The ubiquitin-proteasome system

Phosphorylation meets ubiquitination: the control of NF-κB activity

Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766

In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184

Genes required for mycobacterial growth defined by high density mutagenesis

Sassetti, C. M., Boyd, D. H., & Rubin, E. J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03425.x · Cited by 2,544

Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules.

Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., & Goldberg, A. L. (1994) · Cell · doi:10.1016/s0092-8674(94)90462-6 · Cited by 2,524

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 2,257

Aggresomes: A Cellular Response to Misfolded Proteins

Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148

The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis

Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608

Inhibition of Proteasome Activities and Subunit-Specific Amino-Terminal Threonine Modification by Lactacystin

Fenteany, G., Standaert, R. F., Lane, W. S., Choi, S., Corey, E. J., & Schreiber, S. L. (1995) · Science · doi:10.1126/science.7732382 · Cited by 1,583

Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution

Löwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., & Huber, R. (1995) · Science · doi:10.1126/science.7725097 · Cited by 1,525

Themes and variations on ubiquitylation

Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,482

Regulated Intramembrane Proteolysis

Brown, M. S., Ye, J., Rawson, R. B., & Goldstein, J. L. (2000) · Cell · doi:10.1016/s0092-8674(00)80675-3 · Cited by 1,329

Degradation of CFTR by the ubiquitin-proteasome pathway

Ward, C. L., Omura, S., & Kopito, R. R. (1995) · Cell · doi:10.1016/0092-8674(95)90240-6 · Cited by 1,304

UBE3A/E6-AP mutations cause Angelman syndrome

Kishino, T., Lalande, M., & Wagstaff, J. (1997) · Nature Genetics · doi:10.1038/ng0197-70 · Cited by 1,298

Protein regulation by monoubiquitin

Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,211

Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown.

Hershko, A., Heller, H., Elias, S., & Ciechanover, A. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82050-x · Cited by 1,160

The SCF ubiquitin ligase: insights into a molecular machine

Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114

A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly

Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,056

Recycling the Cell Cycle

Murray, A. W. (2004) · Cell · doi:10.1016/s0092-8674(03)01080-8 · Cited by 1,053

Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome

Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075898 · Cited by 1,000

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 920

Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis.

Hershko, A., Ciechanover, A., Heller, H., Haas, A. L., & Rose, I. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.4.1783 · Cited by 765

NEW EMBO MEMBERS' REVIEW: Lysosomal cysteine proteases: facts and opportunities

Turk, V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4629 · Cited by 756

Proteasomes and their kin: proteases in the machine age

Pickart, C. M., & Cohen, R. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1336 · Cited by 735

A cryptic protease couples deubiquitination and degradation by the proteasome

Yao, T., & Cohen, R. E. (2002) · Nature · doi:10.1038/nature01071 · Cited by 725

Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and ‘aggresomes’ during oxidative stress, aging, and disease

Grune, T., Jung, T., Merker, K., & Davies, K. J. A. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.04.020 · Cited by 655

A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes

Ciehanover, A., Hod, Y., & Hershko, A. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91249-4 · Cited by 648

Proteasome from Thermoplasma acidophilum : a Threonine Protease

Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R., & Baumeister, W. (1995) · Science · doi:10.1126/science.7725107 · Cited by 634

Multiple Associated Proteins Regulate Proteasome Structure and Function

Leggett, D. S., Hanna, J., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R. T., Walz, T., Ploegh, H., & Finley, D. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00638-x · Cited by 631

Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination

Staub, O., Gautschi, I., Ishikawa, T., Breitschopf, K., Ciechanover, A., Schild, L., & Rotin, D. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6325 · Cited by 601

The Sizes of Peptides Generated from Protein by Mammalian 26 and 20 S Proteasomes

Kisselev, A. F., Akopian, T. N., Woo, K. M., & Goldberg, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3363 · Cited by 573

Proteasome Inhibition As a Novel Therapeutic Target in Human Cancer

Rajkumar, S. V., Richardson, P. G., Hideshima, T., & Anderson, K. C. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.11.030 · Cited by 569

A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes.

Etlinger, J. D., & Goldberg, A. L. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.1.54 · Cited by 563

Proteasomal Proteomics: Identification of Nucleotide-sensitive Proteasome-interacting Proteins by Mass Spectrometric Analysis of Affinity-purified Proteasomes

Verma, R., Chen, S., Feldman, R., Schieltz, D., Yates, J., Dohmen, J., & Deshaies, R. J. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.10.3425 · Cited by 540

The Proteasome of Mycobacterium tuberculosis Is Required for Resistance to Nitric Oxide

Darwin, K. H., Ehrt, S., Gutierrez-Ramos, J.-C., Weich, N., & Nathan, C. F. (2003) · Science · doi:10.1126/science.1091176 · Cited by 535

Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85

Ciechanover, A., Finley, D., & Varshavsky, A. (1984) · Cell · doi:10.1016/0092-8674(84)90300-3 · Cited by 533

MHC Class I Expression in Mice Lacking the Proteasome Subunit LMP-7

Fehling, H. J., Swat, W., Laplace, C., Kühn, R., Rajewsky, K., Müller, U., & von Boehmer, H. (1994) · Science · doi:10.1126/science.8066463 · Cited by 525

Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85

Finley, D., Ciechanover, A., & Varshavsky, A. (1984) · Cell · doi:10.1016/0092-8674(84)90299-x · Cited by 522

The Active Sites of the Eukaryotic 20 S Proteasome and Their Involvement in Subunit Precursor Processing

Heinemeyer, W., Fischer, M., Krimmer, T., Stachon, U., & Wolf, D. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25200 · Cited by 519

The Structure of the Mammalian 20S Proteasome at 2.75 Å Resolution

Unno, M., Mizushima, T., Morimoto, Y., Tomisugi, Y., Tanaka, K., Yasuoka, N., & Tsukihara, T. (2002) · Structure · doi:10.1016/s0969-2126(02)00748-7 · Cited by 519

Dynamic Association of Proteasomal Machinery with the Centrosome

Christian Wigley, W., Fabunmi, R. P., Lee, M. G., Marino, C. R., Muallem, S., DeMartino, G. N., & Thomas, P. J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.3.481 · Cited by 513

Structural basis for the activation of 20S proteasomes by 11S regulators

Whitby, F. G., Masters, E. I., Kramer, L., Knowlton, J. R., Yao, Y., Wang, C. C., & Hill, C. P. (2000) · Nature · doi:10.1038/35040607 · Cited by 490

The Regulatory Particle of the Saccharomyces cerevisiae Proteasome

Glickman, M. H., Rubin, D. M., Fried, V. A., & Finley, D. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3149 · Cited by 483

CHIP: a link between the chaperone and proteasome systems

McDonough, H., & Patterson, C. (2003) · Cell Stress & Chaperones · doi:10.1379/1466-1268(2003)008<0303:calbtc>2.0.co;2 · Cited by 468

Rad23 links DNA repair to the ubiquitin/proteasome pathway

Schauber, C., Chen, L., Tongaonkar, P., Vega, I., Lambertson, D., Potts, W., & Madura, K. (1998) · Nature · doi:10.1038/35661 · Cited by 457

Altered peptidase and viral-specific T cell response in LMP2 mutant mice

Van Kaert, L., Ashton-Rickardt, P. G., Eichelberger, M., Gaczynska, M., Nagashima, K., Rock, K. L., Goldberg, A. L., Doherty, P. C., & Tonegawa, S. (1994) · Immunity · doi:10.1016/1074-7613(94)90043-4 · Cited by 447

Immunoproteasome Assembly: Cooperative Incorporation of Interferon γ (IFN-γ)–inducible Subunits

Griffin, T. A., Nandi, D., Cruz, M., Fehling, H. J., Kaer, L. V., Monaco, J. J., & Colbert, R. A. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.1.97 · Cited by 444

Endoproteolytic Activity of the Proteasome

Liu, C.-W., Corboy, M. J., DeMartino, G. N., & Thomas, P. J. (2003) · Science · doi:10.1126/science.1079293 · Cited by 421

NEW EMBO MEMBER'S REVIEW: For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection

Kostova, Z. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg227 · Cited by 411

Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)

Arrigo, A.-P., Tanaka, K., Goldberg, A. L., & Welch, W. J. (1988) · Nature · doi:10.1038/331192a0 · Cited by 405

Autocatalytic Subunit Processing Couples Active Site Formation in the 20S Proteasome to Completion of Assembly

Chen, P., & Hochstrasser, M. (1996) · Cell · doi:10.1016/s0092-8674(00)80171-3 · Cited by 404

Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes.

Wilkinson, K. D., Urban, M. K., & Haas, A. L. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43857-x · Cited by 399

Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors

Rechsteiner, M., & Hill, C. P. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.11.003 · Cited by 371

Delivery of ubiquitinated substrates to protein-unfolding machines

Elsasser, S., & Finley, D. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-742 · Cited by 364

N-terminal ubiquitination: more protein substrates join in

Ciechanover, A. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.01.004 · Cited by 359

Evidence that Pituitary Cation‐Sensitive Neutral Endopeptidase Is a Multicatalytic Protease Complex

Wilk, S., & Orlowski, M. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb08056.x · Cited by 358

Intracellular localization of proteasomes

Wójcik, C., & DeMartino, G. N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00380-1 · Cited by 352

Disruption of the Murine Calpain Small Subunit Gene, Capn4: Calpain Is Essential for Embryonic Development but Not for Cell Growth and Division

Arthur, J. S. C., Elce, J. S., Hegadorn, C., Williams, K., & Greer, P. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.12.4474-4481.2000 · Cited by 331

PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone

Benaroudj, N., & Goldberg, A. L. (2000) · Nature Cell Biology · doi:10.1038/35041081 · Cited by 328

Ump1p Is Required for Proper Maturation of the 20S Proteasome and Becomes Its Substrate upon Completion of the Assembly

Ramos, P. C., Höckendorff, J., Johnson, E. S., Varshavsky, A., & Dohmen, R. J. (1998) · Cell · doi:10.1016/s0092-8674(00)80942-3 · Cited by 326

PA200, a nuclear proteasome activator involved in DNA repair

Ustrell, V. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf333 · Cited by 326

A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution.

Tanaka, K., Ii, K., Ichihara, A., Waxman, L., & Goldberg, A. L. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66853-x · Cited by 324

Inhibition of Proteasome Activity Induces Concerted Expression of Proteasome Genes and de Novo Formation of Mammalian Proteasomes

Meiners, S., Heyken, D., Weller, A., Ludwig, A., Stangl, K., Kloetzel, P.-M., & Krüger, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301032200 · Cited by 318

Crystal Structure of Epoxomicin:20S Proteasome Reveals a Molecular Basis for Selectivity of α‘,β‘-Epoxyketone Proteasome Inhibitors

Groll, M., Kim, K. B., Kairies, N., Huber, R., & Crews, C. M. (2000) · Journal of the American Chemical Society · doi:10.1021/ja993588m · Cited by 304

The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study

Groll, M., Heinemeyer, W., Jäger, S., Ullrich, T., Bochtler, M., Wolf, D. H., & Huber, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.10976 · Cited by 300

Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins.

Hershko, A., Eytan, E., Ciechanover, A., & Haas, A. L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45327-1 · Cited by 290

IFN-γ-induced immune adaptation of the proteasome system is an accelerated and transient response

Heink, S., Ludwig, D., Kloetzel, P.-M., & Krüger, E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501711102 · Cited by 288

Ubiquitin-lysozyme conjugates. Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates.

Hough, R., Pratt, G., & Rechsteiner, M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35950-1 · Cited by 286

Regulated protein degradation

Varshavsky, A. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.04.005 · Cited by 281

Coordinated Dual Cleavages Induced by the Proteasome Regulator PA28 Lead to Dominant MHC Ligands

Dick, T. P., Ruppert, T., Groettrup, M., Kloetzel, P. M., Kuehn, L., Koszinowski, U. H., Stevanovic, S., Schild, H., & Rammensee, H.-G. (1996) · Cell · doi:10.1016/s0092-8674(00)80097-5 · Cited by 280

The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria

Dahlmann, B., Kopp, F., Kuehn, L., Niedel, B., Pfeifer, G., Hegerl, R., & Baumeister, W. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81441-3 · Cited by 278

Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability

Rao, H., Uhlmann, F., Nasmyth, K., & Varshavsky, A. (2001) · Nature · doi:10.1038/35073627 · Cited by 276

Dynamics of proteasome distribution in living cells

Reits, E. A. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.20.6087 · Cited by 273

A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes

Hirano, Y., Hendil, K. B., Yashiroda, H., Iemura, S.-I., Nagane, R., Hioki, Y., Natsume, T., Tanaka, K., & Murata, S. (2005) · Nature · doi:10.1038/nature04106 · Cited by 254

Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity of alpha,beta-epoxyketone proteasome inhibitors: 1g65

Groll, M., Kim, K. B., Kairies, N., Huber, R., & Crews, C. (2000) · Worldwide Protein Data Bank · doi:10.2210/pdb1g65/pdb · Cited by 253

ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation

Benaroudj, N., Zwickl, P., Seemüller, E., Baumeister, W., & Goldberg, A. L. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00775-x · Cited by 245

Potential for proteasome inhibition in the treatment of cancer

Adams, J. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02647-3 · Cited by 245

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

The 1.9 Å Structure of a Proteasome-11S Activator Complex and Implications for Proteasome-PAN/PA700 Interactions

Förster, A., Masters, E. I., Whitby, F. G., Robinson, H., & Hill, C. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.016 · Cited by 236

Hepatitis B Virus X Protein Is both a Substrate and a Potential Inhibitor of the Proteasome Complex

Hu, Z., Zhang, Z., Doo, E., Coux, O., Goldberg, A. L., & Liang, T. J. (1999) · Journal of Virology · doi:10.1128/jvi.73.9.7231-7240.1999 · Cited by 232

Components of a system that ligates cyclin to ubiquitin and their regulation by the protein kinase cdc2.

Hershko, A., Ganoth, D., Sudakin, V., Dahan, A., Cohen, L. H., Luca, F. C., Ruderman, J. V., & Eytan, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37636-6 · Cited by 229

Multiple forms of the 20 S multicatalytic and the 26 S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate.

Hoffman, L., Pratt, G., & Rechsteiner, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41680-8 · Cited by 229

Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP.

Hershko, A., Ciechanover, A., & Rose, I. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.7.3107 · Cited by 223

Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes

HENDIL, K. B., KHAN, S., & TANAKA, K. (1998) · Biochemical Journal · doi:10.1042/bj3320749 · Cited by 218

Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast

Enenkel, C., Lehmann, A., & Kloetzel, P.-M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.21.6144 · Cited by 215

Range of Sizes of Peptide Products Generated during Degradation of Different Proteins by Archaeal Proteasomes

Kisselev, A. F., Akopian, T. N., & Goldberg, A. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.1982 · Cited by 212

Degradation of Proteasomes by Lysosomes in Rat Liver

Cuervo, A. M., Palmer, A., Rivett, A. J., & Knecht, E. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0792p.x · Cited by 207

Critical elements in proteasome assembly

Zwickl, P., Kleinz, J., & Baumeister, W. (1994) · Nature Structural Biology · doi:10.1038/nsb1194-765 · Cited by 199

The proteasome and MHC class I antigen processing

Kloetzel, P.-M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.10.004 · Cited by 197

Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach

Groll, M., & Huber, R. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.025 · Cited by 193

Structure of the proteasome activator REGα (PA28α)

Knowlton, J. R., Johnston, S. C., Whitby, F. G., Realini, C., Zhang, Z., Rechsteiner, M., & Hill, C. P. (1997) · Nature · doi:10.1038/37670 · Cited by 186

Growth Retardation in Mice Lacking the Proteasome Activator PA28γ

Murata, S., Kawahara, H., Tohma, S., Yamamoto, K., Kasahara, M., Nabeshima, Y.-I., Tanaka, K., & Chiba, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38211 · Cited by 182

Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits

Nandi, D. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5363 · Cited by 182

Caspase Activation Inhibits Proteasome Function during Apoptosis

Sun, X.-M., Butterworth, M., MacFarlane, M., Dubiel, W., Ciechanover, A., & Cohen, G. M. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00156-x · Cited by 179

The protein substrate binding site of the ubiquitin-protein ligase system.

Hershko, A., Heller, H., Eytan, E., & Reiss, Y. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67192-3 · Cited by 178

Loss of Calpain 3 Proteolytic Activity Leads to Muscular Dystrophy and to Apoptosis-Associated Iκbα/Nuclear Factor κb Pathway Perturbation in Mice

Richard, I., Roudaut, C., Marchand, S., Baghdiguian, S., Herasse, M., Stockholm, D., Ono, Y., Suel, L., Bourg, N., Sorimachi, H., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1583 · Cited by 177

The prosome: an ubiquitous morphologically distinct RNP particle associated with repressed mRNPs and containing specific ScRNA and a characteristic set of proteins.

Schmid, H. P., Akhayat, O., Martins De Sa, C., Puvion, F., Koehler, K., & Scherrer, K. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01757.x · Cited by 175

Activity and Regulation of the Centrosome-associated Proteasome

Fabunmi, R. P., Wigley, W. C., Thomas, P. J., & DeMartino, G. N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.409 · Cited by 173

An Archaebacterial ATPase, Homologous to ATPases in the Eukaryotic 26 S Proteasome, Activates Protein Breakdown by 20 S Proteasomes

Zwickl, P., Ng, D., Woo, K. M., Goldberg, A. L., & Klenk, H.-P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26008 · Cited by 169

Molecular clearance of ataxin‐3 is regulated by a mammalian E4

Matsumoto, M., Yada, M., Hatakeyama, S., Ishimoto, H., Tanimura, T., Tsuji, S., Kakizuka, A., Kitagawa, M., & Nakayama, K. I. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600081 · Cited by 166

Immunoproteasomes Largely Replace Constitutive Proteasomes During an Antiviral and Antibacterial Immune Response in the Liver

Khan, S., van den Broek, M., Schwarz, K., de Giuli, R., Diener, P.-A., & Groettrup, M. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.12.6859 · Cited by 164

Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta

Murata, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5898 · Cited by 163

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