The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.
Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
Open accessPublished version of a preprint
Abstract
The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“P320 in PSMC5 is located outside of the AAA ATPase domain (Fig. 3C) and at the interface of the 19S RP and the 20S CP [34] (Fig. 3D).”
From PSMC5 insufficiency and P320R mutation impair proteasome function (2024) · cites this paper as [34]
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.
Citations
Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Inference of Macromolecular Assemblies from Crystalline State
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,007
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
Automated electron microscope tomography using robust prediction of specimen movements
Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,136
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,417
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
Quantifying the local resolution of cryo-EM density maps
Kucukelbir, A., Sigworth, F. J., & Tagare, H. D. (2013) · Nature Methods · doi:10.1038/nmeth.2727 · Cited by 1,791
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
Self-citationAutomated molecular microscopy: The new Leginon system
Suloway, C. J. M., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J. D., Stagg, S. M., Potter, C. S., & Carragher, B. O. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,695
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 1,540
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
The logic of the 26S proteasome.
Collins, G. A., & Goldberg, A. L. (2017) · Cell · doi:10.1016/j.cell.2017.04.023 · Cited by 933
Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
Kimanius, D., Forsberg, B. O., Scheres, S. H. W., & Lindahl, E. R. (2016) · eLife · doi:10.7554/elife.18722 · Cited by 903
Structure and Function of the 26S Proteasome
Bard, J. A. M., Goodall, E. A., Greene, E. R., Jönsson, E., Dong, K. C., & Martin, A. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011931 · Cited by 867
AAA+ Proteases: ATP-Fueled Machines of Protein Destruction
Sauer, R. T., & Baker, T. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-172623 · Cited by 771
Complete subunit architecture of the proteasome regulatory particle
Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608
The Structure of the Mammalian 20S Proteasome at 2.75 Å Resolution
Unno, M., Mizushima, T., Morimoto, Y., Tomisugi, Y., Tanaka, K., Yasuoka, N., & Tomitake Tsukihara, A. (2002) · Structure · doi:10.1016/s0969-2126(02)00748-7 · Cited by 520
Mechanism of DNA translocation in a replicative hexameric helicase
Enemark, E. J., & Joshua‐Tor, L. (2006) · Nature · doi:10.1038/nature04943 · Cited by 512
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 491
Verma, R., Oania, R. S., Graumann, J., & Deshaies, R. J. (2004) · Cell · doi:10.1016/j.cell.2004.06.014 · Cited by 446
Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
Lasker, K., Förster, F. G., Bohn, S., Walzthoeni, T., Villa, E., Unverdorben, P., Beck, F., Aebersold, R. H., Šali, A., & Baumeister, W. P. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120559109 · Cited by 442
Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
Galan, J., & Haguenauer‐Tsapis, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.19.5847 · Cited by 402
Molecular Architecture and Assembly of the Eukaryotic Proteasome
Tomko, R. J., & Hochstrasser, M. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060410-150257 · Cited by 376
Livneh, I., Cohen‐Kaplan, V., Cohen-Rosenzweig, C., Avni, N., & Ciechanover, A. J. (2016) · Cell Research · doi:10.1038/cr.2016.86 · Cited by 344
Running in Reverse: The Structural Basis for Translocation Polarity in Hexameric Helicases
Thomsen, N. D., & Berger, J. M. (2009) · Cell · doi:10.1016/j.cell.2009.08.043 · Cited by 303
Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome
Shi, Y., Chen, X., Elsasser, S., Stocks, B. B., Tian, G., Lee, B., Shi, Y., Zhang, N., de Poot, S. A. H., Tübing, F., et al. (2016) · Science · doi:10.1126/science.aad9421 · Cited by 297
Self-citationGlynn, S. E., Martin, A., Nager, A. R., Baker, T. A., & Sauer, R. T. (2009) · Cell · doi:10.1016/j.cell.2009.09.034 · Cited by 266
Near-atomic resolution structural model of the yeast 26S proteasome
Beck, F., Unverdorben, P., Bohn, S., Schweitzer, A., Pfeifer, G., Sakata, E., Nickell, S., Plitzko, J. M., Villa, E., Baumeister, W. P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213333109 · Cited by 262
Gates, Channels, and Switches: Elements of the Proteasome Machine
Finley, D. J., Chen, X., & Walters, K. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.10.009 · Cited by 262
Self-citationMass Spectrometric Characterization of the Affinity-Purified Human 26S Proteasome Complex
Wang, X., Chen, C.-F., Baker, P. R., Chen, P.-L., Kaiser, P., & Huang, L. (2007) · Biochemistry · doi:10.1021/bi061994u · Cited by 260
Conformational switching of the 26S proteasome enables substrate degradation
Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2616 · Cited by 251
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
Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104
Gates, S. N., Yokom, A. L., Lin, J., Jackrel, M. E., Rizo, A. N., Kendsersky, N. M., Buell, C. E., Sweeny, E. A., Mack, K. L., Chuang, E., et al. (2017) · Science · doi:10.1126/science.aan1052 · Cited by 243
An atomic structure of the human 26S proteasome
Huang, X., Luan, B., Wu, J., & Shi, Y. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3273 · Cited by 240
Structural Biology of the Proteasome
Kish‐Trier, E., & Hill, C. P. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130417 · Cited by 229
Puchades, C., Rampello, A. J., Shin, M., Giuliano, C. J., Wiseman, R. L., Glynn, S. E., & Lander, G. C. (2017) · Science · doi:10.1126/science.aao0464 · Cited by 223
Substrate degradation by the proteasome: A single-molecule kinetic analysis
Lu, Y., Lee, B., King, R. W., Finley, D. J., & Kirschner, M. W. (2015) · Science · doi:10.1126/science.1250834 · Cited by 218
Self-citationMolecular Model of the Human 26S Proteasome
da Fonseca, P. C. A., He, J., & Morris, E. P. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.026 · Cited by 214
OB-fold domains: a snapshot of the evolution of sequence, structure and function
Arcus, V. L. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00392-5 · Cited by 210
Smith, D. M., Fraga, H., Reis, C. R. S., Kafri, G., & Goldberg, A. (2011) · Cell · doi:10.1016/j.cell.2011.02.005 · Cited by 202
Structure of the human 26S proteasome at a resolution of 3.9 Å
Schweitzer, A., Aufderheide, A., Rudack, T., Beck, F., Pfeifer, G., Plitzko, J. M., Sakata, E., Schulten, K. J., Förster, F. G., & Baumeister, W. P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608050113 · Cited by 198
Structural basis for dynamic regulation of the human 26S proteasome
Chen, S., Wu, J., Lu, Y., Ma, Y.-B., Lee, B., Yu, Z., Ouyang, Q., Finley, D. J., Kirschner, M. W., & Mao, Y. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614614113 · Cited by 175
Self-citationZhang, F., Hu, M., Tian, G., Zhang, P., Finley, D., Jeffrey, P., & Shi, Y. (2009) · Molecules and Cells · doi:10.1016/j.molcel.2009.04.021 · Cited by 171
Self-citationCrystal Structure of the Human 20S Proteasome in Complex with Carfilzomib
Harshbarger, W. D., Miller, C. S., Diedrich, C., & Sacchettini, J. C. (2015) · Structure · doi:10.1016/j.str.2014.11.017 · Cited by 171
Worden, E. J., Padovani, C., & Martin, A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2771 · Cited by 164
Structural insights into the functional cycle of the ATPase module of the 26S proteasome
Wehmer, M., Rudack, T., Beck, F., Aufderheide, A., Pfeifer, G., Plitzko, J. M., Förster, F. G., Schulten, K. J., Baumeister, W. P., & Sakata, E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1621129114 · Cited by 162
Sledz, P., Unverdorben, P., Beck, F., Pfeifer, G., Schweitzer, A., Förster, F. G., & Baumeister, W. P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305782110 · Cited by 159
Zhu, Y., Ouyang, Q., & Mao, Y. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1757-y · Cited by 145
Self-citationCrystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11
Pathare, G. R., Nagy, I., Sledz, P., Anderson, D. J., Zhou, H.-J., Pardon, E., Steyaert, J., Förster, F. G., Bracher, A., & Baumeister, W. P. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400546111 · Cited by 141
Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13
Zhang, N., Wang, Q., Ehlinger, A. C., Randles, L., Lary, J. W., Yang, K., Haririnia, A., Storaska, A. J., Cole, J. L., Fushman, D., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.010 · Cited by 140
Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase
Beckwith, R., Estrin, E., Worden, E. J., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2659 · Cited by 136
Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase
Deville, C., Carroni, M., Franke, K. B., Topf, M., Bukau, B., Mogk, A., & Saibil, H. R. (2017) · Science Advances · doi:10.1126/sciadv.1701726 · Cited by 124
Eisele, M. R., Reed, R. G., Rudack, T., Schweitzer, A., Beck, F., Nagy, I., Pfeifer, G., Plitzko, J. M., Baumeister, W. P., Tomko, R. J., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.004 · Cited by 124
Structure of a AAA+ unfoldase in the process of unfolding substrate
Ripstein, Z. A., Huang, R., Augustyniak, R., Kay, L. E., & Rubinstein, J. L. (2017) · eLife · doi:10.7554/elife.25754 · Cited by 122
Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase
Monroe, N., Han, H., Shen, P. S., Sundquist, W. I., & Hill, C. P. (2017) · eLife · doi:10.7554/elife.24487 · Cited by 120
The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins
Zhang, X., & Wigley, D. B. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1501 · Cited by 118
An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome
Worden, E. J., Dong, K. C., & Martin, A. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.023 · Cited by 108
Saeki, Y., Isono, E., & Toh‐e, A. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99014-9 · Cited by 107
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
Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition
Dambacher, C. M., Worden, E. J., Herzik, M. A., Martin, A., & Lander, G. C. (2016) · eLife · doi:10.7554/elife.13027 · Cited by 101
Zhu, Y., Wang, W. L., Yu, D., Ouyang, Q., Lu, Y., & Mao, Y. (2018) · Nature Communications · doi:10.1038/s41467-018-03785-w · Cited by 93
Self-citationAn 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
Self-citationHan, H., Monroe, N., Sundquist, W. I., Shen, P. S., & Hill, C. P. (2017) · eLife · doi:10.7554/elife.31324 · Cited by 88
Structure of an endogenous yeast 26S proteasome reveals two major conformational states
Luan, B., Huang, X., Wu, J., Mei, Z., Wang, Y., Xue, X., Yan, C., Wang, J., Finley, D. J., Shi, Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601561113 · Cited by 82
Self-citationHigh-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx
Ding, Z., Fu, Z., Xu, C., Wang, Y., Wang, Y., Li, J., Kong, L., Chen, J., Li, N., Zhang, R., et al. (2017) · Cell Research · doi:10.1038/cr.2017.12 · Cited by 68
He, J., Kulkarni, K. A., da Fonseca, P. C. A., Krutauz, D., Glickman, M. H., Barford, D., & Morris, E. P. (2012) · Structure · doi:10.1016/j.str.2011.12.015 · Cited by 62
Kim, Y., Snoberger, A. M., Schupp, J. E., & Smith, D. M. (2015) · Nature Communications · doi:10.1038/ncomms9520 · Cited by 60
Functional Asymmetries of Proteasome Translocase Pore
Erales, J., Hoyt, M. A., Troll, F., & Coffino, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.357327 · Cited by 57
Mechanism of Substrate Translocation by a Ring-Shaped ATPase Motor at Millisecond Resolution
Ma, W., & Schulten, K. J. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512605w · Cited by 54
Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle
Lu, Y., Wu, J., Dong, Y., Chen, S., Sun, S., Ma, Y.-B., Ouyang, Q., Finley, D. J., Kirschner, M. W., & Mao, Y. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.007 · Cited by 48
Self-citationWu, J., Ma, Y.-B., Congdon, C., Brett, B. R., Chen, S., Xu, Y., Ouyang, Q., & Mao, Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182130 · Cited by 45
Self-citationATP-induced Structural Transitions in PAN, the Proteasome-regulatory ATPase Complex in Archaea
Horwitz, A. A., Navon, A., Groll, M., Smith, D. M., Reis, C., & Goldberg, A. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702846200 · Cited by 43
Snoberger, A., Brettrager, E. J., & Smith, D. M. (2018) · Nature Communications · doi:10.1038/s41467-018-04731-6 · Cited by 30
Cited by
Sorted by citations
An expanded lexicon for the ubiquitin code
Đikić, I., & Schulman, B. A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00543-1 · Cited by 426
Antigen presentation in cancer — mechanisms and clinical implications for immunotherapy
Yang, K., Halima, A., & Chan, T. A.-T. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00789-4 · Cited by 352
Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding
Twomey, E. C., Ji, Z., Wales, T. E., Bodnar, N. O., Ficarro, S. B., Marto, J. A., Engen, J. R., & Rapoport, T. A. (2019) · Science · doi:10.1126/science.aax1033 · Cited by 293
Functional Modules of the Proteostasis NetworkPreprint
Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 254
The molecular principles governing the activity and functional diversity of AAA+ proteins
Puchades, C., Sandate, C. R., & Lander, G. C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0183-6 · Cited by 239
Metadata
- Authors
- Dong, Y., Zhang, S., Wu, Z., Li, X., Wang, W. L., Zhu, Y., Stoilova-McPhie, S., Lu, Y., Finley, D., & Mao, Y.
- Affiliations
- Harvard University (US)
- Peking University (CN)
- Corresponding author
- Mao, Youdong
- ORCID
- Venue
- Nature
- Published
- 2018-11-12
- Volume
- 565
- Issue
- 7737
- Pages
- 49-55
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC6370054
- OpenAlex
- W2900290772
- Cited by
- 328
- References
- 77
- Citations by year
- 2026: 27 · 2025: 47 · 2024: 30 · 2023: 36 · 2022: 44 · 2021: 46 · 2020: 49 · 2019: 48
- FWCI
- 12.90
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Science Foundation (1541959)
- Harvard University (1541959)
- National Natural Science Foundation of China (11774012, 91530321)
- Peking University
- Recruitment Program of Global Experts
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM043601, R37GM043601)
- National Institute of Allergy and Infectious Diseases (UM1AI100645)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- 26S proteasome, ATP hydrolysis, substrate translocation, deubiquitination, ubiquitin recognition, protein unfolding
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Allosteric Regulation, Humans, Hydrolysis, Models, Molecular, Protein Conformation, Substrate Specificity, Holoenzymes, Cryoelectron Microscopy, Protein Structure, Quaternary, Proteasome Endopeptidase Complex, Ubiquitination, Protein Unfolding
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
