Targeting proteins for degradation.
Open accessAbstract
Protein degradation plays a central role in many cellular functions. Misfolded and damaged proteins are removed from the cell to avoid toxicity. The concentrations of regulatory proteins are adjusted by degradation at the appropriate time. Both foreign and native proteins are digested into small peptides as part of the adaptive immune response. In eukaryotic cells, an ATP-dependent protease called the proteasome is responsible for much of this proteolysis. Proteins are targeted for proteasomal degradation by a two-part degron, which consists of a proteasome binding signal and a degradation initiation site. Here we describe how both components contribute to the specificity of degradation.
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
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?
Most proteasomal substrates must be ubiquitinated before degradation.
“Because most proteasomal substrates must be ubiquitinated before degradation (Schrader et al., 2009), we next analyzed ubiquitinated proteins in the tibialis anterior muscles by immunoblotting and, as expected, found that their amounts were markedly higher in Rpt3-KO mice than in the Con mice (Figure 4A).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Schrader et al., 2009
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., & Deshaies, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141230798 · Cited by 2,609 · see citing works
Structure of 20S proteasome from yeast at 2.4Å resolution
Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,265 · see citing works
Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,192 · see citing works
In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue
Bachmair, A., Finley, D. J., & Varshavsky, A. J. (1986) · Science · doi:10.1126/science.3018930 · Cited by 1,976 · 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
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,718 · see citing works
A proteomics approach to understanding protein ubiquitination
Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D. J., & Gygi, S. P. (2003) · Nature Biotechnology · doi:10.1038/nbt849 · Cited by 1,601 · see citing works
Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution
Löwe, J., Stock, D., Jap, B. K., Zwickl, P., Baumeister, W. P., & Huber, R. (1995) · Science · doi:10.1126/science.7725097 · Cited by 1,527 · see citing works
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,472 · see citing works
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Jeffrey, P. D., Russo, A. A., Polyák, K., Gibbs, E., Hurwitz, J., Massagué, J., & Pavletich, N. P. (1995) · Nature · doi:10.1038/376313a0 · Cited by 1,441 · see citing works
How Proteolysis Drives the Cell Cycle
King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273 · see citing works
Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, A. J., Hochstrasser, M., Finley, D. J., & Peng, J. (2009) · Cell · doi:10.1016/j.cell.2009.01.041 · Cited by 1,125 · see citing works
Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
Keiler, K. C., Waller, P. R. H., & Sauer, R. T. (1996) · Science · doi:10.1126/science.271.5251.990 · Cited by 1,125 · see citing works
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099 · see citing works
Polyubiquitin chains: polymeric protein signals
Pickart, C. M., & Fushman, D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.09.009 · Cited by 1,052 · see citing works
Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome
Verma, R., Aravind, L., Oania, R. S., McDonald, W. H., Yates, J. R., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075898 · Cited by 994 · see citing works
Mechanism and function of deubiquitinating enzymes
Amerik, A. Y., & Hochstrasser, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.10.003 · Cited by 978 · see citing works
Misfolded proteins partition between two distinct quality control compartments
Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932 · see citing works
The Anaphase-Promoting Complex
Peters, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00540-3 · Cited by 909 · see citing works
Banaszynski, L. A., Chen, L.-C., Maynard-Smith, L. A., Ooi, A. G. L., & Wandless, T. J. (2006) · Cell · doi:10.1016/j.cell.2006.07.025 · Cited by 902 · see citing works
The proteasome: overview of structure and functions
TANAKA, K. (2009) · Proceedings of the Japan Academy, Series B · doi:10.2183/pjab.85.12 · Cited by 862 · see citing works
Controlling Signal Transduction with Synthetic Ligands
Spencer, D. M., Wandless, T. J., Schreiber, S. L., & Crabtree, G. R. (1993) · Science · doi:10.1126/science.7694365 · Cited by 845 · see citing works
A gated channel into the proteasome core particle.
Groll, M., Glickman, M. H., Finley, D. J., Bajorek, M., Köhler, A., Moroder, L., Rubin, D. M., & Huber, R. (2000) · Nature Structural Biology · doi:10.1038/80992 · Cited by 810 · see citing works
Hicke, L., Schubert, H., & Hill, C. P. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1701 · Cited by 795 · see citing works
Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K., & Ichihara, A. (1992) · Nature · doi:10.1038/360597a0 · Cited by 783 · see citing works
Ubiquitination of a Yeast Plasma Membrane Receptor Signals Its Ligand-Stimulated Endocytosis
Hicke, L., & Riezman, H. (1996) · Cell · doi:10.1016/s0092-8674(00)80982-4 · Cited by 783 · see citing works
A 26 S protease subunit that binds ubiquitin conjugates.
Deveraux, Q. L., Ustrell, V., Pickart, C. M., & Rechsteiner, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37244-7 · Cited by 763 · see citing works
A cryptic protease couples deubiquitination and degradation by the proteasome
Yao, T., & Cohen, R. E. (2002) · Nature · doi:10.1038/nature01071 · Cited by 727 · see citing works
Proteasome subunit Rpn13 is a novel ubiquitin receptor
Husnjak, K., Elsasser, S., Zhang, N., Chen, X., Randles, L., Shi, Y., Hofmann, K., Walters, K. J., Finley, D. J., & Đikić, I. (2008) · Nature · doi:10.1038/nature06926 · Cited by 662 · see citing works
Flynn, J. M., Neher, S. B., Kim, Y., Sauer, R. T., & Baker, T. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00060-1 · Cited by 605 · see citing works
Tobias, J. W., Shrader, T. E., Rocap, G., & Varshavsky, A. J. (1991) · Science · doi:10.1126/science.1962196 · Cited by 542 · see citing works
Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex
Jin, L., Williamson, A. P., Banerjee, S., Philipp, I., & Rapé, M. (2008) · Cell · doi:10.1016/j.cell.2008.04.012 · Cited by 536 · see citing works
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
Jarosch, E., Taxis, C., Volkwein, C., Bordallo, J., Finley, D. J., Wolf, D. H., & Sommer, T. (2002) · Nature Cell Biology · doi:10.1038/ncb746 · Cited by 532 · see citing works
Richly, H., Rapé, M., Braun, S. J., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523 · see citing works
Chemical Genetic Control of Protein Levels: Selective in Vivo Targeted Degradation
Schneekloth, J. S., Fonseca, F. N., Koldobskiy, M. A., Mandal, A., Deshaies, R. J., Sakamoto, K. M., & Crews, C. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039025z · Cited by 502 · see citing works
Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
Sauer, R. T., Bolon, D. N. A., Burton, B. M., Burton, R. E., Flynn, J. M., Grant, R. A., Hersch, G. L., Joshi, S. A., Kenniston, J. A., Levchenko, I. V., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.020 · Cited by 462 · see citing works
An unstructured initiation site is required for efficient proteasome-mediated degradation
Prakash, S., Tian, L., Ratliff, K. S., Lehotzky, R. E., & Matouschek, A. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb814 · Cited by 458 · see citing works
Self-citationRad23 links DNA repair to the ubiquitin/proteasome pathway
Schauber, C., Chen, L., Tongaonkar, P., Vega, I. E., Lambertson, D., Potts, W., & Madura, K. (1998) · Nature · doi:10.1038/35661 · Cited by 457 · see citing works
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
Lam, Y. A., Xu, W., Demartino, G., & Cohen, R. E. (1997) · Nature · doi:10.1038/385737a0 · Cited by 455 · see citing works
Verma, R., Oania, R. S., Graumann, J., & Deshaies, R. J. (2004) · Cell · doi:10.1016/j.cell.2004.06.014 · Cited by 449 · see citing works
A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
Lam, Y. A., Lawson, T. G., Velayutham, M., Zweier, J. L., & Pickart, C. M. (2002) · Nature · doi:10.1038/416763a · Cited by 446 · see citing works
The degradation signal in a short-lived protein
Bachmair, A., & Varshavsky, A. J. (1989) · Cell · doi:10.1016/0092-8674(89)90635-1 · Cited by 431 · see citing works
Endoproteolytic Activity of the Proteasome
Liu, C.-W., Corboy, M. J., Demartino, G., & Thomas, P. (2003) · Science · doi:10.1126/science.1079293 · Cited by 422 · see citing works
Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
Wilkinson, C. R. M., Seeger, M., Hartmann‐Petersen, R., Stone, M., Wallace, M., Semple, C. A. M., & Gordon, C. (2001) · Nature Cell Biology · doi:10.1038/ncb1001-939 · Cited by 407 · see citing works
Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase
Cadwell, K., & Coscoy, L. (2005) · Science · doi:10.1126/science.1110340 · Cited by 406 · see citing works
Lee, C., Schwartz, M. P., Prakash, S., Iwakura, M., & Matouschek, A. T. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00209-x · Cited by 393 · see citing works
Self-citationUbiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis
Pearce, M. J., Mintseris, J., Ferreyra, J. A., Gygi, S. P., & Darwin, K. H. (2008) · Science · doi:10.1126/science.1163885 · Cited by 377 · see citing works
Delivery of ubiquitinated substrates to protein-unfolding machines
Elsasser, S., & Finley, D. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-742 · Cited by 364 · see citing works
N-terminal ubiquitination: more protein substrates join in
Ciechanover, A. J. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.01.004 · Cited by 356 · see citing works
Deubiquitinating Enzyme Ubp6 Functions Noncatalytically to Delay Proteasomal Degradation
Hanna, J. W., Hathaway, N. A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D. S., Leggett, D., Gygi, S. P., King, R. W., & Finley, D. J. (2006) · Cell · doi:10.1016/j.cell.2006.07.038 · Cited by 354 · see citing works
Rad23 and Rpn10 Serve as Alternative Ubiquitin Receptors for the Proteasome
Elsasser, S., Chandler-Militello, D., Mueller, B., Hanna, J. W., & Finley, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404020200 · Cited by 349 · see citing works
Heat-Inducible Degron: a Method for Constructing Temperature-Sensitive Mutants
Dohmen, R. J., Wu, P., & Varshavsky, A. J. (1994) · Science · doi:10.1126/science.8122109 · Cited by 348 · see citing works
A Specificity-Enhancing Factor for the ClpXP Degradation Machine
Levchenko, I. V., Seidel, M., Sauer, R. T., & Baker, T. A. (2000) · Science · doi:10.1126/science.289.5488.2354 · Cited by 324 · see citing works
Gonzalez, S. L., Stremlau, M., He, X., Basile, J. R., & Münger, K. (2001) · Journal of Virology · doi:10.1128/jvi.75.16.7583-7591.2001 · Cited by 312 · see citing works
Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1
Nussbaum, A. K., Dick, T. P., Keilholz, W., Schirle, M., Stevanović, S., Dietz, K., Heinemeyer, W., Groll, M., Wolf, D. H., Huber, R., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12504 · Cited by 311 · see citing works
Crosas, B., Hanna, J. W., Kirkpatrick, D. S., Zhang, D. P., Tone, Y., Hathaway, N. A., Buecker, C., Leggett, D., Schmidt, M., King, R. W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.051 · Cited by 305 · see citing works
ATP-dependent proteases of bacteria: recognition logic and operating principles
Baker, T. A., & Sauer, R. T. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.10.006 · Cited by 303 · see citing works
Rad23 Promotes the Targeting of Proteolytic Substrates to the Proteasome
Chen, L., & Madura, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4902-4913.2002 · Cited by 291 · see citing works
The RssB response regulator directly targets ςS for degradation by ClpXPPreprint
Zhou, Y., Gottesman, S., Hoskins, J. R., Maurizi, M. R., & Wickner, S. (2001) · Genes & Development · doi:10.1101/gad.864401 · Cited by 290 · see citing works
ClpS, a Substrate Modulator of the ClpAP Machine
Dougan, D. A., Reid, B. G., Horwich, A. L., & Bukau, B. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00485-9 · Cited by 289 · see citing works
King, R. W., Glotzer, M., & Kirschner, M. W. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.9.1343 · Cited by 281 · see citing works
Cdc48 (p97): a ‘molecular gearbox’ in the ubiquitin pathway?
Jentsch, S., & Rumpf, S. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.005 · Cited by 280 · see citing works
The Processivity of Multiubiquitination by the APC Determines the Order of Substrate Degradation
Rapé, M., Reddy, S., & Kirschner, M. W. (2006) · Cell · doi:10.1016/j.cell.2005.10.032 · Cited by 280 · see citing works
Hiyama, H., Yokoi, M., Masutani, C., Sugasawa, K., Maekawa, T., Tanaka, K., Hoeijmakers, J. H. J., & Hanaoka, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.28019 · Cited by 263 · see citing works
The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies
Mogk, A., Schmidt, R., & Bukau, B. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.02.001 · Cited by 261 · see citing works
Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
Martin, A., Baker, T. A., & Sauer, R. T. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1503 · Cited by 260 · see citing works
Lysine 63‐linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh‐e, A., & Tanaka, K. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.305 · Cited by 260 · see citing works
Muffler, A., Fischer, D., Altuvia, S., Storz, G., & Hengge‐Aronis, R. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00475.x · Cited by 253 · see citing works
In Vitro Assembly and Recognition of Lys-63 Polyubiquitin Chains
Hofmann, R. M., & Pickart, C. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103378200 · Cited by 253 · see citing works
Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin‐like domain
Sakata, E., Yamaguchi, Y., Kurimoto, E., Kikuchi, J., Yokoyama, S., Yamada, S., Kawahara, H., Yokosawa, H., Hattori, N., Mizuno, Y., et al. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor764 · Cited by 243 · see citing works
In vivo degradation of a transcriptional regulator: The yeast α2 repressor
Hochstrasser, M., & Varshavsky, A. J. (1990) · Cell · doi:10.1016/0092-8674(90)90481-s · Cited by 240 · see citing works
Multiubiquitylation by E4 enzymes: ‘one size’ doesn't fit all
Hoppe, T. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.02.004 · Cited by 237 · see citing works
Wang, J., Song, J., Franklin, M. C., Kamtekar, S., Im, Y. J., Rho, S., Seong, I. S., Lee, C. S., Chung, C. H., & Eom, S. H. (2001) · Structure · doi:10.1016/s0969-2126(01)00570-6 · Cited by 237 · see citing works
ClpS is an essential component of the N-end rule pathway in Escherichia coli
Erbse, A. H., Schmidt, R., Bornemann, T., Schneider‐Mergener, J., Mogk, A., Zahn, R., Dougan, D. A., & Bukau, B. (2006) · Nature · doi:10.1038/nature04412 · Cited by 229 · see citing works
Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation
Hinnerwisch, J., Fenton, W. A., Furtak, K., Farr, G. W., & Horwich, A. L. (2005) · Cell · doi:10.1016/j.cell.2005.04.012 · Cited by 220 · see citing works
Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin‐independent substrate
Zhang, M., Pickart, C. M., & Coffino, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg158 · Cited by 219 · 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
Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
Ye, Y. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.01.005 · Cited by 213 · see citing works
Ubiquitin-independent proteolytic functions of the proteasome
Orłowski, M., & Wilk, S. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00197-8 · Cited by 213 · see citing works
Rao, H., & Sastry, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200245200 · Cited by 209 · see citing works
Liberles, S. D., Diver, S. T., Austin, D. J., & Schreiber, S. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.7825 · Cited by 199 · 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
Boutet, S. C., Disatnik, M., Chan, L. S., Iori, K., & Rando, T. A. (2007) · Cell · doi:10.1016/j.cell.2007.05.044 · Cited by 179 · see citing works
Modulating RssB activity: IraP, a novel regulator of σ S stability in Escherichia coliPreprint
Bougdour, A., Wickner, S., & Gottesman, S. (2006) · Genes & Development · doi:10.1101/gad.1400306 · Cited by 179 · see citing works
Kim, I., Mi, K., & Rao, H. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-11-0835 · Cited by 171 · see citing works
Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU
Wang, J., Song, J., Seong, I. S., Franklin, M. C., Kamtekar, S., Eom, S. H., & Chung, C. H. (2001) · Structure · doi:10.1016/s0969-2126(01)00670-0 · Cited by 169 · see citing works
Harnessing the Ubiquitination Machinery to Target the Degradation of Specific Cellular Proteins
Zhou, P., Bogacki, R., McReynolds, L., & Howley, P. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00074-5 · Cited by 164 · see citing works
Cis-trans recognition and subunit-specific degradation of short-lived proteins
Johnson, E. S., Gonda, D. K., & Varshavsky, A. (1990) · Nature · doi:10.1038/346287a0 · Cited by 152 · see citing works
Context of Multiubiquitin Chain Attachment Influences the Rate of Sic1 Degradation
Petroski, M. D., & Deshaies, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00221-1 · Cited by 149 · see citing works
Berezutskaya, E., & Bagchi, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30135 · Cited by 148 · see citing works
Burns, K. E., Liu, W.-T., Boshoff, H. I., Dorrestein, P. C., & Barry, C. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808032200 · Cited by 142 · see citing works
Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes
Striebel, F., Kress, W., & Weber-Ban, E. U. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.02.006 · Cited by 142 · see citing works
Yamada-Inagawa, T., Okuno, T., Karata, K., Yamanaka, K., & Ogura, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308327200 · Cited by 132 · see citing works
Verma, R., & Deshaies, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)80843-0 · Cited by 129 · see citing works
Conditional Protein Alleles Using Knockin Mice and a Chemical Inducer of Dimerization
Stankunas, K., Bayle, J. H., Gestwicki, J. E., Lin, Y., Wandless, T. J., & Crabtree, G. R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00491-x · Cited by 129 · see citing works
Proteasome substrate degradation requires association plus extended peptide
Takeuchi, J. S., Chen, H., & Coffino, P. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601476 · Cited by 128 · see citing works
Localization to the Proteasome Is Sufficient for Degradation
Janse, D. M., Crosas, B., Finley, D. J., & Church, G. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402954200 · Cited by 121 · see citing works
Dougan, D. A., Weber-Ban, E. U., & Bukau, B. (2003) · Molecular Cell · doi:10.1016/j.molcel.2003.08.012 · Cited by 119 · see citing works
Methotrexate Inhibits Proteolysis of Dihydrofolate Reductase by the N-end Rule Pathway
Johnston, J. A., Johnson, E. S., Waller, P. R., & Varshavsky, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.8172 · Cited by 118 · see citing works
Substrate selection by the proteasome during degradation of protein complexes
Prakash, S., Inobe, T., Hatch, A. J., & Matouschek, A. T. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.130 · Cited by 117 · see citing works
Self-citationHeessen, S., Masucci, M. G., & Dantuma, N. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.015 · Cited by 114 · see citing works
Tian, L. H., Holmgren, R. A., & Matouschek, A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1018 · Cited by 105 · see citing works
Self-citationUnraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination
Iyer, L. M., Burroughs, A. M., & Aravind, L. (2008) · Biology Direct · doi:10.1186/1745-6150-3-45 · Cited by 104 · see citing works
Verma, R., McDonald, W. H., Yates, J. R., & Deshaies, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00308-2 · Cited by 103 · see citing works
Kaplun, L., Tzirkin, R., Bakhrat, A., Shabek, N., Ivantsiv, Y., & Raveh, D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5355-5362.2005 · Cited by 101 · see citing works
Kravtsova‐Ivantsiv, Y., Cohen, S., & Ciechanover, A. J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.023 · Cited by 98 · see citing works
Conditional Control of Protein Function
Banaszynski, L. A., & Wandless, T. J. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.10.010 · Cited by 97 · see citing works
Ninnis, R. L., Spall, S. K., Talbo, G. H., Truscott, K. N., & Dougan, D. A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.134 · Cited by 96 · see citing works
Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
Piwko, W., & Jentsch, S. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1122 · Cited by 95 · see citing works
The Molecular Basis of N-End Rule Recognition
Wang, K. H., Roman-Hernandez, G., Grant, R. A., Sauer, R. T., & Baker, T. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.032 · Cited by 94 · see citing works
Small-molecule-mediated rescue of protein function by an inducible proteolytic shunt
Pratt, M. R., Schwartz, E. C., & Muir, T. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700816104 · Cited by 89 · see citing works
Park, E., Rho, Y. M., Koh, O. J., Ahn, S. W., Seong, I. S., Song, J., Bang, O., Seol, J. H., Wang, J., Eom, S. H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500035200 · Cited by 86 · see citing works
Schuenemann, V. J., Kralik, S. M., Albrecht, R., Spall, S. K., Truscott, K. N., Dougan, D. A., & Zeth, K. (2009) · EMBO Reports · doi:10.1038/embor.2009.62 · Cited by 85 · see citing works
Rad23 and Rpn10: perennial wallflowers join the m�l�e
Madura, K. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.10.008 · Cited by 82 · see citing works
ATP-dependent Proteases Differ Substantially in Their Ability to Unfold Globular Proteins
Koodathingal, P., Jaffe, N. E., Kraut, D. A., Prakash, S., Fishbain, S., Herman, C., & Matouschek, A. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900783200 · Cited by 77 · see citing works
Self-citationKlotzbücher, A., Stewart, E., Harrison, D., & Hunt, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00668.x · Cited by 75 · see citing works
Lupas, A. N., & Koretke, K. K. (2003) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00582-8 · Cited by 67 · see citing works
Nishiyama, A., Tachibana, K., Igarashi, Y., Yasuda, H., Tanahashi, N., Tanaka, K., Ohsumi, K., & Kishimoto, T. (2000) · Genes & Development · doi:10.1101/gad.823200 · Cited by 67 · see citing works
A strategy for the generation of conditional mutations by protein destabilization.
Park, E. C., Finley, D., & Szostak, J. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.4.1249 · Cited by 66 · see citing works
Dang, Y., Siew, L. M., & Zheng, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708728200 · Cited by 60 · see citing works
Eradication of pathogenic β-catenin by Skp1/Cullin/F box ubiquitination machinery
Su, Y., Ishikawa, S., Kojima, M., & Liu, B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2133261100 · Cited by 58 · see citing works
Proteasomes Begin Ornithine Decarboxylase Digestion at the C Terminus
Zhang, M., Macdonald, A. I., Hoyt, M. A., & Coffino, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314043200 · Cited by 54 · see citing works
Minimal length requirement for proteasomal degradation of ubiquitin‐dependent substrates
Verhoef, L. G. G. C., Heinen, C., Selivanova, A. V., Halff, E. F., Salomons, F. A., & Dantuma, N. P. (2008) · The FASEB Journal · doi:10.1096/fj.08-115055 · Cited by 54 · see citing works
Redirecting the specificity of ubiquitination by modifying ubiquitin-conjugating enzymes.
Gosink, M. M., & Vierstra, R. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9117 · Cited by 53 · see citing works
Degradation of Monoubiquitinated .alpha.-Globin by 26S Proteasomes
Shaeffer, J. R., & Kania, M. A. (1995) · Biochemistry · doi:10.1021/bi00012a020 · Cited by 52 · see citing works
Matsuzawa, S., Cuddy, M., Fukushima, T., & Reed, J. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507512102 · Cited by 47 · see citing works
Hoskins, J. R., & Wickner, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509154103 · Cited by 42 · see citing works
To degrade or release: ubiquitin-chain remodeling
Kraut, D. A., Prakash, S., & Matouschek, A. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.06.008 · Cited by 31 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- [81]Hoyt MA Coffino P Ubiquitin-free routes into the proteasome Cell Mol Life Sci 2004 61 1596 1600 15224184 PMC11138684
Cited by
Sorted by citations
Classification of Intrinsically Disordered Regions and Proteins
van der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., et al. (2014) · Chemical Reviews · doi:10.1021/cr400525m · Cited by 2,155 · see citing works
The Heat Shock Response: Life on the Verge of Death
Richter, K., Haslbeck, M., & Büchner, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.006 · Cited by 2,045 · see citing works
Enhancement of proteasome activity by a small-molecule inhibitor of USP14
Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works
The N‐end rule pathway and regulation by proteolysis
Varshavsky, A. J. (2011) · Protein Science · doi:10.1002/pro.666 · Cited by 696 · see citing works
Intrinsically disordered proteins: regulation and disease
Babu, M. M., van der Lee, R., de Groot, N. S., & Gsponer, J. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.011 · Cited by 597 · see citing works
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F., Binolfi, A., Frembgen-Kesner, T., Hingorani, K. S., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L. M., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 504 · see citing works
The Ubiquitin–Proteasome System of Saccharomyces cerevisiae
Finley, D. J., Ulrich, H. D., Sommer, T., & Kaiser, P. (2012) · Genetics · doi:10.1534/genetics.112.140467 · Cited by 427 · see citing works
Lee, H., Park, S., Weng, M.-W., Wang, H., Huang, W. C. W., Lepor, H., Wu, X., Chen, L., & Tang, M.-S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718185115 · Cited by 343 · see citing works
The FAD2 Gene in Plants: Occurrence, Regulation, and Role
Dar, A. A., Choudhury, A. R., Kancharla, P. K., & Arumugam, N. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.01789 · Cited by 314 · see citing works
The eukaryotic linear motif resource ELM: 10 years and counting
Dinkel, H., Roey, K. V., Michael, S., Davey, N. E., Weatheritt, R. J., Born, D., Speck, T., Krüger, D., Grebnev, G., Kubań, M., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1047 · Cited by 291 · see citing works
Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine
Aubin‐Tam, M., Olivares, A. O., Sauer, R. T., Baker, T. A., & Lang, M. J. (2011) · Cell · doi:10.1016/j.cell.2011.03.036 · Cited by 291 · see citing works
Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines
Olivares, A. O., Baker, T. A., & Sauer, R. T. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2015.4 · Cited by 292 · see citing works
Current strategies in extending half-lives of therapeutic proteins
Zaman, R., Islam, R. A., Ibnat, N., Othman, I., Zaini, A., Lee, C. Y., & Chowdhury, E. H. (2019) · Journal of Controlled Release · doi:10.1016/j.jconrel.2019.02.016 · Cited by 282 · see citing works
Maniaci, C., Hughes, S. J., Testa, A., Chen, W., Lamont, D. J., Rocha, S., Alessi, D. R., Romeo, R., & Ciulli, A. (2017) · Nature Communications · doi:10.1038/s41467-017-00954-1 · Cited by 245 · see citing works
Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes
Lee, M. J., Lee, B., Hanna, J. W., King, R. W., & Finley, D. J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r110.003871 · Cited by 239 · see citing works
Cdc48: a power machine in protein degradation
Stolz, A., Hilt, W., Buchberger, A., & Wolf, D. H. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.001 · Cited by 226 · see citing works
Targeted Intracellular Delivery of Antibodies: The State of the Art
Slastnikova, T. A., Ulasov, A. V., Rosenkranz, A. A., & Sobolev, A. S. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01208 · Cited by 214 · see citing works
Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
Verma, R., Oania, R., Fang, R., Smith, G. T., & Deshaies, R. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.017 · Cited by 196 · see citing works
The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions
Gibbs, D. J., Bacardit, J., Bachmair, A., & Holdsworth, M. J. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.001 · Cited by 182 · see citing works
α-synuclein aggregation and its modulation
Ghosh, D., Mehra, S., Sahay, S., Singh, P. K., & Maji, S. K. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.10.021 · Cited by 177 · see citing works
Defining the geometry of the two-component proteasome degron
Inobe, T., Fishbain, S., Prakash, S., & Matouschek, A. T. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.521 · Cited by 173 · see citing works
Self-citationFOXM1 and Cancer: Faulty Cellular Signaling Derails Homeostasis
Kalathil, D., John, S., & Nair, S. A. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.626836 · Cited by 169 · see citing works
Antolín‐Llovera, M., Ried, M. K., & Parniske, M. (2014) · Current Biology · doi:10.1016/j.cub.2013.12.053 · Cited by 156 · see citing works
The complexity of recognition of ubiquitinated substrates by the 26S proteasome
Ciechanover, A. J., & Stanhill, A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.07.007 · Cited by 152 · see citing works
A Caspase Cleaved Form of Tau Is Preferentially Degraded through the Autophagy Pathway
Dolan, P. J., & Johnson, G. V. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110940 · Cited by 147 · see citing works
Disordered Proteinaceous Machines
Fuxreiter, M., Tóth-Petróczy, Á., Kraut, D. A., Matouschek, A. T., Lim, R. Y. H., Xue, B., Kurgan, L., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr4007329 · Cited by 133 · see citing works
Self-citationSequence composition of disordered regions fine-tunes protein half-life
Fishbain, S., Inobe, T., Israeli, E., Chavali, S., Yu, H., Kago, G., Babu, M. M., & Matouschek, A. T. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2958 · Cited by 132 · see citing works
Self-citationProteolytic Control of the Oncoprotein Transcription Factor Myc
Thomas, L. R., & Tansey, W. P. (2011) · Advances in cancer research · doi:10.1016/b978-0-12-386469-7.00004-9 · Cited by 129 · see citing works
Knowing your friends and foes – plant receptor‐like kinases as initiators of symbiosis or defence
Antolín‐Llovera, M., Petutschnig, E. K., Ried, M. K., Lipka, V., Nürnberger, T., Robatzek, S., & Parniske, M. (2014) · New Phytologist · doi:10.1111/nph.13117 · Cited by 130 · see citing works
Mahammad, S., Murthy, S. N. P., Didonna, A., Grin, B., Israeli, E., Perrot, R., Bomont, P., Julien, J., Kuczmarski, E. R., Opal, P., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66387 · Cited by 129 · see citing works
Striebel, F., Hunkeler, M., Summer, H., & Weber-Ban, E. U. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.23 · Cited by 128 · see citing works
The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome
Olszewski, M. M., Williams, C., Dong, K. C., & Martin, A. (2019) · Communications Biology · doi:10.1038/s42003-019-0283-z · Cited by 127 · see citing works
Ubiquitin-Independent Degradation of Antiapoptotic MCL-1
Stewart, D. P., Koss, B. S., Bathina, M., Perciavalle, R. M., Bisanz, K. M., & Opferman, J. T. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01266-09 · Cited by 123 · see citing works
Rpn1 and Rpn2 Coordinate Ubiquitin Processing Factors at Proteasome*
Rosenzweig, R., Bronner, V., Zhang, D.-N., Fushman, D., & Glickman, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316323 · Cited by 123 · see citing works
Recognition of Client Proteins by the Proteasome
Yu, H., & Matouschek, A. T. (2017) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070816-033719 · Cited by 109 · see citing works
Self-citationBcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis
Sun, H., Kapuria, V., Peterson, L. F., Fang, D., Bornmann, W. G., Bartholomeusz, G. A., Talpaz, M., & Donato, N. J. (2011) · Blood · doi:10.1182/blood-2010-03-276477 · Cited by 112 · see citing works
Proteasomal dysfunction in aging and Huntington disease
Li, X., & Li, S. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.11.018 · Cited by 109 · see citing works
Chen, J., Ding, C., Chen, Y., Hu, W., Lu, Y., Wu, W., Zhang, Y., Yang, B., Wu, H., Peng, C., et al. (2020) · Oncogenesis · doi:10.1038/s41389-020-0226-z · Cited by 107 · see citing works
Target-induced clustering activates Trim-Away of pathogens and proteins
Zeng, J., Santos, A. F., Mukadam, A. S., Osswald, M., Jacques, D. A., Dickson, C. F., McLaughlin, S. H., Johnson, C. M., Kiss, L., Lupták, J., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00560-2 · Cited by 106 · see citing works
Assembly and Function of the Proteasome
Saeki, Y., & Tanaka, K. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_22 · Cited by 105 · see citing works
The bacterial N-end rule pathway: expect the unexpected
Dougan, D. A., Truscott, K. N., & Zeth, K. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07120.x · Cited by 105 · see citing works
Ubiquitin-independent proteasomal degradation driven by C-degron pathways
Makaros, Y., Raiff, A., Timms, R. T., Wagh, A. R., Israel-Gueta, M., Bekturova, A., Guez-Haddad, J., Brodsky, S., Opatowsky, Y., Glickman, M. H., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.04.023 · Cited by 101 · see citing works
Rad23 escapes degradation because it lacks a proteasome initiation region
Fishbain, S., Prakash, S., Herrig, A., Elsasser, S., & Matouschek, A. T. (2011) · Nature Communications · doi:10.1038/ncomms1194 · Cited by 101 · see citing works
Self-citationGrowing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin
Dantuma, N. P., & Hoppe, T. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.06.003 · Cited by 101 · see citing works
Effect of Carcinogenic Acrolein on DNA Repair and Mutagenic Susceptibility
Wang, H., Hu, Y., Tong, D., Huang, J., Gu, L., Wu, X., Chung, F., Li, G., & Tang, M.-S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329623 · Cited by 96 · see citing works
An asymmetric interface between the regulatory and core particles of the proteasome
Tian, G., Park, S., Lee, M. J., Huck, B., McAllister, F. E., Hill, C. P., Gygi, S. P., & Finley, D. J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2147 · Cited by 89 · see citing works
Khmelinskii, A., Meurer, M., Ho, C.-T., Besenbeck, B., Fueller, J., Lemberg, M. K., Bukau, B., Mogk, A., & Knop, M. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-07-0525 · Cited by 82 · see citing works
Structure, Assembly and Homeostatic Regulation of the 26S Proteasome
Xie, Y. (2010) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjq030 · Cited by 85 · see citing works
de Almeida, M. R., Ruedell, C. M., Ricachenevsky, F. K., Sperotto, R. A., Pasquali, G., & Fett‐Neto, A. G. (2010) · BMC Molecular Biology · doi:10.1186/1471-2199-11-73 · Cited by 84 · see citing works
Mehrzadi, S., Karimi, M. Y., Fatemi, A., Reiter, R. J., & Hosseinzadeh, A. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107825 · Cited by 83 · see citing works
Structure characterization of the 26S proteasome
Kim, H. M., Yu, Y., & Cheng, Y. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.08.008 · Cited by 78 · see citing works
Control of Tobacco mosaic virus Movement Protein Fate by CELL-DIVISION-CYCLE Protein48
Niehl, A., Amari, K., Gereige, D., Brandner, K., Mély, Y., & Heinlein, M. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.207399 · Cited by 77 · see citing works
Modification-specific proteomics in plant biology
Ytterberg, A. J., & Jensen, O. N. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.06.002 · Cited by 76 · see citing works
The Ubiquitin-Proteasome System Is Indispensable for the Maintenance of Muscle Stem Cells
Kitajima, Y., Suzuki, N., Nunomiya, A., Osana, S., Yoshioka, K., Tashiro, Y., Takahashi, R., Ono, Y., Aoki, M., & Nagatomi, R. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.10.009 · Cited by 75 · see citing works
Dynamics of protein synthesis and degradation through the cell cycle
Alber, A. B., & Suter, D. M. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1598725 · Cited by 73 · see citing works
Astier, J., Besson‐Bard, A., Lamotte, O., Bertoldo, J. B., Bourque, S., Terenzi, H. F., & Wendehenne, D. (2012) · Biochemical Journal · doi:10.1042/bj20120257 · Cited by 74 · see citing works
TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
Chen, L., Zhu, G., Johns, E., & Yang, X. (2018) · Nature Communications · doi:10.1038/s41467-018-03499-z · Cited by 70 · see citing works
Park, S., Kim, W., Tian, G., Gygi, S. P., & Finley, D. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.285924 · Cited by 70 · see citing works
Huang, W., Miao, M., Kud, J., Niu, X., Ouyang, B., Zhang, J., Ye, Z., Kuhl, J. C., Liu, Y., & Xiao, F. (2012) · New Phytologist · doi:10.1111/nph.12096 · Cited by 69 · see citing works
Wang, X., Yi, K., & Zhao, Y. (2017) · Food & Function · doi:10.1039/c7fo00662d · Cited by 68 · see citing works
The Ubiquitin Ligase Hul5 Promotes Proteasomal Processivity
Aviram, S., & Kornitzer, D. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00909-09 · Cited by 68 · see citing works
Zecha, J., Gabriel, W., Spallek, R., Chang, Y.-C., Mergner, J., Wilhelm, M., Bassermann, F. C., & Küster, B. (2022) · Nature Communications · doi:10.1038/s41467-021-27639-0 · Cited by 67 · see citing works
Craxton, A., Butterworth, M., Harper, N. W., Fairall, L., Schwabe, J. W. R., Ciechanover, A. J., & Cohen, G. M. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.16 · Cited by 67 · see citing works
Role of trypanosomatid's arginase in polyamine biosynthesis and pathogenesis
Balaña‐Fouce, R., Alvarez, E. C., Álvarez‐Velilla, R., Fernandez‐Prada, C., Pérez‐Pertejo, Y., & Reguera, R. M. (2011) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2011.10.007 · Cited by 67 · see citing works
Thompson, J. W., Nagel, J., Sjouke Hoving, B., Gerrits, B., Bauer, A., Thomas, J. R., Kirschner, M. W., Schirle, M., & Luchansky, S. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573352 · Cited by 66 · see citing works
Chou, T., & Deshaies, R. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.215319 · Cited by 64 · see citing works
A small-molecule inhibitor of deubiquitinating enzyme USP14 inhibits Dengue virus replication
Nag, D. K., & Finley, D. J. (2012) · Virus Research · doi:10.1016/j.virusres.2012.01.009 · Cited by 64 · see citing works
Prokaryotic Ubiquitin-Like Protein Provides a Two-Part Degron toMycobacteriumProteasome Substrates
Burns, K. E., Pearce, M. J., & Darwin, K. H. (2010) · Journal of Bacteriology · doi:10.1128/jb.01639-09 · Cited by 60 · see citing works
Interactions of the Proteasomal System with Chaperones
Kästle, M., & Grune, T. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00004-3 · Cited by 56 · see citing works
Targeted protein depletion in Saccharomyces cerevisiae by activation of a bidirectional degron
Jungbluth, M., Renicke, C. C., & Taxis, C. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-176 · Cited by 55 · see citing works
Ligand-switchable Substrates for a Ubiquitin-Proteasome System
Egeler, E. L., Urner, L. M., Rakhit, R., Liu, C. W., & Wandless, T. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264101 · Cited by 56 · see citing works
Intrinsic Disorder in Ubiquitination Substrates
Hagai, T., Azia, A., Tóth-Petróczy, Á., & Levy, Y. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.07.024 · Cited by 57 · see citing works
Sequence- and Species-Dependence of Proteasomal Processivity
Kraut, D. A., Israeli, E., Schrader, E. K., Patil, A., Nakai, K., Nanavati, D. M., Inobe, T., & Matouschek, A. T. (2012) · ACS Chemical Biology · doi:10.1021/cb3001155 · Cited by 56 · see citing works
Self-citationZhu, J., Li, Y., Chen, C., Ma, J., Sun, W., Tian, Z., Li, J., Xu, J., Liu, C. S., Zhang, D., et al. (2017) · Neoplasia · doi:10.1016/j.neo.2017.06.002 · Cited by 56 · see citing works
Regulation of histone modifying enzymes by the ubiquitin–proteasome system
Zou, C., & Mallampalli, R. K. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.12.016 · Cited by 53 · see citing works
Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway
Oh, J., Hyun, J.-Y., & Varshavsky, A. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705898114 · Cited by 55 · see citing works
Mota‐Peynado, A. D. L., Lee, S. Y.-C., Pierce, B. M., Wani, P. S., Singh, C. R., & Roelofs, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491662 · Cited by 53 · see citing works
Singh, R. K., Zerath, S., Kleifeld, O., Scheffner, M., Glickman, M. H., & Fushman, D. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.022467 · Cited by 51 · see citing works
Aleidi, S. M., Howe, V., Sharpe, L. J., Yang, A., Rao, G., Brown, A. J., & Gelissen, I. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.675579 · Cited by 49 · see citing works
ArPIKfyve Regulates Sac3 Protein Abundance and Turnover
Ikonomov, O. C., Sbrissa, D., Fligger, J., Delvecchio, K., & Shisheva, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.154658 · Cited by 49 · see citing works
Subcellular Clearance and Accumulation of Huntington Disease Protein: A Mini-Review
Zhao, T., Hong, Y., Li, X., & Li, S.-H. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00027 · Cited by 47 · see citing works
Abraham‐Juárez, M. J., Schrager‐Lavelle, A., Man, J., Whipple, C., Handakumbura, P., Babbitt, C. C., & Bartlett, M. E. (2020) · The Plant Cell · doi:10.1105/tpc.20.00300 · Cited by 47 · see citing works
Mansour, W., Nakasone, M. A., von Delbrück, M., Yu, Z., Krutauz, D., Reis, N., Kleifeld, O., Sommer, T., Fushman, D., & Glickman, M. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.568295 · Cited by 47 · see citing works
Zhang, S., Wang, X., Iqbal, S. A., Wang, Y., Osunkoya, A. O., Chen, Z., Chen, Z., Shin, D. M., Yuan, H., Wang, Y. A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.438341 · Cited by 47 · see citing works
Machines of Destruction – AAA+ Proteases and the Adaptors That Control Them
Gur, E., Ottofueling, R., & Dougan, D. A. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5940-4_1 · Cited by 45 · see citing works
Hempel, F., Felsner, G., & Maier, U. G. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07142.x · Cited by 46 · see citing works
Remote Activation of Enzyme Nanohybrids for Cancer Prodrug Therapy Controlled by Magnetic Heating
Torres‐Herrero, B., Armenia, I., Alleva, M., Asín, L., Correa, S., Ortiz, C., Fernández‐Afonso, Y., Gutiérrez, L., de la Fuente, J. M., Betancor, L., et al. (2023) · ACS Nano · doi:10.1021/acsnano.3c01599 · Cited by 45 · see citing works
Gödderz, D., Schäfer, E., Palanimurugan, R., & Dohmen, R. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.051 · Cited by 46 · see citing works
An Inducible System for Rapid Degradation of Specific Cellular Proteins Using Proteasome Adaptors
Wilmington, S. R., & Matouschek, A. T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152679 · Cited by 44 · see citing works
Self-citationPupylation versus ubiquitylation: tagging for proteasome-dependent degradation
Burns, K. E., & Darwin, K. H. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01447.x · Cited by 43 · see citing works
Kulka, L. A. M., Fangmann, P.-V., Panfilova, D., & Olzscha, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00425 · Cited by 40 · see citing works
Protein unfolding and degradation by the AAA+ Lon protease
Gur, E., Vishkautzan, M., & Sauer, R. T. (2011) · Protein Science · doi:10.1002/pro.2013 · Cited by 43 · see citing works
RelB/NF-κB2 Regulates Corticotropin-Releasing Hormone in the Human Placenta
Wang, B., Parobchak, N., & Rosen, T. (2012) · Molecular Endocrinology · doi:10.1210/me.2012-1035 · Cited by 43 · see citing works
Williams, C., Dong, K. C., Arkinson, C., & Martin, A. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.01.016 · Cited by 41 · see citing works
Snyers, L., Erhart, R., Laffer, S., Pusch, O., Weipoltshammer, K., & Schöfer, C. (2017) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2017.12.001 · Cited by 41 · see citing works
Opportunities for nanomaterials in enzyme therapy
Torres‐Herrero, B., Armenia, I., Ortiz, C., de la Fuente, J. M., Betancor, L., & Grazú, V. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.06.035 · Cited by 40 · see citing works
Delboy, M. G., & Nicola, A. V. (2011) · Journal of Virology · doi:10.1128/jvi.00267-11 · Cited by 40 · see citing works
Atkinson, S. P., Collin, J., Neganova, I. E., Anyfantis, G., Kim, K. B., Lako, M., & Armstrong, L. (2012) · Stem Cells · doi:10.1002/stem.1113 · Cited by 40 · see citing works
Myc proteins in brain tumor development and maintenance
Swartling, F. J. (2012) · Upsala Journal of Medical Sciences · doi:10.3109/03009734.2012.658975 · Cited by 41 · 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
- Authors
- Schrader, E. K., Harstad, K. G., & Matouschek, A.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Matouschek, Andreas
- ORCID
- Matouschek, Andreas
- Venue
- Nature Chemical Biology
- Published
- 2009-10-19
- Volume
- 5
- Issue
- 11
- Pages
- 815-822
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC4228941
- OpenAlex
- W4211006098
- Cited by
- 287
- References
- 127
- Citations by year
- 2026: 9 · 2025: 6 · 2024: 14 · 2023: 17 · 2022: 20 · 2021: 15 · 2020: 17 · 2019: 18 · 2018: 14 · 2017: 19 · 2016: 9 · 2015: 10 · 2014: 20 · 2013: 9 · 2012: 25
- FWCI
- 2.27
- Type
- journal article
- Language
- en
- Update notices
- erratum (2009-12-01)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (U54CA143869, T32CA080621)
- National Institute of General Medical Sciences (R01GM64003, R01GM063004, T32GM008061)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- protein degradation, proteasome, proteasomal degradation, degron, ubiquitin ligase, protein targeting, misfolded proteins, adaptive immune response, proteolysis
- MeSH terms
- Valosin Containing Protein, Adenosine Triphosphatases, Adenosine Triphosphate, Bacterial Proteins, Binding Sites, Cell Physiological Phenomena, Ornithine Decarboxylase, Peptide Chain Initiation, Translational, Peptide Hydrolases, Peptides, Proteins, Protein Folding, Cell Cycle Proteins, Ubiquitin, Proteasome Endopeptidase Complex
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
