메뉴 건너뛰기




Volumn 114, Issue 6, 2017, Pages 1305-1310

Structural insights into the functional cycle of the ATPase module of the 26S proteasome

Author keywords

26S proteasome; AAA+ ATpase; Cryo electron microscopy; Integrative modeling; Single particle analysis

Indexed keywords

26S PROTEASOME; ADENOSINE TRIPHOSPHATASE; FUNGAL ENZYME; PROTEASOME; UNCLASSIFIED DRUG; ATP DEPENDENT 26S PROTEASE; NUCLEOTIDE;

EID: 85011681247     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1621129114     Document Type: Article
Times cited : (130)

References (61)
  • 1
    • 0034296394 scopus 로고    scopus 로고
    • Basic medical research award. The ubiquitin system
    • Hershko A, Ciechanover A, Varshavsky A (2000) Basic Medical Research Award. The ubiquitin system. Nat Med 6(10):1073-1081.
    • (2000) Nat Med , vol.6 , Issue.10 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 2
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu Rev Biochem 68:1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 3
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78:477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 5
    • 0026600786 scopus 로고
    • Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum
    • Pühler G, et al. (1992) Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum. EMBO J 11(4):1607-1616.
    • (1992) EMBO J , vol.11 , Issue.4 , pp. 1607-1616
    • Pühler, G.1
  • 6
    • 0029060166 scopus 로고
    • Proteasome from Thermoplasma acidophilum: A threonine protease
    • Seemüller E, et al. (1995) Proteasome from Thermoplasma acidophilum: A threonine protease. Science 268(5210):579-582.
    • (1995) Science , vol.268 , Issue.5210 , pp. 579-582
    • Seemüller, E.1
  • 7
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll M, et al. (1997) Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386(6624):463-471.
    • (1997) Nature , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1
  • 8
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a selfcompartmentalizing protease
    • Baumeister W, Walz J, Zühl F, Seemüller E (1998) The proteasome: Paradigm of a selfcompartmentalizing protease. Cell 92(3):367-380.
    • (1998) Cell , vol.92 , Issue.3 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 9
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • Smith DM, et al. (2007) Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol Cell 27(5):731-744.
    • (2007) Mol Cell , vol.27 , Issue.5 , pp. 731-744
    • Smith, D.M.1
  • 10
    • 77649243592 scopus 로고    scopus 로고
    • Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening
    • Sadre-Bazzaz K, Whitby FG, Robinson H, Formosa T, Hill CP (2010) Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol Cell 37(5):728-735.
    • (2010) Mol Cell , vol.37 , Issue.5 , pp. 728-735
    • Sadre-Bazzaz, K.1    Whitby, F.G.2    Robinson, H.3    Formosa, T.4    Hill, C.P.5
  • 11
    • 76349089770 scopus 로고    scopus 로고
    • Interactions of PAN's C-Termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions
    • Yu Y, et al. (2010) Interactions of PAN's C-Termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions. EMBO J 29(3):692-702.
    • (2010) EMBO J , vol.29 , Issue.3 , pp. 692-702
    • Yu, Y.1
  • 12
    • 84959019581 scopus 로고    scopus 로고
    • Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome
    • Shi Y, et al. (2016) Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome. Science 351(6275):aad9421.
    • (2016) Science , vol.351 , Issue.6275 , pp. aad9421
    • Shi, Y.1
  • 13
    • 44349116590 scopus 로고    scopus 로고
    • Proteasome subunit Rpn13 is a novel ubiquitin receptor
    • Husnjak K, et al. (2008) Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453(7194):481-488.
    • (2008) Nature , vol.453 , Issue.7194 , pp. 481-488
    • Husnjak, K.1
  • 14
    • 0028235965 scopus 로고
    • A 26 S protease subunit that binds ubiquitin conjugates
    • Deveraux Q, Ustrell V, Pickart C, Rechsteiner M (1994) A 26 S protease subunit that binds ubiquitin conjugates. J Biol Chem 269(10):7059-7061.
    • (1994) J Biol Chem , vol.269 , Issue.10 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 15
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma R, et al. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298(5593):611-615.
    • (2002) Science , vol.298 , Issue.5593 , pp. 611-615
    • Verma, R.1
  • 16
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T, Cohen RE (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419(6905):403-407.
    • (2002) Nature , vol.419 , Issue.6905 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 17
    • 84856976866 scopus 로고    scopus 로고
    • Complete subunit architecture of the proteasome regulatory particle
    • Lander GC, et al. (2012) Complete subunit architecture of the proteasome regulatory particle. Nature 482(7384):186-191.
    • (2012) Nature , vol.482 , Issue.7384 , pp. 186-191
    • Lander, G.C.1
  • 18
    • 84857134729 scopus 로고    scopus 로고
    • Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
    • Lasker K, et al. (2012) Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci USA 109(5):1380-1387.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.5 , pp. 1380-1387
    • Lasker, K.1
  • 19
    • 79959389010 scopus 로고    scopus 로고
    • AAA+ proteases: ATP-fueled machines of protein destruction
    • Sauer RT, Baker TA (2011) AAA+ proteases: ATP-fueled machines of protein destruction. Annu Rev Biochem 80:587-612.
    • (2011) Annu Rev Biochem , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 20
    • 84892882219 scopus 로고    scopus 로고
    • Marching to the beat of the ring: Polypeptide translocation by AAA+ proteases
    • Nyquist K, Martin A (2014) Marching to the beat of the ring: Polypeptide translocation by AAA+ proteases. Trends Biochem Sci 39(2):53-60.
    • (2014) Trends Biochem Sci , vol.39 , Issue.2 , pp. 53-60
    • Nyquist, K.1    Martin, A.2
  • 21
    • 84898807479 scopus 로고    scopus 로고
    • Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
    • Unverdorben P, et al. (2014) Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proc Natl Acad Sci USA 111(15):5544-5549.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.15 , pp. 5544-5549
    • Unverdorben, P.1
  • 22
    • 84978042613 scopus 로고    scopus 로고
    • Structure of the human 26S proteasome at a resolution of 3.9
    • Schweitzer A, et al. (2016) Structure of the human 26S proteasome at a resolution of 3.9 Å. Proc Natl Acad Sci USA 113(28):7816-7821.
    • (2016) Proc Natl Acad Sci USA , vol.113 , Issue.28 , pp. 7816-7821
    • Schweitzer, A.1
  • 23
    • 84960934506 scopus 로고    scopus 로고
    • Structure of an endogenous yeast 26S proteasome reveals two major conformational states
    • Luan B, et al. (2016) Structure of an endogenous yeast 26S proteasome reveals two major conformational states. Proc Natl Acad Sci USA 113(10):2642-2647.
    • (2016) Proc Natl Acad Sci USA , vol.113 , Issue.10 , pp. 2642-2647
    • Luan, B.1
  • 24
    • 84978676943 scopus 로고    scopus 로고
    • An atomic structure of the human 26S proteasome
    • Huang X, Luan B, Wu J, Shi Y (2016) An atomic structure of the human 26S proteasome. Nat Struct Mol Biol 23(9):778-785.
    • (2016) Nat Struct Mol Biol , vol.23 , Issue.9 , pp. 778-785
    • Huang, X.1    Luan, B.2    Wu, J.3    Shi, Y.4
  • 25
    • 84995618106 scopus 로고    scopus 로고
    • Structural basis for dynamic regulation of the human 26S proteasome
    • Chen S, et al. (2016) Structural basis for dynamic regulation of the human 26S proteasome. Proc Natl Acad Sci USA 113(46):12991-12996.
    • (2016) Proc Natl Acad Sci USA , vol.113 , Issue.46 , pp. 12991-12996
    • Chen, S.1
  • 26
    • 84866269021 scopus 로고    scopus 로고
    • Near-Atomic resolution structural model of the yeast 26S proteasome
    • Beck F, et al. (2012) Near-Atomic resolution structural model of the yeast 26S proteasome. Proc Natl Acad Sci USA 109(37):14870-14875.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.37 , pp. 14870-14875
    • Beck, F.1
  • 27
    • 70349267547 scopus 로고    scopus 로고
    • Molecular dynamics flexible fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography
    • Trabuco LG, Villa E, Schreiner E, Harrison CB, Schulten K (2009) Molecular dynamics flexible fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography. Methods 49(2):174-180.
    • (2009) Methods , vol.49 , Issue.2 , pp. 174-180
    • Trabuco, L.G.1    Villa, E.2    Schreiner, E.3    Harrison, C.B.4    Schulten, K.5
  • 28
    • 77951972141 scopus 로고    scopus 로고
    • Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2
    • Chen X, Lee BH, Finley D, Walters KJ (2010) Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. Mol Cell 38(3):404-415.
    • (2010) Mol Cell , vol.38 , Issue.3 , pp. 404-415
    • Chen, X.1    Lee, B.H.2    Finley, D.3    Walters, K.J.4
  • 29
    • 84876909425 scopus 로고    scopus 로고
    • Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
    • Sledz P, et al. (2013) Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation. Proc Natl Acad Sci USA 110(18):7264-7269.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.18 , pp. 7264-7269
    • Sledz, P.1
  • 30
    • 84937111175 scopus 로고    scopus 로고
    • Structural characterization of the interaction of Ubp6 with the 26S proteasome
    • Aufderheide A, et al. (2015) Structural characterization of the interaction of Ubp6 with the 26S proteasome. Proc Natl Acad Sci USA 112(28):8626-8631.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.28 , pp. 8626-8631
    • Aufderheide, A.1
  • 31
    • 84960840621 scopus 로고    scopus 로고
    • A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasom
    • Huber EM, et al. (2016) A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasom. Nat Commun 7:10900.
    • (2016) Nat Commun , vol.7 , pp. 10900
    • Huber, E.M.1
  • 32
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Förster A, Masters EI, Whitby FG, Robinson H, Hill CP (2005) The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol Cell 18(5):589-599.
    • (2005) Mol Cell , vol.18 , Issue.5 , pp. 589-599
    • Förster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 33
    • 84855198520 scopus 로고    scopus 로고
    • Structure and function of the AAA+ nucleotide binding pocket
    • Wendler P, Ciniawsky S, Kock M, Kube S (2012) Structure and function of the AAA+ nucleotide binding pocket. Biochim Biophys Acta 1823(1):2-14.
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 2-14
    • Wendler, P.1    Ciniawsky, S.2    Kock, M.3    Kube, S.4
  • 34
    • 70350772363 scopus 로고    scopus 로고
    • Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
    • Glynn SE, Martin A, Nager AR, Baker TA, Sauer RT (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 139(4):744-756.
    • (2009) Cell , vol.139 , Issue.4 , pp. 744-756
    • Glynn, S.E.1    Martin, A.2    Nager, A.R.3    Baker, T.A.4    Sauer, R.T.5
  • 35
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA (2012) The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 151(2):267-277.
    • (2012) Cell , vol.151 , Issue.2 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 36
    • 84880157841 scopus 로고    scopus 로고
    • Conformational switching of the 26S proteasome enables substrate degradation
    • Matyskiela ME, Lander GC, Martin A (2013) Conformational switching of the 26S proteasome enables substrate degradation. Nat Struct Mol Biol 20(7):781-788.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.7 , pp. 781-788
    • Matyskiela, M.E.1    Lander, G.C.2    Martin, A.3
  • 37
    • 84899876795 scopus 로고    scopus 로고
    • Mechanical operation and intersubunit coordination of ring-shaped molecular motors: Insights from single-molecule studies
    • Liu S, Chistol G, Bustamante C (2014) Mechanical operation and intersubunit coordination of ring-shaped molecular motors: Insights from single-molecule studies. Biophys J 106(9):1844-1858.
    • (2014) Biophys J , vol.106 , Issue.9 , pp. 1844-1858
    • Liu, S.1    Chistol, G.2    Bustamante, C.3
  • 38
    • 0034597824 scopus 로고    scopus 로고
    • Structural basis for the activation of 20S proteasomes by 11S regulators
    • Whitby FG, et al. (2000) Structural basis for the activation of 20S proteasomes by 11S regulators. Nature 408(6808):115-120.
    • (2000) Nature , vol.408 , Issue.6808 , pp. 115-120
    • Whitby, F.G.1
  • 39
    • 84886776909 scopus 로고    scopus 로고
    • The ClpXP protease unfolds substrates using a constant rate of pulling but different gears
    • Sen M, et al. (2013) The ClpXP protease unfolds substrates using a constant rate of pulling but different gears. Cell 155(3):636-646.
    • (2013) Cell , vol.155 , Issue.3 , pp. 636-646
    • Sen, M.1
  • 40
    • 39549084936 scopus 로고    scopus 로고
    • Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-Tagged substrates
    • Martin A, Baker TA, Sauer RT (2008) Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-Tagged substrates. Mol Cell 29(4):441-450.
    • (2008) Mol Cell , vol.29 , Issue.4 , pp. 441-450
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 41
    • 13844264476 scopus 로고    scopus 로고
    • TOM software toolbox: Acquisition and analysis for electron tomography
    • Nickell S, et al. (2005) TOM software toolbox: Acquisition and analysis for electron tomography. J Struct Biol 149(3):227-234.
    • (2005) J Struct Biol , vol.149 , Issue.3 , pp. 227-234
    • Nickell, S.1
  • 42
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH (2012) RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180(3):519-530.
    • (2012) J Struct Biol , vol.180 , Issue.3 , pp. 519-530
    • Scheres, S.H.1
  • 43
    • 84978399515 scopus 로고    scopus 로고
    • Computational methodologies for real-space structural refinement of large macromolecular complexes
    • Goh BC, et al. (2016) Computational methodologies for real-space structural refinement of large macromolecular complexes. Annu Rev Biophys 45:253-278.
    • (2016) Annu Rev Biophys , vol.45 , pp. 253-278
    • Goh, B.C.1
  • 44
    • 84971222608 scopus 로고    scopus 로고
    • QwikMD-integrative molecular dynamics toolkit for novices and experts
    • Ribeiro JV, et al. (2016) QwikMD-integrative molecular dynamics toolkit for novices and experts. Sci Rep 6:26536.
    • (2016) Sci Rep , vol.6 , pp. 26536
    • Ribeiro, J.V.1
  • 45
  • 46
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips JC, et al. (2005) Scalable molecular dynamics with NAMD. J Comput Chem 26(16):1781-1802.
    • (2005) J Comput Chem , vol.26 , Issue.16 , pp. 1781-1802
    • Phillips, J.C.1
  • 47
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox J, et al. (2014) Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol Cell Proteomics 13(9):2513-2526.
    • (2014) Mol Cell Proteomics , vol.13 , Issue.9 , pp. 2513-2526
    • Cox, J.1
  • 48
    • 84874590157 scopus 로고    scopus 로고
    • A method to measure hydrolytic activity of adenosinetriphosphatases (ATPases)
    • Bartolommei G, Moncelli MR, Tadini-Buoninsegni F (2013) A method to measure hydrolytic activity of adenosinetriphosphatases (ATPases). PLoS One 8(3):e58615.
    • (2013) PLoS One , vol.8 , Issue.3 , pp. e58615
    • Bartolommei, G.1    Moncelli, M.R.2    Tadini-Buoninsegni, F.3
  • 49
    • 79960898027 scopus 로고    scopus 로고
    • Computer controlled cryo-electron microscopy-TOM2 a software package for high-Throughput applications
    • Korinek A, Beck F, Baumeister W, Nickell S, Plitzko JM (2011) Computer controlled cryo-electron microscopy-TOM2 a software package for high-Throughput applications. J Struct Biol 175(3):394-405.
    • (2011) J Struct Biol , vol.175 , Issue.3 , pp. 394-405
    • Korinek, A.1    Beck, F.2    Baumeister, W.3    Nickell, S.4    Plitzko, J.M.5
  • 50
    • 84946481951 scopus 로고    scopus 로고
    • Automatic estimation and correction of anisotropic magnification distortion in electron microscopes
    • Grant T, Grigorieff N (2015) Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J Struct Biol 192(2):204-208.
    • (2015) J Struct Biol , vol.192 , Issue.2 , pp. 204-208
    • Grant, T.1    Grigorieff, N.2
  • 51
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic- resolution single-particle cryo-EM
    • Li X, et al. (2013) Electron counting and beam-induced motion correction enable nearatomic- resolution single-particle cryo-EM. Nat Methods 10(6):584-590.
    • (2013) Nat Methods , vol.10 , Issue.6 , pp. 584-590
    • Li, X.1
  • 52
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142(3):334-347.
    • (2003) J Struct Biol , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 53
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 54
    • 78650450552 scopus 로고    scopus 로고
    • Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution
    • Bohn S, et al. (2010) Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution. Proc Natl Acad Sci USA 107(49):20992-20997.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.49 , pp. 20992-20997
    • Bohn, S.1
  • 55
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234(3):779-815.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 56
    • 84857935771 scopus 로고    scopus 로고
    • 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, et al. (2012) The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric α-helical rings. Structure 20(3):513-521.
    • (2012) Structure , vol.20 , Issue.3 , pp. 513-521
    • He, J.1
  • 57
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell AD Jr, Feig M, Brooks CL 3rd (2004) Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comput Chem 25(11):1400-1415.
    • (2004) J Comput Chem , vol.25 , Issue.11 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 58
    • 84908089880 scopus 로고    scopus 로고
    • GPU-Accelerated analysis and visualization of large structures solved by molecular dynamics flexible fitting
    • Stone JE, McGreevy R, Isralewitz B, Schulten K (2014) GPU-Accelerated analysis and visualization of large structures solved by molecular dynamics flexible fitting. Faraday Discuss 169:265-283.
    • (2014) Faraday Discuss , vol.169 , pp. 265-283
    • Stone, J.E.1    McGreevy, R.2    Isralewitz, B.3    Schulten, K.4
  • 59
    • 84922065877 scopus 로고    scopus 로고
    • The complete structure of the large subunit of the mammalian mitochondrial ribosome
    • Greber BJ, et al. (2014) The complete structure of the large subunit of the mammalian mitochondrial ribosome. Nature 515(7526):283-286.
    • (2014) Nature , vol.515 , Issue.7526 , pp. 283-286
    • Greber, B.J.1
  • 60
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58(Pt 11):1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.