Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome

The Sequence Alignment/Map format and SAMtools

Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041 · see citing works

Differential gene and transcript expression analysis of RNA-seq experiments with TopHat and Cufflinks

Trapnell, C., Roberts, A., Goff, L. A., Pertea, G. M., Kim, D., Kelley, D. R., Pimentel, H., Salzberg, S. L., Rinn, J. L., & Pachter, L. S. (2012) · Nature Protocols · doi:10.1038/nprot.2012.016 · Cited by 11,930 · see citing works

Genomics of Drug Sensitivity in Cancer (GDSC): a resource for therapeutic biomarker discovery in cancer cells

Yang, W., Soares, J., Greninger, P., Edelman, E. J., Lightfoot, H., Forbes, S., Bindal, N., Beare, D., Smith, J. A., Thompson, I. R., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1111 · Cited by 4,051 · see citing works

GOrilla: a tool for discovery and visualization of enriched GO terms in ranked gene lists

Eden, E., Navon, R., Steinfeld, I., Lipson, D., & Yakhini, Z. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-48 · Cited by 3,356 · see citing works

A Chromatin-Mediated Reversible Drug-Tolerant State in Cancer Cell Subpopulations

Sharma, S. V., Lee, D. Y., Li, B., Quinlan, M. P., Takahashi, F., Maheswaran, S., McDermott, U., Azizian, N., Zou, L., Fischbach, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.02.027 · Cited by 2,770 · 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

Systematic identification of genomic markers of drug sensitivity in cancer cells

Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456 · see citing works

Tumour heterogeneity and cancer cell plasticity

Meacham, C., & Morrison, S. (2013) · Nature · doi:10.1038/nature12624 · Cited by 2,350 · 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

UBIQUITIN-DEPENDENT PROTEIN DEGRADATION

Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,695 · see citing works

FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells.

Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489 · 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

Translational control in stress and apoptosis

Holčı́k, M., & Sonenberg, N. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1618 · Cited by 1,366 · see citing works

Ebola virus entry requires the cholesterol transporter Niemann–Pick C1

Carette, J. E., Raaben, M., Wong, A., Herbert, A. S., Obernosterer, G., Mulherkar, N., Kuehne, A. I., Kranzusch, P. J., Griffin, A. M., Ruthel, G. T., et al. (2011) · Nature · doi:10.1038/nature10348 · Cited by 1,309 · see citing works

Protein disaggregation mediated by heat-shock protein Hspl04

Parsell, D. A., Kowal, A. S., Singer, M. A., & Lindquist, S. L. (1994) · Nature · doi:10.1038/372475a0 · Cited by 864 · see citing works

Cumulative haploinsufficiency and triplosensitivity drive aneuploidy patterns and shape the cancer genome

Davoli, T., Xu, A. W., Mengwasser, K. E., Sack, L. M., Yoon, J. C., Park, P. J., & Elledge, S. J. (2013) · Cell · doi:10.1016/j.cell.2013.10.011 · Cited by 815 · see citing works

Bortezomib as the First Proteasome Inhibitor Anticancer Drug: Current Status and Future Perspectives

Chen, D., Frezza, M., Schmitt, S. M., Kanwar, J., & Dou, Q. P. (2011) · Current Cancer Drug Targets · doi:10.2174/156800911794519752 · Cited by 796 · see citing works

HSF1 Drives a Transcriptional Program Distinct from Heat Shock to Support Highly Malignant Human Cancers

Mendillo, M. L., Santagata, S., Koeva, M., Bell, G. W., Hu, R., Tamimi, R. M., Fraenkel, E., Ince, T. A., Whitesell, L. J., & Lindquist, S. L. (2012) · Cell · doi:10.1016/j.cell.2012.06.031 · Cited by 696 · see citing works

Relating Whole-Genome Expression Data with Protein-Protein InteractionsPreprint

Jansen, R., Greenbaum, D. S., & Gerstein, M. (2002) · Genome Research · doi:10.1101/gr.205602 · Cited by 657 · see citing works

Proteasome Inhibitors: An Expanding Army Attacking a Unique Target

Kisselev, A. F., van der Linden, W. A., & Overkleeft, H. S. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.003 · Cited by 528 · see citing works

Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells

Radhakrishnan, S. K., Lee, C. S., Young, P., Beskow, A., Chan, J. Y., & Deshaies, R. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.029 · Cited by 526 · see citing works

A comprehensive strategy enabling high-resolution functional analysis of the yeast genome

Breslow, D. K., Cameron, D. M., Collins, S. R., Schuldiner, M., Stewart-Ornstein, J., Newman, H. W., Braun, S. J., Madhani, H. D., Krogan, N. J., & Weissman, J. S. (2008) · Nature Methods · doi:10.1038/nmeth.1234 · Cited by 517 · see citing works

Haploid Genetic Screens in Human Cells Identify Host Factors Used by Pathogens

Carette, J., Guimarães, C. P., Varadarajan, M., Park, A. S., Wuethrich, I., Godarova, A., Kotecki, M., Cochran, B., Spooner, E., Ploegh, H., et al. (2009) · Science · doi:10.1126/science.1178955 · Cited by 508 · see citing works

Selective degradation of oxidatively modified protein substrates by the proteasome

Grune, T., Merker, K., Sandig, G., & Davies, K. J. A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00809-x · Cited by 471 · see citing works

Comparative resistance of the 20S and 26S proteasome to oxidative stress

REINHECKEL, T., SITTE, N., ULLRICH, O., KUCKELKORN, U., DAVIES, K. J. A., & GRUNE, T. (1998) · Biochemical Journal · doi:10.1042/bj3350637 · Cited by 447 · see citing works

Importance of the Different Proteolytic Sites of the Proteasome and the Efficacy of Inhibitors Varies with the Protein Substrate

Kisselev, A. F., Callard, A., & Goldberg, A. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509043200 · Cited by 415 · see citing works

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

Vilchez, D., Boyer, L., Morantte, I., Lutz, M., Merkwirth, C., Joyce, D., Spencer, B., Page, L., Masliah, E., Berggren, W. T., et al. (2012) · Nature · doi:10.1038/nature11468 · Cited by 388 · see citing works

The Reprogramming of Tumor Stroma by HSF1 Is a Potent Enabler of Malignancy

Scherz-Shouval, R., Santagata, S., Mendillo, M. L., Sholl, L. M., Ben-Aharon, I., Beck, A. H., Dias-Santagata, D., Koeva, M., Stemmer, S. M., Whitesell, L., et al. (2014) · Cell · doi:10.1016/j.cell.2014.05.045 · Cited by 386 · see citing works

Molecular Architecture and Assembly of the Eukaryotic Proteasome

Tomko, R. J., & Hochstrasser, M. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060410-150257 · Cited by 376 · see citing works

Proteasomal Degradation Is Transcriptionally Controlled by TCF11 via an ERAD-Dependent Feedback Loop

Steffen, J., Seeger, M., Koch, A., & Krüger, E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.012 · Cited by 370 · see citing works

An epigenetic mechanism of resistance to targeted therapy in T cell acute lymphoblastic leukemia

Knoechel, B., Roderick, J. E., Williamson, K. E., Zhu, J., Lohr, J. G., Cotton, M. J., Gillespie, S. M., Fernandez, D. E., Ku, M., Wang, H., et al. (2014) · Nature Genetics · doi:10.1038/ng.2913 · Cited by 369 · see citing works

Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy

Deshaies, R. J. (2014) · BMC Biology · doi:10.1186/s12915-014-0094-0 · Cited by 334 · see citing works

Widespread Regulation of Translation by Elongation Pausing in Heat Shock

Shalgi, R., Hurt, J. A., Krykbaeva, I., Taipale, M., Lindquist, S. L., & Burge, C. B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.028 · Cited by 334 · see citing works

Regulating the 20S Proteasome Ubiquitin-Independent Degradation Pathway

Ben‐Nissan, G., & Sharon, M. (2014) · Biomolecules · doi:10.3390/biom4030862 · Cited by 333 · see citing works

A molecular census of 26 S proteasomes in intact neurons

Asano, S. M., Fukuda, Y., Beck, F., Aufderheide, A., Förster, F. G., Danev, R., & Baumeister, W. P. (2015) · Science · doi:10.1126/science.1261197 · Cited by 307 · see citing works

Development of proteasome inhibitors as research tools and cancer drugs

Goldberg, A. L. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201210077 · Cited by 295 · see citing works

Tight Coordination of Protein Translation and HSF1 Activation Supports the Anabolic Malignant State

Santagata, S., Mendillo, M. L., Tang, Y., Subramanian, A., Perley, C. C., Roche, S. P., Wong, B., Narayan, R., Kwon, H., Koeva, M., et al. (2013) · Science · doi:10.1126/science.1238303 · Cited by 281 · see citing works

Megabase-scale deletion using CRISPR/Cas9 to generate a fully haploid human cell linePreprint

Essletzbichler, P., Konopka, T., Santoro, F., Chen, D., Gapp, B. V., Královics, R., Brummelkamp, T. R., Nijman, S. M. B., & Bürckstümmer, T. (2014) · Genome Research · doi:10.1101/gr.177220.114 · Cited by 266 · see citing works

Regulation of the 26 S Proteasome Complex During Oxidative Stress

Wang, X., Yen, J. L., Kaiser, P., & Huang, L. (2010) · Science Signaling · doi:10.1126/scisignal.2001232 · Cited by 256 · see citing works

The Stress of Protein Misfolding: From Single Cells to Multicellular OrganismsPreprint

Gidalevitz, T., Prahlad, V., & Morimoto, R. I. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009704 · Cited by 254 · see citing works

Conformational switching of the 26S proteasome enables substrate degradation

Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2616 · Cited by 251 · see citing works

Proteasome Inhibition: a New Strategy in Cancer Treatment

Adams, J., Palombella, V. J., & Elliott, P. J. (2000) · Investigational New Drugs · doi:10.1023/a:1006321828515 · Cited by 248 · see citing works

Forward and Reverse Genetics through Derivation of Haploid Mouse Embryonic Stem Cells

Elling, U., Taubenschmid, J., Wirnsberger, G., O’Malley, R. C., Demers, S.-P., Vanhaelen, Q., Иванович, Ш. А., Schmauss, G., Schramek, D., Schnütgen, F., et al. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.10.012 · Cited by 232 · see citing works

Generation of iPSCs from cultured human malignant cells

Carette, J. E., Pruszak, J., Varadarajan, M., Blomen, V. A., Gokhale, S., Camargo, F. D., Wernig, M., Jaenisch, R., & Brummelkamp, T. R. (2010) · Blood · doi:10.1182/blood-2009-07-231845 · Cited by 229 · see citing works

Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones

Ullrich, O., Reinheckel, T., Sitte, N., Hass, R., Grune, T., & Davies, K. J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6223 · Cited by 229 · see citing works

Cancer vulnerabilities unveiled by genomic loss

Nijhawan, D., Zack, T., Ren, Y., Strickland, M., Lamothe, R., Schumacher, S., Tsherniak, A., Besche, H. C., Rosenbluh, J., Shehata, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.07.023 · Cited by 224 · see citing works

Proteasomes Can Degrade a Significant Proportion of Cellular Proteins Independent of Ubiquitination

Baugh, J. M., Viktorova, E. G., & Pilipenko, E. V. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.081 · Cited by 216 · 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

p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition

Radhakrishnan, S. K., den Besten, W., & Deshaies, R. J. (2014) · eLife · doi:10.7554/elife.01856 · Cited by 211 · see citing works

Ubiquitin-independent degradation of proteins by the proteasome

Jariel‐Encontre, I., Bossis, G., & Piechaczyk, M. (2008) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.05.004 · Cited by 198 · see citing works

Reversible 26S Proteasome Disassembly upon Mitochondrial Stress

Livnat‐Levanon, N., Kevei, É., Kleifeld, O., Krutauz, D., Segref, A., Rinaldi, T., Erpapazoglou, Z., Cohen, M. M., Reis, N., Hoppe, T., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.030 · Cited by 185 · see citing works

20S proteasomes and protein degradation “by default”

Asher, G., Reuven, N. B., & Shaul, Y. (2006) · BioEssays · doi:10.1002/bies.20447 · Cited by 184 · see citing works

Protein synthesis in long-term stationary-phase cultures of Saccharomyces cerevisiae

Fuge, E. K., Braun, E. L., & Werner‐Washburne, M. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.18.5802-5813.1994 · Cited by 176 · see citing works

The solute carrier SLC35F2 enables YM155-mediated DNA damage toxicity

Winter, G. E., Radic, B., Mayor-Ruiz, C., Blomen, V. A., Trefzer, C., Kandasamy, R. K., Huber, K. V. M., Gridling, M., Chen, D., Klampfl, T., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1590 · Cited by 175 · see citing works

Proteasome Disassembly and Downregulation Is Correlated with Viability during Stationary Phase

Bajorek, M., Finley, D. J., & Glickman, M. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00417-2 · Cited by 172 · see citing works

Converting Cancer Therapies into Cures: Lessons from Infectious Diseases

Glickman, M. S., & Sawyers, C. L. (2012) · Cell · doi:10.1016/j.cell.2012.02.015 · Cited by 169 · see citing works

A Genome-wide siRNA Screen Identifies Proteasome Addiction as a Vulnerability of Basal-like Triple-Negative Breast Cancer Cells

Petrocca, F., Altschuler, G. M., Tan, S. M., Mendillo, M. L., Yan, H., Jerry, D. J., Kung, A. L., Hide, W. A., Ince, T. A., & Lieberman, J. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.07.008 · Cited by 165 · see citing works

Proteasome Regulation by ADP-Ribosylation

Cho-Park, P. F., & Steller, H. (2013) · Cell · doi:10.1016/j.cell.2013.03.040 · Cited by 140 · see citing works

Characterization of the brain 26S proteasome and its interacting proteins

Tai, H. (2010) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2010.00012 · Cited by 136 · see citing works

Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entry

Deriziotis, P., André, R., Smith, D. M., Goold, R., Kinghorn, K. J., Kristiansen, M., Nathan, J. A., Rosenzweig, R., Krutauz, D., Glickman, M. H., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.224 · Cited by 122 · see citing works

Proteasome Inhibition in Wild-Type Yeast Saccharomyces Cerevisiae Cells

Liu, C., Apodaca, J., Davis, L. E., & Rao, H. (2007) · BioTechniques · doi:10.2144/000112389 · Cited by 114 · see citing works

The nanny model for IDPs

Tsvetkov, P., Reuven, N. B., & Shaul, Y. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.233 · Cited by 108 · see citing works

A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin

Reiling, J. H., Clish, C. B., Carette, J. E., Varadarajan, M., Brummelkamp, T. R., & Sabatini, D. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018098108 · Cited by 104 · see citing works

Genome-Wide siRNA Screen for Modulators of Cell Death Induced by Proteasome Inhibitor Bortezomib

Chen, S., Blank, J. L., Peters, T., Liu, X. J., Rappoli, D. M., Pickard, M. D., Menon, S., Yu, J., Driscoll, D. L., Lingaraj, T., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4428 · Cited by 102 · see citing works

Molecular Mechanisms of Acquired Proteasome Inhibitor Resistance

Kale, A. J., & Moore, B. S. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300434z · Cited by 94 · see citing works

20S Proteasome Differentially Alters Translation of Different mRNAs via the Cleavage of eIF4F and eIF3

Baugh, J. M., & Pilipenko, E. V. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.017 · Cited by 87 · see citing works

Pivotal Advance: Protein synthesis modulates responsiveness of differentiating and malignant plasma cells to proteasome inhibitors

Cenci, S., Oliva, L., Cerruti, F., Milan, E., Bianchi, G., Raule, M., Mezghrani, A., Pasqualetto, E., Sitia, R., & Cascio, P. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.1011497 · Cited by 83 · see citing works

Getting to First Base in Proteasome Assembly

Besche, H. C., Peth, A., & Goldberg, A. L. (2009) · Cell · doi:10.1016/j.cell.2009.06.035 · Cited by 73 · see citing works

Targeting the ubiquitin proteasome system in haematological malignancies

Crawford, L., & Irvine, A. E. (2013) · Blood Reviews · doi:10.1016/j.blre.2013.10.002 · Cited by 72 · see citing works

Proteasomes of the yeastS. cerevisiae: genes, structure and functions

Hilt, W., & Wolf, D. H. (1995) · Molecular Biology Reports · doi:10.1007/bf00990964 · Cited by 71 · see citing works

BIMEL, an intrinsically disordered protein, is degraded by 20S proteasomes in the absence of poly-ubiquitylation

Wiggins, C. M., Tsvetkov, P., Johnson, M., Joyce, C. L., Lamb, C. A., Bryant, N. J., Komander, D., Shaul, Y., & Cook, S. J. (2011) · Journal of Cell Science · doi:10.1242/jcs.058438 · Cited by 70 · see citing works

Identification of host cell factors required for intoxication through use of modified cholera toxin

Guimarães, C. P., Carette, J. E., Varadarajan, M., Antos, J. M., Popp, M. W., Spooner, E., Brummelkamp, T. R., & Ploegh, H. L. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201108103 · Cited by 66 · see citing works

Proteins in aggregates functionally impact multiple neurodegenerative disease models by forming proteasome‐blocking complexes

Ayyadevara, S., Balasubramaniam, M., Gao, Y., Yu, L., Alla, R., & Reis, R. J. S. (2014) · Aging Cell · doi:10.1111/acel.12296 · Cited by 55 · see citing works

Susceptibility of p53 Unstructured N Terminus to 20 S Proteasomal Degradation Programs the Stress Response

Tsvetkov, P., Reuven, N. B., Prives, C. L., & Shaul, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040493 · Cited by 54 · see citing works

c-Fos Proteasomal Degradation Is Activated by a Default Mechanism, and Its Regulation by NAD(P)H:Quinone Oxidoreductase 1 Determines c-Fos Serum Response Kinetics

Adler, J., Reuven, N. B., Kahana, C., & Shaul, Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00899-09 · Cited by 46 · see citing works

NADH binds and stabilizes the 26S proteasomes independent of ATP

Tsvetkov, P., Myers, N., Eliav, R., Adamovich, Y., Hagai, T., Adler, J., Navon, A., & Shaul, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537175 · Cited by 42 · see citing works

Natural Product Inhibitors of the Ubiquitin-Proteasome Pathway

Schneekloth, J. S., & Crews, C. M. (2011) · Current Drug Targets · doi:10.2174/138945011798109491 · Cited by 21 · see citing works

Three Decades of Studies to Understand the Functions of the Ubiquitin Family

Varshavsky, A. J. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_1 · Cited by 14 · see citing works

Global gene disruption in human cells to assign genes to phenotypes

Carette, J. E., Guimarães, C. P., Wüthrich, I., Blomen, V. A., Varadarajan, M., Sun, C., Bell, G. W., Yuan, B., Muellner, M. K., Nijman, S. M. B., et al. (2011) · PubMed Central · doi:10.1038/nbt.1857

A global genetic interaction network maps a wiring diagram of cellular function

Costanzo, M., VanderSluis, B., Koch, E. N., Baryshnikova, A., Pons, C., Tan, G., Wang, W., Usaj, M., Hanchard, J., Lee, S. D., et al. (2016) · Science · doi:10.1126/science.aaf1420 · Cited by 1,240 · see citing works

Proteostasis and aging

Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899 · see citing works

Mitochondrial metabolism promotes adaptation to proteotoxic stress

Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645 · see citing works

mTOR inhibition activates overall protein degradation by the ubiquitin proteasome system as well as by autophagy

Zhao, J., Zhai, B., Gygi, S. P., & Goldberg, A. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521919112 · Cited by 471 · see citing works

Systematic comparison of CRISPR/Cas9 and RNAi screens for essential genes

Morgens, D. W., Deans, R. M., Li, A., & Bassik, M. C. (2016) · Nature Biotechnology · doi:10.1038/nbt.3567 · Cited by 384 · 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

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

Sahu, I., Mali, S. M., Sulkshane, P., Xu, C., Rozenberg, A., Morag, R., Sahoo, M. P., Singh, S. K., Ding, Z., Wang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26427-0 · Cited by 146 · see citing works

Proteotoxicity from aberrant ribosome biogenesis compromises cell fitness

Tye, B., Commins, N., Ryazanova, L. V., Wühr, M., Springer, M., Pincus, D., & Churchman, L. S. (2019) · eLife · doi:10.7554/elife.43002 · Cited by 134 · see citing works

Spectrum and functional validation of PSMB5 mutations in multiple myeloma

Barrio, S., Stühmer, T., Vià, M. D., Barrio-Garcia, C., Lehners, N., Bešše, A., Cuenca, I., Garitano-Trojaola, A., Fink, S., Leich, E., et al. (2018) · Leukemia · doi:10.1038/s41375-018-0216-8 · Cited by 124 · see citing works

The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges

Tundo, G. R., Sbardella, D., Santoro, A. M., Coletta, A., Oddone, F., Grasso, G., Milardi, D., Lacal, P. M., Marini, S., Purrello, R., et al. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107579 · Cited by 115 · see citing works

Rapid induction of p62 and GABARAPL1 upon proteasome inhibition promotes survival before autophagy activation

Sha, Z., Schnell, H. M., Ruoff, K., & Goldberg, A. L. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201708168 · Cited by 113 · 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

Antifungal Volatile Organic Compounds from Streptomyces setonii WY228 Control Black Spot Disease of Sweet Potato

Gong, Y., Liu, J., Xu, M., Zhang, C., Jun, G., Li, C., Xing, K., & Qin, S. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.02317-21 · Cited by 104 · see citing works

Proteasome stress in skeletal muscle mounts a long-range protective response that delays retinal and brain aging

Rai, M., Coleman, Z., Curley, M., Nityanandam, A., Platt, A., Robles‐Murguia, M., Jiao, J., Finkelstein, D., Wang, Y., Xu, B., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.03.005 · Cited by 96 · see citing works

Integrative analysis of the genomic and transcriptomic landscape of double-refractory multiple myeloma

Ziccheddu, B., Biancon, G., Bagnoli, F., Philippis, C. D., Maura, F., Rustad, E. H., Dugo, M., Devecchi, A., Cecco, L. D., Sensi, M., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019000779 · Cited by 74 · see citing works

Proteasome Inhibitors: Harnessing Proteostasis to Combat Disease

Sherman, D. J., & Li, J. (2020) · Molecules · doi:10.3390/molecules25030671 · Cited by 76 · 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

Structural Insights into Substrate Recognition and Processing by the 20S Proteasome

Sahu, I., & Glickman, M. H. (2021) · Biomolecules · doi:10.3390/biom11020148 · Cited by 69 · see citing works

Inhibition of Proteasome Activity Induces Formation of Alternative Proteasome Complexes

Welk, V., Coux, O., Kleene, V., Abéza, C., Trümbach, D., Eickelberg, O., & Meiners, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.717652 · Cited by 62 · see citing works

CRISPR Genome-Wide Screening Identifies Dependence on the Proteasome Subunit PSMC6 for Bortezomib Sensitivity in Multiple Myeloma

Shi, C.-X., Kortüm, K. M., Zhu, Y. X., Bruins, L. A., Jedlowski, P. M., Votruba, P. G., Luo, M., Stewart, R. A., Ahmann, J. M., Braggio, E., et al. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0130 · Cited by 61 · see citing works

Suppression of 19S proteasome subunits marks emergence of an altered cell state in diverse cancers

Tsvetkov, P., Sokol, E. S., Jin, D. X., Brune, Z., Thiru, P., Ghandi, M., Garraway, L. A., Gupta, P. B., Santagata, S., Whitesell, L. J., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619067114 · Cited by 56 · see citing works

Time-resolved proteomic profiling reveals compositional and functional transitions across the stress granule life cycle

Hu, S., Zhang, Y., Yi, Q., Yang, C., Liu, Y., & Bai, Y. (2023) · Nature Communications · doi:10.1038/s41467-023-43470-1 · Cited by 53 · see citing works

Exploring the proteasome system: A novel concept of proteasome inhibition and regulation

Wang, X., Meul, T., & Meiners, S. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107526 · Cited by 50 · see citing works

Mitochondrial Regulation of the 26S Proteasome

Meul, T., Berschneider, K., Schmitt, S., Mayr, C. H., Mattner, L. F., Schiller, H. B., Yazgili, A. S., Wang, X., Lukas, C., Schlesser, C., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108059 · Cited by 48 · see citing works

Replacement of miR-155 Elicits Tumor Suppressive Activity and Antagonizes Bortezomib Resistance in Multiple Myeloma

Amodio, N., Cantafio, M. E. G., Botta, C., Agosti, V., Federico, C., Caracciolo, D., Ronchetti, D., Rossi, M., Driessen, C., Neri, A., et al. (2019) · Cancers · doi:10.3390/cancers11020236 · Cited by 42 · see citing works

An adaptive stress response that confers cellular resilience to decreased ubiquitination

Hunt, L. C., Pagala, V., Stephan, A., Xie, B., Kodali, K., Kavdia, K., Wang, Y., Shirinifard, A., Curley, M., Graça, F. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43262-7 · Cited by 37 · see citing works

The Proteasome System in Health and Disease

Coux, O., Zieba, B. A., & Meiners, S. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_3 · Cited by 38 · see citing works

Systems level profiling of chemotherapy-induced stress resolution in cancer cells reveals druggable trade-offs

Saavedra-García, P., Román-Trufero, M., Al-Sadah, H. A., Blighe, K., López-Jiménez, E. A., Christoforou, M., Penfold, L., Capece, D., Xiong, X., Miao, Y., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2018229118 · Cited by 37 · see citing works

Proteome Comparisons between Hemolymph of Two Honeybee Strains (Apis mellifera ligustica) Reveal Divergent Molecular Basis in Driving Hemolymph Function and High Royal Jelly Secretion

Hora, Z. A., Ma, C., Qi, Y., Mao, F., Han, B., Hu, H., Meng, L., & Li, J. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00621 · Cited by 36 · see citing works

Tuning the proteasome to brighten the end of the journey

Mayor, T., Sharon, M., & Glickman, M. H. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00198.2016 · Cited by 33 · see citing works

Autophagic sequestration of SQSTM1 disrupts the aggresome formation of ubiquitinated proteins during proteasome inhibition

Zhang, C., Huang, C. L., Xia, H., Xu, H., Tang, Q., & Bi, F. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05061-8 · Cited by 32 · see citing works

Allosteric regulation of the 20S proteasome by the Catalytic Core Regulators (CCRs) family

Deshmukh, F. K., Ben‐Nissan, G., Olshina, M. A., Füzesi-Levi, M. G., Polkinghorn, C. R., Arkind, G., Leushkin, Y., Fainer, I., Fleishman, S. J., Tawfik, D. S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38404-w · Cited by 31 · see citing works

ROS Overproduction Sensitises Myeloma Cells to Bortezomib-Induced Apoptosis and Alleviates Tumour Microenvironment-Mediated Cell Resistance

Caillot, M., Zylbersztejn, F., Maître, E., Bourgeais, J., Hérault, O., & Sola, B. (2020) · Cells · doi:10.3390/cells9112357 · Cited by 29 · see citing works

Proteasome inhibition by bortezomib parallels a reduction in head and neck cancer cells growth, and an increase in tumor-infiltrating immune cells

Benvenuto, M., Ciuffa, S., Focaccetti, C., Sbardella, D., Fazi, S., Scimeca, M., Tundo, G. R., Barillari, G., Segni, M., Bonanno, E., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-98450-6 · Cited by 30 · see citing works

Allosteric HSP70 inhibitors perturb mitochondrial proteostasis and overcome proteasome inhibitor resistance in multiple myeloma

Ferguson, I., Lin, Y.-H. T., Lam, C., Shao, H., Tharp, K. M., Hale, M., Kasap, C., Mariano, M. C., Kishishita, A., Patiño-Escobar, B., et al. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.06.010 · Cited by 29 · see citing works

Overcoming proteasome inhibitor resistance in the immunotherapy era

Patiño-Escobar, B., Talbot, A., & Wiita, A. P. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.05.006 · Cited by 26 · see citing works

Contribution of the Tumor Microenvironment to Metabolic Changes Triggering Resistance of Multiple Myeloma to Proteasome Inhibitors

Schwestermann, J., Bešše, A., Driessen, C., & Bešše, L. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.899272 · Cited by 25 · see citing works

Single-Nucleotide Variants and Epimutations Induce Proteasome Inhibitor Resistance in Multiple Myeloma

Haertle, L., Barrio, S., Munawar, U., Han, S., Zhou, X., Šimíček, M., Vogt, C., Truger, M. S., Alonso, R., Steinhardt, M., et al. (2022) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-22-1161 · Cited by 20 · see citing works

Thiolutin has complex effects in vivo but is a direct inhibitor of RNA polymerase II in vitro

Qiu, C., Arora, P., Malik, I., LaPeruta, A. J., Pavlovic, E. M., Ugochukwu, S., Naik, M. T., & Kaplan, C. D. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1258 · Cited by 20 · see citing works

The molecular mechanism and challenge of targeting XPO1 in treatment of relapsed and refractory myeloma

Sellin, M., Berg, S. A., Hagen, P. A., & Zhang, J. (2022) · Translational Oncology · doi:10.1016/j.tranon.2022.101448 · Cited by 17 · see citing works

Pan-cancer analysis of genomic and transcriptomic data reveals the prognostic relevance of human proteasome genes in different cancer types

Larsson, P., Pettersson, D., Engqvist, H., Rönnerman, E. W., Forssell-Aronsson, E. B., Kovács, A., Karlsson, P., Helou, K., & Parris, T. Z. (2022) · BMC Cancer · doi:10.1186/s12885-022-10079-4 · Cited by 14 · see citing works

The ubiquitin proteasome system as a potential therapeutic target for systemic sclerosis

Meiners, S., Evankovich, J. W., & Mallampalli, R. K. (2018) · Translational research · doi:10.1016/j.trsl.2018.03.003 · Cited by 14 · see citing works

Metformin Induces Resistance of Cancer Cells to the Proteasome Inhibitor Bortezomib

Schlesser, C., Meul, T., Stathopoulos, G. T., & Meiners, S. (2022) · Biomolecules · doi:10.3390/biom12060756 · Cited by 13 · see citing works

The mitochondrial pyruvate carrier complex potentiates the efficacy of proteasome inhibitors in multiple myeloma

Findlay, S., Nair, R., Merrill, R. A., Kaiser, Z., Cajelot, A., Aryanpour, Z., Heath, J., St‐Louis, C., Papadopoli, D. J., Topisirović, I., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2022008345 · Cited by 13 · see citing works

Lessons Learned from Proteasome Inhibitors, the Paradigm for Targeting Protein Homeostasis in Cancer

Kambhampati, S., & Wiita, A. P. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_10 · Cited by 13 · see citing works

Downregulation of PA28α induces proteasome remodeling and results in resistance to proteasome inhibitors in multiple myeloma

Gu, Y., Barwick, B. G., Shanmugam, M., Hofmeister, C. C., Kaufman, J. L., Nooka, A. K., Gupta, V. A., Dhodapkar, M. V., Boise, L., & Lonial, S. (2020) · Blood Cancer Journal · doi:10.1038/s41408-020-00393-0 · Cited by 13 · see citing works

Genetic Alterations in Members of the Proteasome 26S Subunit, AAA-ATPase (PSMC) Gene Family in the Light of Proteasome Inhibitor Resistance in Multiple Myeloma

Haertle, L., Buenache, N., Hernández, H. N. C., Šimíček, M., Šnaurová, R., Rapado, I., Martı́nez, N., López‐Muñoz, N., Sánchez‐Pina, J. M., Munawar, U., et al. (2023) · Cancers · doi:10.3390/cancers15020532 · Cited by 12 · see citing works

Substrate-specific effects of natural genetic variation on proteasome activity

Collins, M. A., Avery, R., & Albert, F. W. (2023) · PLOS Genetics · doi:10.1371/journal.pgen.1010734 · Cited by 11 · see citing works

Integrated proteomics spotlight the proteasome as a therapeutic vulnerability in embryonal tumors with multilayered rosettes

Dottermusch, M., Biabani, A., Lempertz, T., Schumann, Y., Navolić, J., Godbole, S., Obrecht, D., Frank, S., Dorostkar, M. M., Voß, H., et al. (2023) · Neuro-Oncology · doi:10.1093/neuonc/noad265 · Cited by 8 · see citing works

Constitutive Activation of p62/Sequestosome-1-Mediated Proteaphagy Regulates Proteolysis and Impairs Cell Death in Bortezomib-Resistant Mantle Cell Lymphoma

Quinet, G., Xolalpa, W., Reyes-Garau, D., Profitós-Pelejà, N., Azkargorta, M., Ceccato, L., Gonzalez-Santamarta, M., Marsal, M., Andilla, J., Aillet, F., et al. (2022) · Cancers · doi:10.3390/cancers14040923 · Cited by 11 · see citing works

Effect of ionizing radiation exposure on Trypanosoma cruzi ubiquitin-proteasome system

Cerqueira, P. G., Passos-Silva, D. G., Vieira‐da‐Rocha, J. P., Mendes, I. C., de Oliveira, K. A., Oliveira, C. F. B., Felicori, L. F., Nagem, R. A. P., Cardoso, J., Nardelli, S. C., et al. (2017) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2017.01.005 · Cited by 11 · see citing works

Enhanced O-GlcNAcylation Mediates Cytoprotection under Proteasome Impairment by Promoting Proteasome Turnover in Cancer Cells

Hashimoto, E., Okuno, S., Hirayama, S., Arata, Y., Goto, T., Kosako, H., Hamazaki, J., & Murata, S. (2020) · iScience · doi:10.1016/j.isci.2020.101299 · Cited by 11 · see citing works

The prognostic value of 19S ATPase proteasome subunits in acute myeloid leukemia and other forms of cancer

Tychhon, B., Allen, J. C., Gonzalez, M. A., Olivas, I. M., Solecki, J. P., Keivan, M., Velazquez, V. V., McCall, E. B., Tapia, D. N., Rubio, A. J., et al. (2023) · Frontiers in Medicine · doi:10.3389/fmed.2023.1209425 · Cited by 10 · see citing works

Signature activities of 20S proteasome include degradation of the ubiquitin-tag with the protein under hypoxiaPreprint

Sahu, I., Mali, S. M., Sulkshane, P., Rozenberg, A., Xu, C., Morag, R., Sahoo, M. P., Singh, S. K., Ding, Z., Wang, Y., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.20.883942 · Cited by 10 · see citing works

The coherence between PSMC6 and α-ring in the 26S proteasome is associated with Alzheimer’s disease

Xiong, J., Pang, X., Song, X., Yang, L., & Pang, C.-Y. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1330853 · Cited by 9 · see citing works

Proteasomal adaptations to FDA-approved proteasome inhibitors: a potential mechanism for drug resistance?

Kim, K. B. (2021) · Cancer Drug Resistance · doi:10.20517/cdr.2021.27 · Cited by 8 · see citing works

Depleting the 19S proteasome regulatory PSMD1 subunit as a cancer therapy strategy

Adler, J., Oren, R., & Shaul, Y. (2023) · Cancer Medicine · doi:10.1002/cam4.5775 · Cited by 6 · see citing works

DiPTAC: A degradation platform via directly targeting proteasome

Tu, Y., Yu, Q., Li, M., Gao, L., Mao, J., Ma, J., Dong, X., Che, J., Zhang, C., Zeng, L., et al. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.09.003 · Cited by 6 · see citing works

Association of intronic polymorphisms (rs1549339, rs13402242) and mRNA expression variations in PSMD1 gene in arsenic-exposed workers

Ahmad, S., Arif, B., Akram, Z., Ahmed, M. W., Khan, A. U., Hussain, M. Z., Rahman, F., Kayani, M. A., & Mahjabeen, I. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-019-07422-x · Cited by 6 · see citing works

A 20S proteasome receptor for degradation of intrinsically disordered proteinsPreprint

Biran, A., Myers, N., Adler, J., Broennimann, K., Reuven, N. B., & Shaul, Y. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/210898 · Cited by 6 · see citing works

An up‐To‐Date Review of Elesclomol and Its Nano‐Formulations in Cancer Therapy

Wang, Q., Li, F., Tiwari, A. K., & Babu, R. J. (2025) · Cancer Reports · doi:10.1002/cnr2.70193 · Cited by 5 · see citing works

Loss of correlated proteasomal subunit expression selectively promotes the 20SHigh state which underlies luminal breast tumorigenicity

Sundararajan, R., Hegde, S. R., Panda, A. K., Christie, J., Gadewal, N. S., & Venkatraman, P. (2025) · Communications Biology · doi:10.1038/s42003-024-07432-7 · Cited by 5 · see citing works

The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo

Oliveri, F., Keller, S. J., Goebel, H., Salinas, G. O. A., & Basler, M. (2023) · Life Science Alliance · doi:10.26508/lsa.202201760 · Cited by 5 · see citing works

Distinct patterns of proteostasis network gene expression are associated with different prognoses in melanoma patients

Wellman, R., Jacobson, D. H., Secrier, M., & Labbadia, J. P. (2024) · Scientific Reports · doi:10.1038/s41598-023-50640-0 · Cited by 4 · see citing works

Uncoupling phototoxicity‐elicited neural dysmorphology and death by insidious function and selective impairment of Ran‐binding protein 2 (Ranbp2)

Cho, K., Haney, V. O., Yoon, D., Hao, Y., & Ferreira, P. A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.11.037 · Cited by 4 · see citing works

The versatility of the proteasome in gene expression and silencing: Unraveling proteolytic and non-proteolytic functions

Lee, H. K., Kim, S., & Lee, D. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194978 · Cited by 3 · see citing works

Coordinated control of proteasome subunit gene expression promotes stress resistance, proteostasis, and longevity

Topalidou, I., & Lehrbach, N. J. (2026) · GeroScience · doi:10.1007/s11357-026-02146-6 · Cited by 2 · see citing works

A lowered 26S proteasome activity correlates with mantle lymphoma cell lines resistance to genotoxic stress

Younes, K. B., Body, S., Costé, É., Viailly, P., Miloudi, H., Coudre, C., Jardin, F., Aissa‐Fennira, F. B., & Sola, B. (2017) · BMC Cancer · doi:10.1186/s12885-017-3530-z · Cited by 2 · see citing works

Within and beyond the boundaries of proteasomal assembly: PSMD9 chaperone as a multifunctional protein

Sundararajan, R., Harish, M., Anthony, M. C., Christie, J., Jaiswal, D., & Venkatraman, P. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253044 · Cited by 1 · see citing works

Analysis of proteasome stress in different cell types defines a conserved transcriptional response signature and its modulation with aging

Rai, M., Wang, Y., Stephan, A., Nityanandam, A., & Demontis, F. (2026) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkag245 · Cited by 1 · see citing works

Ubiquitin receptor–mediated, ubiquitin-independent targeted protein degradation via 26 S proteasomes

Park, S. H., Jang, Y., Lee, S.-Y., Kim, E., Jeong, D., Byun, I., Kim, J., Yang, J., Lee, C., Han, D., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeh0227 · Cited by 1 · see citing works

Adaptive mitochondrial regulation of the proteasomePreprint

Meul, T., Berschneider, K., Schmitt, S., Mayr, C. H., Mattner, L. F., Schiller, H. B., Yazgili, A. S., Wang, X., Lukas, C., Prehn, C. P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.07.026161 · Cited by 1 · see citing works

Is 26S proteasome non-ATPase regulatory subunit 6 a potential molecular target for intrahepatic cholangiocarcinoma?

Zhuang, Y., Tong, L.-Q., & Sun, X. (2024) · World Journal of Hepatology · doi:10.4254/wjh.v16.i11.1219 · Cited by 1 · see citing works

The targeting of non-fibrillar polyQ via distinct VCP-proteasome couplingPreprint

Zhao, D. Y., Mi, C., Wagner, J., Jiang, W., Saha, I., Poege, M., Xu, P., Plitzko, J. M., Guo, Q., Beck, F., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.01.646186 · Cited by 1 · see citing works

Multi-Omic Profiling Reveals Epigenetic Drivers of Immunotherapy Resistance in Multiple MyelomaPreprint

Haertle, L., Buenache, N., González, F. J. V., Díaz, I. E., del Campo, P. L., Rosa-Rosa, J. M., Fernández, R. A. A., Muñoz, M. N. L., Sánchez‐Pina, J. M., García-Ortiz, A., et al. (2025) · medRxiv · doi:10.1101/2025.04.15.25325788 · Cited by 1 · see citing works

Oops! EMS mistakes--they're inevitable, stressful, painful and oh-so educational. This guide helps you classify them and avoid sweating the small stuff.

Murphy, P., & Taigman, M. (1998) · PubMed

The Proteasome Inhibitor Bortezomib Induces Tongue, Pharynx and Salivary Gland Cancer Cells Death in Vitro and Delays Tumor Growth of Salivary Gland Cancer Cells Transplanted in MicePreprint

Benvenuto, M., Ciuffa, S., Focaccetti, C., Sbardella, D., Fazi, S., Tundo, G. R., Barillari, G., Segni, M., Manzari, V., Modesti, A., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-561856/v1

Genome-Wide CRISPR-Cas9 Knockout Screening Identifies NUDCD2 Depletion as Sensitizer for Bortezomib, Carfilzomib and Ixazomib in Multiple Myeloma

Vlayen, S., Dierckx, T., Caruso, M., Sieben, S., Keersmaecker, K. D., Daelemans, D., & Delforge, M. (2025) · Hemato · doi:10.3390/hemato6030021

Additional file 2 of Pan-cancer analysis of genomic and transcriptomic data reveals the prognostic relevance of human proteasome genes in different cancer types

Larsson, P., Pettersson, D., Engqvist, H., Rönnerman, E. W., Forssell-Aronsson, E. B., Kovács, A., Karlsson, P., Helou, K., & Parris, T. Z. (2022) · Figshare · doi:10.6084/m9.figshare.21162570

Additional file 1 of Pan-cancer analysis of genomic and transcriptomic data reveals the prognostic relevance of human proteasome genes in different cancer types

Larsson, P., Pettersson, D., Engqvist, H., Rönnerman, E. W., Forssell-Aronsson, E. B., Kovács, A., Karlsson, P., Helou, K., & Parris, T. Z. (2022) · Figshare · doi:10.6084/m9.figshare.21162567

Étude des anomalies de XPO1 dans les lymphomes B

Miloudi, H. (2020) · theses.fr (ABES) · doi:10.70675/bed6d2d2zab43z4363z8153zaf694852437a

Profilage de l'ubiquitylation des protéines dans les cellules résistantes au bortézomib : rôle des enzymes de ubiquitylation

Gonzalez-Santamarta, M. (2022) · theses.fr (ABES) · doi:10.70675/7321c487z9a40z470eza548zb4a43e4d0322

Composition and activity of the proteasome in human iPSC-derived neuronal model of early-stage sporadic Alzheimer’s diseasePreprint

Aladeokin, A. C., Jeltsch, M., Davtyan, H., Blurton-Jones, M. M., & Koıstınaho, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.23.734021

Proteasome Disassembly and Downregulation Is Correlated with Viability during Stationary Phase

Bajorek, M., Finley, D. J., & Glickman, M. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00417-2 · Cited by 172 · see citing works

elifesciences.org RESEARCH ARTICLE Compromising the 19S 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. (2016)

Adaptive modification and flexibility of the proteasome system in response to proteasome inhibition

Naujokat, C., Fuchs, D., & Berges, C. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.05.007 · Cited by 45 · see citing works

The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes

Pickering, A. M., Koop, A. L., Teoh, C., Ermak, G., Grune, T., & Davies, K. J. A. (2010) · Biochemical Journal · doi:10.1042/bj20100878 · Cited by 319 · see citing works

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

Sahu, I., Mali, S. M., Sulkshane, P., Xu, C., Rozenberg, A., Morag, R., Sahoo, M. P., Singh, S. K., Ding, Z., Wang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26427-0 · Cited by 146 · see citing works