메뉴 건너뛰기




Volumn 159, Issue 5, 2014, Pages 995-1014

A glimpse of structural biology through X-ray crystallography

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BCR ABL PROTEIN; CARRIER PROTEIN; CYCLIC AMP; CYCLIN DEPENDENT KINASE; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN; PROTEIN KINASE; PROTEIN;

EID: 84911481951     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.10.051     Document Type: Review
Times cited : (242)

References (225)
  • 2
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • J.P. Abrahams, A.G. Leslie, R. Lutter, and J.E. Walker Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 4
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution
    • R. Acharya, E. Fry, D. Stuart, G. Fox, D. Rowlands, and F. Brown The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution Nature 337 1989 709 716
    • (1989) Nature , vol.337 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 6
    • 84934442553 scopus 로고    scopus 로고
    • Crystallization of membrane proteins in bicelles
    • S. Agah, and S. Faham Crystallization of membrane proteins in bicelles Methods Mol. Biol. 914 2012 3 16
    • (2012) Methods Mol. Biol. , vol.914 , pp. 3-16
    • Agah, S.1    Faham, S.2
  • 7
    • 0024284650 scopus 로고
    • Recognition of a DNA operator by the repressor of phage 434: A view at high resolution
    • A.K. Aggarwal, D.W. Rodgers, M. Drottar, M. Ptashne, and S.C. Harrison Recognition of a DNA operator by the repressor of phage 434: a view at high resolution Science 242 1988 899 907
    • (1988) Science , vol.242 , pp. 899-907
    • Aggarwal, A.K.1    Rodgers, D.W.2    Drottar, M.3    Ptashne, M.4    Harrison, S.C.5
  • 9
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • J.P. Allen, G. Feher, T.O. Yeates, H. Komiya, and D.C. Rees Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits Proc. Natl. Acad. Sci. USA 84 1987 6162 6166
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 11
    • 0023202898 scopus 로고
    • Structure of the repressor-operator complex of bacteriophage 434
    • J.E. Anderson, M. Ptashne, and S.C. Harrison Structure of the repressor-operator complex of bacteriophage 434 Nature 326 1987 846 852
    • (1987) Nature , vol.326 , pp. 846-852
    • Anderson, J.E.1    Ptashne, M.2    Harrison, S.C.3
  • 13
    • 84879130126 scopus 로고    scopus 로고
    • Advances in recombinant protein expression for use in pharmaceutical research
    • R. Assenberg, P.T. Wan, S. Geisse, and L.M. Mayr Advances in recombinant protein expression for use in pharmaceutical research Curr. Opin. Struct. Biol. 23 2013 393 402
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 393-402
    • Assenberg, R.1    Wan, P.T.2    Geisse, S.3    Mayr, L.M.4
  • 15
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 A resolution Science 289 2000 905 920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 16
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation
    • D.W. Banner, A. D'Arcy, W. Janes, R. Gentz, H.J. Schoenfeld, C. Broger, H. Loetscher, and W. Lesslauer Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation Cell 73 1993 431 445
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5    Broger, C.6    Loetscher, H.7    Lesslauer, W.8
  • 18
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • R.B. Bass, P. Strop, M. Barclay, and D.C. Rees Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel Science 298 2002 1582 1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 20
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • A. Ben-Shem, D. Fass, and E. Bibi Structural basis for intramembrane proteolysis by rhomboid serine proteases Proc. Natl. Acad. Sci. USA 104 2007 462 466
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 21
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution
    • C.C. Blake, D.F. Koenig, G.A. Mair, A.C. North, D.C. Phillips, and V.R. Sarma Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution Nature 206 1965 757 761
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.4    Phillips, D.C.5    Sarma, V.R.6
  • 22
    • 0018223550 scopus 로고
    • Protein disk of tobacco mosaic virus at 2.8 A resolution showing the interactions within and between subunits
    • A.C. Bloomer, J.N. Champness, G. Bricogne, R. Staden, and A. Klug Protein disk of tobacco mosaic virus at 2.8 A resolution showing the interactions within and between subunits Nature 276 1978 362 368
    • (1978) Nature , vol.276 , pp. 362-368
    • Bloomer, A.C.1    Champness, J.N.2    Bricogne, G.3    Staden, R.4    Klug, A.5
  • 23
    • 0034661856 scopus 로고    scopus 로고
    • Screening for phasing atoms in protein crystallography
    • T.J. Boggon, and L. Shapiro Screening for phasing atoms in protein crystallography Structure 8 2000 R143 R149
    • (2000) Structure , vol.8 , pp. 143-R149
    • Boggon, T.J.1    Shapiro, L.2
  • 24
    • 70350336247 scopus 로고    scopus 로고
    • The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation
    • F. Bonneau, J. Basquin, J. Ebert, E. Lorentzen, and E. Conti The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation Cell 139 2009 547 559
    • (2009) Cell , vol.139 , pp. 547-559
    • Bonneau, F.1    Basquin, J.2    Ebert, J.3    Lorentzen, E.4    Conti, E.5
  • 25
    • 34250333069 scopus 로고    scopus 로고
    • Selectivity in K+ channels is due to topological control of the permeant ion's coordinated state
    • D.L. Bostick, and C.L. Brooks 3rd Selectivity in K+ channels is due to topological control of the permeant ion's coordinated state Proc. Natl. Acad. Sci. USA 104 2007 9260 9265
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9260-9265
    • Bostick, D.L.1    Brooks, C.L.2
  • 29
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • M.S. Brown, J. Ye, R.B. Rawson, and J.L. Goldstein Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans Cell 100 2000 391 398
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 31
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brünger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 34
    • 66049128793 scopus 로고    scopus 로고
    • Crystallizing membrane proteins for structure determination: Use of lipidic mesophases
    • M. Caffrey Crystallizing membrane proteins for structure determination: use of lipidic mesophases Annu. Rev. Biophys. 38 2009 29 51
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 29-51
    • Caffrey, M.1
  • 35
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • G. Chang, R.H. Spencer, A.T. Lee, M.T. Barclay, and D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel Science 282 1998 2220 2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 37
    • 84880511070 scopus 로고    scopus 로고
    • Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography
    • S. Chen, M.L. Oldham, A.L. Davidson, and J. Chen Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography Nature 499 2013 364 368
    • (2013) Nature , vol.499 , pp. 364-368
    • Chen, S.1    Oldham, M.L.2    Davidson, A.L.3    Chen, J.4
  • 38
    • 84907261039 scopus 로고    scopus 로고
    • X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism
    • L. Chen, K.L. Duerr, and E. Gouaux X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism Science 345 2014 1021 1026
    • (2014) Science , vol.345 , pp. 1021-1026
    • Chen, L.1    Duerr, K.L.2    Gouaux, E.3
  • 40
    • 78049502261 scopus 로고    scopus 로고
    • Recent progress in the structure determination of GPCRs, a membrane protein family with high potential as pharmaceutical targets
    • V. Cherezov, E. Abola, and R.C. Stevens Recent progress in the structure determination of GPCRs, a membrane protein family with high potential as pharmaceutical targets Methods Mol. Biol. 654 2010 141 168
    • (2010) Methods Mol. Biol. , vol.654 , pp. 141-168
    • Cherezov, V.1    Abola, E.2    Stevens, R.C.3
  • 41
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • H.S. Cho, K. Mason, K.X. Ramyar, A.M. Stanley, S.B. Gabelli, D.W. Denney Jr., and D.J. Leahy Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab Nature 421 2003 756 760
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney, D.W.6    Leahy, D.J.7
  • 42
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • C.P. Collaborative Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
    • Collaborative, C.P.1
  • 43
    • 84911474456 scopus 로고    scopus 로고
    • A tale of chromatin and transcription in 100 structures
    • this issue
    • P. Cramer A tale of chromatin and transcription in 100 structures Cell 159 2014 985 994 this issue
    • (2014) Cell , vol.159 , pp. 985-994
    • Cramer, P.1
  • 44
    • 77958010505 scopus 로고    scopus 로고
    • Structure of a fucose transporter in an outward-open conformation
    • S. Dang, L. Sun, Y. Huang, F. Lu, Y. Liu, H. Gong, J. Wang, and N. Yan Structure of a fucose transporter in an outward-open conformation Nature 467 2010 734 738
    • (2010) Nature , vol.467 , pp. 734-738
    • Dang, S.1    Sun, L.2    Huang, Y.3    Lu, F.4    Liu, Y.5    Gong, H.6    Wang, J.7    Yan, N.8
  • 45
    • 27744544953 scopus 로고    scopus 로고
    • Use of polynuclear metal clusters in protein crystallography
    • Z. Dauter Use of polynuclear metal clusters in protein crystallography C. R. Chim. 8 2005 1808 1814
    • (2005) C. R. Chim. , vol.8 , pp. 1808-1814
    • Dauter, Z.1
  • 46
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • R.J. Dawson, and K.P. Locher Structure of a bacterial multidrug ABC transporter Nature 443 2006 180 185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 48
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • A.M. de Vos, M. Ultsch, and A.A. Kossiakoff Human growth hormone and extracellular domain of its receptor: crystal structure of the complex Science 255 1992 306 312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 49
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber, and H. Michel Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution Nature 318 1985 618 624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 50
    • 84902002905 scopus 로고    scopus 로고
    • Crystal structure of the human glucose transporter GLUT1
    • D. Deng, C. Xu, P. Sun, J. Wu, C. Yan, M. Hu, and N. Yan Crystal structure of the human glucose transporter GLUT1 Nature 510 2014 121 125
    • (2014) Nature , vol.510 , pp. 121-125
    • Deng, D.1    Xu, C.2    Sun, P.3    Wu, J.4    Yan, C.5    Hu, M.6    Yan, N.7
  • 51
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • D.A. Doyle, A. Lee, J. Lewis, E. Kim, M. Sheng, and R. MacKinnon Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ Cell 85 1996 1067 1076
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    Mackinnon, R.6
  • 56
  • 58
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • L. Feng, H. Yan, Z. Wu, N. Yan, Z. Wang, P.D. Jeffrey, and Y. Shi Structure of a site-2 protease family intramembrane metalloprotease Science 318 2007 1608 1612
    • (2007) Science , vol.318 , pp. 1608-1612
    • Feng, L.1    Yan, H.2    Wu, Z.3    Yan, N.4    Wang, Z.5    Jeffrey, P.D.6    Shi, Y.7
  • 59
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • K.M. Ferguson, M.A. Lemmon, J. Schlessinger, and P.B. Sigler Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain Cell 83 1995 1037 1046
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 61
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • E.H. Fischer, and E.G. Krebs Conversion of phosphorylase b to phosphorylase a in muscle extracts J. Biol. Chem. 216 1955 121 132
    • (1955) J. Biol. Chem. , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 64
  • 65
    • 76749095057 scopus 로고    scopus 로고
    • Mechanism of substrate recognition and transport by an amino acid antiporter
    • X. Gao, L. Zhou, X. Jiao, F. Lu, C. Yan, X. Zeng, J. Wang, and Y. Shi Mechanism of substrate recognition and transport by an amino acid antiporter Nature 463 2010 828 832
    • (2010) Nature , vol.463 , pp. 828-832
    • Gao, X.1    Zhou, L.2    Jiao, X.3    Lu, F.4    Yan, C.5    Zeng, X.6    Wang, J.7    Shi, Y.8
  • 66
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • D.N. Garboczi, P. Ghosh, U. Utz, Q.R. Fan, W.E. Biddison, and D.C. Wiley Structure of the complex between human T-cell receptor, viral peptide and HLA-A2 Nature 384 1996 134 141
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 69
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • S. Gerber, M. Comellas-Bigler, B.A. Goetz, and K.P. Locher Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter Science 321 2008 246 250
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 73
    • 0014693815 scopus 로고
    • Structure of tomato bushy stunt virus. I. The spherically averaged electron density
    • S.C. Harrison Structure of tomato bushy stunt virus. I. The spherically averaged electron density J. Mol. Biol. 42 1969 457 483
    • (1969) J. Mol. Biol. , vol.42 , pp. 457-483
    • Harrison, S.C.1
  • 74
    • 0016772446 scopus 로고
    • Structure of tomato bushy stunt virus. Three-dimensional x-ray diffraction analysis at 16 A resolution
    • S.C. Harrison, and A. Jack Structure of tomato bushy stunt virus. Three-dimensional x-ray diffraction analysis at 16 A resolution J. Mol. Biol. 97 1975 173 191
    • (1975) J. Mol. Biol. , vol.97 , pp. 173-191
    • Harrison, S.C.1    Jack, A.2
  • 77
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Y. Huang, M.J. Lemieux, J. Song, M. Auer, and D.N. Wang Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli Science 301 2003 616 620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 78
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • R.N. Hvorup, B.A. Goetz, M. Niederer, K. Hollenstein, E. Perozo, and K.P. Locher Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF Science 317 2007 1387 1390
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 79
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • O. Jardetzky Simple allosteric model for membrane pumps Nature 211 1966 969 970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 81
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Y. Jiang, A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon Crystal structure and mechanism of a calcium-gated potassium channel Nature 417 2002 515 522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    Mackinnon, R.6
  • 82
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K+ channel
    • Y. Jiang, V. Ruta, J. Chen, A. Lee, and R. MacKinnon The principle of gating charge movement in a voltage-dependent K+ channel Nature 423 2003 42 48
    • (2003) Nature , vol.423 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    Mackinnon, R.5
  • 83
    • 70349901077 scopus 로고    scopus 로고
    • High-throughput crystallography for structural genomics
    • A. Joachimiak High-throughput crystallography for structural genomics Curr. Opin. Struct. Biol. 19 2009 573 584
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 573-584
    • Joachimiak, A.1
  • 84
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 85
    • 20444419395 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease
    • H.R. Kaback Structure and mechanism of the lactose permease C. R. Biol. 328 2005 557 567
    • (2005) C. R. Biol. , vol.328 , pp. 557-567
    • Kaback, H.R.1
  • 86
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. Coli methionine ABC transporter: Structure and allosteric regulation
    • N.S. Kadaba, J.T. Kaiser, E. Johnson, A. Lee, and D.C. Rees The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation Science 321 2008 250 253
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 87
    • 84901640125 scopus 로고    scopus 로고
    • Crystal structure of a heterotetrameric NMDA receptor ion channel
    • E. Karakas, and H. Furukawa Crystal structure of a heterotetrameric NMDA receptor ion channel Science 344 2014 992 997
    • (2014) Science , vol.344 , pp. 992-997
    • Karakas, E.1    Furukawa, H.2
  • 88
    • 0014192404 scopus 로고
    • Tertiary structure of ribonuclease
    • G. Kartha, J. Bello, and D. Harker Tertiary structure of ribonuclease Nature 213 1967 862 865
    • (1967) Nature , vol.213 , pp. 862-865
    • Kartha, G.1    Bello, J.2    Harker, D.3
  • 89
  • 92
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • D. Khare, M.L. Oldham, C. Orelle, A.L. Davidson, and J. Chen Alternating access in maltose transporter mediated by rigid-body rotations Mol. Cell 33 2009 528 536
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 93
    • 13244291292 scopus 로고    scopus 로고
    • Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA
    • C. Kim, N.H. Xuong, and S.S. Taylor Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA Science 307 2005 690 696
    • (2005) Science , vol.307 , pp. 690-696
    • Kim, C.1    Xuong, N.H.2    Taylor, S.S.3
  • 94
    • 33646755415 scopus 로고    scopus 로고
    • Allosteric action in real time: Time-resolved crystallographic studies of a cooperative dimeric hemoglobin
    • J.E. Knapp, R. Pahl, V. Srajer, and W.E. Royer Jr. Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin Proc. Natl. Acad. Sci. USA 103 2006 7649 7654
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7649-7654
    • Knapp, J.E.1    Pahl, R.2    Srajer, V.3    Royer, W.E.4
  • 96
    • 0003083826 scopus 로고
    • CDNA for the human beta 2-adrenergic receptor: A protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor
    • B.K. Kobilka, R.A. Dixon, T. Frielle, H.G. Dohlman, M.A. Bolanowski, I.S. Sigal, T.L. Yang-Feng, U. Francke, M.G. Caron, and R.J. Lefkowitz cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor Proc. Natl. Acad. Sci. USA 84 1987 46 50
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 46-50
    • Kobilka, B.K.1    Dixon, R.A.2    Frielle, T.3    Dohlman, H.G.4    Bolanowski, M.A.5    Sigal, I.S.6    Yang-Feng, T.L.7    Francke, U.8    Caron, M.G.9    Lefkowitz, R.J.10
  • 98
    • 0023889603 scopus 로고
    • Chimeric alpha 2-,beta 2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity
    • B.K. Kobilka, T.S. Kobilka, K. Daniel, J.W. Regan, M.G. Caron, and R.J. Lefkowitz Chimeric alpha 2-,beta 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity Science 240 1988 1310 1316
    • (1988) Science , vol.240 , pp. 1310-1316
    • Kobilka, B.K.1    Kobilka, T.S.2    Daniel, K.3    Regan, J.W.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 100
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • W. Kühlbrandt, D.N. Wang, and Y. Fujiyoshi Atomic model of plant light-harvesting complex by electron crystallography Nature 367 1994 614 621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 101
    • 84904199124 scopus 로고    scopus 로고
    • NMDA receptor structures reveal subunit arrangement and pore architecture
    • C.H. Lee, W. Lü, J.C. Michel, A. Goehring, J. Du, X. Song, and E. Gouaux NMDA receptor structures reveal subunit arrangement and pore architecture Nature 511 2014 191 197
    • (2014) Nature , vol.511 , pp. 191-197
    • Lee, C.H.1    Lü, W.2    Michel, J.C.3    Goehring, A.4    Du, J.5    Song, X.6    Gouaux, E.7
  • 102
    • 33846543356 scopus 로고    scopus 로고
    • The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
    • M.J. Lemieux, S.J. Fischer, M.M. Cherney, K.S. Bateman, and M.N. James The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis Proc. Natl. Acad. Sci. USA 104 2007 750 754
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 750-754
    • Lemieux, M.J.1    Fischer, S.J.2    Cherney, M.M.3    Bateman, K.S.4    James, M.N.5
  • 103
    • 79957601559 scopus 로고    scopus 로고
    • Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis
    • A.K. Leung, K. Nagai, and J. Li Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis Nature 473 2011 536 539
    • (2011) Nature , vol.473 , pp. 536-539
    • Leung, A.K.1    Nagai, K.2    Li, J.3
  • 104
  • 105
    • 84871725890 scopus 로고    scopus 로고
    • Structure of a presenilin family intramembrane aspartate protease
    • X. Li, S. Dang, C. Yan, X. Gong, J. Wang, and Y. Shi Structure of a presenilin family intramembrane aspartate protease Nature 493 2013 56 61
    • (2013) Nature , vol.493 , pp. 56-61
    • Li, X.1    Dang, S.2    Yan, C.3    Gong, X.4    Wang, J.5    Shi, Y.6
  • 106
    • 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
  • 109
    • 0014569166 scopus 로고
    • The structure of carboxypeptidase A. IX. The x-ray diffraction results in the light of the chemical sequence
    • W.N. Lipscomb, J.A. Hartsuck, F.A. Quiocho, and G.N. Reeke Jr. The structure of carboxypeptidase A. IX. The x-ray diffraction results in the light of the chemical sequence Proc. Natl. Acad. Sci. USA 64 1969 28 35
    • (1969) Proc. Natl. Acad. Sci. USA , vol.64 , pp. 28-35
    • Lipscomb, W.N.1    Hartsuck, J.A.2    Quiocho, F.A.3    Reeke, G.N.4
  • 110
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Q. Liu, J.C. Greimann, and C.D. Lima Reconstitution, activities, and structure of the eukaryotic RNA exosome Cell 127 2006 1223 1237
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 112
    • 0037052565 scopus 로고    scopus 로고
    • The E. Coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • K.P. Locher, A.T. Lee, and D.C. Rees The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism Science 296 2002 1091 1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 113
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • S.B. Long, E.B. Campbell, and R. Mackinnon Crystal structure of a mammalian voltage-dependent Shaker family K+ channel Science 309 2005 897 903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 114
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. Acidophilum at 3.4 A resolution
    • J. Löwe, D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution Science 268 1995 533 539
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 116
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • K. Luger, A.W. Mäder, R.K. Richmond, D.F. Sargent, and T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 A resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 119
    • 84862819559 scopus 로고    scopus 로고
    • Structure and mechanism of a glutamate-GABA antiporter
    • D. Ma, P. Lu, C. Yan, C. Fan, P. Yin, J. Wang, and Y. Shi Structure and mechanism of a glutamate-GABA antiporter Nature 483 2012 632 636
    • (2012) Nature , vol.483 , pp. 632-636
    • Ma, D.1    Lu, P.2    Yan, C.3    Fan, C.4    Yin, P.5    Wang, J.6    Shi, Y.7
  • 120
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • R. MacKinnon Potassium channels FEBS Lett. 555 2003 62 65
    • (2003) FEBS Lett. , vol.555 , pp. 62-65
    • Mackinnon, R.1
  • 121
    • 84874742223 scopus 로고    scopus 로고
    • Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex
    • D.L. Makino, M. Baumgärtner, and E. Conti Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex Nature 495 2013 70 75
    • (2013) Nature , vol.495 , pp. 70-75
    • Makino, D.L.1    Baumgärtner, M.2    Conti, E.3
  • 122
    • 0346436100 scopus 로고
    • The three dimensional structure of the lysozyme from bacteriophage T4
    • B.W. Matthews, and S.J. Remington The three dimensional structure of the lysozyme from bacteriophage T4 Proc. Natl. Acad. Sci. USA 71 1974 4178 4182
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4178-4182
    • Matthews, B.W.1    Remington, S.J.2
  • 123
    • 0014201592 scopus 로고
    • Three-dimensional structure of tosyl-alpha-chymotrypsin
    • B.W. Matthews, P.B. Sigler, R. Henderson, and D.M. Blow Three-dimensional structure of tosyl-alpha-chymotrypsin Nature 214 1967 652 656
    • (1967) Nature , vol.214 , pp. 652-656
    • Matthews, B.W.1    Sigler, P.B.2    Henderson, R.3    Blow, D.M.4
  • 126
    • 0035499447 scopus 로고    scopus 로고
    • Energetic optimization of ion conduction rate by the K+ selectivity filter
    • J.H. Morais-Cabral, Y. Zhou, and R. MacKinnon Energetic optimization of ion conduction rate by the K+ selectivity filter Nature 414 2001 37 42
    • (2001) Nature , vol.414 , pp. 37-42
    • Morais-Cabral, J.H.1    Zhou, Y.2    Mackinnon, R.3
  • 129
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • A. Musacchio, M. Saraste, and M. Wilmanns High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides Nat. Struct. Biol. 1 1994 546 551
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 130
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • B. Nagar, W.G. Bornmann, P. Pellicena, T. Schindler, D.R. Veach, W.T. Miller, B. Clarkson, and J. Kuriyan Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571) Cancer Res. 62 2002 4236 4243
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 131
    • 84867743209 scopus 로고    scopus 로고
    • Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges
    • R. Neutze, and K. Moffat Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges Curr. Opin. Struct. Biol. 22 2012 651 659
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 651-659
    • Neutze, R.1    Moffat, K.2
  • 132
    • 0034680144 scopus 로고    scopus 로고
    • Potential for biomolecular imaging with femtosecond X-ray pulses
    • R. Neutze, R. Wouts, D. van der Spoel, E. Weckert, and J. Hajdu Potential for biomolecular imaging with femtosecond X-ray pulses Nature 406 2000 752 757
    • (2000) Nature , vol.406 , pp. 752-757
    • Neutze, R.1    Wouts, R.2    Van Der Spoel, D.3    Weckert, E.4    Hajdu, J.5
  • 134
    • 7244251461 scopus 로고    scopus 로고
    • Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands
    • S.Y. Noskov, S. Bernèche, and B. Roux Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands Nature 431 2004 830 834
    • (2004) Nature , vol.431 , pp. 830-834
    • Noskov, S.Y.1    Bernèche, S.2    Roux, B.3
  • 136
    • 79957932347 scopus 로고    scopus 로고
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state
    • M.L. Oldham, and J. Chen Crystal structure of the maltose transporter in a pretranslocation intermediate state Science 332 2011 1202 1205
    • (2011) Science , vol.332 , pp. 1202-1205
    • Oldham, M.L.1    Chen, J.2
  • 137
    • 80053091327 scopus 로고    scopus 로고
    • Snapshots of the maltose transporter during ATP hydrolysis
    • M.L. Oldham, and J. Chen Snapshots of the maltose transporter during ATP hydrolysis Proc. Natl. Acad. Sci. USA 108 2011 15152 15156
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 15152-15156
    • Oldham, M.L.1    Chen, J.2
  • 138
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • M.L. Oldham, D. Khare, F.A. Quiocho, A.L. Davidson, and J. Chen Crystal structure of a catalytic intermediate of the maltose transporter Nature 450 2007 515 521
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 139
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • C. Olesen, T.L. Sørensen, R.C. Nielsen, J.V. Møller, and P. Nissen Dephosphorylation of the calcium pump coupled to counterion occlusion Science 306 2004 2251 2255
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sørensen, T.L.2    Nielsen, R.C.3    Møller, J.V.4    Nissen, P.5
  • 144
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • N.S. Pannu, and R.J. Read Improved structure refinement through maximum likelihood Acta Crystallogr. A 52 1996 659 668
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 145
    • 0004792589 scopus 로고
    • Atomic coordinates and structure factors for two helical configurations of polypeptide chains
    • L. Pauling, and R.B. Corey Atomic coordinates and structure factors for two helical configurations of polypeptide chains Proc. Natl. Acad. Sci. USA 37 1951 235 240
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 235-240
    • Pauling, L.1    Corey, R.B.2
  • 146
    • 0001444341 scopus 로고
    • Configuration of polypeptide chains
    • L. Pauling, and R.B. Corey Configuration of polypeptide chains Nature 168 1951 550 551
    • (1951) Nature , vol.168 , pp. 550-551
    • Pauling, L.1    Corey, R.B.2
  • 147
    • 0006347847 scopus 로고
    • The polypeptide-chain configuration in hemoglobin and other globular proteins
    • L. Pauling, and R.B. Corey The polypeptide-chain configuration in hemoglobin and other globular proteins Proc. Natl. Acad. Sci. USA 37 1951 282 285
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 282-285
    • Pauling, L.1    Corey, R.B.2
  • 148
    • 76549252207 scopus 로고
    • The structure of proteins; Two hydrogen-bonded helical configurations of the polypeptide chain
    • L. Pauling, R.B. Corey, and H.R. Branson The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain Proc. Natl. Acad. Sci. USA 37 1951 205 211
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 149
    • 0027771333 scopus 로고
    • The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots
    • N.P. Pavletich, K.A. Chambers, and C.O. Pabo The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots Genes Dev. 7 12B 1993 2556 2564
    • (1993) Genes Dev. , vol.7 , Issue.12 B , pp. 2556-2564
    • Pavletich, N.P.1    Chambers, K.A.2    Pabo, C.O.3
  • 150
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • E. Pebay-Peyroula, G. Rummel, J.P. Rosenbusch, and E.M. Landau X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases Science 277 1997 1676 1681
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 151
    • 36949066642 scopus 로고
    • Structure of haemoglobin: A three-dimensional Fourier synthesis at 5.5-A. Resolution, obtained by X-ray analysis
    • M.F. Perutz, M.G. Rossmann, A.F. Cullis, H. Muirhead, G. Will, and A.C. North Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis Nature 185 1960 416 422
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, H.4    Will, G.5    North, A.C.6
  • 152
    • 0014404921 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: (1) x-ray analysis
    • M.F. Perutz, H. Miurhead, J.M. Cox, L.C. Goaman, F.S. Mathews, E.L. McGandy, and L.E. Webb Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: (1) x-ray analysis Nature 219 1968 29 32
    • (1968) Nature , vol.219 , pp. 29-32
    • Perutz, M.F.1    Miurhead, H.2    Cox, J.M.3    Goaman, L.C.4    Mathews, F.S.5    McGandy, E.L.6    Webb, L.E.7
  • 153
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: The atomic model
    • M.F. Perutz, H. Muirhead, J.M. Cox, and L.C. Goaman Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: the atomic model Nature 219 1968 131 139
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.4
  • 154
    • 0000019861 scopus 로고
    • The use of anomalous scattering effects to phase diffraction patterns from macromolecules
    • J.C. Phillips, and K.O. Hodgson The use of anomalous scattering effects to phase diffraction patterns from macromolecules Acta Crystallogr. A 36 1980 856 864
    • (1980) Acta Crystallogr. A , vol.36 , pp. 856-864
    • Phillips, J.C.1    Hodgson, K.O.2
  • 156
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • H.W. Pinkett, A.T. Lee, P. Lum, K.P. Locher, and D.C. Rees An inward-facing conformation of a putative metal-chelate-type ABC transporter Science 315 2007 373 377
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 157
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • D.A. Pomeranz Krummel, C. Oubridge, A.K. Leung, J. Li, and K. Nagai Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution Nature 458 2009 475 480
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 162
    • 61949479923 scopus 로고    scopus 로고
    • Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP
    • S. Ressl, A.C. Terwisscha van Scheltinga, C. Vonrhein, V. Ott, and C. Ziegler Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP Nature 458 2009 47 52
    • (2009) Nature , vol.458 , pp. 47-52
    • Ressl, S.1    Terwisscha Van Scheltinga, A.C.2    Vonrhein, C.3    Ott, V.4    Ziegler, C.5
  • 163
    • 0021760689 scopus 로고
    • Structure of the nucleosome core particle at 7 A resolution
    • T.J. Richmond, J.T. Finch, B. Rushton, D. Rhodes, and A. Klug Structure of the nucleosome core particle at 7 A resolution Nature 311 1984 532 537
    • (1984) Nature , vol.311 , pp. 532-537
    • Richmond, T.J.1    Finch, J.T.2    Rushton, B.3    Rhodes, D.4    Klug, A.5
  • 164
    • 0028774714 scopus 로고
    • Cryocrystallography
    • D.W. Rodgers Cryocrystallography Structure 2 1994 1135 1140
    • (1994) Structure , vol.2 , pp. 1135-1140
    • Rodgers, D.W.1
  • 165
    • 0000105113 scopus 로고
    • Synchrotron radiation as a source for X-ray diffraction
    • G. Rosenbaum, and K. Holmes Synchrotron radiation as a source for X-ray diffraction Nature 230 1971 434 437
    • (1971) Nature , vol.230 , pp. 434-437
    • Rosenbaum, G.1    Holmes, K.2
  • 168
    • 0033516590 scopus 로고    scopus 로고
    • The cavity and pore helices in the KcsA K+ channel: Electrostatic stabilization of monovalent cations
    • B. Roux, and R. MacKinnon The cavity and pore helices in the KcsA K+ channel: electrostatic stabilization of monovalent cations Science 285 1999 100 102
    • (1999) Science , vol.285 , pp. 100-102
    • Roux, B.1    Mackinnon, R.2
  • 169
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • A.A. Russo, P.D. Jeffrey, A.K. Patten, J. Massagué, and N.P. Pavletich Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex Nature 382 1996 325 331
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massagué, J.4    Pavletich, N.P.5
  • 170
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • A.A. Russo, P.D. Jeffrey, and N.P. Pavletich Structural basis of cyclin-dependent kinase activation by phosphorylation Nat. Struct. Biol. 3 1996 696 700
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 171
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
    • A.A. Russo, L. Tong, J.O. Lee, P.D. Jeffrey, and N.P. Pavletich Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a Nature 395 1998 237 243
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1    Tong, L.2    Lee, J.O.3    Jeffrey, P.D.4    Pavletich, N.P.5
  • 177
    • 0345688603 scopus 로고    scopus 로고
    • Mechanisms of resistance to STI571 in Philadelphia chromosome-associated leukemias
    • N.P. Shah, and C.L. Sawyers Mechanisms of resistance to STI571 in Philadelphia chromosome-associated leukemias Oncogene 22 2003 7389 7395
    • (2003) Oncogene , vol.22 , pp. 7389-7395
    • Shah, N.P.1    Sawyers, C.L.2
  • 178
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • K. Shah, Y. Liu, C. Deirmengian, and K.M. Shokat Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates Proc. Natl. Acad. Sci. USA 94 1997 3565 3570
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 180
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • F. Sicheri, I. Moarefi, and J. Kuriyan Crystal structure of the Src family tyrosine kinase Hck Nature 385 1997 602 609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 181
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • A.I. Sobolevsky, M.P. Rosconi, and E. Gouaux X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor Nature 462 2009 745 756
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 183
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • T.L. Sørensen, J.V. Møller, and P. Nissen Phosphoryl transfer and calcium ion occlusion in the calcium pump Science 304 2004 1672 1675
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sørensen, T.L.1    Møller, J.V.2    Nissen, P.3
  • 186
    • 0037093403 scopus 로고    scopus 로고
    • From structure to mechanism: Electron crystallographic studies of bacteriorhodopsin
    • S. Subramaniam, T. Hirai, and R. Henderson From structure to mechanism: electron crystallographic studies of bacteriorhodopsin Philos. Trans. A, Math. Phys. Eng. Sci. 360 2002 859 874
    • (2002) Philos. Trans. A, Math. Phys. Eng. Sci. , vol.360 , pp. 859-874
    • Subramaniam, S.1    Hirai, T.2    Henderson, R.3
  • 187
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • H. Sui, B.G. Han, J.K. Lee, P. Walian, and B.K. Jap Structural basis of water-specific transport through the AQP1 water channel Nature 414 2001 872 878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 188
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • L. Sun, X. Zeng, C. Yan, X. Sun, X. Gong, Y. Rao, and N. Yan Crystal structure of a bacterial homologue of glucose transporters GLUT1-4 Nature 490 2012 361 366
    • (2012) Nature , vol.490 , pp. 361-366
    • Sun, L.1    Zeng, X.2    Yan, C.3    Sun, X.4    Gong, X.5    Rao, Y.6    Yan, N.7
  • 189
    • 0001268037 scopus 로고
    • Inactivation and activation of liver phosphorylase
    • E.W. Sutherland Jr., and W.D. Wosilait Inactivation and activation of liver phosphorylase Nature 175 1955 169 170
    • (1955) Nature , vol.175 , pp. 169-170
    • Sutherland, E.W.1    Wosilait, W.D.2
  • 191
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • C. Toyoshima, and T. Mizutani Crystal structure of the calcium pump with a bound ATP analogue Nature 430 2004 529 535
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 192
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • C. Toyoshima, and H. Nomura Structural changes in the calcium pump accompanying the dissociation of calcium Nature 418 2002 605 611
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 193
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • C. Toyoshima, M. Nakasako, H. Nomura, and H. Ogawa Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution Nature 405 2000 647 655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 194
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • C. Toyoshima, H. Nomura, and T. Tsuda Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues Nature 432 2004 361 368
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 195
    • 77449091710 scopus 로고    scopus 로고
    • Structure and mechanism of a pentameric formate channel
    • A.B. Waight, J. Love, and D.N. Wang Structure and mechanism of a pentameric formate channel Nat. Struct. Mol. Biol. 17 2010 31 37
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 31-37
    • Waight, A.B.1    Love, J.2    Wang, D.N.3
  • 198
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Y. Wang, Y. Zhang, and Y. Ha Crystal structure of a rhomboid family intramembrane protease Nature 444 2006 179 180
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 199
    • 70849106457 scopus 로고    scopus 로고
    • Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
    • Y. Wang, Y. Huang, J. Wang, C. Cheng, W. Huang, P. Lu, Y.N. Xu, P. Wang, N. Yan, and Y. Shi Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel Nature 462 2009 467 472
    • (2009) Nature , vol.462 , pp. 467-472
    • Wang, Y.1    Huang, Y.2    Wang, J.3    Cheng, C.4    Huang, W.5    Lu, P.6    Xu, Y.N.7    Wang, P.8    Yan, N.9    Shi, Y.10
  • 200
    • 84877766581 scopus 로고    scopus 로고
    • Structure of a bacterial energy-coupling factor transporter
    • T. Wang, G. Fu, X. Pan, J. Wu, X. Gong, J. Wang, and Y. Shi Structure of a bacterial energy-coupling factor transporter Nature 497 2013 272 276
    • (2013) Nature , vol.497 , pp. 272-276
    • Wang, T.1    Fu, G.2    Pan, X.3    Wu, J.4    Gong, X.5    Wang, J.6    Shi, Y.7
  • 201
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • A. Ward, C.L. Reyes, J. Yu, C.B. Roth, and G. Chang Flexibility in the ABC transporter MsbA: Alternating access with a twist Proc. Natl. Acad. Sci. USA 104 2007 19005 19010
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 202
    • 84904821452 scopus 로고    scopus 로고
    • Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA
    • E.V. Wasmuth, K. Januszyk, and C.D. Lima Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA Nature 511 2014 435 439
    • (2014) Nature , vol.511 , pp. 435-439
    • Wasmuth, E.V.1    Januszyk, K.2    Lima, C.D.3
  • 203
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids; A structure for deoxyribose nucleic acid
    • J.D. Watson, and F.H. Crick Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid Nature 171 1953 737 738
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.2
  • 205
    • 77049146099 scopus 로고
    • Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer
    • W.F. Widdas Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer J. Physiol. 118 1952 23 39
    • (1952) J. Physiol. , vol.118 , pp. 23-39
    • Widdas, W.F.1
  • 206
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • C. Wiesmann, G. Fuh, H.W. Christinger, C. Eigenbrot, J.A. Wells, and A.M. de Vos Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor Cell 91 1997 695 704
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    De Vos, A.M.6
  • 209
    • 0014682668 scopus 로고
    • Structure of subtilisin BPN' at 2.5 angström resolution
    • C.S. Wright, R.A. Alden, and J. Kraut Structure of subtilisin BPN' at 2.5 angström resolution Nature 221 1969 235 242
    • (1969) Nature , vol.221 , pp. 235-242
    • Wright, C.S.1    Alden, R.A.2    Kraut, J.3
  • 211
    • 35348885465 scopus 로고    scopus 로고
    • PKA type IIalpha holoenzyme reveals a combinatorial strategy for isoform diversity
    • J. Wu, S.H. Brown, S. von Daake, and S.S. Taylor PKA type IIalpha holoenzyme reveals a combinatorial strategy for isoform diversity Science 318 2007 274 279
    • (2007) Science , vol.318 , pp. 274-279
    • Wu, J.1    Brown, S.H.2    Von Daake, S.3    Taylor, S.S.4
  • 214
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • W. Xu, S.C. Harrison, and M.J. Eck Three-dimensional structure of the tyrosine kinase c-Src Nature 385 1997 595 602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 215
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Z. Xu, A.L. Horwich, and P.B. Sigler The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex Nature 388 1997 741 750
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 216
    • 84877756304 scopus 로고    scopus 로고
    • Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis
    • K. Xu, M. Zhang, Q. Zhao, F. Yu, H. Guo, C. Wang, F. He, J. Ding, and P. Zhang Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis Nature 497 2013 268 271
    • (2013) Nature , vol.497 , pp. 268-271
    • Xu, K.1    Zhang, M.2    Zhao, Q.3    Yu, F.4    Guo, H.5    Wang, C.6    He, F.7    Ding, J.8    Zhang, P.9
  • 217
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl - Dependent neurotransmitter transporters
    • A. Yamashita, S.K. Singh, T. Kawate, Y. Jin, and E. Gouaux Crystal structure of a bacterial homologue of Na+/Cl - dependent neurotransmitter transporters Nature 437 2005 215 223
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 218
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein
    • W. Yang, W.A. Hendrickson, R.J. Crouch, and Y. Satow Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein Science 249 1990 1398 1405
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4
  • 219
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Y. Yin, X. He, P. Szewczyk, T. Nguyen, and G. Chang Structure of the multidrug transporter EmrD from Escherichia coli Science 312 2006 741 744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 220
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • M.A. Young, S. Gonfloni, G. Superti-Furga, B. Roux, and J. Kuriyan Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation Cell 105 2001 115 126
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 221
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • X. Zhang, J. Gureasko, K. Shen, P.A. Cole, and J. Kuriyan An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor Cell 125 2006 1137 1149
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 222
    • 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
  • 224
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • Y. Zhou, J.H. Morais-Cabral, A. Kaufman, and R. MacKinnon Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution Nature 414 2001 43 48
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4
  • 225
    • 84893774907 scopus 로고    scopus 로고
    • Crystal structures of the Lsm complex bound to the 3′ end sequence of U6 small nuclear RNA
    • L. Zhou, J. Hang, Y. Zhou, R. Wan, G. Lu, P. Yin, C. Yan, and Y. Shi Crystal structures of the Lsm complex bound to the 3′ end sequence of U6 small nuclear RNA Nature 506 2014 116 120
    • (2014) Nature , vol.506 , pp. 116-120
    • Zhou, L.1    Hang, J.2    Zhou, Y.3    Wan, R.4    Lu, G.5    Yin, P.6    Yan, C.7    Shi, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.