inflammaging, and Immunosenescence
Bauer, M. E., & la Fuente, M. D. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397803-5.00004-6 · Cited by 229
Organelle-Based Aggregation and Retention of Damaged Proteins in Asymmetrically Dividing Cells
Zhou, C., Slaughter, B. D., Unruh, J. R., Guo, F., Yu, Z., Mickey, K., Narkar, A., Trimble, R., McClain, M. L., & Li, R. (2014) · Cell · doi:10.1016/j.cell.2014.09.026 · Cited by 241
Coordination of Translational Control and Protein Homeostasis during Severe Heat Stress
Cherkasov, V., Hofmann, S., Druffel‐Augustin, S., Mogk, A., Tyedmers, J., Stoecklin, G., & Bukau, B. (2013) · Current Biology · doi:10.1016/j.cub.2013.09.058 · Cited by 224
Malinovska, L., Kroschwald, S., Munder, M. C., Richter, D., & Alberti, S. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-03-0194 · Cited by 221
Firefly luciferase mutants as sensors of proteome stress
Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219
Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4
Webster, B. M., Colombi, P., Jäger, J., & Lusk, C. P. (2014) · Cell · doi:10.1016/j.cell.2014.09.012 · Cited by 228
Protein aggregation and degradation mechanisms in neurodegenerative diseases.
Takalo, M., Salminen, A., Soininen, H. S., Hiltunen, M. O., & Haapasalo, A. (2013) · Europe PMC (PubMed Central) · Cited by 221
The SND proteins constitute an alternative targeting route to the endoplasmic reticulum
Aviram, N., Ast, T., Boydston, E. A., Arakel, E. C., Chuartzman, S. G., Jan, C. H., Haßdenteufel, S., Dudek, J., Jung, M., Schorr, S., et al. (2016) · Nature · doi:10.1038/nature20169 · Cited by 211
Wang, J., Farr, G. W., Hall, D. H., Li, F., Furtak, K., Dreier, L., & Horwich, A. L. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000350 · Cited by 214
A novel single-cell screening platform reveals proteome plasticity during yeast stress responses
Breker, M., Gymrek, M., & Schuldiner, M. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201301120 · Cited by 214
Role for Lipid Droplet Biogenesis and Microlipophagy in Adaptation to Lipid Imbalance in Yeast
Vevea, J., Garcia, E. J., Chan, R., Zhou, B., Schultz, M., Paolo, G. D., McCaffery, J. M., & Pon, L. A. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.11.010 · Cited by 214
Ori, A., Toyama, B. H., Harris, M. S., Bock, T., Iskar, M., Bork, P., Ingolia, N. T., Hetzer, M. W., & Beck, M. (2015) · Cell Systems · doi:10.1016/j.cels.2015.08.012 · Cited by 201
Uchiki, T., Weikel, K. A., Jiao, W., Shang, F., Caceres, A., Pawlak, D., Handa, J. T., Brownlee, M., Nagaraj, R., & Taylor, A. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2011.00752.x · Cited by 200
Budding yeast as a model organism to study the effects of age
Denoth‐Lippuner, A., Julou, T., & Barral, Y. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12060 · Cited by 211
A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins
Sung, M., Porras-Yakushi, T. R., Reitsma, J. M., Huber, F. M., Sweredoski, M. J., Hoelz, A., Hess, S. Y., & Deshaies, R. J. (2016) · eLife · doi:10.7554/elife.19105 · Cited by 205
A Network of Cytosolic Factors Targets SRP-Independent Proteins to the Endoplasmic Reticulum
Ast, T., Cohen, G., & Schuldiner, M. (2013) · Cell · doi:10.1016/j.cell.2013.02.003 · Cited by 193
Cell death: protein misfolding and neurodegenerative diseases
Nakamura, T., & Lipton, S. A. (2009) · APOPTOSIS · doi:10.1007/s10495-008-0301-y · Cited by 195
Spokoini, R., Moldavski, O., Nahmias, Y., England, J. L., Schuldiner, M., & Kaganovich, D. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.08.024 · Cited by 191
Self-citationA thiol probe for measuring unfolded protein load and proteostasis in cells
Chen, M. Z., Moily, N. S., Bridgford, J. L., Wood, R. J., Radwan, M., Smith, T. A., Song, Z., Tang, B. Z., Tilley, L. M., Xu, X., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00203-5 · Cited by 197
Spatially Organized Aggregation of Misfolded Proteins as Cellular Stress Defense Strategy
Miller, S. B. M., Mogk, A., & Bukau, B. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.006 · Cited by 193
Cellular Functions and Mechanisms of Action of Small Heat Shock Proteins
Mogk, A., Ruger-Herreros, C., & Bukau, B. (2019) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-115515 · Cited by 194
Protein disorder, prion propensities, and self-organizing macromolecular collectives
Malinovska, L., Kroschwald, S., & Alberti, S. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.01.003 · Cited by 195
Ogrodnik, M., Salmonowicz, H., & Gladyshev, V. N. (2019) · Aging Cell · doi:10.1111/acel.12841 · Cited by 184
A ribosome assembly stress response regulates transcription to maintain proteome homeostasis
Albert, B., Kos‐Braun, I. C., Henras, A. K., Dez, C., Rueda-Mejia, M. P., Zhang, X., Gadal, O., Koš, M., & Shore, D. (2019) · eLife · doi:10.7554/elife.45002 · Cited by 191
Effects of in vivo conditions on amyloid aggregation
Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 181
Duennwald, M. L., Echeverria, A., & Shorter, J. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001346 · Cited by 184
Heat shock proteins as potential targets for protective strategies in neurodegeneration
Kampinga, H. H., & Bergink, S. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00099-5 · Cited by 176
Distinct proteostasis circuits cooperate in nuclear and cytoplasmic protein quality control
Samant, R. S., Livingston, C. M., Sontag, E. M., & Frydman, J. (2018) · Nature · doi:10.1038/s41586-018-0678-x · Cited by 172
Self-citationSolís, E. J., Pandey, J. P., Zheng, X., Jin, D. X., Gupta, P. B., Airoldi, E. M., Pincus, D., & Denic, V. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.014 · Cited by 173
Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology
Michel, C. H., Kumar, S., Pinotsi, D., Tunnacliffe, A., St. George-Hyslop, P., Mandelkow, E., Mandelkow, E.-M., Kaminski, C. F., & Kaminski Schierle, G. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515445 · Cited by 165
Hyttinen, J. M. T., Amadio, M., Viiri, J., Pascale, A., Salminen, A., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.07.002 · Cited by 172
The role of oxidative and inflammatory stress and persistent viral infections in immunosenescence
Bauer, M. E., & la Fuente, M. D. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.01.001 · Cited by 173
Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins
Hanzén, S., Vielfort, K., Yang, J., Roger, F., Andersson, V., Zamarbide-Forés, S., Andersson, R., Malm, L., Palais, G., Biteau, B., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.006 · Cited by 166
The mutational landscape of a prion-like domain
Bolognesi, B., Faure, A. J., Seuma, M., Schmiedel, J. M., Tartaglia, G. G., & Lehner, B. (2019) · Nature Communications · doi:10.1038/s41467-019-12101-z · Cited by 165
Metadata
- Authors
- Kaganovich, D., Kopito, R., & Frydman, J.
- Affiliations
- Stanford University (US)
- Corresponding author
- Frydman, Judith
- Venue
- Nature
- Published
- 2008-08
- Volume
- 454
- Issue
- 7208
- Pages
- 1088-1095
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2746971
- OpenAlex
- W1967025628
- Cited by
- 932
- References
- 57
- Citations by year
- 2026: 24 · 2025: 29 · 2024: 41 · 2023: 47 · 2022: 40 · 2021: 52 · 2020: 55 · 2019: 53 · 2018: 54 · 2017: 76 · 2016: 74 · 2015: 65 · 2014: 71 · 2013: 59 · 2012: 58
- FWCI
- 18.36
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM056433)
- National Institute of Neurological Disorders and Stroke (R01NS042842)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- protein misfolding, protein quality control, ubiquitination, proteasome, protein aggregation, huntingtin, prion protein, autophagy, neurodegenerative diseases, yeast, mammalian cells
- MeSH terms
- Ubiquitin-Conjugating Enzyme UBC9, Cytosol, HeLa Cells, Humans, Prions, Proteins, Saccharomyces cerevisiae, Solubility, Protein Folding, Ubiquitin-Conjugating Enzymes, Proteasome Endopeptidase Complex, Von Hippel-Lindau Tumor Suppressor Protein, Ubiquitination
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
