The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Abstract
▪ Abstract In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built from ∼31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. The regulatory complexes are also implicated in unfolding and translocation of ubiquitinated targets into the interior of the 20S complex, where they are degraded to oligopeptides. Structure, assembly and enzymatic mechanism of the 20S complex have been elucidated, but the functional organization of the 19S complex is less well understood. Most subunits of the 19S complex have been identified, however, specific functions have been assigned to only a few. A low-resolution structure of the 26S proteasome has been obtained by electron microscopy, but the precise arrangement of subunits in the 19S complex is unclear.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
Chains linked via K48 in ubiquitin typically lead to degradation of the substrate by the proteasome.
“Chains linked via Lys48 (K48) in Ub, the best-characterized type of Ub conjugation, typically lead to degradation of the substrate by the proteasome (Voges et al, 1999).”
From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Voges et al, 1999
Citations
Cites
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids
Adams, J., Behnke, M., Chen, S., Cruickshank, A. A., Dick, L. R., Grenier, L., Klunder, J. M., Ma, Y.-T., Plamondon, L., & Stein, R. L. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00029-8 · Cited by 685
Flagged first, then by citations
Research works printed but not linked: 411
- 10.1016/S0968-0004(97)01117-1 · DOI
- 10.1016/S0092-8674(00)80929-0 · DOI
- 10.1016/S0092-8674(00)80427-4 · DOI
- 10.1016/S0092-8674(00)80428-6 · DOI
- 10.1016/S0968-0004(96)10038-4 · DOI
- 10.1101/gad.11.7.815 · DOI
- 10.1002/pro.5560061001 · DOI
- 10.1038/nsb0297-133 · DOI
- 10.1016/S0092-8674(00)81603-7 · DOI
- 10.1146/annurev.ge.26.120192.001143 · DOI
- 10.1146/annurev.genet.30.1.405 · DOI
- 10.1016/S0968-0004(97)01122-5 · DOI
- 10.1146/annurev.biochem.67.1.425 · DOI · Paper page
- 10.1101/SQB.1995.060.01.055 · DOI
- 10.1146/annurev.bi.65.070196.004101 · DOI
- 10.1515/bchm.1997.378.3-4.121 · DOI
- 10.1016/0005-2736(68)90157-0 · DOI
- 10.1111/j.1471-4159.1980.tb07873.x · DOI
- 10.1016/0006-291X(81)91823-4 · DOI
- 10.1111/j.1471-4159.1983.tb08056.x · DOI
- 10.1016/0005-2744(80)90056-X · DOI
- Kleinschmidt JA, 1983, Eur. J. Cell Biol., 32, 143
- 10.1042/bj2280161 · DOI
- Rivett AJ, 1985, J. Biol. Chem., 260, 12600, 10.1016/S0021-9258(17)38913-5 · DOI
- 10.1002/j.1460-2075.1984.tb01757.x · DOI
- 10.1016/0014-4827(87)90130-3 · DOI
- 10.1038/331192a0 · DOI
- 10.1038/331190a0 · DOI
- 10.1073/pnas.79.9.3001 · DOI
- 10.1038/309797a0 · DOI
- 10.1038/353355a0 · DOI
- 10.1038/353357a0 · DOI
- 10.1016/0014-5793(89)81441-3 · DOI
- Zwickl P, Goldberg AL, Baumeister W. 1999. InProteasomes, ed. DH Wolf, W Hilt. Austin: Landes Biosci. In press
- 10.1016/S0960-9822(95)00153-9 · DOI
- 10.1016/S0966-842X(98)01432-2 · DOI
- 10.1074/jbc.270.48.28617 · DOI
- Maupin-Furlow JA, 1998, J. Bacteriol., 180, 1480, 10.1128/JB.180.6.1480-1487.1998 · DOI
- Bauer MW, 1997, Appl. Eviron. Microbiol., 63, 1160, 10.1128/aem.63.3.1160-1164.1997 · DOI
- 10.1126/science.273.5278.1058 · DOI
- 10.1128/jb.179.22.7135-7155.1997 · DOI
- 10.1038/37052 · DOI
- 10.1093/dnares/5.2.55 · DOI
- 10.1046/j.1365-2958.1997.4721837.x · DOI
- Nagy I, 1998, J. Bacteriol., 180, 5448, 10.1128/JB.180.20.5448-5453.1998 · DOI
- 10.1126/science.7725107 · DOI
- 10.1016/S0968-0004(96)10012-8 · DOI
- 10.1038/386463a0 · DOI
- 10.1146/annurev.ge.29.120195.003501 · DOI
- 10.1146/annurev.immunol.16.1.323 · DOI
- Yuan X, 1996, Genetics, 144, 147, 10.1093/genetics/144.1.147 · DOI
- Fu HY, 1998, Genetics, 149, 677, 10.1093/genetics/149.2.677 · DOI
- 10.1016/0014-5793(92)80925-7 · DOI
- 10.1021/bi00119a004 · DOI
- 10.1038/382468a0 · DOI
- 10.1038/nsb1194-765 · DOI
- 10.1111/j.1432-1033.1994.tb19084.x · DOI
- 10.1006/jsbi.1998.4068 · DOI
- 10.1016/S0014-5793(96)01403-2 · DOI
- 10.1016/S0014-5793(97)01370-7 · DOI
- 10.1074/jbc.272.3.1791 · DOI
- 10.1002/pro.5560070401 · DOI
- 10.1096/fasebj.11.14.9409542 · DOI
- 10.1007/s000180050147 · DOI
- 10.1006/jmbi.1997.0947 · DOI
- 10.1016/S0092-8674(00)80942-3 · DOI
- 10.1074/jbc.272.15.10080 · DOI
- 10.1006/jmbi.1997.1429 · DOI
- 10.1093/emboj/16.17.5363 · DOI
- 10.1016/S0092-8674(00)80171-3 · DOI
- 10.1002/j.1460-2075.1996.tb01081.x · DOI
- 10.1016/0014-5793(88)81069-X · DOI
- 10.1016/0014-5793(91)80567-M · DOI
- 10.1016/0014-5793(91)81256-8 · DOI
- 10.1002/j.1460-2075.1992.tb05206.x · DOI
- 10.1006/jsbi.1993.1044 · DOI
- 10.1006/jsbi.1994.1041 · DOI
- 10.1007/BF00990965 · DOI
- 10.1006/jmbi.1995.0220 · DOI
- 10.1126/science.7725097 · DOI
- 10.1006/jmbi.1993.1003 · DOI
- 10.1073/pnas.94.7.2939 · DOI
- 10.1021/bi00224a022 · DOI
- 10.1038/nsb0395-199 · DOI
- 10.1038/378416a0 · DOI
- 10.1016/S0968-0004(98)01254-7 · DOI
- 10.1038/373264a0 · DOI
- 10.1073/pnas.94.14.7156 · DOI
- 10.1074/jbc.272.40.25200 · DOI
- 10.1016/0014-5793(95)00036-9 · DOI
- 10.1006/jmbi.1998.1818 · DOI
- 10.1126/science.7732382 · DOI · Paper page
- 10.1074/jbc.271.13.7273 · DOI
- 10.1073/pnas.94.13.6629 · DOI
- 10.1016/S1074-5521(98)90169-7 · DOI
- 10.1074/jbc.272.42.26103 · DOI
- 10.1021/bi00154a014 · DOI
- 10.1016/S0092-8674(94)90462-6 · DOI · Paper page
- 10.1046/j.1471-4159.1994.63041578.x · DOI
- Vinitsky A, 1994, J. Biol. Chem., 269, 29860, 10.1016/S0021-9258(18)43960-9 · DOI
- Harding CV, 1995, J. Immunol., 155, 1767, 10.4049/jimmunol.155.4.1767 · DOI
- 10.1002/(SICI)1097-0282(1997)43:4<269::AID-BIP2>3.0.CO;2-T · DOI
- 10.1016/S0962-8924(98)01346-4 · DOI · Paper page
- 10.1074/jbc.273.15.8545 · DOI
- 10.1021/bi00497a001 · DOI
- 10.1002/j.1460-2075.1991.tb07982.x · DOI
- Heinemeyer W, 1993, J. Biol. Chem., 268, 5115, 10.1016/S0021-9258(18)53509-2 · DOI
- Hilt W, 1993, J. Biol. Chem., 268, 3479, 10.1016/S0021-9258(18)53719-4 · DOI
- 10.1016/0014-5793(94)80455-9 · DOI
- 10.1074/jbc.273.40.25637 · DOI
- 10.1016/0014-5793(94)00665-2 · DOI
- 10.1111/j.1432-1033.1996.00404.x · DOI
- 10.1016/S0014-5793(98)01010-2 · DOI
- 10.1073/pnas.95.21.12504 · DOI
- 10.1074/jbc.273.4.1982 · DOI
- Ma CP, 1992, J. Biol. Chem., 267, 10515, 10.1016/S0021-9258(19)50047-3 · DOI
- Dubiel W, 1992, J. Biol. Chem., 267, 22369, 10.1016/S0021-9258(18)41681-X · DOI
- 10.1074/jbc.271.30.18237 · DOI
- 10.1074/jbc.271.42.26410 · DOI
- 10.1016/0014-5793(96)00946-5 · DOI
- 10.1006/jmbi.1994.1113 · DOI
- 10.1002/pro.5560061123 · DOI
- 10.1038/37670 · DOI
- 10.1016/S0092-8674(00)80097-5 · DOI
- 10.1038/381166a0 · DOI
- Kohda K, 1998, J. Immunol., 160, 4923, 10.4049/jimmunol.160.10.4923 · DOI
- 10.1016/0014-5793(95)00492-R · DOI
- 10.1046/j.1365-2443.1997.d01-308.x · DOI
- 10.1007/s002510050281 · DOI
- 10.1073/pnas.95.6.2807 · DOI
- 10.1074/jbc.273.16.9501 · DOI
- 10.1007/s002510050246 · DOI
- 10.1073/pnas.74.1.54 · DOI
- 10.1016/0006-291X(78)91249-4 · DOI
- 10.1073/pnas.77.4.1783 · DOI
- Wilkinson KD, 1980, J. Biol. Chem., 255, 7529, 10.1016/S0021-9258(19)43857-X · DOI
- 10.1016/0006-291X(85)91050-2 · DOI
- Hough R, 1986, J. Biol. Chem., 261, 2400, 10.1016/S0021-9258(17)35950-1 · DOI
- Hough R, 1987, J. Biol. Chem., 262, 8303, 10.1016/S0021-9258(18)47564-3 · DOI
- Ganoth D, 1988, J. Biol. Chem., 263, 12412, 10.1016/S0021-9258(18)37771-8 · DOI
- 10.1073/pnas.86.20.7751 · DOI
- Driscoll J, 1990, J. Biol. Chem., 265, 4789, 10.1016/S0021-9258(19)34041-4 · DOI
- 10.1042/bj2800225 · DOI
- 10.1016/0003-9861(92)90487-H · DOI
- Hoffman L, 1992, J. Biol. Chem., 267, 22362, 10.1016/S0021-9258(18)41680-8 · DOI
- Udvardy A, 1993, J. Biol. Chem., 268, 9055, 10.1016/S0021-9258(18)52977-X · DOI
- Chu-Ping M, 1994, J. Biol. Chem., 269, 3539, 10.1016/S0021-9258(17)41897-7 · DOI
- Peters JM, 1994, J. Biol. Chem., 269, 7709, 10.1016/S0021-9258(17)37345-3 · DOI
- 10.1006/jmbi.1993.1646 · DOI
- 10.1074/jbc.271.6.3112 · DOI
- 10.1042/bj3320749 · DOI
- 10.1006/jmbi.1997.1589 · DOI
- 10.1023/A:1006803512761 · DOI
- 10.1146/annurev.genet.30.1.465 · DOI
- 10.1159/000468684 · DOI
- Rechsteiner M. 1998. InUbiquitin and the Biology of the Cell, ed. JM Peters, JR Harris, D Finley, pp. 147–89. New York: Plenum
- 10.1074/jbc.272.20.13437 · DOI
- 10.1126/science.274.5293.1652 · DOI · Paper page
- 10.1016/S0962-8924(98)01268-9 · DOI
- Huibregtse JM, Maki CG, Howley PM. 1998. InUbiquitin and the Biology of the Cell, ed. JM Peters, JR Harris, D Finley, pp. 324–43. New York: Plenum
- Chen ZJ, Maniatis T. 1998. InUbiquitin and the Biology of the Cell, ed. JM Peters, JR Harris, D Finley, pp. 303–22. New York: Plenum
- Hochstrasser M, Kornitzer D. 1998. InUbiquitin and the Biology of the Cell, ed. JM Peters, JR Harris, D Finley, pp. 279–302. New York: Plenum · DOI
- 10.1016/S0962-8924(97)01020-9 · DOI
- 10.1016/S0960-9822(06)00279-X · DOI
- 10.1038/384432a0 · DOI
- 10.1038/42276 · DOI
- 10.1093/emboj/16.15.4540 · DOI
- 10.1146/annurev.bi.65.070196.001415 · DOI
- 10.1016/S0092-8674(94)90482-0 · DOI
- 10.1016/S0092-8674(00)81054-5 · DOI
- 10.1128/MCB.18.1.30 · DOI
- 10.1016/0012-1606(92)90210-8 · DOI
- 10.1073/pnas.90.1.99 · DOI
- 10.1016/0014-5793(90)80367-R · DOI
- 10.1016/0014-5793(91)80120-R · DOI
- 10.1073/pnas.92.26.12060 · DOI
- Wang HR, 1997, Eur. J. Cell Biol., 73, 105
- 10.1093/emboj/16.20.6087 · DOI
- 10.1042/bj3160401 · DOI
- 10.1093/emboj/17.21.6144 · DOI
- 10.1093/emboj/17.22.6465 · DOI
- 10.1006/jsbi.1998.3958 · DOI
- Peters JM, 1991, Eur. J. Cell Biol., 56, 422
- 10.1016/0014-5793(91)80824-M · DOI
- 10.1006/jsbi.1993.1050 · DOI
- Fujinami K, 1994, J. Biol. Chem., 269, 25905, 10.1016/S0021-9258(18)47331-0 · DOI
- 10.1128/MCB.18.6.3149 · DOI
- DeMartino GN, 1994, J. Biol. Chem., 269, 20878, 10.1016/S0021-9258(17)31904-X · DOI
- 10.1007/BF00990967 · DOI
- 10.1016/S0968-0004(98)01222-5 · DOI
- 10.1006/jmbi.1997.1334 · DOI
- 10.1006/geno.1998.5301 · DOI
- 10.1002/bies.950170710 · DOI
- 10.1007/PL00006259 · DOI
- 10.1016/S0962-8924(97)01212-9 · DOI
- 10.1002/j.1460-2075.1982.tb01276.x · DOI · Paper page
- 10.1126/science.274.5290.1199 · DOI
- 10.1091/mbc.6.2.185 · DOI
- 10.1016/0092-8674(95)90338-0 · DOI
- 10.1016/S0968-0004(96)10046-3 · DOI
200 of 411 shown
Cited by
Sorted by citations
Protein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234
Coregulator Function: A Key to Understanding Tissue Specificity of Selective Receptor Modulators
Smith, C. L., & O’Malley, B. W. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0023 · Cited by 931
Mitochondria in the aetiology and pathogenesis of Parkinson's disease
Schapira, A. H. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70327-7 · Cited by 883
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family
Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588
Altered proteasomal function in sporadic Parkinson’s disease
St. P. McNaught, K., Belizaire, R., Isacson, O., Jenner, P., & Olanow, C. W. (2003) · Experimental Neurology · doi:10.1006/exnr.2002.8050 · Cited by 573
CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein
Murata, S., Minami, Y., Minami, M., Chiba, T., & Tanaka, K. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve246 · Cited by 574
Smith, D. M., Chang, S.-C., Park, S., Finley, D., Cheng, Y., & Goldberg, A. L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.033 · Cited by 521
The three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications
Durcan, T. M., & Fon, E. A. (2015) · Genes & Development · doi:10.1101/gad.262758.115 · Cited by 400
USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin
Durcan, T. M., Tang, M. Y., Pérusse, J. R., Dashti, E. A., Aguileta, M. A., McLelland, G., Gros, P., Shaler, T. A., Faubert, D., Coulombe, B., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201489729 · Cited by 375
Bedford, L., Hay, D., Devoy, A., Paine, S., Powe, D. G., Seth, R., Gray, T., Topham, I., Fone, K., Rezvani, N., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2218-08.2008 · Cited by 327
“This ATP-dependent complex is composed of a 20S proteolytic core particle (CP), directly abutted by 19S regulatory particles (RPs) (Voges et al., 1999; Pickart and Cohen, 2004; Schmidt et al., 2005; Demartino and Gillette, 2007).”
BackgroundProteasomal degradation of tau protein
David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327
Axon pruning: An essential step underlying the developmental plasticity of neuronal connections
Low, L. K., & Cheng, H.-J. (2006) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2006.1883 · Cited by 258
Keller, J. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(01)00006-x · Cited by 247
Regulated protein turnover: snapshots of the proteasome in action
Bhattacharyya, S., Yu, H., Mim, C., & Matouschek, A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3741 · Cited by 240
Firefly luciferase mutants as sensors of proteome stress
Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219
Altun, M., Besche, H. C., Overkleeft, H. S., Piccirillo, R., Edelmann, M. J., Kessler, B. M., Goldberg, A. L., & Ulfhake, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129718 · Cited by 226
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson’s disease
McNaught, K. S. P., & Olanow, C. W. (2003) · Annals of Neurology · doi:10.1002/ana.10512 · Cited by 203
Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171
Dietrich, J.-B., Mangeol, A., Revel, M.-O., Burgun, C., Aunis, D., & Zwiller, J. (2005) · Neuropharmacology · doi:10.1016/j.neuropharm.2005.01.018 · Cited by 168
Kessler, B. M., Tortorella, D., Altun, M., Kisselev, A. F., Fiebiger, E., Hekking, B. G., Ploegh, H. L., & Overkleeft, H. S. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00069-2 · Cited by 163
MHC Class I Antigens and Immune Surveillance in Transformed Cells
Aptsiauri, N., Cabrera, T., Garcia‐Lora, A., Lopez‐Nevot, M. A., Ruiz‐Cabello, F., & Garrido, F. (2007) · International Review of Cytology · doi:10.1016/s0074-7696(07)56005-5 · Cited by 145
Impact of ageing on proteasome structure and function in human lymphocytes
Carrard, G., Dieu, M., Raes, M., Toussaint, O., & Friguet, B. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00356-4 · Cited by 131
Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods
Attaix, D., Mosoni, L., Dardevet, D., Combaret, L., Mirand, P. P., & Grizard, J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.009 · Cited by 123
Aso, E., Lomoio, S., López‐González, I., Joda, L., Carmona, M., Fernández‐Yagüe, N., Moreno, J., Juvés, S., Pujol, A., Pamplona, R., et al. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00560.x · Cited by 118
Küry, S., Besnard, T., Ebstein, F., Khan, T. N., Gambin, T., Douglas, J., Bacino, C. A., Craigen, W. J., Sanders, S. J., Lehmann, A., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.01.003 · Cited by 110
Fratta, P., Engel, W. K., McFerrin, J., Davies, K. J. A., Lin, S. W., & Askanas, V. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62994-x · Cited by 111
Babu, A., Wang, Q., Muralidharan, R., Shanker, M., Munshi, A., & Ramesh, R. (2014) · Molecular Pharmaceutics · doi:10.1021/mp500259e · Cited by 94
Failure of protein quality control in amyotrophic lateral sclerosis
Kabashi, E., & Durham, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.006 · Cited by 90
Thioredoxin Txnl1/TRP32 Is a Redox-active Cofactor of the 26 S Proteasome
Andersen, K. M., Madsen, L., Prag, S., Johnsen, A. H., Semple, C. A., Hendil, K. B., & Hartmann-Petersen, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900016200 · Cited by 88
Effects of agricultural production systems and their components on protein profiles of potato tubers
Lehesranta, S. J., Koistinen, K. M., Massat, N., Davies, H. V., Shepherd, L. V. T., McNicol, J. W., Cakmak, I., Cooper, J., Lück, L., Kärenlampi, S. O., et al. (2007) · PROTEOMICS · doi:10.1002/pmic.200600889 · Cited by 83
Nicotine coregulates multiple pathways involved in protein modification/degradation in rat brain
Kane, J. K., Konu, Ö., Ma, J. Z., & Li, M. D. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.010 · Cited by 61
Witchel, S. F., & DeFranco, D. B. (2006) · Nature Clinical Practice Endocrinology & Metabolism · doi:10.1038/ncpendmet0323 · Cited by 58
Marx, F. P., Soehn, A. S., Berg, D., Melle, C., Schiesling, C., Lang, M., Kautzmann, S., Strauss, K. M., Franck, T., Engelender, S., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-6734com · Cited by 52
Naujokat, C., Berges, C., Höh, A., Wieczorek, H., Fuchs, D., Ovens, J., Miltz, M., Sadeghi, M., Opelz, G., & Daniel, V. (2007) · Immunology · doi:10.1111/j.1365-2567.2006.02487.x · Cited by 41
Malik, S., Shukla, A., Sen, P., & Bhaumik, S. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035709 · Cited by 40
New insights into the genome of Rhodococcus ruber strain Chol-4
Guevara, G., Castillo Lopez, M., Alonso, S., Perera, J., & Navarro-Llorens, J. M. (2019) · BMC Genomics · doi:10.1186/s12864-019-5677-2 · Cited by 33
Wahl, C., Kautzmann, S., Krebiehl, G., Strauss, K., Woitalla, D., Müller, T., Bauer, P., Riess, O., & Krüger, R. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0054-3 · Cited by 22
USP7 protects TFEB from proteasome-mediated degradation
Keshri, S., Vicinanza, M., Takla, M., & Rubinsztein, D. C. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114872 · Cited by 8
Metadata
- Authors
- Voges, D., Zwickl, P., & Baumeister, W.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1999-06
- Volume
- 68
- Issue
- 1
- Pages
- 1015-1068
- ISSN
- 0066-4154
- 1545-4509
- Cited by
- 1,608
- References
- 3
- Language
- en
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