메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Volta phase plate cryo-EM of the small protein complex Prx3

Author keywords

[No Author keywords available]

Indexed keywords

PEROXIREDOXIN 3; MULTIPROTEIN COMPLEX; PRDX3 PROTEIN, HUMAN;

EID: 84961367858     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10534     Document Type: Article
Times cited : (53)

References (24)
  • 1
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson, R. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 28, 171-193 (1995).
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 2
    • 84897000286 scopus 로고    scopus 로고
    • Biochemistry. The resolution revolution
    • Kuhlbrandt, W. Biochemistry. The resolution revolution. Science 343, 1443-1444 (2014).
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kuhlbrandt, W.1
  • 3
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 4
    • 84941254172 scopus 로고    scopus 로고
    • An atomic structure of human g-secretase
    • Bai, X. C. et al. An atomic structure of human g-secretase. Nature 525, 212-217 (2015).
    • (2015) Nature , vol.525 , pp. 212-217
    • Bai, X.C.1
  • 5
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 Å resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor
    • Bartesaghi, A. et al. 2.2 Å resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science 348, 1147-1151 (2015).
    • (2015) Science , vol.348 , pp. 1147-1151
    • Bartesaghi, A.1
  • 6
    • 84928379119 scopus 로고    scopus 로고
    • A primer to single-particle cryo-electron microscopy
    • Cheng, Y., Grigorieff, N., Penczek, P. A. & Walz, T. A primer to single-particle cryo-electron microscopy. Cell 161, 438-449 (2015).
    • (2015) Cell , vol.161 , pp. 438-449
    • Cheng, Y.1    Grigorieff, N.2    Penczek, P.A.3    Walz, T.4
  • 7
    • 84859934600 scopus 로고    scopus 로고
    • Practical aspects of Boersch phase contrast electron microscopy of biological specimens
    • Walter, A. et al. Practical aspects of Boersch phase contrast electron microscopy of biological specimens. Ultramicroscopy 116, 62-72 (2012).
    • (2012) Ultramicroscopy , vol.116 , pp. 62-72
    • Walter, A.1
  • 8
    • 73449119968 scopus 로고    scopus 로고
    • Zernike phase plate cryoelectron microscopy facilitates single particle analysis of unstained asymmetric protein complexes
    • Chang, W. H. et al. Zernike phase plate cryoelectron microscopy facilitates single particle analysis of unstained asymmetric protein complexes. Structure 18, 17-27 (2010).
    • (2010) Structure , vol.18 , pp. 17-27
    • Chang, W.H.1
  • 9
    • 84914674933 scopus 로고    scopus 로고
    • Volta potential phase plate for in-focus phase contrast transmission electron microscopy
    • Danev, R., Buijsse, B., Khoshouei, M., Plitzko, J. M. & Baumeister, W. Volta potential phase plate for in-focus phase contrast transmission electron microscopy. Proc. Natl Acad. Sci. USA 111, 15635-15640 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 15635-15640
    • Danev, R.1    Buijsse, B.2    Khoshouei, M.3    Plitzko, J.M.4    Baumeister, W.5
  • 10
    • 84921752079 scopus 로고    scopus 로고
    • Proteasomes. A molecular census of 26S proteasomes in intact neurons
    • Asano, S. et al. Proteasomes. A molecular census of 26S proteasomes in intact neurons. Science 347, 439-442 (2015).
    • (2015) Science , vol.347 , pp. 439-442
    • Asano, S.1
  • 11
    • 84930189772 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone
    • Radjainia, M. et al. Cryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone. Structure 23, 912-920 (2015).
    • (2015) Structure , vol.23 , pp. 912-920
    • Radjainia, M.1
  • 12
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn, C. C. & Hampton, M. B. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 45, 549-561 (2008).
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 13
    • 84900418587 scopus 로고    scopus 로고
    • Peroxiredoxin is a versatile self-assembling tecton for protein nanotechnology
    • Phillips, A. J. et al. Peroxiredoxin is a versatile self-assembling tecton for protein nanotechnology. Biomacromolecules 15, 1871-1881 (2014).
    • (2014) Biomacromolecules , vol.15 , pp. 1871-1881
    • Phillips, A.J.1
  • 14
    • 27644443951 scopus 로고    scopus 로고
    • Bovine mitochondrial peroxiredoxin III forms a two-ring catenane
    • Cao, Z., Roszak, A. W., Gourlay, L. J., Lindsay, J. G. & Isaacs, N. W. Bovine mitochondrial peroxiredoxin III forms a two-ring catenane. Structure 13, 1661-1664 (2005).
    • (2005) Structure , vol.13 , pp. 1661-1664
    • Cao, Z.1    Roszak, A.W.2    Gourlay, L.J.3    Lindsay, J.G.4    Isaacs, N.W.5
  • 15
    • 0343953384 scopus 로고    scopus 로고
    • Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution
    • Schroder, E. et al. Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution. Structure 8, 605-615 (2000).
    • (2000) Structure , vol.8 , pp. 605-615
    • Schroder, E.1
  • 16
    • 77955481741 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions
    • Murata, K. et al. Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure 18, 903-912 (2010).
    • (2010) Structure , vol.18 , pp. 903-912
    • Murata, K.1
  • 17
    • 80052041441 scopus 로고    scopus 로고
    • Another 60 years in electron microscopy: Development of phase-plate electron microscopy and biological applications
    • Nagayama, K. Another 60 years in electron microscopy: development of phase-plate electron microscopy and biological applications. J. Electron. Microsc. (Tokyo). 60(Suppl 1): S43-S62 (2011).
    • (2011) J. Electron. Microsc. (Tokyo) , vol.60 , pp. S43-S62
    • Nagayama, K.1
  • 18
    • 84937217436 scopus 로고    scopus 로고
    • Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy
    • Liang, B. et al. Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy. Cell 162, 314-327 (2015).
    • (2015) Cell , vol.162 , pp. 314-327
    • Liang, B.1
  • 19
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 20
    • 84923447206 scopus 로고    scopus 로고
    • Alignment of direct detection device micrographs using a robust optical flow approach
    • Abrishami, V. et al. Alignment of direct detection device micrographs using a robust optical flow approach. J. Struct. Biol. 189, 163-176 (2015).
    • (2015) J. Struct. Biol. , vol.189 , pp. 163-176
    • Abrishami, V.1
  • 21
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 22
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • Scheres, S. H. A Bayesian view on cryo-EM structure determination. J. Mol. Biol. 415, 406-418 (2012).
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.1
  • 23
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard, T. D., Huang, C. C. & Ferrin, T. E. Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281-287 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 24
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.