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Volumn 112, Issue 30, 2015, Pages E4017-E4025

Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy

Author keywords

AAA atpase; Cryo electron microscopy; Peroxisome; Pex1; Pex6

Indexed keywords

ADENOSINE TRIPHOSPHATASE; N ETHYLMALEIMIDE SENSITIVE FACTOR; NUCLEOTIDE; PEX1 PROTEIN; PEX6 PROTEIN; PROTEIN; UNCLASSIFIED DRUG; ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; PEPTIDE; PEX1 PROTEIN, S CEREVISIAE; PEX6 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84938099473     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1500257112     Document Type: Article
Times cited : (68)

References (64)
  • 2
    • 0034728701 scopus 로고    scopus 로고
    • Structural model of F1-ATPase and the implications for rotary catalysis
    • Leslie AG, Walker JE (2000) Structural model of F1-ATPase and the implications for rotary catalysis. Philos Trans R Soc Lond B Biol Sci 355(1396):465-471.
    • (2000) Philos Trans R Soc Lond B Biol Sci , vol.355 , Issue.1396 , pp. 465-471
    • Leslie, A.G.1    Walker, J.E.2
  • 3
    • 84855195754 scopus 로고    scopus 로고
    • ClpXP, an ATP-powered unfolding and protein-degradation machine
    • Baker TA, Sauer RT (2012) ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta 1823(1):15-28.
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 15-28
    • Baker, T.A.1    Sauer, R.T.2
  • 4
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 76:23-50.
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 5
    • 33749244758 scopus 로고    scopus 로고
    • The molecular chaperone Hsp104-A molecular machine for protein disaggregation
    • Bösl B, Grimminger V, Walter S (2006) The molecular chaperone Hsp104-a molecular machine for protein disaggregation. J Struct Biol 156(1):139-148.
    • (2006) J Struct Biol , vol.156 , Issue.1 , pp. 139-148
    • Bösl, B.1    Grimminger, V.2    Walter, S.3
  • 6
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer H, Bug M, Bremer S (2012) Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat Cell Biol 14(2):117-123.
    • (2012) Nat Cell Biol , vol.14 , Issue.2 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 7
    • 84855189423 scopus 로고    scopus 로고
    • Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF)
    • Zhao C, Smith EC, Whiteheart SW (2012) Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF). Biochim Biophys Acta 1823(1):159-171.
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 159-171
    • Zhao, C.1    Smith, E.C.2    Whiteheart, S.W.3
  • 8
    • 84905390155 scopus 로고    scopus 로고
    • Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine
    • Cordova JC, et al. (2014) Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine. Cell 158(3):647-658.
    • (2014) Cell , vol.158 , Issue.3 , pp. 647-658
    • Cordova, J.C.1
  • 9
    • 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
  • 10
    • 84876903053 scopus 로고    scopus 로고
    • Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine
    • Stinson BM, et al. (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell 153(3):628-639.
    • (2013) Cell , vol.153 , Issue.3 , pp. 628-639
    • Stinson, B.M.1
  • 11
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart SW, et al. (1994) N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J Cell Biol 126(4):945-954.
    • (1994) J Cell Biol , vol.126 , Issue.4 , pp. 945-954
    • Whiteheart, S.W.1
  • 12
    • 0037423187 scopus 로고    scopus 로고
    • ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
    • Song C, Wang Q, Li CC (2003) ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity. J Biol Chem 278(6):3648-3655.
    • (2003) J Biol Chem , vol.278 , Issue.6 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Li, C.C.3
  • 13
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH, Rapoport TA (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162(1):71-84.
    • (2003) J Cell Biol , vol.162 , Issue.1 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 14
    • 33646535590 scopus 로고    scopus 로고
    • Central pore residues mediate the p97/VCP activity required for ERAD
    • De La Barre B, Christianson JC, Kopito RR, Brunger AT (2006) Central pore residues mediate the p97/VCP activity required for ERAD. Mol Cell 22(4):451-462.
    • (2006) Mol Cell , vol.22 , Issue.4 , pp. 451-462
    • De La Barre, B.1    Christianson, J.C.2    Kopito, R.R.3    Brunger, A.T.4
  • 16
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines
    • Martin A, Baker TA, Sauer RT (2005) Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines. Nature 437(7062):1115-1120.
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 17
    • 84885428073 scopus 로고    scopus 로고
    • Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase
    • Beckwith R, Estrin E, Worden EJ, Martin A (2013) Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase. Nat Struct Mol Biol 20(10):1164-1172.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.10 , pp. 1164-1172
    • Beckwith, R.1    Estrin, E.2    Worden, E.J.3    Martin, A.4
  • 18
    • 69749089007 scopus 로고    scopus 로고
    • An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases
    • Augustin S, et al. (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35(5):574-585.
    • (2009) Mol Cell , vol.35 , Issue.5 , pp. 574-585
    • Augustin, S.1
  • 19
    • 42949164124 scopus 로고    scopus 로고
    • Improved structures of full-length p97, an AAA ATPase: Implications for mechanisms of nucleotide-dependent conformational change
    • Davies JM, Brunger AT, Weis WI (2008) Improved structures of full-length p97, an AAA ATPase: Implications for mechanisms of nucleotide-dependent conformational change. Structure 16(5):715-726.
    • (2008) Structure , vol.16 , Issue.5 , pp. 715-726
    • Davies, J.M.1    Brunger, A.T.2    Weis, W.I.3
  • 20
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • Lee S, et al. (2003) The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state. Cell 115(2):229-240.
    • (2003) Cell , vol.115 , Issue.2 , pp. 229-240
    • Lee, S.1
  • 21
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang F, et al. (2011) Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 471(7338):331-335.
    • (2011) Nature , vol.471 , Issue.7338 , pp. 331-335
    • Wang, F.1
  • 22
    • 84899854286 scopus 로고    scopus 로고
    • Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
    • Carroni M, et al. (2014) Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. eLife 3:e02481.
    • (2014) ELife , vol.3 , pp. e02481
    • Carroni, M.1
  • 23
    • 84862803840 scopus 로고    scopus 로고
    • Structural characterization of full-length NSF and 20S particles
    • Chang LF, et al. (2012) Structural characterization of full-length NSF and 20S particles. Nat Struct Mol Biol 19(3):268-275.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.3 , pp. 268-275
    • Chang, L.F.1
  • 24
    • 77952353727 scopus 로고    scopus 로고
    • CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
    • Lee S, Sielaff B, Lee J, Tsai FT (2010) CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci USA 107(18):8135-8140.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.18 , pp. 8135-8140
    • Lee, S.1    Sielaff, B.2    Lee, J.3    Tsai, F.T.4
  • 25
    • 84901044474 scopus 로고    scopus 로고
    • Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy
    • Yeung HO, et al. (2014) Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy. Open Biol 4:130142.
    • (2014) Open Biol , vol.4 , pp. 130142
    • Yeung, H.O.1
  • 26
    • 84923096947 scopus 로고    scopus 로고
    • Mechanistic insights into the recycling machine of the SNARE complex
    • Zhao M, et al. (2015) Mechanistic insights into the recycling machine of the SNARE complex. Nature 518(7537):61-67.
    • (2015) Nature , vol.518 , Issue.7537 , pp. 61-67
    • Zhao, M.1
  • 27
    • 84855198654 scopus 로고    scopus 로고
    • The AAA-type ATPases Pex1p and Pex6p and their role in peroxisomal matrix protein import in Saccharomyces cerevisiae
    • Grimm I, Saffian D, Platta HW, Erdmann R (2012) The AAA-type ATPases Pex1p and Pex6p and their role in peroxisomal matrix protein import in Saccharomyces cerevisiae. Biochim Biophys Acta 1823(1):150-158.
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 150-158
    • Grimm, I.1    Saffian, D.2    Platta, H.W.3    Erdmann, R.4
  • 28
    • 84865279926 scopus 로고    scopus 로고
    • Recent advances in peroxisomal matrix protein import
    • Liu X, Ma C, Subramani S (2012) Recent advances in peroxisomal matrix protein import. Curr Opin Cell Biol 24(4):484-489.
    • (2012) Curr Opin Cell Biol , vol.24 , Issue.4 , pp. 484-489
    • Liu, X.1    Ma, C.2    Subramani, S.3
  • 29
    • 0032555273 scopus 로고    scopus 로고
    • Disruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile Refsum disease
    • Geisbrecht BV, Collins CS, Reuber BE, Gould SJ (1998) Disruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile Refsum disease. Proc Natl Acad Sci USA 95(15):8630-8635.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.15 , pp. 8630-8635
    • Geisbrecht, B.V.1    Collins, C.S.2    Reuber, B.E.3    Gould, S.J.4
  • 30
    • 0030667274 scopus 로고    scopus 로고
    • Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
    • Reuber BE, et al. (1997) Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders. Nat Genet 17(4):445-448.
    • (1997) Nat Genet , vol.17 , Issue.4 , pp. 445-448
    • Reuber, B.E.1
  • 31
    • 84893398229 scopus 로고    scopus 로고
    • Peroxisome biogenesis disorders: Biological, clinical and pathophysiological perspectives
    • Braverman NE, D'Agostino MD, Maclean GE (2013) Peroxisome biogenesis disorders: Biological, clinical and pathophysiological perspectives. Dev Disabil Res Rev 17(3):187-196.
    • (2013) Dev Disabil Res Rev , vol.17 , Issue.3 , pp. 187-196
    • Braverman, N.E.1    D'Agostino, M.D.2    Maclean, G.E.3
  • 32
    • 0031930956 scopus 로고    scopus 로고
    • Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes
    • Faber KN, Heyman JA, Subramani S (1998) Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes. Mol Cell Biol 18(2):936-943.
    • (1998) Mol Cell Biol , vol.18 , Issue.2 , pp. 936-943
    • Faber, K.N.1    Heyman, J.A.2    Subramani, S.3
  • 33
    • 0034698778 scopus 로고    scopus 로고
    • Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p
    • Titorenko VI, Rachubinski RA (2000) Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p. J Cell Biol 150(4):881-886.
    • (2000) J Cell Biol , vol.150 , Issue.4 , pp. 881-886
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 34
    • 84859745968 scopus 로고    scopus 로고
    • Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes
    • Van Der Zand A, Gent J, Braakman I, Tabak HF (2012) Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell 149(2):397-409.
    • (2012) Cell , vol.149 , Issue.2 , pp. 397-409
    • Van Der Zand, A.1    Gent, J.2    Braakman, I.3    Tabak, H.F.4
  • 35
    • 78649403829 scopus 로고    scopus 로고
    • Peroxisomal protein import and ERAD: Variations on a common theme
    • Schliebs W, Girzalsky W, Erdmann R (2010) Peroxisomal protein import and ERAD: Variations on a common theme. Nat Rev Mol Cell Biol 11(12):885-890.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.12 , pp. 885-890
    • Schliebs, W.1    Girzalsky, W.2    Erdmann, R.3
  • 37
    • 84898729879 scopus 로고    scopus 로고
    • Cleaning up in the endoplasmic reticulum: Ubiquitin in charge
    • Christianson JC, Ye Y (2014) Cleaning up in the endoplasmic reticulum: Ubiquitin in charge. Nat Struct Mol Biol 21(4):325-335.
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.4 , pp. 325-335
    • Christianson, J.C.1    Ye, Y.2
  • 38
    • 84885431817 scopus 로고    scopus 로고
    • High-resolution comparative modeling with RosettaCM
    • Song Y, et al. (2013) High-resolution comparative modeling with RosettaCM. Structure 21(10):1735-1742.
    • (2013) Structure , vol.21 , Issue.10 , pp. 1735-1742
    • Song, Y.1
  • 39
    • 84863011784 scopus 로고    scopus 로고
    • Iterative stable alignment and clustering of 2D transmission electron microscope images
    • Yang Z, Fang J, Chittuluru J, Asturias FJ, Penczek PA (2012) Iterative stable alignment and clustering of 2D transmission electron microscope images. Structure 20(2):237-247.
    • (2012) Structure , vol.20 , Issue.2 , pp. 237-247
    • Yang, Z.1    Fang, J.2    Chittuluru, J.3    Asturias, F.J.4    Penczek, P.A.5
  • 40
    • 33845296470 scopus 로고    scopus 로고
    • SPARX, a new environment for Cryo-EM image processing
    • Hohn M, et al. (2007) SPARX, a new environment for Cryo-EM image processing. J Struct Biol 157(1):47-55.
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 47-55
    • Hohn, M.1
  • 41
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Söding J (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21(7):951-960.
    • (2005) Bioinformatics , vol.21 , Issue.7 , pp. 951-960
    • Söding, J.1
  • 42
    • 84926520440 scopus 로고    scopus 로고
    • Atomic accuracy models from 4.5 Å cryo-electron microscopy data with density-guided iterative local rebuilding and refinement
    • Di Maio F, et al. (2015) Atomic accuracy models from 4.5 Å cryo-electron microscopy data with density-guided iterative local rebuilding and refinement. Nat Methods 12(4):361-365.
    • (2015) Nat Methods , vol.12 , Issue.4 , pp. 361-365
    • Di Maio, F.1
  • 43
    • 9644279591 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain
    • Shiozawa K, et al. (2004) Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain. J Biol Chem 279(48):50060-50068.
    • (2004) J Biol Chem , vol.279 , Issue.48 , pp. 50060-50068
    • Shiozawa, K.1
  • 44
    • 84924192159 scopus 로고    scopus 로고
    • The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits
    • Gardner BM, Chowdhury S, Lander GC, Martin A (2015) The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. J Mol Biol 427(6 Pt B):1375-1388.
    • (2015) J Mol Biol , vol.427 , Issue.6 , pp. 1375-1388
    • Gardner, B.M.1    Chowdhury, S.2    Lander, G.C.3    Martin, A.4
  • 45
    • 77954957347 scopus 로고    scopus 로고
    • A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
    • Tang WK, et al. (2010) A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. EMBO J 29(13):2217-2229.
    • (2010) EMBO J , vol.29 , Issue.13 , pp. 2217-2229
    • Tang, W.K.1
  • 46
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu RC, Hanson PI, Jahn R, Brünger AT (1998) Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat Struct Biol 5(9):803-811.
    • (1998) Nat Struct Biol , vol.5 , Issue.9 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brünger, A.T.4
  • 47
    • 84864387306 scopus 로고    scopus 로고
    • ATP-dependent assembly of the heteromeric Pex1p-Pex6p-complex of the peroxisomal matrix protein import machinery
    • Saffian D, Grimm I, Girzalsky W, Erdmann R (2012) ATP-dependent assembly of the heteromeric Pex1p-Pex6p-complex of the peroxisomal matrix protein import machinery. J Struct Biol 179(2):126-132.
    • (2012) J Struct Biol , vol.179 , Issue.2 , pp. 126-132
    • Saffian, D.1    Grimm, I.2    Girzalsky, W.3    Erdmann, R.4
  • 48
    • 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
  • 49
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AG, Lutter R, Walker JE (1994) Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370(6491):621-628.
    • (1994) Nature , vol.370 , Issue.6491 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 50
    • 84910052449 scopus 로고    scopus 로고
    • Allosteric communication in the dynein motor domain
    • Bhabha G, et al. (2014) Allosteric communication in the dynein motor domain. Cell 159(4):857-868.
    • (2014) Cell , vol.159 , Issue.4 , pp. 857-868
    • Bhabha, G.1
  • 51
    • 11444254468 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p
    • Birschmann I, Rosenkranz K, Erdmann R, Kunau WH (2005) Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p. FEBS J 272(1):47-58.
    • (2005) FEBS J , vol.272 , Issue.1 , pp. 47-58
    • Birschmann, I.1    Rosenkranz, K.2    Erdmann, R.3    Kunau, W.H.4
  • 52
    • 0037632981 scopus 로고    scopus 로고
    • Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes
    • Birschmann I, et al. (2003) Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes. Mol Biol Cell 14(6):2226-2236.
    • (2003) Mol Biol Cell , vol.14 , Issue.6 , pp. 2226-2236
    • Birschmann, I.1
  • 53
    • 84890929831 scopus 로고    scopus 로고
    • Altered intersubunit communication is the molecular basis for functional defects of pathogenic p97 mutants
    • Tang WK, Xia D (2013) Altered intersubunit communication is the molecular basis for functional defects of pathogenic p97 mutants. J Biol Chem 288(51):36624-36635.
    • (2013) J Biol Chem , vol.288 , Issue.51 , pp. 36624-36635
    • Tang, W.K.1    Xia, D.2
  • 54
    • 79953855777 scopus 로고    scopus 로고
    • Structural comparison of F1-ATPase: Interplay among enzyme structures, catalysis, and rotations
    • Okazaki K, Takada S (2011) Structural comparison of F1-ATPase: Interplay among enzyme structures, catalysis, and rotations. Structure 19(4):588-598.
    • (2011) Structure , vol.19 , Issue.4 , pp. 588-598
    • Okazaki, K.1    Takada, S.2
  • 55
    • 14644415865 scopus 로고    scopus 로고
    • Nucleotide dependent motion and mechanism of action of p97/VCP
    • De La Barre B, Brunger AT (2005) Nucleotide dependent motion and mechanism of action of p97/VCP. J Mol Biol 347(2):437-452.
    • (2005) J Mol Biol , vol.347 , Issue.2 , pp. 437-452
    • De La Barre, B.1    Brunger, A.T.2
  • 56
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park S, Isaacson R, Kim HT, Silver PA, Wagner G (2005) Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13(7):995-1005.
    • (2005) Structure , vol.13 , Issue.7 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 57
    • 84929513816 scopus 로고    scopus 로고
    • Assembly principles of a unique cage formed by hexameric and decameric E. Coli proteins
    • Malet H, et al. (2014) Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. eLife 3:e03653.
    • (2014) ELife , vol.3 , pp. e03653
    • Malet, H.1
  • 58
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - Powerful tools in modern electron microscopy
    • Ohi M, Li Y, Cheng Y, Walz T (2004) Negative staining and image classification - powerful tools in modern electron microscopy. Biol Proc Online 6:23-34.
    • (2004) Biol Proc Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 59
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for highresolution single-particle reconstructions. J Struct Biol 128(1):82-97.
    • (1999) J Struct Biol , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 60
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116(1):190-199.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1
  • 61
    • 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
  • 62
    • 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
  • 63
    • 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
  • 64
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.