The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Increased proteasome activity in human embryonic stem cells is regulated by PSMD11
Open accessAbstract
Embryonic stem cells can replicate continuously in the absence of senescence and, therefore, are immortal in culture. Although genome stability is essential for the survival of stem cells, proteome stability may have an equally important role in stem-cell identity and function. Furthermore, with the asymmetric divisions invoked by stem cells, the passage of damaged proteins to daughter cells could potentially destroy the resulting lineage of cells. Therefore, a firm understanding of how stem cells maintain their proteome is of central importance. Here we show that human embryonic stem cells (hESCs) exhibit high proteasome activity that is correlated with increased levels of the 19S proteasome subunit PSMD11 (known as RPN-6 in Caenorhabditis elegans) and a corresponding increased assembly of the 26S/30S proteasome. Ectopic expression of PSMD11 is sufficient to increase proteasome assembly and activity. FOXO4, an insulin/insulin-like growth factor-I (IGF-I) responsive transcription factor associated with long lifespan in invertebrates, regulates proteasome activity by modulating the expression of PSMD11 in hESCs. Proteasome inhibition in hESCs affects the expression of pluripotency markers and the levels of specific markers of the distinct germ layers. Our results suggest a new regulation of proteostasis in hESCs that links longevity and stress resistance in invertebrates to hESC function and identity.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“this observation suggests that iPSCs and germ layer cells may compensate for the detrimental effects of PSMC5 variant p.(Arg325Trp) by monoallelic expression of the wild-type PSMC5 allele and/or an enhanced capacity to selectively eliminate defective proteasome assembly intermediates27.”
From Investigating the neuronal role of the proteasomal ATPase subunit gene PSMC5 in neurodevelopmental proteasomopathies (2025) · cites this paper as [26]
Experimental — accuracy not yet measuredIn the citing paper
“FOXO4 promotes proteasome activity in hESCs by regulating PSDM11 expression, thereby encouraging proteostasis and maintenance of pluripotency markers, such as POU5F1, OCT4, NANOG, SOX2, UTF1, DPPA4, DPPA2, ZFP42 and TERT81.”
From Stem cell aging: mechanisms, regulators and therapeutic opportunities (2014) · cites this paper as [81]
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
Takahashi, K., & Yamanaka, S. (2006) · Cell · doi:10.1016/j.cell.2006.07.024 · Cited by 26,673
Induction of Pluripotent Stem Cells from Adult Human Fibroblasts by Defined Factors
Takahashi, K., Tanabe, K., Ohnuki, M., Narita, M., Ichisaka, T., Tomoda, K., & Yamanaka, S. (2007) · Cell · doi:10.1016/j.cell.2007.11.019 · Cited by 20,221
Embryonic Stem Cell Lines Derived from Human Blastocysts
Thomson, J. A., Itskovitz‐Eldor, J., Shapiro, S. S., Waknitz, M. A., Swiergiel, J. J., Marshall, V. S., & Jones, J. M. (1998) · Science · doi:10.1126/science.282.5391.1145 · Cited by 15,947
Induced Pluripotent Stem Cell Lines Derived from Human Somatic Cells
Yu, J., Vodyanik, M. A., Smuga-Otto, K., Antosiewicz-Bourget, J., Frane, J. L., Tian, S., Nie, J., Jonsdottir, G. A., Ruotti, V., Stewart, R., et al. (2007) · Science · doi:10.1126/science.1151526 · Cited by 10,310
Establishment in culture of pluripotential cells from mouse embryos
Evans, M. J., & Kaufman, M. H. (1981) · Nature · doi:10.1038/292154a0 · Cited by 8,623
A C. elegans mutant that lives twice as long as wild type
Kenyon, C., Chang, J., Gensch, E., Rudner, A., & Tabtiang, R. (1993) · Nature · doi:10.1038/366461a0 · Cited by 3,387
Schägger, H. (2006) · Nature Protocols · doi:10.1038/nprot.2006.4 · Cited by 2,519
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
Self-citationSTRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438
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
Flagged first, then by citations
Cited by
Sorted by citations
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
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
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
Quirós, P. M., Prado, M. A., Zamboni, N., D’Amico, D., Williams, R. W., Finley, D., Gygi, S. P., & Auwerx, J. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201702058 · Cited by 832
Stem cell aging: mechanisms, regulators and therapeutic opportunities
Oh, J., Lee, Y. D., & Wagers, A. J. (2014) · Nature Medicine · doi:10.1038/nm.3651 · Cited by 796
Long live FOXO : unraveling the role of FOXO proteins in aging and longevity
Martins, R., Lithgow, G. J., & Link, W. (2015) · Aging Cell · doi:10.1111/acel.12427 · Cited by 758
The role of protein clearance mechanisms in organismal ageing and age-related diseases
Vı́lchez, D., Sáez, I., & Dillin, A. G. (2014) · Nature Communications · doi:10.1038/ncomms6659 · Cited by 710
Self-citationHaematopoietic stem cells require a highly regulated protein synthesis rate
Signer, R. A. J., Magee, J. A., Salic, A., & Morrison, S. J. (2014) · Nature · doi:10.1038/nature13035 · Cited by 674
Proteostasis 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
FOXO transcription factors: key regulators of cellular quality control
Webb, A. E., & Brunet, A. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.003 · Cited by 649
Ubiquitylation at the crossroads of development and disease
Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 621
Asymmetric apportioning of aged mitochondria between daughter cells is required for stemness
Katajisto, P., Döhla, J., Chaffer, C. L., Pentinmikko, N., Marjanovic, N. D., Iqbal, S., Zoncu, R., Chen, W. W., Weinberg, R. A., & Sabatini, D. M. (2015) · Science · doi:10.1126/science.1260384 · Cited by 558
Regulation of proteasome assembly and activity in health and disease
Rousseau, A., & Bertolotti, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0040-z · Cited by 510
Aging Hallmarks and the Role of Oxidative Stress
Maldonado, E., Morales, S., Urbina, F., & Solari, A. (2023) · Antioxidants · doi:10.3390/antiox12030651 · Cited by 491
Neuronal medium that supports basic synaptic functions and activity of human neurons in vitro
Bardy, C., van den Hurk, M., Eames, T., Marchand, C., Hernandez, R. V., Kellogg, M., Gorris, M., Galet, B., Palomares, V., Brown, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504393112 · Cited by 429
Self-citationDantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 354
Transcriptional and epigenetic regulation of autophagy in aging
Lapierre, L. R., Kumsta, C., Sandri, M., Ballabio, A., & Hansen, M. (2015) · Autophagy · doi:10.1080/15548627.2015.1034410 · Cited by 344
Livneh, I., Cohen‐Kaplan, V., Cohen-Rosenzweig, C., Avni, N., & Ciechanover, A. J. (2016) · Cell Research · doi:10.1038/cr.2016.86 · Cited by 344
The Mechanistic Links Between Proteasome Activity, Aging and Agerelated Diseases
Sáez, I., & Vı́lchez, D. (2014) · Current Genomics · doi:10.2174/138920291501140306113344 · Cited by 331
Mechanisms that Regulate Stem Cell Aging and Life Span
Signer, R. A. J., & Morrison, S. J. (2013) · Cell Stem Cell · doi:10.1016/j.stem.2013.01.001 · Cited by 320
Guan, J., Simon, A. K., Prescott, M., Menéndez, J. A., Liu, F., Wang, F., Wang, C., Wolvetang, E. J., Vázquez‐Martín, A., & Zhang, J. (2013) · Autophagy · doi:10.4161/auto.24132 · Cited by 292
Cellular and epigenetic drivers of stem cell ageing
Ermolaeva, M., Neri, F., Ori, A., & Rudolph, K. L. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0020-3 · Cited by 272
Regulation of Pluripotency and Cellular Reprogramming by the Ubiquitin-Proteasome System
Buckley, S. M., Aranda-Orgillés, B., Strikoudis, A., Apostolou, E., Loizou, E., Moran-Crusio, K., Farnsworth, C. L., Koller, A. A., DasGupta, R., Silva, J. C., et al. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.09.011 · Cited by 271
Exercise influence on the microbiome–gut–brain axis
Dalton, A., Mermier, C. M., & Zuhl, M. (2019) · Gut Microbes · doi:10.1080/19490976.2018.1562268 · Cited by 273
Gates, Channels, and Switches: Elements of the Proteasome Machine
Finley, D. J., Chen, X., & Walters, K. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.10.009 · Cited by 262
Functional Modules of the Proteostasis NetworkPreprint
Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 254
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
Self-citationAging and Rejuvenation of Neural Stem Cells and Their Niches
Navarro Negredo, P., Yeo, R. W., & Brunet, A. (2020) · Cell Stem Cell · doi:10.1016/j.stem.2020.07.002 · Cited by 246
Victor, M. B., Richner, M., Olsen, H. E., Lee, S. W., Monteys, A. M., Ma, C., Huh, C. J., Zhang, B., Davidson, B. L., Yang, X. W., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0075-7 · Cited by 246
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
Sha, Z., & Goldberg, A. L. (2014) · Current Biology · doi:10.1016/j.cub.2014.06.004 · Cited by 215
Lokireddy, S., Kukushkin, N. V., & Goldberg, A. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522332112 · Cited by 228
Erythroid mitochondrial retention triggers myeloid-dependent type I interferon in human SLE
Caielli, S., Cardenas, J., de Jesus, A. A., Baisch, J., Walters, L., Blanck, J. P., Balasubramanian, P., Stagnar, C., Ohouo, M., Hong, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.021 · Cited by 228
Cellular Differences in Protein Synthesis Regulate Tissue Homeostasis
Buszczak, M., Signer, R. A. J., & Morrison, S. J. (2014) · Cell · doi:10.1016/j.cell.2014.09.016 · Cited by 224
Autophagy in stem cells: repair, remodelling and metabolic reprogramming
Boya, P., Codogno, P., & Rodriguez-Muela, N. (2018) · Development · doi:10.1242/dev.146506 · Cited by 197
Jang, J., Wang, Y., Kim, H.-S., Lalli, M. A., & Kosik, K. S. (2014) · Stem Cells · doi:10.1002/stem.1764 · Cited by 203
The ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 205
Translational control of stem cell function
Saba, J. A., Liakath‐Ali, K., Green, R., & Watt, F. M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00386-2 · Cited by 205
Proteostasis and neurodegeneration: The roles of proteasomal degradation and autophagy
Tanaka, K., & Matsuda, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.012 · Cited by 198
Energy metabolism and energy-sensing pathways in mammalian embryonic and adult stem cell fate
Rafalski, V. A., Mancini, E., & Brunet, A. (2012) · Journal of Cell Science · doi:10.1242/jcs.114827 · Cited by 181
FOXO Transcriptional Factors and Long‐Term Living
Murtaza, G., Khan, A. K., Rashid, R., Muneer, S., Hasan, S. M. F., & Chen, J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3494289 · Cited by 182
Banerjee, S., Ji, C., Mayfield, J. E., Goel, A., Xiao, J., Dixon, J. E., & Guo, X. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806797115 · Cited by 180
Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis.
Guo, X., Wang, X., Wang, Z., Banerjee, S., Yang, J., Huang, L., & Dixon, J. E. (2016) · Nature Cell Biology · doi:10.1038/ncb3289 · Cited by 169
FOXO3 shares common targets with ASCL1 genome-wide and inhibits ASCL1-dependent neurogenesis
Webb, A. E., Pollina, E. A., Vierbuchen, T., Urbán, N., Ucar, D., Leeman, D. S., Martynoga, B., Sewak, M., Rando, T. A., Guillemot, F., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.035 · Cited by 164
Shiber, A., & Ravid, T. (2014) · Biomolecules · doi:10.3390/biom4030704 · Cited by 165
Signaling networks determining life span
Riera, C. E., Merkwirth, C., De Magalhaes Filho, C. D., & Dillin, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014451 · Cited by 161
Self-citationChung, S., Suzuki, H., Miyamoto, T., Takamatsu, N., Tatsuguchi, A., Ueda, K., Kijima, K., Nakamura, Y., & Matsuo, Y. (2012) · Oncotarget · doi:10.18632/oncotarget.790 · Cited by 153
Fabre, B., Lambour, T., Garrigues, L., Ducoux‐Petit, M., Amalric, F., Monsarrat, B., Burlet‐Schiltz, O., & Bousquet, M. (2014) · Journal of Proteome Research · doi:10.1021/pr500193k · Cited by 148
Ramachandran, K. V., & Margolis, S. S. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3389 · Cited by 151
Proteostasis and aging of stem cells
Vı́lchez, D., Simic, M., & Dillin, A. G. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.09.002 · Cited by 142
Self-citationBhattacharya, K., Weidenauer, L., Luengo, T. M., Pieters, E. C., Echeverría, P. C., Bernasconi, L., Wider, D., Sadian, Y., Koopman, M. B., Villemin, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19783-w · Cited by 142
Heterogeneity of Human Breast Stem and Progenitor Cells as Revealed by Transcriptional Profiling
Colacino, J. A., Azizi, E., Brooks, M. D., Harouaka, R. A., Fouladdel, S., McDermott, S., Lee, M., Hill, D. R., Madden, J. M., Boerner, J. L., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.03.001 · Cited by 140
Rewiring of the ubiquitinated proteome determines ageing in C. elegans
Koyuncu, S., Loureiro, R., Lee, H. J., Wagle, P., Krüger, M., & Vílchez, D. (2021) · Nature · doi:10.1038/s41586-021-03781-z · Cited by 146
Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging
Cuanalo-Contreras, K., Mukherjee, A., & Soto, C. A. (2013) · International Journal of Cell Biology · doi:10.1155/2013/638083 · Cited by 137
Proteasome Activation as a New Therapeutic Approach To Target Proteotoxic Disorders
Njomen, E., & Tepe, J. J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00101 · Cited by 133
Gonos, E. S., Καπετάνου, Μ., Sereikaitė, J., Bartosz, G., Naparło, K., Grzesik, M., & Sadowska‐Bartosz, I. (2018) · Aging · doi:10.18632/aging.101450 · Cited by 135
Proteostatic and Metabolic Control of Stemness
García‐Prat, L., Sousa‐Victor, P., & Muñoz‐Cánoves, P. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.04.011 · Cited by 125
The ubiquitin proteasome system in glia and its role in neurodegenerative diseases
Jansen, A. H. P., Reits, E. A., & Hol, E. M. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00073 · Cited by 133
Chondrogianni, N., Voutetakis, K., Καπετάνου, Μ., Delitsikou, V., Papaevgeniou, N., Sakellari, M., Lefaki, M., Filippopoulou, K., & Gonos, E. S. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.12.003 · Cited by 115
Enhanced lysosomal degradation maintains the quiescent state of neural stem cells
Kobayashi, T., Piao, W., Takamura, T., Kori, H., Miyachi, H., Kitano, S., Iwamoto, Y., Yamada, M., Imayoshi, I., Shioda, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13203-4 · Cited by 111
Vimentin Coordinates Protein Turnover at the Aggresome during Neural Stem Cell Quiescence Exit
Morrow, C. S., Porter, T. J., Xu, N., Arndt, Z. P., Ako-Asare, K., Heo, H. J., Thompson, E. A. N., & Moore, D. L. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.01.018 · Cited by 106
Regulating protein breakdown through proteasome phosphorylation
VerPlank, J. J. S., & Goldberg, A. L. (2017) · Biochemical Journal · doi:10.1042/bcj20160809 · Cited by 109
Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation
Haberecht-Müller, S., Krüger, E., & Fielitz, J. (2021) · Biomolecules · doi:10.3390/biom11091327 · Cited by 108
Enhanced Degradation of Misfolded Proteins Promotes Tumorigenesis
Chen, L., Brewer, M. D., Guo, L., Wang, R., Jiang, P., & Yang, X. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.010 · Cited by 110
Koyuncu, S., Sáez, I., Lee, H. J., Gutiérrez-García, R., Pokrzywa, W., Fatima, A., Hoppe, T., & Vı́lchez, D. (2018) · Nature Communications · doi:10.1038/s41467-018-05320-3 · Cited by 105
Structure, Dynamics and Function of the 26S Proteasome
Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 111
Modest Declines in Proteome Quality Impair Hematopoietic Stem Cell Self-Renewal
Jose, L. H. S., Sunshine, M. J., Dillingham, C. H., Chua, B. A., Krutá, M., Hong, Y., Hatters, D. M., & Signer, R. A. J. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.003 · Cited by 106
The ubiquitin proteasome system in Caenorhabditis elegans and its regulation
Papaevgeniou, N., & Chondrogianni, N. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.007 · Cited by 106
Direct cellular delivery of human proteasomes to delay tau aggregation
Han, D. H., Na, H.-K., Choi, W. H., Lee, J. H., Kim, Y. K., Won, C., Lee, S.-H., Kim, K. P., Kuret, J., Min, D.-H., et al. (2014) · Nature Communications · doi:10.1038/ncomms6633 · Cited by 88
Bulut-Karslioglu, A., Macrae, T. A., Oses-Prieto, J. A., Covarrubias, S., Percharde, M., Ku, G., Diaz, A., McManus, M. T., Burlingame, A. L., & Ramalho-Santos, M. (2018) · Cell Stem Cell · doi:10.1016/j.stem.2018.02.004 · Cited by 97
AK098656, a Novel Vascular Smooth Muscle Cell–Dominant Long Noncoding RNA, Promotes Hypertension
Jin, L., Lin, X., Yang, L., Fan, X., Wang, W., Li, S., Li, J., Liu, X., Bao, M., Cui, X., et al. (2017) · Hypertension · doi:10.1161/hypertensionaha.117.09651 · Cited by 96
Proteasome activation delays aging in vitro and in vivo
Chondrogianni, N., Sakellari, M., Lefaki, M., Papaevgeniou, N., & Gonos, E. S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.031 · Cited by 94
The dialogue between the ubiquitin-proteasome system and autophagy: Implications in ageing
Sun‐Wang, J. L., Ivanova, S., & Antonio Zorzano, A. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101203 · Cited by 98
Tsakiri, E. N., Sykiotis, G. P., Papassideri, I. S., Gorgoulis, V. G., Bohmann, D., & Trougakos, I. P. (2013) · The FASEB Journal · doi:10.1096/fj.12-221408 · Cited by 94
Kang, H. S., Choi, S. H., Kim, B. S., Choi, J. Y., Park, G.-B., Kwon, T. G., & Chun, S. Y. (2015) · Journal of Korean Medical Science · doi:10.3346/jkms.2015.30.12.1764 · Cited by 93
Post-Transcriptional Regulation of Homeostatic, Stressed, and Malignant Stem Cells
Chua, B. A., van der Werf, I. M., Jamieson, C. H. M., & Signer, R. A. J. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.01.005 · Cited by 96
Modulation of the Maladaptive Stress Response to Manage Diseases of Protein Folding
Roth, D., Hutt, D. M., Tong, J., Bouchecareilh, M., Wang, N., Seeley, T., Dekkers, J. F., Beekman, J. M., Garza, D., Drew, L., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001998 · Cited by 92
Self-citationQuality Control of Membraneless Organelles
Alberti, S., & Carra, S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.013 · Cited by 92
DNAJB6, a Key Factor in Neuronal Sensitivity to Amyloidogenesis
Thiruvalluvan, A., de Mattos, E. P., Brunsting, J. F., Bakels, R., Serlidaki, D., Barazzuol, L., Conforti, P., Fatima, A., Koyuncu, S., Cattaneo, E. F., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.022 · Cited by 89
Expanding the role of proteasome homeostasis in Parkinson’s disease: beyond protein breakdown
Bi, M., Du, X., Jiao, Q., Chen, X., & Jiang, H. F. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03441-0 · Cited by 91
Build-UPS and break-downs: metabolism impacts on proteostasis and aging
Ottens, F., Franz, A., & Hoppe, T. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00682-y · Cited by 88
Differentiation Drives Widespread Rewiring of the Neural Stem Cell Chaperone Network
Vonk, W. I. M., Rainbolt, T. K., Dolan, P. T., Webb, A. E., Brunet, A., & Frydman, J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.009 · Cited by 84
Ebrahimi, B. (2015) · Cell Regeneration · doi:10.1186/s13619-015-0024-9 · Cited by 87
Noormohammadi, A., Khodakarami, A., Gutiérrez-García, R., Lee, H. J., Koyuncu, S., König, T., Schindler, C., Sáez, I., Fatima, A., Dieterich, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13649 · Cited by 86
The Proteasome and Its Network: Engineering for AdaptabilityPreprint
Finley, D. J., & Prado, M. A. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033985 · Cited by 86
Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome
Tsvetkov, P., Mendillo, M. L., Zhao, J., Carette, J. E., Merrill, P. H., Cikes, D., Varadarajan, M., van Diemen, F. R., Penninger, J. M., Goldberg, A. L., et al. (2015) · eLife · doi:10.7554/elife.08467 · Cited by 83
Increased proteasomal activity supports photoreceptor survival in inherited retinal degeneration
Lobanova, E. S., Finkelstein, S., Li, J., Travis, A. M., Hao, Y., Klingeborn, M., Skiba, N. P., Deshaies, R. J., & Arshavsky, V. Y. (2018) · Nature Communications · doi:10.1038/s41467-018-04117-8 · Cited by 80
Proteasome expression and activity in cancer and cancer stem cells
Voutsadakis, I. A. (2017) · Tumor Biology · doi:10.1177/1010428317692248 · Cited by 81
Chatty Mitochondria: Keeping Balance in Cellular Protein Homeostasis
Topf, U., Wróbel, L., & Chacińska, A. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.002 · Cited by 76
The Amazing Ubiquitin-Proteasome System: Structural Components and Implication in Aging
Tsakiri, E. N., & Trougakos, I. P. (2014) · International review of cytology · doi:10.1016/bs.ircmb.2014.09.002 · Cited by 81
Chua, B. A., Lennan, C., Sunshine, M. J., Dreifke, D., Chawla, A., Bennett, E. J., & Signer, R. A. J. (2023) · Cell stem cell · doi:10.1016/j.stem.2023.02.010 · Cited by 74
Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD
Khosravi, B., LaClair, K. D., Riemenschneider, H., Zhou, Q., Frottin, F., Mareljic, N., Czuppa, M., Farny, D., Hartmann, H., Michaelsen, M., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102811 · Cited by 70
Hipp, M. S., & Hartl, F. U. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168615 · Cited by 77
Autophagy in stem and progenitor cells
Rodolfo, C., Bartolomeo, S. D., & Cecconi, F. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2071-3 · Cited by 72
Insulin/IGF-1 Signaling Regulates Proteasome Activity through the Deubiquitinating Enzyme UBH-4
Matilainen, O., Arpalahti, L., Rantanen, V., Hautaniemi, S., & Holmberg, C. I. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.05.012 · Cited by 70
Oncogenic addiction to high 26S proteasome level
Tsvetkov, P., Adler, J., Myers, N., Biran, A., Reuven, N. B., & Shaul, Y. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0806-4 · Cited by 71
Vimentin protects differentiating stem cells from stress
Pattabiraman, S., Azad, G. K., Amen, T., Brielle, S., Park, J. E., Sze, S. K., Meshorer, E., & Kaganovich, D. (2020) · Scientific Reports · doi:10.1038/s41598-020-76076-4 · Cited by 66
Rege, J., Nakamura, Y., Wang, T., Merchen, T. D., Sasano, H., & Rainey, W. E. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-3198 · Cited by 65
Metadata
- Authors
- Vilchez, D., Boyer, L., Morantte, I., Lutz, M., Merkwirth, C., Joyce, D., Spencer, B., Page, L., Masliah, E., Berggren, W. T., Gage, F. H., & Dillin, A.
- Affiliations
- Salk Institute for Biological Studies (US)
- University of California San Diego (US)
- Scripps Research Institute (US)
- Corresponding author
- Dillin, Andrew
- ORCID
- Venue
- Nature
- Published
- 2012-09
- Volume
- 489
- Issue
- 7415
- Pages
- 304-308
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5215918
- OpenAlex
- W2089761608
- Cited by
- 388
- References
- 26
- Citations by year
- 2026: 7 · 2025: 25 · 2024: 24 · 2023: 17 · 2022: 24 · 2021: 42 · 2020: 39 · 2019: 35 · 2018: 36 · 2017: 30 · 2016: 24 · 2015: 31 · 2014: 30 · 2013: 19 · 2012: 5
- FWCI
- 10.92
- 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)
- Funders
- Howard Hughes Medical Institute
- National Institute on Aging (R37AG018440, P01AG031097)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- proteasome activity, 19S proteasome, FOXO4, DAF-16, human embryonic stem cells, stem cell differentiation, proteostasis, Caenorhabditis elegans, glucagon-like peptide-1, lifespan extension, proteotoxic stress, genome stability, aging, insulin/IGF-1 signaling
- MeSH terms
- Cell Differentiation, Cell Line, Humans, Transcription Factors, Up-Regulation, Cell Cycle Proteins, Protein Subunits, Pluripotent Stem Cells, Proteasome Endopeptidase Complex, Forkhead Transcription Factors, Embryonic Stem Cells, HEK293 Cells, Proteasome Inhibitors
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
