Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome

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 45,260 · see citing works

<i>Coot</i> : 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 · see citing works

<i>PHENIX</i> : 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 · see citing works

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 10,189 · see citing works

MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works

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 · see citing works

Automated electron microscope tomography using robust prediction of specimen movements.

Mastronarde, D. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,446 · see citing works

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works

Gctf: Real-time CTF determination and correction

Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · 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

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 1,847 · 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

Automated 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 1,681 · 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

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

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 · see citing works

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 · see citing works

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 825 · see citing works

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 763 · see citing works

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 · see citing works

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 · see citing works

Mechanism of DNA translocation in a replicative hexameric helicase

Enemark, E. J., & Joshua‐Tor, L. (2006) · Nature · doi:10.1038/nature04943 · Cited by 512 · see citing works

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 · see citing works

Multiubiquitin Chain Receptors Define a Layer of Substrate Selectivity in the Ubiquitin-Proteasome System

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

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 · see citing works

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 395 · see citing works

Molecular Architecture and Assembly of the Eukaryotic Proteasome

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

The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death

Livneh, I., Cohen‐Kaplan, V., Cohen-Rosenzweig, C., Avni, N., & Ciechanover, A. J. (2016) · Cell Research · doi:10.1038/cr.2016.86 · Cited by 331 · see citing works

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 · see citing works

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 295 · see citing works

Structures of Asymmetric ClpX Hexamers Reveal Nucleotide-Dependent Motions in a AAA+ Protein-Unfolding Machine

Glynn, 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 261 · see citing works

Mass 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 · see citing works

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 254 · see citing works

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 251 · see citing works

Conformational switching of the 26S proteasome enables substrate degradation

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

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 · see citing works

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 · see citing works

An atomic structure of the human 26S proteasome

Huang, X., Luan, B., Wu, J.-P., & Shi, Y. (2016) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.3273 · Cited by 233 · see citing works

Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing

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 230 · see citing works

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 219 · see citing works

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 · see citing works

Molecular 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 213 · see citing works

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 · see citing works

ATP binds to proteasomal ATPases in pairs with distinct functional effects implying an ordered reaction cycle

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 · see citing works

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 193 · see citing works

Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation

Śledź, P., Unverdorben, P., Beck, F., Pfeifer, G., Schweitzer, A., Förster, F., & Baumeister, W. (2013) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1305782110 · Cited by 180 · see citing works

Structural basis for dynamic regulation of the human 26S proteasome

Chen, S., Wu, J., Lu, Y., Ma, Y., Lee, B.-H., Yu, Z., Ouyang, Q., Finley, D., Kirschner, M., & Mao, Y.-D. (2016) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1614614113 · Cited by 173 · see citing works

Structural Insights Into The Regulatory Particle Of The Proteasome From Methanocaldococcus jannaschii

Zhang, 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 · see citing works

Crystal 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 · see citing works

Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation

Worden, E. J., Padovani, C., & Martin, A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2771 · Cited by 161 · see citing works

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., Förster, F., Schulten, K., Baumeister, W., & Sakata, E. (2017) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1621129114 · Cited by 160 · see citing works

Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase

Beckwith, R., Estrin, E., Worden, E., & Martin, A. (2013) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.2659 · Cited by 148 · see citing works

A deep convolutional neural network approach to single-particle recognition in cryo-electron microscopy

Zhu, Y., Ouyang, Q., & Mao, Y. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1757-y · Cited by 147 · see citing works

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 · see citing works

Crystal 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 135 · see citing works

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 · see citing works

Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating

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 123 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 109 · see citing works

Preparation of Ubiquitinated Substrates by the PY Motif‐Insertion Method for Monitoring 26S Proteasome Activity

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 · see citing works

Selective Degradation of Ubiquitinated Sic1 by Purified 26S Proteasome Yields Active S Phase Cyclin-Cdk

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

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 · see citing works

Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome

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 92 · 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

The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets

Han, H., Monroe, N., Sundquist, W. I., Shen, P. S., & Hill, C. P. (2017) · eLife · doi:10.7554/elife.31324 · Cited by 88 · see citing works

Structure of an endogenous yeast 26S proteasome reveals two major conformational states

Luan, B., Huang, X., Wu, J.-P., Mei, Z., Wang, Y., Xue, X., Yan, C., Wang, J.-W., Finley, D., Shi, Y., et al. (2016) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1601561113 · Cited by 82 · see citing works

High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx

Ding, Z.-Y., Fu, Z., Xu, C., Wang, Y., Wang, Y.-X., Li, J., Kong, L., Chen, J.-H., Li, N., Zhang, R.-G., et al. (2017) · Cell Research · doi:10.1038/cr.2017.12 · Cited by 62 · see citing works

The Structure of the 26S Proteasome Subunit Rpn2 Reveals Its PC Repeat Domain as a Closed Toroid of Two Concentric α-Helical Rings

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 59 · see citing works

ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function

Kim, Y.-C., Snoberger, A., Schupp, J. E., & Smith, D. M. (2015) · Nature Communications · doi:10.1038/ncomms9520 · Cited by 59 · see citing works

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 56 · see citing works

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 53 · see citing works

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 49 · see citing works

Massively parallel unsupervised single-particle cryo-EM data clustering via statistical manifold learning

Wu, 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 · see citing works

ATP-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 · see citing works

Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing

Snoberger, A., Brettrager, E. J., & Smith, D. M. (2018) · Nature Communications · doi:10.1038/s41467-018-04731-6 · Cited by 30 · see citing works

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 · see citing works

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 333 · see citing works

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 295 · see citing works

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 249 · see citing works

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 244 · see citing works

Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation

Marshall, R. S., & Vierstra, R. D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00040 · Cited by 230 · see citing works

DeepTracer for fast de novo cryo-EM protein structure modeling and special studies on CoV-related complexes

Pfab, J., Phan, N. M., & Si, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017525118 · Cited by 196 · see citing works

Deep learning-based mixed-dimensional Gaussian mixture model for characterizing variability in cryo-EM

Chen, M., & Ludtke, S. J. (2021) · Nature Methods · doi:10.1038/s41592-021-01220-5 · Cited by 186 · see citing works

Developments, applications, and prospects of cryo‐electron microscopy

Xu, B., & Ling, L. (2019) · Protein Science · doi:10.1002/pro.3805 · Cited by 170 · see citing works

Structure of the Cdc48 segregase in the act of unfolding an authentic substrate

Cooney, I., Han, H., Stewart, M. G., Carson, R. H., Hansen, D. T., Iwasa, J., Price, J. C., Hill, C. P., & Shen, P. S. (2019) · Science · doi:10.1126/science.aax0486 · Cited by 166 · see citing works

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

Fei, X., Bell, T. A., Jenni, S., Stinson, B. M., Baker, T. A., Harrison, S. C., & Sauer, R. T. (2020) · eLife · doi:10.7554/elife.52774 · Cited by 144 · see citing works

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

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

The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation

Bard, J. A. M., Bashore, C., Dong, K. C., & Martin, A. (2019) · Cell · doi:10.1016/j.cell.2019.02.031 · Cited by 136 · see citing works

The AAA+ superfamily: a review of the structural and mechanistic principles of these molecular machines

Khan, Y. A., White, K. I., & Brünger, A. T. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1979460 · Cited by 124 · see citing works

Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP‐dependent substrate translocation

Gates, S. N., & Martin, A. (2019) · Protein Science · doi:10.1002/pro.3743 · Cited by 127 · see citing works

Processive extrusion of polypeptide loops by a Hsp100 disaggregase

Avellaneda, M. J., Franke, K. B., Šunderlíková, V., Bukau, B., Mogk, A., & Tans, S. J. (2020) · Nature · doi:10.1038/s41586-020-1964-y · Cited by 126 · see citing works

AKIRIN2 controls the nuclear import of proteasomes in vertebrates

de Almeida, M., Hinterndorfer, M., Brunner, H. L., Grishkovskaya, I., Singh, K., Schleiffer, A., Jude, J., Deswal, S., Kalis, R., Vunjak, M., et al. (2021) · Nature · doi:10.1038/s41586-021-04035-8 · Cited by 122 · see citing works

Targeted degradation via direct 26S proteasome recruitment

Bashore, C., Prakash, S., Johnson, M. C., Conrad, R. J., Kekessie, I. A., Scales, S. J., Ishisoko, N., Kleinheinz, T., Liu, P. S., Popovych, N., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01218-w · Cited by 118 · see citing works

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

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

USP14-regulated allostery of the human proteasome by time-resolved cryo-EM

Zhang, S., Zou, S., Yin, D., Zhao, L., Finley, D. J., Wu, Z., & Mao, Y. (2022) · Nature · doi:10.1038/s41586-022-04671-8 · Cited by 112 · see citing works

Deep Learning to Predict Protein Backbone Structure from High-Resolution Cryo-EM Density Maps

Si, D., Moritz, S. A., Pfab, J., Hou, J., Cao, R., Wang, L., Wu, T., & Cheng, J. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-60598-y · Cited by 108 · see citing works

Targeted protein degradation directly engaging lysosomes or proteasomes

Kim, J., Byun, I., Kim, D. Y., Joh, H., Kim, H. J., & Lee, M. J. (2024) · Chemical Society Reviews · doi:10.1039/d3cs00344b · Cited by 106 · see citing works

The pre-synaptic fusion machinery

Brünger, A. T., Choi, U. B., Lai, Y., Leitz, J., White, K. I., & Zhou, Q. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.03.007 · Cited by 104 · see citing works

Mechanisms and regulation of substrate degradation by the 26S proteasome

Arkinson, C., Dong, K. C., Gee, C. L., & Martin, A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00778-0 · Cited by 112 · see citing works

Structure, Dynamics and Function of the 26S Proteasome

Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 105 · see citing works

Proteasome in action: substrate degradation by the 26S proteasome

Sahu, I., & Glickman, M. H. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200382 · Cited by 101 · see citing works

Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome

Eickhoff, P., Kose, H. B., Martino, F., Petojevic, T., Ali, F. A., Locke, J., Tamberg, N., Nans, A., Berger, J., Botchan, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.104 · Cited by 84 · see citing works

Ubiquitin–proteasome system and the role of its inhibitors in cancer therapy

Aliabadi, F., Sohrabi, B., Mostafavi, E., Pazoki–Toroudi, H., & Webster, T. J. (2021) · Open Biology · doi:10.1098/rsob.200390 · Cited by 100 · see citing works

Proteasome Inhibition Activates Autophagy-Lysosome Pathway Associated With TFEB Dephosphorylation and Nuclear Translocation

Li, C., Wang, X., Li, X., Qiu, K., Jiao, F., Liu, Y., Kong, Q., Liu, Y., & Wu, Y. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00170 · Cited by 90 · see citing works

The proteasome and its role in the nervous system

Türker, F., Cook, E. K., & Margolis, S. S. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.003 · Cited by 92 · see citing works

Integration of Mass Spectrometry Data for Structural Biology

Britt, H. M., Cragnolini, T., & Thalassinos, K. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00356 · Cited by 84 · see citing works

Mechanisms of σ54-Dependent Transcription Initiation and Regulation

Danson, A. E., Jovanovic, M., Buck, M., & Zhang, X. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.022 · Cited by 84 · see citing works

The Proteasome and Its Network: Engineering for AdaptabilityPreprint

Finley, D. J., & Prado, M. A. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033985 · Cited by 84 · see citing works

K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle

Yu, Y., Zheng, Q., Erramilli, S. K., Pan, M., Park, S.-J., Xie, Y., Li, J., Fei, J., Kossiakoff, A. A., Liu, L., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00823-5 · Cited by 78 · see citing works

Nanoarchitectonics from Atom to Life

Ariga, K., & Yamauchi, Y. (2020) · Chemistry - An Asian Journal · doi:10.1002/asia.202000106 · Cited by 80 · see citing works

Structural basis for distinct operational modes and protease activation in AAA+ protease Lon

Shin, M., Puchades, C., Asmita, A., Puri, N., Adjei, E., Wiseman, R. L., Karzai, A. W., & Lander, G. C. (2020) · Science Advances · doi:10.1126/sciadv.aba8404 · Cited by 76 · see citing works

Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation

Collins, G. A., & Goldberg, A. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915534117 · Cited by 76 · see citing works

A modular toolbox to generate complex polymeric ubiquitin architectures using orthogonal sortase enzymes

Fottner, M., Weyh, M., Gaussmann, S., Schwarz, D., Sattler, M., & Lang, K. (2021) · Nature Communications · doi:10.1038/s41467-021-26812-9 · Cited by 73 · see citing works

Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins

Galves, M., Rathi, R., Prag, G., & Ashkenazi, A. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.04.007 · Cited by 73 · see citing works

Proteotoxic Stress and Cell Death in Cancer Cells

Brancolini, C., & Iuliano, L. (2020) · Cancers · doi:10.3390/cancers12092385 · Cited by 70 · see citing works

Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM

Piper, S. J., Johnson, R. M., Wootten, D. L., & Sexton, P. M. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00837 · Cited by 70 · see citing works

Structural Snapshots of 26S Proteasome Reveal Tetraubiquitin-Induced Conformations

Ding, Z., Xu, C., Sahu, I., Wang, Y., Fu, Z., Huang, M., Wong, C. C. L., Glickman, M. H., & Cong, Y. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.018 · Cited by 70 · see citing works

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

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

Mechanisms of substrate recognition by the 26S proteasome

Davis, C., Spaller, B. L., & Matouschek, A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.010 · Cited by 66 · see citing works

Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes

Flecken, M., Wang, H., Popilka, L., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. K. (2020) · Cell · doi:10.1016/j.cell.2020.09.010 · Cited by 66 · see citing works

Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry

Vimer, S., Ben-Nissan, G., Morgenstern, D., Kumar-Deshmukh, F., Polkinghorn, C., Quintyn, R. S., Vasil’ev, Y. V., Beckman, J. S., Elad, N., Wysocki, V. H., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00080 · Cited by 63 · see citing works

Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis

Lopez, K. E., Rizo, A. N., Tse, E., Lin, J., Scull, N. W., Thwin, A. C., Lucius, A. L., Shorter, J., & Southworth, D. R. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0409-5 · Cited by 63 · see citing works

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor

Deville, C., Franke, K. B., Mogk, A., Bukau, B., & Saibil, H. R. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.075 · Cited by 63 · see citing works

AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms

Zhang, S., & Mao, Y. (2020) · Biomolecules · doi:10.3390/biom10040629 · Cited by 61 · see citing works

Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction

Wang, L., Myasnikov, A. G., Pan, X., & Walter, P. (2020) · eLife · doi:10.7554/elife.54031 · Cited by 61 · see citing works

Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies

Chen, X., Htet, Z. M., López-Alfonzo, E. M., Martin, A., & Walters, K. J. (2020) · FEBS Journal · doi:10.1111/febs.15638 · Cited by 61 · see citing works

Protein degradation: expanding the toolbox to restrain cancer drug resistance

Ming, H., Li, B., Jiang, J., Qin, S., Nice, E. C., He, W., Lang, T., & Huang, C. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01398-5 · Cited by 60 · see citing works

Inhibition of dual-specificity tyrosine phosphorylation-regulated kinase 2 perturbs 26S proteasome-addicted neoplastic progression

Banerjee, S., Wei, T., Wang, J., Lee, J. J., Gutierrez, H. L., Chapman, O. S., Wiley, S. E., Mayfield, J. E., Tandon, V., Juarez, E. F., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912033116 · Cited by 60 · see citing works

PA28γ: New Insights on an Ancient Proteasome Activator

Cascio, P. (2021) · Biomolecules · doi:10.3390/biom11020228 · Cited by 59 · see citing works

Molecular and cellular dynamics of the 26S proteasome

Sakata, E., Eisele, M. R., & Baumeister, W. P. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140583 · Cited by 58 · see citing works

Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10

Buel, G. R., Chen, X., Chari, R., O’Neill, M. J., Ebelle, D. L., Jenkins, C., Sridharan, V., Tarasov, S. G., Tarasova, N. I., Andrésson, Þ., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15073-7 · Cited by 52 · see citing works

Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins

Habib, J. A., Plaen, E. D., Stroobant, V., Živković, D., Bousquet, M., Guillaume, B., Wahni, K., Messens, J., Busse, A., Vigneron, N., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71550-5 · Cited by 55 · see citing works

AAA+ ATPases: structural insertions under the magnifying glass

Jessop, M., Félix, J., & Gutsche, I. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.027 · Cited by 55 · see citing works

Proteasome substrate receptors and their therapeutic potential

Amponsa, V. O., & Walters, K. J. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.06.006 · Cited by 54 · see citing works

Advances that facilitate the study of large RNA structure and dynamics by nuclear magnetic resonance spectroscopy

Zhang, H., & Keane, S. C. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1541 · Cited by 53 · see citing works

Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function

Liu, X., Xiao, W., Zhang, Y., Wiley, S. E., Zuo, T., Zheng, Y., Chen, N., Chen, L., Wang, X., Zheng, Y., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912531117 · Cited by 52 · see citing works

A large expert-curated cryo-EM image dataset for machine learning protein particle picking

Dhakal, A., Gyawali, R., Wang, L., & Cheng, J. J. (2023) · Scientific Data · doi:10.1038/s41597-023-02280-2 · Cited by 54 · see citing works

Simulation-Based Methods for Model Building and Refinement in Cryoelectron Microscopy

Dodd, T., Yan, C., & Ivanov, I. N. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00087 · Cited by 52 · see citing works

Nanoarchitectonics beyond perfect order – not quite perfect but quite useful

Cao, L., Huang, Y., Parakhonskiy, B. V., & Skirtach, A. G. (2022) · Nanoscale · doi:10.1039/d2nr02537j · Cited by 48 · see citing works

Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective

Greene, E. R., Dong, K. C., & Martin, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.004 · Cited by 49 · see citing works

Immunoproteasome-selective inhibitors: An overview of recent developments as potential drugs for hematologic malignancies and autoimmune diseases

Xi, J., Zhuang, R., Kong, L., He, R., Zhu, H., & Zhang, J. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111646 · Cited by 48 · see citing works

Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein

Tang, W. K., Borgnia, M. J., Hsu, A. L., Esser, L., Fox, T. L., de Val, N., & Xia, D. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0373-0 · Cited by 48 · see citing works

Deubiquitination Reactions on the Proteasome for Proteasome Versatility

Shin, J. Y., Muniyappan, S., Tran, N.-N., Park, H., Lee, S. B., & Lee, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155312 · Cited by 48 · see citing works

Degradation of SERRATE via ubiquitin-independent 20S proteasome to survey RNA metabolism

Li, Y., Sun, D., Ma, Z., Yamaguchi, K., Wang, L., Zhong, S., Yan, X., Shang, B., Nagashima, Y., Koiwa, H., et al. (2020) · Nature Plants · doi:10.1038/s41477-020-0721-4 · Cited by 47 · see citing works

Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis

Sauer, R. T., Fei, X., Bell, T. A., & Baker, T. A. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1979461 · Cited by 46 · see citing works

Proteasomes: unfoldase-assisted protein degradation machines

Majumder, P., & Baumeister, W. (2019) · Biological chemistry · doi:10.1515/hsz-2019-0344 · Cited by 40 · see citing works

Msp1/ATAD1 in Protein Quality Control and Regulation of Synaptic Activities

Wang, L., & Walter, P. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-031220-015840 · Cited by 44 · see citing works

Allosteric control of Ubp6 and the proteasome via a bidirectional switch

Hung, K. Y. S., Klumpe, S., Eisele, M. R., Elsasser, S., Tian, G., Sun, S., Moroco, J. A., Cheng, T. C., Joshi, T., Seibel, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28186-y · Cited by 44 · see citing works

Structural insights into the human PA28–20S proteasome enabled by efficient tagging and purification of endogenous proteins

Zhao, J., Makhija, S., Zhou, C., Zhang, H., Wang, Y., Muralidharan, M., Huang, B., & Cheng, Y. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207200119 · Cited by 43 · see citing works

Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders

Loh, D., & Reiter, R. J. (2021) · Antioxidants · doi:10.3390/antiox10091483 · Cited by 43 · see citing works

Cryo-EM structures of Helicobacter pylori vacuolating cytotoxin A oligomeric assemblies at near-atomic resolution

Zhang, K., Zhang, H., Li, S., Pintilie, G. D., Mou, T., Gao, Y., Zhang, Q., Bedem, H. V. D., Schmid, M. F., Au, S. W. N., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821959116 · Cited by 42 · see citing works

Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation

Han, H., Schubert, H., McCullough, J., Monroe, N., Purdy, M. D., Yeager, M. J., Sundquist, W. I., & Hill, C. P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ac119.009890 · Cited by 42 · see citing works

More than an on-and-off switch: Post-translational modifications of plant pattern recognition receptor complexes

Kong, L., Rodrigues, B., Kim, J. H., He, P., & Shan, L. (2021) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2021.102051 · Cited by 41 · see citing works

Advances in Proteasome Enhancement by Small Molecules

George, D. E., & Tepe, J. J. (2021) · Biomolecules · doi:10.3390/biom11121789 · Cited by 40 · see citing works

The Conceivable Functions of Protein Ubiquitination and Deubiquitination in Reproduction

Wang, J., Zhou, Q., Ding, J., Yin, T., Ye, P., & Zhang, Y. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.886261 · Cited by 40 · see citing works

Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases

Han, H., Fulcher, J. M., Dandey, V. P., Iwasa, J., Sundquist, W. I., Kay, M. S., Shen, P. S., & Hill, C. P. (2019) · eLife · doi:10.7554/elife.44071 · Cited by 40 · see citing works

Proteasome Activation to Combat Proteotoxicity

Jones, C. L., & Tepe, J. J. (2019) · Molecules · doi:10.3390/molecules24152841 · Cited by 41 · see citing works

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.

Deville, C., & Saibil, H. R. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6qs4/pdb · Cited by 38 · see citing works

Characterizing ATP processing by the AAA+ protein p97 at the atomic level

Shein, M., Hitzenberger, M., Cheng, T. C., Rout, S. R., Leitl, K. D., Sato, Y., Zacharias, M., Sakata, E., & Schütz, A. K. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01440-0 · Cited by 37 · see citing works

Substrate selection by the proteasome through initiation regions

Tomita, T., & Matouschek, A. T. (2019) · Protein Science · doi:10.1002/pro.3642 · Cited by 37 · see citing works

PSMC2 promotes the progression of gastric cancer via induction of RPS15A/mTOR pathway

Liu, T., Zhang, J., Chen, H., Bianba, T., Pan, Y., Wang, X., Jiang, Y. H., & Yang, Z. (2022) · Oncogenesis · doi:10.1038/s41389-022-00386-7 · Cited by 37 · see citing works

PSMC3 proteasome subunit variants are associated with neurodevelopmental delay and type I interferon production

Ebstein, F., Küry, S., Most, V., Rosenfelt, C., Scott-Boyer, M.-P., van Woerden, G. M., Besnard, T., Papendorf, J. J., Studencka-Turski, M., Wang, T., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo3189 · Cited by 36 · see citing works

Roles of Ubiquitination and SUMOylation in DNA Damage Response

Su, S., Zhang, Y., & Liu, P. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.059 · Cited by 34 · see citing works

Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma

Lu, X., Sabbasani, V. R., Amponsa, V. O., Evans, C. N., King, J. C., Tarasov, S. G., Dyba, M., Das, S., Chan, K. C., Schwieters, C. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27570-4 · Cited by 35 · see citing works

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation

Greene, E. R., Goodall, E. A., de la Peña, A. H., Matyskiela, M. E., Lander, G. C., & Martin, A. (2019) · eLife · doi:10.7554/elife.49806 · Cited by 35 · see citing works

Active conformation of the p97-p47 unfoldase complex

Xu, Y. J., Han, H., Cooney, I., Guo, Y., Moran, N. G., Zuniga, N. R., Price, J. C., Hill, C. P., & Shen, P. S. (2022) · Nature Communications · doi:10.1038/s41467-022-30318-3 · Cited by 35 · see citing works

Protein quality control by the proteasome and autophagy: A regulatory role of ubiquitin and liquid-liquid phase separation

Lei, L., Wu, Z., & Winklhofer, K. F. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.11.003 · Cited by 34 · see citing works

Structure, Function, and Allosteric Regulation of the 20S Proteasome by the 11S/PA28 Family of Proteasome Activators

Thomas, T. A., Salcedo-Tacuma, D., & Smith, D. M. (2023) · Biomolecules · doi:10.3390/biom13091326 · Cited by 33 · see citing works

Visualizing chaperone-mediated multistep assembly of the human 20S proteasome

Adolf, F., Du, J., Goodall, E. A., Walsh, R. M., Rawson, S., von Gronau, S., Harper, J. W., Hanna, J., & Schulman, B. A. (2024) · Nature Structural &amp; Molecular Biology · doi:10.1038/s41594-024-01268-9 · Cited by 33 · see citing works

An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure

Lu, X., Ebelle, D. L., Matsuo, H., & Walters, K. J. (2020) · Structure · doi:10.1016/j.str.2020.02.007 · Cited by 33 · see citing works

Mechanism of AAA+ ATPase-mediated RuvAB–Holliday junction branch migration

Wald, J., Fahrenkamp, D., Goessweiner‐Mohr, N., Lugmayr, W., Ciccarelli, L., Vesper, O., & Marlovits, T. C. (2022) · Nature · doi:10.1038/s41586-022-05121-1 · Cited by 31 · see citing works

Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs

Lutter, L., Serpell, C. J., Tuite, M. F., Serpell, L. C., & Xue, W. (2020) · BioMolecular Concepts · doi:10.1515/bmc-2020-0009 · Cited by 30 · see citing works

Fluspirilene Analogs Activate the 20S Proteasome and Overcome Proteasome Impairment by Intrinsically Disordered Protein Oligomers

Fiolek, T. J., Keel, K. L., & Tepe, J. J. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00099 · Cited by 30 · see citing works

McsB forms a gated kinase chamber to mark aberrant bacterial proteins for degradation

Hajdusits, B., Suskiewicz, M. J., Hundt, N., Meinhart, A., Kurzbauer, R., Leodolter, J., Kukura, P., & Clausen, T. (2021) · eLife · doi:10.7554/elife.63505 · Cited by 28 · see citing works

Improving resolution and resolvability of single-particle cryoEM structures using Gaussian mixture models

Chen, M., Schmid, M. F., & Chiu, W. (2023) · Nature Methods · doi:10.1038/s41592-023-02082-9 · Cited by 29 · see citing works

Substrate-engaged 26 S proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation

de la Peña, A. H., Goodall, E. A., Gates, S. N., Lander, G. C., & Martin, A. (2018) · Science · doi:10.1126/science.aav0725 · Cited by 293 · see citing works

Structure, Dynamics and Function of the 26S Proteasome

Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 105 · see citing works

Molecular mechanisms of substrate degradation by the 26S proteasome revealed by CryoEM (952.6)

Matyskiela, M. E., Lander, G. C., & Martin, A. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.952.6

Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective

Greene, E. R., Dong, K. C., & Martin, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.004 · Cited by 49 · see citing works

Substrate degradation by the 26S proteasome (478.2)

Martin, A., Matyskiela, M. E., Beckwith, R., Nyquist, K., Worden, E. J., Estrin, E., & Lander, G. C. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.478.2