Increased proteasome activity in human embryonic stem cells is regulated by PSMD11

Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors

Takahashi, K., & Yamanaka, S. (2006) · Cell · doi:10.1016/j.cell.2006.07.024 · Cited by 26,673 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Tricine–SDS-PAGE

Schägger, H. (2006) · Nature Protocols · doi:10.1038/nprot.2006.4 · Cited by 2,519 · see citing works

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 · see citing works

STRUCTURE 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 · see citing works

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 · see citing works

A Mutant Drosophila Insulin Receptor Homolog That Extends Life-Span and Impairs Neuroendocrine Function

Tatar, M., Kopelman, A. H., Epstein, D., Tu, M., Yin, C. ‐., & Garofalo, R. S. (2001) · Science · doi:10.1126/science.1057987 · Cited by 1,630 · see citing works

Modelling schizophrenia using human induced pluripotent stem cells

Brennand, K. J., Simone, A., Jou, J., Gelboin-Burkhart, C., Tran, N., Sangar, S., Li, Y., Mu, Y., Chen, G., Yu, D., et al. (2011) · Nature · doi:10.1038/nature09915 · Cited by 1,375 · see citing works

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 · see citing works

BMP4 initiates human embryonic stem cell differentiation to trophoblast

Xu, R., Chen, X., Li, D. S., Li, R., Addicks, G. C., Glennon, C., Zwaka, T. P., & Thomson, J. A. (2002) · Nature Biotechnology · doi:10.1038/nbt761 · Cited by 1,118 · see citing works

Direct control of the Forkhead transcription factor AFX by protein kinase B

Kops, G. J. P. L., de Ruiter, N. D., de Vries-Smits, A. M. M., Powell, D. R., Bos, J. L., & Burgering, B. M. T. (1999) · Nature · doi:10.1038/19328 · Cited by 1,085 · see citing works

Marked differences in differentiation propensity among human embryonic stem cell lines

Osafune, K., Caron, L., Borowiak, M., Martinez, R. J., Fitzgerald, C., Sato, Y., Cowan, C. A., Chien, K. R., & Melton, D. A. (2008) · Nature Biotechnology · doi:10.1038/nbt1383 · Cited by 815 · see citing works

Pluripotency and Cellular Reprogramming: Facts, Hypotheses, Unresolved Issues

Hanna, J. H., Saha, K., & Jaenisch, R. (2010) · Cell · doi:10.1016/j.cell.2010.10.008 · Cited by 695 · see citing works

The Axial Channel of the Proteasome Core Particle Is Gated by the Rpt2 ATPase and Controls Both Substrate Entry and Product Release

Köhler, A., Cascio, P., Leggett, D., Woo, K. M., Goldberg, A. L., & Finley, D. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00274-x · Cited by 409 · see citing works

Monitoring Activity and Inhibition of 26S Proteasomes with Fluorogenic Peptide Substrates

Kisselev, A. F., & Goldberg, A. L. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)98030-0 · Cited by 343 · see citing works

Generation of keratinocytes from normal and recessive dystrophic epidermolysis bullosa-induced pluripotent stem cells

Itoh, M., Kiuru, M., Cairo, M. S., & Christiano, A. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100332108 · Cited by 282 · see citing works

The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together

Pathare, G. R., Nagy, I., Bohn, S., Unverdorben, P., Hubert, Á., Körner, R., Nickell, S., Lasker, K., Šali, A., Tamura, T., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117648108 · Cited by 154 · see citing works

Design and cloning of lentiviral vectors expressing small interfering RNAs

Tiscórnia, G., Singer, O., & Verma, I. M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.36 · Cited by 92 · see citing works

Functional Analysis of Rpn6p, a Lid Component of the 26 S Proteasome, Using Temperature-sensitive rpn6 Mutants of the Yeast Saccharomyces cerevisiae

Isono, E., Saito, N., Kamata, N., Saeki, Y., & Toh‐e, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409364200 · Cited by 69 · see citing works

iPSCs: Induced Back to Controversy

Panopoulos, A. D., Ruiz, S., & Belmonte, J. C. I. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.03.003 · Cited by 58 · see citing works

Rpn6p, a Proteasome Subunit from Saccharomyces cerevisiae, Is Essential for the Assembly and Activity of the 26 S Proteasome*

Santamaría, P. G., Finley, D., Ballesta, J., & Remacha, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209420200 · Cited by 50 · see citing works

Regulation of Intracellular Localization and Transcriptional Activity of FOXO4 by Protein Kinase B through Phosphorylation at the Motif Sites Conserved among the FOXO Family

Matsuzaki, H., Ichino, A., Hayashi, T., Yamamoto, T., & Kikkawa, U. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi146 · Cited by 44 · see citing works

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 · see citing works

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 · see citing works

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 1,432 · see citing works

Multi-omics analysis identifies ATF4 as a key regulator of the mitochondrial stress response in mammals

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 · see citing works

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 · see citing works

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 728 · see citing works

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 684 · see citing works

Haematopoietic 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 · see citing works

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 656 · see citing works

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 620 · see citing works

Ubiquitylation at the crossroads of development and disease

Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 608 · see citing works

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 542 · see citing works

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 · see citing works

Aging Hallmarks and the Role of Oxidative Stress

Maldonado, E., Morales-Pison, S., Urbina, F., & Solari, A. (2023) · Antioxidants · doi:10.3390/antiox12030651 · Cited by 421 · see citing works

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 428 · see citing works

The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution

Dantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 336 · see citing works

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 339 · see citing works

The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death

Livneh, I., Cohen‐Kaplan, V., Cohen-Rosenzweig, C., Avni, N., & Ciechanover, A. J. (2016) · Cell Research · doi:10.1038/cr.2016.86 · Cited by 331 · see citing works

The Mechanistic Links Between Proteasome Activity, Aging and Agerelated Diseases

Sáez, I., & Vı́lchez, D. (2014) · Current Genomics · doi:10.2174/138920291501140306113344 · Cited by 318 · see citing works

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 · see citing works

Autophagy in stem cells

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 285 · see citing works

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 · see citing works

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 268 · see citing works

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 252 · see citing works

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 251 · see citing works

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 249 · see citing works

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 247 · see citing works

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 243 · see citing works

Aging 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 · see citing works

Striatal neurons directly converted from Huntington’s disease patient fibroblasts recapitulate age-associated disease phenotypes

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 · see citing works

Proteome complexity and the forces that drive proteome imbalance

Harper, J. W., & Bennett, E. J. (2016) · Nature · doi:10.1038/nature19947 · Cited by 234 · see citing works

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 230 · see citing works

Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97

Sha, Z., & Goldberg, A. L. (2014) · Current Biology · doi:10.1016/j.cub.2014.06.004 · Cited by 215 · see citing works

cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins

Lokireddy, S., Kukushkin, N. V., & Goldberg, A. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522332112 · Cited by 222 · see citing works

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 · see citing works

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 215 · see citing works

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 · see citing works

Nrf2, a Regulator of the Proteasome, Controls Self-Renewal and Pluripotency in Human Embryonic Stem Cells

Jang, J., Wang, Y., Kim, H.-S., Lalli, M. A., & Kosik, K. S. (2014) · Stem Cells · doi:10.1002/stem.1764 · Cited by 198 · see citing works

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 196 · see citing works

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 200 · see citing works

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 190 · see citing works

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 179 · see citing works

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 178 · see citing works

Ancient drug curcumin impedes 26S proteasome activity by direct inhibition of dual-specificity tyrosine-regulated kinase 2

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 176 · see citing works

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 · see citing works

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 · see citing works

Chaperoning Proteins for Destruction: Diverse Roles of Hsp70 Chaperones and their Co-Chaperones in Targeting Misfolded Proteins to the Proteasome

Shiber, A., & Ravid, T. (2014) · Biomolecules · doi:10.3390/biom4030704 · Cited by 162 · see citing works

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 · see citing works

Development of an orally-administrative MELK-targeting inhibitor that suppresses the growth of various types of human cancer

Chung, 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 152 · see citing works

Label-Free Quantitative Proteomics Reveals the Dynamics of Proteasome Complexes Composition and Stoichiometry in a Wide Range of Human Cell Lines

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 · see citing works

A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function

Ramachandran, K. V., & Margolis, S. S. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3389 · Cited by 147 · see citing works

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 140 · see citing works

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Bhattacharya, 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 140 · see citing works

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 · see citing works

Rewiring of the ubiquitinated proteome determines ageing in C. elegans

Koyuncu, S., Loureiro, R., Lee, H. J., Wagle, P., Krüger, M., & Vı́lchez, D. (2021) · Nature · doi:10.1038/s41586-021-03781-z · Cited by 138 · see citing works

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 130 · see citing works

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 129 · see citing works

Origin and pathophysiology of protein carbonylation, nitration and chlorination in age-related brain diseases and aging

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 133 · see citing works

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 123 · see citing works

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 127 · see citing works

Proteasome activation: An innovative promising approach for delaying aging and retarding age-related diseases

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 112 · see citing works

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 109 · see citing works

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 105 · see citing works

Regulating protein breakdown through proteasome phosphorylation

VerPlank, J. J. S., & Goldberg, A. L. (2017) · Biochemical Journal · doi:10.1042/bcj20160809 · Cited by 110 · see citing works

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 107 · see citing works

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 · see citing works

The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients

Koyuncu, S., Saez, I., Lee, H. J., Gutiérrez-García, R., Pokrzywa, W., Fatima, A., Hoppe, T., & Vilchez, D. (2018) · Nature Communications · doi:10.1038/s41467-018-05320-3 · Cited by 97 · see citing works

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 105 · see citing works

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 102 · see citing works

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 97 · see citing works

Direct cellular delivery of human proteasomes to delay tau aggregation

Han, D. H., Na, H., Choi, W. H., Lee, J. H., Kim, Y. K., Won, C., Lee, S., Kim, K. P., Kuret, J., Min, D., et al. (2014) · Nature Communications · doi:10.1038/ncomms6633 · Cited by 97 · see citing works

The Transcriptionally Permissive Chromatin State of Embryonic Stem Cells Is Acutely Tuned to Translational Output

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 · see citing works

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 · see citing works

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 · see citing works

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 96 · see citing works

Differential regulation of proteasome functionality in reproductive vs. somatic tissues of Drosophila during aging or oxidative stress

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 92 · see citing works

Advanced Properties of Urine Derived Stem Cells Compared to Adipose Tissue Derived Stem Cells in Terms of Cell Proliferation, Immune Modulation and Multi Differentiation

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 · see citing works

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 94 · see citing works

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 89 · see citing works

Quality Control of Membraneless Organelles

Alberti, S., & Carra, S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.013 · Cited by 89 · see citing works

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 90 · see citing works

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 87 · see citing works

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 85 · see citing works

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 · see citing works

Reprogramming barriers and enhancers: strategies to enhance the efficiency and kinetics of induced pluripotency

Ebrahimi, B. (2015) · Cell Regeneration · doi:10.1186/s13619-015-0024-9 · Cited by 84 · see citing works

Somatic increase of CCT8 mimics proteostasis of human pluripotent stem cells and extends C. elegans lifespan

Noormohammadi, A., Khodakarami, A., Gutiérrez-García, R., Lee, H. J., Koyuncu, S., König, T., Schindler, C., Saez, I., Fatima, A., Dieterich, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13649 · Cited by 83 · see citing works

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 84 · see citing works

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 · see citing works

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 82 · see citing works

Proteasome expression and activity in cancer and cancer stem cells

Voutsadakis, I. A. (2017) · Tumor Biology · doi:10.1177/1010428317692248 · Cited by 80 · see citing works

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 75 · see citing works

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 78 · see citing works

Hematopoietic stem cells preferentially traffic misfolded proteins to aggresomes and depend on aggrephagy to maintain protein homeostasis

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 73 · see citing works

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 73 · see citing works

Interplay of Proteostasis Capacity and Protein Aggregation: Implications for Cellular Function and Disease

Hipp, M. S., & Hartl, F. U. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168615 · Cited by 72 · see citing works

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 71 · see citing works

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 69 · see citing works

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 69 · see citing works

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 · see citing works

Transcriptome Profiling Reveals Differentially Expressed Transcripts Between the Human Adrenal Zona Fasciculata and Zona Reticularis

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 · see citing works

Proteostasis of aging and stem cells

Guerrero, D. V. (2013) · RECERCAT (Consorci de Serveis Universitaris de Catalunya)

FOXO 4 is necessary for neural differentiation of human embryonic stem cells

Vı́lchez, D., Boyer, L. F., Lutz, M. K., Merkwirth, C., Morantte, I. G., Tse, C., Spencer, B. J., Page, L. J., Masliah, E., Berggren, W. T., et al. (2013) · Aging Cell · doi:10.1111/acel.12067 · Cited by 49 · see citing works

RPN-6 determines C. elegans longevity under proteotoxic stress conditions

Vilchez, D., Morantte, I., Liu, Z., Douglas, P. M., Merkwirth, C., Rodrigues, A. P. C., Manning, G., & Dillin, A. (2012) · Nature · doi:10.1038/nature11315 · Cited by 413 · see citing works

Proteasome activation enhances stemness and lifespan of human mesenchymal stem cells

Καπετάνου, Μ., Chondrogianni, N., Petrakis, S., Koliakos, G., & Gonos, E. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.035 · Cited by 53 · see citing works

Mechanism suppressing proteostasis collapse in pluripotent stem cells and its demise in Huntington’s disease

Koyuncu, S. (2019) · Kölner Universitäts PublikationsServer (Universität zu Köln)