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Volumn 165, Issue 7, 2016, Pages 1698-1707

Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE 1; LACTATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; POLYPEPTIDE; PYRUVIC ACID; TENIDAP; TETRAMER; AMINOQUINOLINE DERIVATIVE; GSK2837808A; SULFONAMIDE;

EID: 84969983828     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2016.05.040     Document Type: Article
Times cited : (400)

References (49)
  • 3
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human γ-secretase
    • X.C. Bai, E. Rajendra, G. Yang, Y. Shi, and S.H. Scheres Sampling the conformational space of the catalytic subunit of human γ-secretase eLife 4 2015 e11182
    • (2015) ELife , vol.4 , pp. e11182
    • Bai, X.C.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.5
  • 7
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
    • A. Bartesaghi, A. Merk, S. Banerjee, D. Matthies, X. Wu, J.L. Milne, and S. Subramaniam 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor Science 348 2015 1147 1151
    • (2015) Science , vol.348 , pp. 1147-1151
    • Bartesaghi, A.1    Merk, A.2    Banerjee, S.3    Matthies, D.4    Wu, X.5    Milne, J.L.6    Subramaniam, S.7
  • 8
    • 84991531381 scopus 로고    scopus 로고
    • Electron Microscopy and Image Processing: Essential Tools for Structural Analysis of Macromolecules
    • D.M. Belnap Electron Microscopy and Image Processing: Essential Tools for Structural Analysis of Macromolecules Curr. Protoc. Protein Sci. 82 2015 17.2.1 17.2.61
    • (2015) Curr. Protoc. Protein Sci. , vol.82 , pp. 1721-17261
    • Belnap, D.M.1
  • 11
    • 84928400353 scopus 로고    scopus 로고
    • Single-Particle Cryo-EM at Crystallographic Resolution
    • Y. Cheng Single-Particle Cryo-EM at Crystallographic Resolution Cell 161 2015 450 457
    • (2015) Cell , vol.161 , pp. 450-457
    • Cheng, Y.1
  • 12
    • 84968725663 scopus 로고    scopus 로고
    • Cryo-EM single particle analysis with the Volta phase plate
    • R. Danev, and W. Baumeister Cryo-EM single particle analysis with the Volta phase plate eLife 5 2016 e13046
    • (2016) ELife , vol.5 , pp. e13046
    • Danev, R.1    Baumeister, W.2
  • 15
    • 84920973012 scopus 로고    scopus 로고
    • Selective inhibition of mutant isocitrate dehydrogenase 1 (IDH1) via disruption of a metal binding network by an allosteric small molecule
    • G. Deng, J. Shen, M. Yin, J. McManus, M. Mathieu, P. Gee, T. He, C. Shi, O. Bedel, L.R. McLean, and et al. Selective inhibition of mutant isocitrate dehydrogenase 1 (IDH1) via disruption of a metal binding network by an allosteric small molecule J. Biol. Chem. 290 2015 762 774
    • (2015) J. Biol. Chem. , vol.290 , pp. 762-774
    • Deng, G.1    Shen, J.2    Yin, M.3    McManus, J.4    Mathieu, M.5    Gee, P.6    He, T.7    Shi, C.8    Bedel, O.9    McLean, L.R.10
  • 17
    • 84944273234 scopus 로고    scopus 로고
    • Glycine receptor mechanism elucidated by electron cryo-microscopy
    • J. Du, W. Lü, S. Wu, Y. Cheng, and E. Gouaux Glycine receptor mechanism elucidated by electron cryo-microscopy Nature 526 2015 224 229
    • (2015) Nature , vol.526 , pp. 224-229
    • Du, J.1    Lü, W.2    Wu, S.3    Cheng, Y.4    Gouaux, E.5
  • 19
    • 84928560614 scopus 로고    scopus 로고
    • Structure of the E. Coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
    • N. Fischer, P. Neumann, A.L. Konevega, L.V. Bock, R. Ficner, M.V. Rodnina, and H. Stark Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM Nature 520 2015 567 570
    • (2015) Nature , vol.520 , pp. 567-570
    • Fischer, N.1    Neumann, P.2    Konevega, A.L.3    Bock, L.V.4    Ficner, R.5    Rodnina, M.V.6    Stark, H.7
  • 20
    • 84896995569 scopus 로고    scopus 로고
    • Inhibition of lactate dehydrogenase activity as an approach to cancer therapy
    • L. Fiume, M. Manerba, M. Vettraino, and G. Di Stefano Inhibition of lactate dehydrogenase activity as an approach to cancer therapy Future Med. Chem. 6 2014 429 445
    • (2014) Future Med. Chem. , vol.6 , pp. 429-445
    • Fiume, L.1    Manerba, M.2    Vettraino, M.3    Di Stefano, G.4
  • 21
    • 79959347866 scopus 로고    scopus 로고
    • Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches
    • P. Ge, and Z.H. Zhou Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches Proc. Natl. Acad. Sci. USA 108 2011 9637 9642
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9637-9642
    • Ge, P.1    Zhou, Z.H.2
  • 22
    • 79959668319 scopus 로고    scopus 로고
    • Reaching the information limit in cryo-EM of biological macromolecules: Experimental aspects
    • R.M. Glaeser, and R.J. Hall Reaching the information limit in cryo-EM of biological macromolecules: experimental aspects Biophys. J. 100 2011 2331 2337
    • (2011) Biophys. J. , vol.100 , pp. 2331-2337
    • Glaeser, R.M.1    Hall, R.J.2
  • 23
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • R. Henderson The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules Q. Rev. Biophys. 28 1995 171 193
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 24
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, and K.H. Downing Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy J. Mol. Biol. 213 1990 899 929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 26
    • 84955516320 scopus 로고    scopus 로고
    • Structures of the E. Coli translating ribosome with SRP and its receptor and with the translocon
    • A. Jomaa, D. Boehringer, M. Leibundgut, and N. Ban Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon Nat. Commun. 7 2016 10471
    • (2016) Nat. Commun. , vol.7 , pp. 10471
    • Jomaa, A.1    Boehringer, D.2    Leibundgut, M.3    Ban, N.4
  • 28
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • M. Liao, E. Cao, D. Julius, and Y. Cheng Structure of the TRPV1 ion channel determined by electron cryo-microscopy Nature 504 2013 107 112
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 29
  • 34
    • 84908056429 scopus 로고    scopus 로고
    • Comparison of optimal performance at 300keV of three direct electron detectors for use in low dose electron microscopy
    • G. McMullan, A.R. Faruqi, D. Clare, and R. Henderson Comparison of optimal performance at 300keV of three direct electron detectors for use in low dose electron microscopy Ultramicroscopy 147 2014 156 163
    • (2014) Ultramicroscopy , vol.147 , pp. 156-163
    • McMullan, G.1    Faruqi, A.R.2    Clare, D.3    Henderson, R.4
  • 37
    • 0037468573 scopus 로고    scopus 로고
    • Expression profile of genes from 12p in testicular germ cell tumors of adolescents and adults associated with i(12p) and amplification at 12p11.2-p12.1
    • S. Rodriguez, O. Jafer, H. Goker, B.M. Summersgill, G. Zafarana, A.J. Gillis, R.J. van Gurp, J.W. Oosterhuis, Y.J. Lu, R. Huddart, and et al. Expression profile of genes from 12p in testicular germ cell tumors of adolescents and adults associated with i(12p) and amplification at 12p11.2-p12.1 Oncogene 22 2003 1880 1891
    • (2003) Oncogene , vol.22 , pp. 1880-1891
    • Rodriguez, S.1    Jafer, O.2    Goker, H.3    Summersgill, B.M.4    Zafarana, G.5    Gillis, A.J.6    Van Gurp, R.J.7    Oosterhuis, J.W.8    Lu, Y.J.9    Huddart, R.10
  • 39
    • 84975197728 scopus 로고    scopus 로고
    • Single-particle cryo-electron microscopy of macromolecular complexes
    • G. Skiniotis, and D.R. Southworth Single-particle cryo-electron microscopy of macromolecular complexes Microscopy (Oxf.) 65 2016 9 22
    • (2016) Microscopy (Oxf.) , vol.65 , pp. 9-22
    • Skiniotis, G.1    Southworth, D.R.2
  • 40
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • T.J. Smith, T. Schmidt, J. Fang, J. Wu, G. Siuzdak, and C.A. Stanley The structure of apo human glutamate dehydrogenase details subunit communication and allostery J. Mol. Biol. 318 2002 765 777
    • (2002) J. Mol. Biol. , vol.318 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 41
    • 84961135724 scopus 로고    scopus 로고
    • An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology
    • R.F. Thompson, M. Walker, C.A. Siebert, S.P. Muench, and N.A. Ranson An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology Methods 100 2016 3 15
    • (2016) Methods , vol.100 , pp. 3-15
    • Thompson, R.F.1    Walker, M.2    Siebert, C.A.3    Muench, S.P.4    Ranson, N.A.5
  • 44
    • 84941578432 scopus 로고    scopus 로고
    • Inhibition of Cancer-Associated Mutant Isocitrate Dehydrogenases by 2-Thiohydantoin Compounds
    • F. Wu, H. Jiang, B. Zheng, M. Kogiso, Y. Yao, C. Zhou, X.N. Li, and Y. Song Inhibition of Cancer-Associated Mutant Isocitrate Dehydrogenases by 2-Thiohydantoin Compounds J. Med. Chem. 58 2015 6899 6908
    • (2015) J. Med. Chem. , vol.58 , pp. 6899-6908
    • Wu, F.1    Jiang, H.2    Zheng, B.3    Kogiso, M.4    Yao, Y.5    Zhou, C.6    Li, X.N.7    Song, Y.8
  • 45
    • 4043105583 scopus 로고    scopus 로고
    • Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
    • X. Xu, J. Zhao, Z. Xu, B. Peng, Q. Huang, E. Arnold, and J. Ding Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity J. Biol. Chem. 279 2004 33946 33957
    • (2004) J. Biol. Chem. , vol.279 , pp. 33946-33957
    • Xu, X.1    Zhao, J.2    Xu, Z.3    Peng, B.4    Huang, Q.5    Arnold, E.6    Ding, J.7
  • 46
    • 78049480082 scopus 로고    scopus 로고
    • Molecular mechanisms of "off-on switch" of activities of human IDH1 by tumor-associated mutation R132H
    • B. Yang, C. Zhong, Y. Peng, Z. Lai, and J. Ding Molecular mechanisms of "off-on switch" of activities of human IDH1 by tumor-associated mutation R132H Cell Res. 20 2010 1188 1200
    • (2010) Cell Res. , vol.20 , pp. 1188-1200
    • Yang, B.1    Zhong, C.2    Peng, Y.3    Lai, Z.4    Ding, J.5
  • 47
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • X. Yu, L. Jin, and Z.H. Zhou 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy Nature 453 2008 415 419
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 48
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • X. Zhang, L. Jin, Q. Fang, W.H. Hui, and Z.H. Zhou 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry Cell 141 2010 472 482
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5


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