{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:04:56Z","timestamp":1791396296745,"version":"4.3.3"},"reference-count":50,"publisher":"National Academy of Sciences","issue":"46","license":[{"start":{"date-parts":[[2017,4,21]],"date-time":"2017-04-21T00:00:00Z","timestamp":1492732800000},"content-version":"vor","delay-in-days":182,"URL":"http:\/\/www.pnas.org\/site\/misc\/userlicense.xhtml"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM026875"],"award-info":[{"award-number":["GM026875"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["91530321"],"award-info":[{"award-number":["91530321"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM43601"],"award-info":[{"award-number":["GM43601"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2016,11,15]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>The proteasome holoenzyme is an ATP-dependent protease in eukaryotes that degrades ubiquitylated substrates. It is involved in numerous important biological processes, such as cell division, differentiation, innate immunity, adaptive immunity, regulation of gene expression, and response to proteotoxic stress. Using cryoelectron microscopy, we have examined multiple conformational states of the human proteasome at medium to high resolution. Our results reveal that the substrate-conducting channel in the core particle is transiently opened and accompanied by dynamic changes in structure of the particle. These observations provide new insights into how the proteasome recognizes ubiquitylated substrates and translocates them through a channel and gate to degradation sites in the core particle.<\/jats:p>","DOI":"10.1073\/pnas.1614614113","type":"journal-article","created":{"date-parts":[[2016,10,21]],"date-time":"2016-10-21T23:40:38Z","timestamp":1477093238000},"page":"12991-12996","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":185,"title":["Structural basis for dynamic regulation of the human 26S proteasome"],"prefix":"10.1073","volume":"113","author":[{"given":"Shuobing","family":"Chen","sequence":"first","affiliation":[{"name":"Center for Quantitative Biology, Peking University, Beijing 100871, China;"},{"name":"State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Peking University, Beijing 100871, China;"},{"name":"Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiayi","family":"Wu","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Peking University, Beijing 100871, China;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ying","family":"Lu","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong-Bei","family":"Ma","sequence":"additional","affiliation":[{"name":"Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byung-Hoon","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhou","family":"Yu","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, Graduate School of Arts and Sciences, Harvard University, Cambridge, MA 02138;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qi","family":"Ouyang","sequence":"additional","affiliation":[{"name":"Center for Quantitative Biology, Peking University, Beijing 100871, China;"},{"name":"State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Peking University, Beijing 100871, China;"},{"name":"Peking-Tsinghua Joint Center for Life Sciences, Peking University, Beijing 100871, China;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel J.","family":"Finley","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc W.","family":"Kirschner","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Youdong","family":"Mao","sequence":"additional","affiliation":[{"name":"Center for Quantitative Biology, Peking University, Beijing 100871, China;"},{"name":"State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Peking University, Beijing 100871, China;"},{"name":"Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215;"},{"name":"Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA 02115;"},{"name":"Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2016,10,21]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.tibs.2015.10.009","article-title":"Gates, channels, and switches: Elements of the proteasome machine","volume":"41","author":"Finley D","year":"2016","unstructured":"D Finley, X Chen, KJ Walters, Gates, channels, and switches: Elements of the proteasome machine. Trends Biochem Sci 41, 77\u201393 (2016).","journal-title":"Trends Biochem Sci"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1146\/annurev-biochem-060410-150257","article-title":"Molecular architecture and assembly of the eukaryotic proteasome","volume":"82","author":"Tomko RJ","year":"2013","unstructured":"Jr RJ Tomko, M Hochstrasser, Molecular architecture and assembly of the eukaryotic proteasome. Annu Rev Biochem 82, 415\u2013445 (2013).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1146\/annurev-biophys-083012-130417","article-title":"Structural biology of the proteasome","volume":"42","author":"Kish-Trier E","year":"2013","unstructured":"E Kish-Trier, CP Hill, Structural biology of the proteasome. Annu Rev Biophys 42, 29\u201349 (2013).","journal-title":"Annu Rev Biophys"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1146\/annurev.biochem.78.081507.101607","article-title":"Recognition and processing of ubiquitin-protein conjugates by the proteasome","volume":"78","author":"Finley D","year":"2009","unstructured":"D Finley, Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78, 477\u2013513 (2009).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/j.str.2014.11.017","article-title":"Crystal structure of the human 20S proteasome in complex with carfilzomib","volume":"23","author":"Harshbarger W","year":"2015","unstructured":"W Harshbarger, C Miller, C Diedrich, J Sacchettini, Crystal structure of the human 20S proteasome in complex with carfilzomib. Structure 23, 418\u2013424 (2015).","journal-title":"Structure"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"8708","DOI":"10.1002\/anie.201201616","article-title":"Inhibitors for the immuno- and constitutive proteasome: Current and future trends in drug development","volume":"51","author":"Huber EM","year":"2012","unstructured":"EM Huber, M Groll, Inhibitors for the immuno- and constitutive proteasome: Current and future trends in drug development. Angew Chem Int Ed Engl 51, 8708\u20138720 (2012).","journal-title":"Angew Chem Int Ed Engl"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"14870","DOI":"10.1073\/pnas.1213333109","article-title":"Near-atomic resolution structural model of the yeast 26S proteasome","volume":"109","author":"Beck F","year":"2012","unstructured":"F Beck, , Near-atomic resolution structural model of the yeast 26S proteasome. Proc Natl Acad Sci USA 109, 14870\u201314875 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1073\/pnas.1120559109","article-title":"Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach","volume":"109","author":"Lasker K","year":"2012","unstructured":"K Lasker, , Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci USA 109, 1380\u20131387 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nature10774","article-title":"Complete subunit architecture of the proteasome regulatory particle","volume":"482","author":"Lander GC","year":"2012","unstructured":"GC Lander, , Complete subunit architecture of the proteasome regulatory particle. Nature 482, 186\u2013191 (2012).","journal-title":"Nature"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.molcel.2012.03.026","article-title":"Molecular model of the human 26S proteasome","volume":"46","author":"da Fonseca PC","year":"2012","unstructured":"PC da Fonseca, J He, EP Morris, Molecular model of the human 26S proteasome. Mol Cell 46, 54\u201366 (2012).","journal-title":"Mol Cell"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1126\/science.7725097","article-title":"Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 \u00c5 resolution","volume":"268","author":"L\u00f6we J","year":"1995","unstructured":"J L\u00f6we, , Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 \u00c5 resolution. Science 268, 533\u2013539 (1995).","journal-title":"Science"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1038\/386463a0","article-title":"Structure of 20S proteasome from yeast at 2.4\u00c5 resolution","volume":"386","author":"Groll M","year":"1997","unstructured":"M Groll, , Structure of 20S proteasome from yeast at 2.4\u00c5 resolution. Nature 386, 463\u2013471 (1997).","journal-title":"Nature"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/S0969-2126(02)00748-7","article-title":"The structure of the mammalian 20S proteasome at 2.75 \u00c5 resolution","volume":"10","author":"Unno M","year":"2002","unstructured":"M Unno, , The structure of the mammalian 20S proteasome at 2.75 \u00c5 resolution. Structure 10, 609\u2013618 (2002).","journal-title":"Structure"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1073\/pnas.1117648108","article-title":"The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together","volume":"109","author":"Pathare GR","year":"2012","unstructured":"GR Pathare, , The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together. Proc Natl Acad Sci USA 109, 149\u2013154 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"2984","DOI":"10.1073\/pnas.1400546111","article-title":"Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11","volume":"111","author":"Pathare GR","year":"2014","unstructured":"GR Pathare, , Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proc Natl Acad Sci USA 111, 2984\u20132989 (2014).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"33992","DOI":"10.1074\/jbc.M110.134510","article-title":"Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12","volume":"285","author":"Riedinger C","year":"2010","unstructured":"C Riedinger, , Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12. J Biol Chem 285, 33992\u201334003 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.jmb.2005.03.007","article-title":"Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition","volume":"348","author":"Wang Q","year":"2005","unstructured":"Q Wang, P Young, KJ Walters, Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J Mol Biol 348, 727\u2013739 (2005).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1038\/nsmb.2771","article-title":"Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation","volume":"21","author":"Worden EJ","year":"2014","unstructured":"EJ Worden, C Padovani, A Martin, Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation. Nat Struct Mol Biol 21, 220\u2013227 (2014).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.molcel.2009.06.010","article-title":"Structure of the S5a:K48-linked diubiquitin complex and its interactions with Rpn13","volume":"35","author":"Zhang N","year":"2009","unstructured":"N Zhang, , Structure of the S5a:K48-linked diubiquitin complex and its interactions with Rpn13. Mol Cell 35, 280\u2013290 (2009).","journal-title":"Mol Cell"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"e13027","DOI":"10.7554\/eLife.13027","article-title":"Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition","volume":"5","author":"Dambacher CM","year":"2016","unstructured":"CM Dambacher, EJ Worden, MA Herzik, A Martin, GC Lander, Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition. eLife 5, e13027 (2016).","journal-title":"eLife"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1042\/BJ20120542","article-title":"Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation","volume":"448","author":"Boehringer J","year":"2012","unstructured":"J Boehringer, , Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation. Biochem J 448, 55\u201365 (2012).","journal-title":"Biochem J"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.str.2011.12.015","article-title":"The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric \u03b1-helical rings","volume":"20","author":"He J","year":"2012","unstructured":"J He, , The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric \u03b1-helical rings. Structure 20, 513\u2013521 (2012).","journal-title":"Structure"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.molcel.2009.04.021","article-title":"Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii","volume":"34","author":"Zhang F","year":"2009","unstructured":"F Zhang, , Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol Cell 34, 473\u2013484 (2009).","journal-title":"Mol Cell"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.molcel.2009.04.022","article-title":"Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii","volume":"34","author":"Zhang F","year":"2009","unstructured":"F Zhang, , Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol Cell 34, 485\u2013496 (2009).","journal-title":"Mol Cell"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"2642","DOI":"10.1073\/pnas.1601561113","article-title":"Structure of an endogenous yeast 26S proteasome reveals two major conformational states","volume":"113","author":"Luan B","year":"2016","unstructured":"B Luan, , Structure of an endogenous yeast 26S proteasome reveals two major conformational states. Proc Natl Acad Sci USA 113, 2642\u20132647 (2016).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/nsmb.2616","article-title":"Conformational switching of the 26S proteasome enables substrate degradation","volume":"20","author":"Matyskiela ME","year":"2013","unstructured":"ME Matyskiela, GC Lander, A Martin, Conformational switching of the 26S proteasome enables substrate degradation. Nat Struct Mol Biol 20, 781\u2013788 (2013).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"7264","DOI":"10.1073\/pnas.1305782110","article-title":"Structure of the 26S proteasome with ATP-\u03b3S bound provides insights into the mechanism of nucleotide-dependent substrate translocation","volume":"110","author":"\u015aled\u017a P","year":"2013","unstructured":"P \u015aled\u017a, , Structure of the 26S proteasome with ATP-\u03b3S bound provides insights into the mechanism of nucleotide-dependent substrate translocation. Proc Natl Acad Sci USA 110, 7264\u20137269 (2013).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"5544","DOI":"10.1073\/pnas.1403409111","article-title":"Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome","volume":"111","author":"Unverdorben P","year":"2014","unstructured":"P Unverdorben, , Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proc Natl Acad Sci USA 111, 5544\u20135549 (2014).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1016\/j.str.2013.06.023","article-title":"Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid","volume":"21","author":"Estrin E","year":"2013","unstructured":"E Estrin, JR Lopez-Blanco, P Chac\u00f3n, A Martin, Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid. Structure 21, 1624\u20131635 (2013).","journal-title":"Structure"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1021\/bi061994u","article-title":"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex","volume":"46","author":"Wang X","year":"2007","unstructured":"X Wang, , Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46, 3553\u20133565 (2007).","journal-title":"Biochemistry"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1038\/nmeth992","article-title":"Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization","volume":"4","author":"Scheres SH","year":"2007","unstructured":"SH Scheres, , Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nat Methods 4, 27\u201329 (2007).","journal-title":"Nat Methods"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.jmb.2011.11.010","article-title":"A Bayesian view on cryo-EM structure determination","volume":"415","author":"Scheres SH","year":"2012","unstructured":"SH Scheres, A Bayesian view on cryo-EM structure determination. J Mol Biol 415, 406\u2013418 (2012).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1038\/35040607","article-title":"Structural basis for the activation of 20S proteasomes by 11S regulators","volume":"408","author":"Whitby FG","year":"2000","unstructured":"FG Whitby, , Structural basis for the activation of 20S proteasomes by 11S regulators. Nature 408, 115\u2013120 (2000).","journal-title":"Nature"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1146\/annurev-biochem-060408-172623","article-title":"AAA+ proteases: ATP-fueled machines of protein destruction","volume":"80","author":"Sauer RT","year":"2011","unstructured":"RT Sauer, TA Baker, AAA+ proteases: ATP-fueled machines of protein destruction. Annu Rev Biochem 80, 587\u2013612 (2011).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1046\/j.1365-2443.2001.00447.x","article-title":"AAA+ superfamily ATPases: Common structure\u2013diverse function","volume":"6","author":"Ogura T","year":"2001","unstructured":"T Ogura, AJ Wilkinson, AAA+ superfamily ATPases: Common structure\u2013diverse function. Genes Cells 6, 575\u2013597 (2001).","journal-title":"Genes Cells"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1038\/nsmb.2659","article-title":"Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase","volume":"20","author":"Beckwith R","year":"2013","unstructured":"R Beckwith, E Estrin, EJ Worden, A Martin, Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase. Nat Struct Mol Biol 20, 1164\u20131172 (2013).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.cell.2009.09.034","article-title":"Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine","volume":"139","author":"Glynn SE","year":"2009","unstructured":"SE Glynn, A Martin, AR Nager, TA Baker, RT Sauer, Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 139, 744\u2013756 (2009).","journal-title":"Cell"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/nchembio.1732","article-title":"Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine","volume":"11","author":"Iosefson O","year":"2015","unstructured":"O Iosefson, AR Nager, TA Baker, RT Sauer, Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine. Nat Chem Biol 11, 201\u2013206 (2015).","journal-title":"Nat Chem Biol"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1038\/nsmb.1501","article-title":"The \u2018glutamate switch\u2019 provides a link between ATPase activity and ligand binding in AAA+ proteins","volume":"15","author":"Zhang X","year":"2008","unstructured":"X Zhang, DB Wigley, The \u2018glutamate switch\u2019 provides a link between ATPase activity and ligand binding in AAA+ proteins. Nat Struct Mol Biol 15, 1223\u20131227 (2008).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1038\/nsmb.2147","article-title":"An asymmetric interface between the regulatory and core particles of the proteasome","volume":"18","author":"Tian G","year":"2011","unstructured":"G Tian, , An asymmetric interface between the regulatory and core particles of the proteasome. Nat Struct Mol Biol 18, 1259\u20131267 (2011).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1074\/jbc.C109.070425","article-title":"Structural models for interactions between the 20S proteasome and its PAN\/19S activators","volume":"285","author":"Stadtmueller BM","year":"2010","unstructured":"BM Stadtmueller, , Structural models for interactions between the 20S proteasome and its PAN\/19S activators. J Biol Chem 285, 13\u201317 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"26652","DOI":"10.1074\/jbc.M111.246793","article-title":"C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome","volume":"286","author":"Kim YC","year":"2011","unstructured":"YC Kim, GN DeMartino, C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome. J Biol Chem 286, 26652\u201326666 (2011).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"9269","DOI":"10.1074\/jbc.M111.316208","article-title":"Stable incorporation of ATPase subunits into 19 S regulatory particle of human proteasome requires nucleotide binding and C-terminal tails","volume":"287","author":"Lee SH","year":"2012","unstructured":"SH Lee, JH Moon, SK Yoon, JB Yoon, Stable incorporation of ATPase subunits into 19 S regulatory particle of human proteasome requires nucleotide binding and C-terminal tails. J Biol Chem 287, 9269\u20139279 (2012).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1038\/80992","article-title":"A gated channel into the proteasome core particle","volume":"7","author":"Groll M","year":"2000","unstructured":"M Groll, , A gated channel into the proteasome core particle. Nat Struct Biol 7, 1062\u20131067 (2000).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"18535","DOI":"10.1074\/jbc.M112.357327","article-title":"Functional asymmetries of proteasome translocase pore","volume":"287","author":"Erales J","year":"2012","unstructured":"J Erales, MA Hoyt, F Troll, P Coffino, Functional asymmetries of proteasome translocase pore. J Biol Chem 287, 18535\u201318543 (2012).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_46_2","doi-asserted-by":"crossref","first-page":"7781","DOI":"10.1074\/jbc.M112.441907","article-title":"Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs","volume":"288","author":"Peth A","year":"2013","unstructured":"A Peth, N Kukushkin, M Boss\u00e9, AL Goldberg, Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs. J Biol Chem 288, 7781\u20137790 (2013).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_47_2","doi-asserted-by":"crossref","first-page":"7816","DOI":"10.1073\/pnas.1608050113","article-title":"Structure of the human 26S proteasome at a resolution of 3.9 \u00c5","volume":"113","author":"Schweitzer A","year":"2016","unstructured":"A Schweitzer, , Structure of the human 26S proteasome at a resolution of 3.9 \u00c5. Proc Natl Acad Sci USA 113, 7816\u20137821 (2016).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_48_2","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1038\/nsmb.3273","article-title":"An atomic structure of the human 26S proteasome","volume":"23","author":"Huang X","year":"2016","unstructured":"X Huang, B Luan, J Wu, Y Shi, An atomic structure of the human 26S proteasome. Nat Struct Mol Biol 23, 778\u2013785 (2016).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_49_2","unstructured":"J Wu Unsupervised single-particle deep classification via statistical manifold learning. arXiv:1604.04539. (2016)."},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/S0263-7855(97)00009-X","article-title":"HOLE: A program for the analysis of the pore dimensions of ion channel structural models","volume":"14","author":"Smart OS","year":"1996","unstructured":"OS Smart, JG Neduvelil, X Wang, BA Wallace, MS Sansom, HOLE: A program for the analysis of the pore dimensions of ion channel structural models. J Mol Graph 14, 354\u2013360, 376 (1996).","journal-title":"J Mol Graph"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1614614113","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1614614113","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T11:03:54Z","timestamp":1654599834000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1614614113"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,10,21]]},"references-count":50,"journal-issue":{"issue":"46","published-print":{"date-parts":[[2016,11,15]]}},"alternative-id":["10.1073\/pnas.1614614113"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1614614113","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,10,21]]},"assertion":[{"value":"2016-10-21","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}