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Elsevier BV
Structure (78)
References
129
Referenced
56
10.1038/nature11778
/ Nature / Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures by Arai (2013)10.1073/pnas.1116538109
/ Proc. Natl. Acad. Sci. USA / Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly by Barrault (2012)10.1126/science.1224352
/ Science / Identification of the Cdc48⋅20S proteasome as an ancient AAA+ proteolytic machine by Barthelme (2012)10.1073/pnas.1213333109
/ Proc. Natl. Acad. Sci. USA / Near-atomic resolution structural model of the yeast 26S proteasome by Beck (2012)10.1021/bi802198q
/ Biochemistry / Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins by Besche (2009)10.1073/pnas.1015530107
/ Proc. Natl. Acad. Sci. USA / Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution by Bohn (2010)10.1016/j.bbrc.2013.04.069
/ Biochem. Biophys. Res. Commun. / Localization of the regulatory particle subunit Sem1 in the 26S proteasome by Bohn (2013)10.1016/j.molcel.2010.04.019
/ Mol. Cell / Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2 by Chen (2010)10.1126/science.1075901
/ Science / Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1 by Cope (2002)10.1016/j.molcel.2012.03.026
/ Mol. Cell / Molecular model of the human 26S proteasome by da Fonseca (2012)10.1016/0014-5793(89)81441-3
/ FEBS Lett. / The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria by Dahlmann (1989)10.1016/j.molcel.2009.04.030
/ Mol. Cell / Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases by Djuranovic (2009)10.1073/pnas.1209345110
/ Proc. Natl. Acad. Sci. USA / Insights into the regulation of the human COP9 signalosome catalytic subunit, CSN5/Jab1 by Echalier (2013)10.1038/nsmb.2235
/ Nat. Struct. Mol. Biol. / Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex by Ellisdon (2012)10.1038/ncb845
/ Nat. Cell Biol. / Proteasome subunit Rpn1 binds ubiquitin-like protein domains by Elsasser (2002){'key': '10.1016/j.str.2013.08.010_bib16', 'first-page': '616', 'article-title': 'Structural basis for a reciprocal regulation between SCF and CSN. Cell Rep', 'volume': '2', 'author': 'Enchev', 'year': '2012'}
/ Structural basis for a reciprocal regulation between SCF and CSN. Cell Rep by Enchev (2012)10.1016/j.str.2013.06.023
/ Structure / Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid by Estrin (2013)10.1073/pnas.74.1.54
/ Proc. Natl. Acad. Sci. USA / A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes by Etlinger (1977)10.1074/jbc.M112.386458
/ J. Biol. Chem. / The archaeal proteasome is regulated by a network of AAA ATPases by Forouzan (2012)10.1016/j.bbrc.2009.07.145
/ Biochem. Biophys. Res. Commun. / An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome by Förster (2009)10.1074/mcp.R000002-MCP201
/ Mol. Cell. Proteomics / Toward an integrated structural model of the 26S proteasome by Förster (2010)10.1016/S0076-6879(10)83003-4
/ Methods Enzymol. / Integration of cryo-EM with atomic and protein-protein interaction data by Förster (2010){'key': '10.1016/j.str.2013.08.010_bib23', 'series-title': 'Three-Dimensional Electron Microscopy of Macromolecular Assemblies', 'author': 'Frank', 'year': '2006'}
/ Three-Dimensional Electron Microscopy of Macromolecular Assemblies by Frank (2006)10.1038/35018597
/ Nature / A ratchet-like inter-subunit reorganization of the ribosome during translocation by Frank (2000)10.1016/j.bbrc.2010.05.061
/ Biochem. Biophys. Res. Commun. / Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae by Fukunaga (2010)10.1016/j.cell.2009.04.061
/ Cell / Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base by Funakoshi (2009)10.1016/S0959-440X(99)00057-3
/ Curr. Opin. Struct. Biol. / Winged helix proteins by Gajiwala (2000)10.1016/S0092-8674(00)81603-7
/ Cell / A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3 by Glickman (1998)10.1016/j.cell.2009.09.034
/ Cell / Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine by Glynn (2009)10.1038/nsmb.2288
/ Nat. Struct. Mol. Biol. / Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine by Glynn (2012)10.1016/S0092-8674(00)80428-6
/ Cell / Regulatory subunits of energy-dependent proteases by Gottesman (1997)10.1038/386463a0
/ Nature / Structure of 20S proteasome from yeast at 2.4 A resolution by Groll (1997)10.1038/sj.emboj.7601338
/ EMBO J. / A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes by Hamazaki (2006)10.1016/j.cell.2006.07.038
/ Cell / Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation by Hanna (2006)10.1016/j.cell.2012.08.011
/ Cell / A census of human soluble protein complexes by Havugimana (2012)10.1016/j.str.2011.12.015
/ Structure / The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric α-helical rings by He (2012)10.1038/80384
/ Nat. Med. / Basic Medical Research Award. The ubiquitin system by Hershko (2000)10.1016/S0968-0004(98)01217-1
/ Trends Biochem. Sci. / The PCI domain: a common theme in three multiprotein complexes by Hofmann (1998)10.1016/S0021-9258(18)47564-3
/ J. Biol. Chem. / Purification of two high molecular weight proteases from rabbit reticulocyte lysate by Hough (1987)10.1038/nature06926
/ Nature / Proteasome subunit Rpn13 is a novel ubiquitin receptor by Husnjak (2008)10.1016/j.molcel.2010.05.001
/ Mol. Cell / Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome by Isasa (2010)10.1073/pnas.081543698
/ Proc. Natl. Acad. Sci. USA / Translocation pathway of protein substrates in ClpAP protease by Ishikawa (2001)10.1016/j.cell.2012.09.014
/ Cell / The hexameric helicase DnaB adopts a nonplanar conformation during translocation by Itsathitphaisarn (2012)10.1074/jbc.M204982200
/ J. Biol. Chem. / What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome by Kajava (2002)10.1016/j.cell.2009.05.008
/ Cell / Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones by Kaneko (2009)10.1146/annurev-biophys-083012-130417
/ Annu. Rev. Biophys. / Structural biology of the proteasome by Kish-Trier (2013)10.1038/nsmb1335
/ Nat. Struct. Mol. Biol. / Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites by Kleijnen (2007)10.1038/416763a
/ Nature / A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal by Lam (2002)10.1038/nature10774
/ Nature / Complete subunit architecture of the proteasome regulatory particle by Lander (2012)10.1073/pnas.1120559109
/ Proc. Natl. Acad. Sci. USA / Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach by Lasker (2012)10.1074/mcp.R110.000067
/ Mol. Cell. Proteomics / Integrative structure modeling of macromolecular assemblies from proteomics data by Lasker (2010)10.1016/S1097-2765(02)00638-X
/ Mol. Cell / Multiple associated proteins regulate proteasome structure and function by Leggett (2002)10.1126/science.7725097
/ Science / Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution by Löwe (1995)10.1016/S0968-0004(97)01058-X
/ Trends Biochem. Sci. / A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (anaphase-promoting complex) by Lupas (1997)10.1016/S0968-0004(97)01117-1
/ Trends Biochem. Sci. / Self-compartmentalizing proteases by Lupas (1997)10.1159/000468684
/ Enzyme Protein / Structural features of 26S and 20S proteasomes by Lupas (1993)10.1126/science.1059780
/ Science / Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome by Lyapina (2001)10.1038/nature04031
/ Nature / Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines by Martin (2005)10.1038/nsmb.2616
/ Nat. Struct. Mol. Biol. / Conformational switching of the 26S proteasome enables substrate degradation by Matyskiela (2013)10.1371/journal.pbio.1000545
/ PLoS Biol. / The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation by Moretti (2010)10.1093/emboj/20.21.5898
/ EMBO J. / Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta by Murata (2001)10.1073/pnas.0905081106
/ Proc. Natl. Acad. Sci. USA / Insights into the molecular architecture of the 26S proteasome by Nickell (2009)10.1016/j.jsb.2003.11.008
/ J. Struct. Biol. / Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases by Ogura (2004)10.1016/S0014-5793(97)00138-5
/ FEBS Lett. / Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum by Pamnani (1997)10.1038/nature12123
/ Nature / Reconfiguration of the proteasome during chaperone-mediated assembly by Park (2013)10.1038/nature08065
/ Nature / Hexameric assembly of the proteasomal ATPases is templated through their C termini by Park (2009)10.1073/pnas.1117648108
/ Proc. Natl. Acad. Sci. USA / The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together by Pathare (2012)10.1126/science.1163885
/ Science / Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis by Pearce (2008)10.1006/jmbi.1993.1646
/ J. Mol. Biol. / Structural features of the 26 S proteasome complex by Peters (1993)10.1016/j.molcel.2009.11.015
/ Mol. Cell / Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening by Peth (2009)10.1074/jbc.M112.441907
/ J. Biol. Chem. / Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 by Peth (2013)10.1016/j.molcel.2010.11.002
/ Mol. Cell / ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation by Peth (2010)10.1038/nchembio.130
/ Nat. Chem. Biol. / Substrate selection by the proteasome during degradation of protein complexes by Prakash (2009)10.1002/j.1460-2075.1992.tb05206.x
/ EMBO J. / Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum by Pühler (1992)10.1016/j.cell.2013.04.032
/ Cell / Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis by Qian (2013)10.1038/sj.emboj.7601450
/ EMBO J. / hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37 by Qiu (2006)10.1016/j.str.2013.04.002
/ Structure / Architecture of human translation initiation factor 3 by Querol-Audi (2013)10.1016/j.molcel.2008.03.004
/ Mol. Cell / Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases by Rabl (2008)10.1016/S0092-8674(02)00619-0
/ Cell / Ribosome structure and the mechanism of translation by Ramakrishnan (2002)10.1016/S0021-9258(18)53218-X
/ J. Biol. Chem. / The multicatalytic and 26 S proteases by Rechsteiner (1993)10.1038/nature08063
/ Nature / Chaperone-mediated pathway of proteasome regulatory particle assembly by Roelofs (2009)10.1038/nsb0297-133
/ Nat. Struct. Biol. / The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome by Rohrwild (1997)10.1038/nature09444
/ Nature / The proteasome antechamber maintains substrates in an unfolded state by Ruschak (2010)10.1371/journal.pbio.1001244
/ PLoS Biol. / Putting the pieces together: integrative modeling platform software for structure determination of macromolecular assemblies by Russel (2012)10.1007/978-1-61779-474-2_22
/ Methods Mol. Biol. / Assembly and function of the proteasome by Saeki (2012)10.1016/j.cell.2009.05.005
/ Cell / Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle by Saeki (2009)10.1073/pnas.1119394109
/ Proc. Natl. Acad. Sci. USA / Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy by Sakata (2012)10.1016/j.molcel.2011.04.021
/ Mol. Cell / The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle by Sakata (2011)10.1016/j.jmb.2007.04.084
/ J. Mol. Biol. / The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer by Sanches (2007)10.1038/nature07254
/ Nature / Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains by Sato (2008)10.1146/annurev-biochem-060408-172623
/ Annu. Rev. Biochem. / AAA+ proteases: ATP-fueled machines of protein destruction by Sauer (2011)10.1186/1471-2105-6-71
/ BMC Bioinformatics / Prediction of a common structural scaffold for proteasome lid, COP9-signalosome and eIF3 complexes by Scheel (2005)10.1038/nature08403
/ Nature / What recent ribosome structures have revealed about the mechanism of translation by Schmeing (2009)10.1038/nature06924
/ Nature / Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction by Schreiner (2008)10.1042/bj2800225
/ Biochem. J. / Molecular interaction of the proteasome (multicatalytic proteinase). Evidence that the proteasome is not a constituent of the ‘26 S’ multienzyme complex by Seelig (1991)10.1126/science.7725107
/ Science / Proteasome from Thermoplasma acidophilum: a threonine protease by Seemüller (1995)10.1074/jbc.M511951200
/ J. Biol. Chem. / 20S proteasomes have the potential to keep substrates in store for continual degradation by Sharon (2006)10.1016/j.jmb.2013.01.036
/ J. Mol. Biol. / Allosteric effects in the regulation of 26S proteasome activities by Sledź (2013)10.1073/pnas.1305782110
/ Proc. Natl. Acad. Sci. USA / Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation by Śledź (2013)10.1016/j.molcel.2007.06.033
/ Mol. Cell / Docking of the proteasomal ATPases’ carboxyl termini in the 20S proteasome’s alpha ring opens the gate for substrate entry by Smith (2007)10.1016/j.cell.2011.02.005
/ Cell / ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle by Smith (2011)10.1016/j.molcel.2005.10.019
/ Mol. Cell / ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins by Smith (2005)10.1016/S0092-8674(00)00166-5
/ Cell / Crystal and solution structures of an HslUV protease-chaperone complex by Sousa (2000)10.1074/jbc.C109.070425
/ J. Biol. Chem. / Structural models for interactions between the 20S proteasome and its PAN/19S activators by Stadtmueller (2010)10.1073/pnas.1116821108
/ Proc. Natl. Acad. Sci. USA / Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3) by Sun (2011)10.1016/S0960-9822(95)00153-9
/ Curr. Biol. / The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus by Tamura (1995)10.2183/pjab.85.12
/ Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. / The proteasome: overview of structure and functions by Tanaka (2009)10.1016/j.cell.2009.08.043
/ Cell / Running in reverse: the structural basis for translocation polarity in hexameric helicases by Thomsen (2009)10.1038/nsmb.2147
/ Nat. Struct. Mol. Biol. / An asymmetric interface between the regulatory and core particles of the proteasome by Tian (2011)10.1016/j.molcel.2010.02.035
/ Mol. Cell / Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly by Tomko (2010)10.1016/j.molcel.2011.11.020
/ Mol. Cell / Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining by Tomko (2011)10.1016/j.str.2008.03.005
/ Structure / Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics by Trabuco (2008)10.1128/MCB.16.11.6020
/ Mol. Cell. Biol. / The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover by van Nocker (1996)10.1126/science.1075898
/ Science / Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome by Verma (2002)10.1091/mbc.11.10.3425
/ Mol. Biol. Cell / Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes by Verma (2000)10.1038/nature11468
/ Nature / Increased proteasome activity in human embryonic stem cells is regulated by PSMD11 by Vilchez (2012)10.1038/nature11315
/ Nature / RPN-6 determines C. elegans longevity under proteotoxic stress conditions by Vilchez (2012)10.1146/annurev.biochem.68.1.1015
/ Annu. Rev. Biochem. / The 26S proteasome: a molecular machine designed for controlled proteolysis by Voges (1999)10.1038/nsmb.1918
/ Nat. Struct. Mol. Biol. / Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation by Wang (2010)10.1038/nsb0395-199
/ Nat. Struct. Biol. / Conformational constraints in protein degradation by the 20S proteasome by Wenzel (1995)10.1006/jmbi.1997.1589
/ J. Mol. Biol. / Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis by Wolf (1998)10.1093/oxfordjournals.molbev.a003897
/ Mol. Biol. Evol. / Evolution of proteasomal ATPases by Wollenberg (2001)10.1038/nature01071
/ Nature / A cryptic protease couples deubiquitination and degradation by the proteasome by Yao (2002)10.1038/ncb1460
/ Nat. Cell Biol. / Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1 by Yao (2006)10.1038/emboj.2009.382
/ EMBO J. / Interactions of PAN’s C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions by Yu (2009)10.1016/j.molcel.2009.04.021
/ Mol. Cell / Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii by Zhang (2009)10.1016/j.molcel.2009.06.010
/ Mol. Cell / Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13 by Zhang (2009)10.1016/0014-5793(92)80925-7
/ FEBS Lett. / Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coli by Zwickl (1992)10.1074/jbc.274.37.26008
/ J. Biol. Chem. / An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes by Zwickl (1999)
Dates
Type | When |
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Created | 11 years, 11 months ago (Sept. 3, 2013, 11:33 a.m.) |
Deposited | 3 years, 9 months ago (Nov. 2, 2021, 9:37 p.m.) |
Indexed | 11 months, 2 weeks ago (Sept. 11, 2024, 2:11 p.m.) |
Issued | 11 years, 11 months ago (Sept. 1, 2013) |
Published | 11 years, 11 months ago (Sept. 1, 2013) |
Published Print | 11 years, 11 months ago (Sept. 1, 2013) |
@article{F_rster_2013, title={Unveiling the Long-Held Secrets of the 26S Proteasome}, volume={21}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/j.str.2013.08.010}, DOI={10.1016/j.str.2013.08.010}, number={9}, journal={Structure}, publisher={Elsevier BV}, author={Förster, Friedrich and Unverdorben, Pia and Śledź, Paweł and Baumeister, Wolfgang}, year={2013}, month=sep, pages={1551–1562} }