메뉴 건너뛰기




Volumn 78, Issue 4, 2000, Pages 191-202

Three-dimensional electron cryo-microscopy as a powerful structural tool in molecular medicine

Author keywords

Electron cryo microscopy; Electron crystallography; Image reconstruction; Three dimensional electron microscopy; Two dimensional crystallization

Indexed keywords

M PROTEIN;

EID: 0033946805     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001090000101     Document Type: Review
Times cited : (17)

References (104)
  • 1
    • 0033025637 scopus 로고    scopus 로고
    • Chance favors the prepared mind - From serendipity to rational drug design
    • 1. Kubinyi H (1999) Chance favors the prepared mind - from serendipity to rational drug design. J Recept Signal Transduct Res 19:15-39
    • (1999) J Recept Signal Transduct Res , vol.19 , pp. 15-39
    • Kubinyi, H.1
  • 2
    • 0033084066 scopus 로고    scopus 로고
    • Atomic force microscopy: A powerful tool to observe biomolecules at work
    • 2. Engel A, Lyubchenko Y, Müller D (1999) Atomic force microscopy: a powerful tool to observe biomolecules at work. Trends Cell Biol 9:77-80
    • (1999) Trends Cell Biol , vol.9 , pp. 77-80
    • Engel, A.1    Lyubchenko, Y.2    Müller, D.3
  • 4
    • 0032986388 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure
    • 4. Fu R, Cross TA (1999) Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure. Annu Rev Biophys Biomol Struct 28:235-268
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 235-268
    • Fu, R.1    Cross, T.A.2
  • 5
    • 0031764019 scopus 로고    scopus 로고
    • NMR structural studies of membrane proteins
    • 5. Marassi FM, Opella S (1998) NMR structural studies of membrane proteins. Curr Opin Struct Biol 8:640-648
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 640-648
    • Marassi, F.M.1    Opella, S.2
  • 6
    • 85143335047 scopus 로고
    • Useful principles for the crystallization of proteins
    • Michel H (ed) CRC, Boca Rotan
    • 6. McPherson A (1991) Useful principles for the crystallization of proteins. In Michel H (ed) Crystallization of membrane proteins. CRC, Boca Rotan, pp 2-51
    • (1991) Crystallization of Membrane Proteins , pp. 2-51
    • McPherson, A.1
  • 7
    • 0032428794 scopus 로고    scopus 로고
    • Structures of membrane proteins determined at atomic resolution
    • 7. Sakai H, Tsukihara T (1998) Structures of membrane proteins determined at atomic resolution. J Biochem (Tokyo) 124: 1051-1059
    • (1998) J Biochem (Tokyo) , vol.124 , pp. 1051-1059
    • Sakai, H.1    Tsukihara, T.2
  • 8
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • 8. Pautsch A, Schulz GE (1998) Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 5: 1013-1017
    • (1998) Nat Struct Biol , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 11
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signalling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • 11. Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbush JP, Moras D (1998) Transmembrane signalling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 95:771-778
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbush, J.P.6    Moras, D.7
  • 12
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • 12. Ferguson AD, Hofmann E, Coulton JW, Diederichs W, Welte W (1998) Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282: 2215-2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, W.4    Welte, W.5
  • 13
    • 0033570111 scopus 로고    scopus 로고
    • The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanism of virulence
    • 13. Vogt J, Schulz GE (1999) The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanism of virulence. Struct Fold Design 7:1301-1309
    • (1999) Struct Fold Design , vol.7 , pp. 1301-1309
    • Vogt, J.1    Schulz, G.E.2
  • 14
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • 14. Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282: 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
  • 15
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • 15. Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999) Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284:1961-1966
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 16
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenesat 2.2 Å resolution
    • 16. Lancaster CR, Kröger A, Auer M, Michel H (1999) Structure of fumarate reductase from Wolinella succinogenesat 2.2 Å resolution. Nature 402:377-385
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.1    Kröger, A.2    Auer, M.3    Michel, H.4
  • 17
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotatory motor in ATP synthase
    • 17. Stock D, Leslie AGW, Walker JE (1999) Molecular architecture of the rotatory motor in ATP synthase. Science 286: 1700-1704
    • (1999) Science , vol.286 , pp. 1700-1704
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 18
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • 18. DeRosier DJ, Klug A (1968) Reconstruction of three-dimensional structures from electron micrographs. Nature 217: 130-134
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.J.1    Klug, A.2
  • 19
    • 0014894609 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its applications to electron microscopy
    • 19. Crowther RA, DeRosier DJ, Klug A (1970) The reconstruction of a three-dimensional structure from projections and its applications to electron microscopy. Proc R Soc Lond A 317: 319-340
    • (1970) Proc R Soc Lond A , vol.317 , pp. 319-340
    • Crowther, R.A.1    DeRosier, D.J.2    Klug, A.3
  • 21
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • 21. Taylor KA, Glaeser RM (1974) Electron diffraction of frozen, hydrated protein crystals. Science 186:1036-1037
    • (1974) Science , vol.186 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 23
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • 23. Unwin PNT, Henderson R (1975) Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 94:425-440
    • (1975) J Mol Biol , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 24
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • 24. Wang DN, Kühlbrandt W (1991) High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J Mol Biol 217:691-699
    • (1991) J Mol Biol , vol.217 , pp. 691-699
    • Wang, D.N.1    Kühlbrandt, W.2
  • 25
    • 0032618726 scopus 로고    scopus 로고
    • High-pressure freezing for preservation of high resolution fine structure and antigenicity for immunolabeling
    • 25. McDonald K (1999) High-pressure freezing for preservation of high resolution fine structure and antigenicity for immunolabeling. Methods Mol Biol 117:77-97
    • (1999) Methods Mol Biol , vol.117 , pp. 77-97
    • McDonald, K.1
  • 26
    • 0024426168 scopus 로고
    • High-pressure freezing for the preservation of biological structure: Theory and practice
    • 26. Dahl R, Staehelin LA (1989) High-pressure freezing for the preservation of biological structure: theory and practice. J Electron Microsc Tech 13:165-174
    • (1989) J Electron Microsc Tech , vol.13 , pp. 165-174
    • Dahl, R.1    Staehelin, L.A.2
  • 27
    • 0025739185 scopus 로고
    • A model for cryosectioning based on the morphology of vitrified ultrathin sections
    • 27. Richter K, Gnagi H, Dubochet J (1991) A model for cryosectioning based on the morphology of vitrified ultrathin sections. J Microsc 163:19-28
    • (1991) J Microsc , vol.163 , pp. 19-28
    • Richter, K.1    Gnagi, H.2    Dubochet, J.3
  • 28
    • 0027414416 scopus 로고
    • The impact of freeze substitution on biological electron microscopy
    • 28. Hippe-Sanwald (1993) The impact of freeze substitution on biological electron microscopy. Microsc Res Tech 24:400-422
    • (1993) Microsc Res Tech , vol.24 , pp. 400-422
  • 29
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • 29. Henderson R (1995) 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) Q Rev Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 31
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tolt series applied to the 50S ribosomal subunit of Escherichia coli
    • 31. Radermacher M, Wagenknecht T, Verschoor A, Frank J (1987) Three-dimensional reconstruction from a single-exposure, random conical tolt series applied to the 50S ribosomal subunit of Escherichia coli. J Microsc 146:113-136
    • (1987) J Microsc , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 32
    • 0023666171 scopus 로고
    • The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid
    • 32. Fuller SD (1987) The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid. Cell 48:923-934
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 33
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry
    • 33. DeRosier DJ, Moore PB (1970) Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J Mol Biol 52:355-369
    • (1970) J Mol Biol , vol.52 , pp. 355-369
    • DeRosier, D.J.1    Moore, P.B.2
  • 34
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • 34. Amos LA, Henderson R, Unwin PN (1982) Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Prog Biophys Mol Biol 39:183-231
    • (1982) Prog Biophys Mol Biol , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.3
  • 35
    • 0029379689 scopus 로고
    • The relevance of dose-fractionation in tomography of radiation-sensitive specimens
    • 35. McEwen BF, Downing KH, Glaeser RM (1995) The relevance of dose-fractionation in tomography of radiation-sensitive specimens. Ultramicroscopy 60:357-373
    • (1995) Ultramicroscopy , vol.60 , pp. 357-373
    • McEwen, B.F.1    Downing, K.H.2    Glaeser, R.M.3
  • 36
    • 0028953758 scopus 로고
    • Three-dimensional structure of lipid vesicles embedded in vitreous ice and investigated by automated electron tomography
    • 36. Dierksen K, Typke D, Hegerl R, Walz J, Sackmann E, Baumeister W (1995) Three-dimensional structure of lipid vesicles embedded in vitreous ice and investigated by automated electron tomography. Biophys J 68:1416-1422
    • (1995) Biophys J , vol.68 , pp. 1416-1422
    • Dierksen, K.1    Typke, D.2    Hegerl, R.3    Walz, J.4    Sackmann, E.5    Baumeister, W.6
  • 37
    • 0028206095 scopus 로고
    • Cryo automated electron tomography: Towards high-resolution reconstructions of plastic-embedded structures
    • 37. Braunfeld MB, Koster AJ, Sedat JW, Agard DA (1994) Cryo automated electron tomography: towards high-resolution reconstructions of plastic-embedded structures. J Microsc 174: 75-84
    • (1994) J Microsc , vol.174 , pp. 75-84
    • Braunfeld, M.B.1    Koster, A.J.2    Sedat, J.W.3    Agard, D.A.4
  • 39
    • 0033082710 scopus 로고    scopus 로고
    • Electron tomography of molecules and cells
    • 39. Baumeister W, Grimm R, Walz J (1999) Electron tomography of molecules and cells. Trends Cell Biol 9:81-85
    • (1999) Trends Cell Biol , vol.9 , pp. 81-85
    • Baumeister, W.1    Grimm, R.2    Walz, J.3
  • 43
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • 43. Böttcher B, Wynne SA, Crowther RA (1997) Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386:88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 44
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • 44. Conway JF, Cheng N, Zlotnick A, Wingfield PT, Stahl SJ, Steven AC (1997) Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386:91-94
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 45
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 Å resolution: Transverse tunnels in the channel wall
    • 45. Miyazawa A, Fujiyoshi Y, Stowell M, Unwin N (1999) Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channel wall. J Mol Biol 288:765-786
    • (1999) J Mol Biol , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 46
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution
    • 46. Zhang P, Toyoshima C, Yonekura K, Green M, Stokes DL (1998) Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution. Nature 392:835-839
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, M.4    Stokes, D.L.5
  • 47
    • 0029042213 scopus 로고
    • Structure of bacterial flagellar filaments at 11 Å resolution: Packing of the alpha-helices
    • 47. Morgan DG, Owen C, Melanson LA, DeRosier DJ (1995) Structure of bacterial flagellar filaments at 11 Å resolution: packing of the alpha-helices. J Mol Biol 249:88-110
    • (1995) J Mol Biol , vol.249 , pp. 88-110
    • Morgan, D.G.1    Owen, C.2    Melanson, L.A.3    DeRosier, D.J.4
  • 48
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • 48. Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J Mol Biol 213:899-929
    • (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
  • 49
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implications of the charge distribution
    • 49. Mitsuoka K, Hirai T, Murata K, Miyazawa A, Kidera A, Kimura Y, Fujiyoshi Y (1999) The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implications of the charge distribution. J Mol Biol 286:861-882
    • (1999) J Mol Biol , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 50
    • 0028147508 scopus 로고
    • Atomic model of light-harvesting complex by electron crystallography
    • 50. Kühlbrandt W, Wang DN, Fujiyoshi Y (1994) Atomic model of light-harvesting complex by electron crystallography. Nature 367:614-621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 51
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha-beta tubulin dimer by electron-crystallography
    • 51. Nogales E, Wolf SG, Downing KH (1998) Structure of the alpha-beta tubulin dimer by electron-crystallography. Nature 391:199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 52
    • 0031042723 scopus 로고    scopus 로고
    • Electron diffraction studies of light-induced conformational changes in the Leu-93→Ala bacteriorhopsin mutant
    • 52. Subramaniam S, Faruqi AR, Oesterhelt D, Henderson R (1997) Electron diffraction studies of light-induced conformational changes in the Leu-93→Ala bacteriorhopsin mutant. Proc Natl Acad Sci USA 94:1767-1772
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1767-1772
    • Subramaniam, S.1    Faruqi, A.R.2    Oesterhelt, D.3    Henderson, R.4
  • 53
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • 53. Unwin N (1995) Acetylcholine receptor channel imaged in the open state. Nature 373:37-43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 54
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • 54. Griesshammer R, Tate CG (1995) Overexpression of integral membrane proteins for structural Studies. Q Rev Biophys 28:315-422
    • (1995) Q Rev Biophys , vol.28 , pp. 315-422
    • Griesshammer, R.1    Tate, C.G.2
  • 55
    • 0018905597 scopus 로고
    • Structure of the junction between communicating cells
    • 55. Unwin PNT, Zampighi G (1980) Structure of the junction between communicating cells. Nature 283:545-549
    • (1980) Nature , vol.283 , pp. 545-549
    • Unwin, P.N.T.1    Zampighi, G.2
  • 56
    • 0021723207 scopus 로고
    • Tubular crystals of acetylcholine receptor
    • 56. Brisson A, Unwin PNT (1984) Tubular crystals of acetylcholine receptor. J Cell Biol 99:202-1211
    • (1984) J Cell Biol , vol.99 , pp. 202-1211
    • Brisson, A.1    Unwin, P.N.T.2
  • 57
    • 0020580035 scopus 로고
    • 2+-ATPase vesicles treated with vanadate
    • 2+-ATPase vesicles treated with vanadate. J Biol Chem 258:2599-2603
    • (1983) J Biol Chem , vol.258 , pp. 2599-2603
    • Dux, L.1    Martonosi, A.2
  • 58
    • 0026506038 scopus 로고
    • Two-dimensional crystallization of membrane proteins
    • 58. Kühlbrandt W (1992) Two-dimensional crystallization of membrane proteins. Q Rev Biophys 25:1-49
    • (1992) Q Rev Biophys , vol.25 , pp. 1-49
    • Kühlbrandt, W.1
  • 60
    • 0030949437 scopus 로고    scopus 로고
    • Bio-beads: An efficient strategy for two-dimensional crystallization of membrane proteins
    • 60. Rigaud JL, Mosser G, Lacapere JJ, Olofsson A, Levi D, Ranck JL (1997) Bio-beads: an efficient strategy for two-dimensional crystallization of membrane proteins. J Struct Biol 118:226-235
    • (1997) J Struct Biol , vol.118 , pp. 226-235
    • Rigaud, J.L.1    Mosser, G.2    Lacapere, J.J.3    Olofsson, A.4    Levi, D.5    Ranck, J.L.6
  • 61
    • 0029030012 scopus 로고
    • 2-D-structure of the Neurospora crassa plasma membrane ATPase as determined by electron cryomicroscopy
    • 61. Cyrklaff M, Auer M, Kühlbrandt W, Scarborough GA (1995) 2-D-structure of the Neurospora crassa plasma membrane ATPase as determined by electron cryomicroscopy. EMBO J 14:1854-1857
    • (1995) EMBO J , vol.14 , pp. 1854-1857
    • Cyrklaff, M.1    Auer, M.2    Kühlbrandt, W.3    Scarborough, G.A.4
  • 64
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • 64. Fuller SD, Wilk T, Gowen BE, Krausslich HG, Vogt VM (1997) Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr Biol 7:729-738
    • (1997) Curr Biol , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Krausslich, H.G.4    Vogt, V.M.5
  • 65
    • 0033117918 scopus 로고    scopus 로고
    • Towards the structure of the human immunodeficiency virus: Divide and conquer
    • 65. Wilk T, Fuller SD (1999) Towards the structure of the human immunodeficiency virus: divide and conquer. Curr Opin Struct Biol 9:231-243
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 231-243
    • Wilk, T.1    Fuller, S.D.2
  • 66
    • 0033045991 scopus 로고    scopus 로고
    • Capsid structure of simian cytomegalovirus from cryoelectron microscopy: Evidence for tegument attachment sites
    • published erratum appears in 73:4530
    • 66. Trus BL, Gibson W, Cheng N, Steven AC (1999) Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites. J Virol 73: 2181-2192 (published erratum appears in 73:4530)
    • (1999) J Virol , vol.73 , pp. 2181-2192
    • Trus, B.L.1    Gibson, W.2    Cheng, N.3    Steven, A.C.4
  • 68
    • 0014840152 scopus 로고
    • Experimental models for arthritis and related connective tissue diseases and some naturally occurring counterparts in animals
    • 68. (1970) Experimental models for arthritis and related connective tissue diseases and some naturally occurring counterparts in animals. Arthritis Rheum 13:621-663
    • (1970) Arthritis Rheum , vol.13 , pp. 621-663
  • 69
    • 0029052283 scopus 로고
    • Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex
    • 69. Fuller SD, Berriman JA, Butcher SJ, Gowen BE (1995) Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Cell 81:715-725
    • (1995) Cell , vol.81 , pp. 715-725
    • Fuller, S.D.1    Berriman, J.A.2    Butcher, S.J.3    Gowen, B.E.4
  • 74
    • 0030564927 scopus 로고    scopus 로고
    • Three-dimensional structure of ncd-decorated microtubules obtained by a back-projection method
    • 74. Sosa H, Milligan RA (1996) Three-dimensional structure of ncd-decorated microtubules obtained by a back-projection method. J Mol Biol 260:743-755
    • (1996) J Mol Biol , vol.260 , pp. 743-755
    • Sosa, H.1    Milligan, R.A.2
  • 76
    • 0030893857 scopus 로고    scopus 로고
    • Lansoprazole: A comprehensive review
    • 76. Zimmermann AE, Katona BG (1997) Lansoprazole: a comprehensive review. Pharmacotherapy 17:308-326
    • (1997) Pharmacotherapy , vol.17 , pp. 308-326
    • Zimmermann, A.E.1    Katona, B.G.2
  • 80
    • 0033166241 scopus 로고    scopus 로고
    • 2+-ATPase structures suggests a large conformation change occurs during the reaction cycle of P-type ion pumps
    • 2+-ATPase structures suggests a large conformation change occurs during the reaction cycle of P-type ion pumps, Curr Biol 9:672-679
    • (1999) Curr Biol , vol.9 , pp. 672-679
    • Stokes, D.L.1    Auer, M.2    Zhang, P.3    Kühlbrandt, W.4
  • 82
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • 82. Baldwin JM, Schertler GF, Unger VM (1997) An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J Mol Biol 272:144-164
    • (1997) J Mol Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 83
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • 83. Unger VM, Kumar NM, Gilula NB, Yeager M (1999) Three-dimensional structure of a recombinant gap junction membrane channel. Science 283:1176-1180
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 84
    • 0031765429 scopus 로고    scopus 로고
    • Diverse functions of vertebrate gap junctions
    • 84. Simon AM, Goodenough DA (1998) Diverse functions of vertebrate gap junctions. Trends Cell Biol 8:477-483
    • (1998) Trends Cell Biol , vol.8 , pp. 477-483
    • Simon, A.M.1    Goodenough, D.A.2
  • 85
    • 0032932108 scopus 로고    scopus 로고
    • Gap junctions: More roles and new structural data
    • 85. Simon AM (1999) Gap junctions: more roles and new structural data. Trends Cell Biol 9:169-170
    • (1999) Trends Cell Biol , vol.9 , pp. 169-170
    • Simon, A.M.1
  • 86
    • 0033002783 scopus 로고    scopus 로고
    • Genetic diseases and gene knockouts reveal diverse connexin function
    • 86. White TW, Paul DL (1999) Genetic diseases and gene knockouts reveal diverse connexin function. Annu Rev Physiol 61:283-310
    • (1999) Annu Rev Physiol , vol.61 , pp. 283-310
    • White, T.W.1    Paul, D.L.2
  • 87
    • 0030983283 scopus 로고    scopus 로고
    • The aquaporin family of water channel proteins in clinical medicine
    • 87. Lee MD, King LS, Agre P (1997) The aquaporin family of water channel proteins in clinical medicine. Medicine (Baltimore) 76:141-156
    • (1997) Medicine (Baltimore) , vol.76 , pp. 141-156
    • Lee, M.D.1    King, L.S.2    Agre, P.3
  • 88
    • 0029942399 scopus 로고    scopus 로고
    • Pathophysiology of the aquaporin water channels
    • 88. King LS, Agre P (1996) Pathophysiology of the aquaporin water channels. Annu Rev Physiol 58:619-648
    • (1996) Annu Rev Physiol , vol.58 , pp. 619-648
    • King, L.S.1    Agre, P.2
  • 91
    • 0030915303 scopus 로고    scopus 로고
    • Molecular design of aquaporin-1 water channel as revealed by electron crystallography
    • 91. Li H, Lee S, Jap BK (1997) Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Nat Struct Biol 4:263-265
    • (1997) Nat Struct Biol , vol.4 , pp. 263-265
    • Li, H.1    Lee, S.2    Jap, B.K.3
  • 92
    • 0031242019 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors in health and disease
    • 92. Lindstrom J (1997) Nicotinic acetylcholine receptors in health and disease. Mol Neurobiol 15:193-222
    • (1997) Mol Neurobiol , vol.15 , pp. 193-222
    • Lindstrom, J.1
  • 93
    • 0029143458 scopus 로고
    • Three-dimensional location of the main immunogenic region of the acetylcholine receptor
    • 93. Beroukhim R, Unwin N (1995) Three-dimensional location of the main immunogenic region of the acetylcholine receptor. Neuron 15:323-331
    • (1995) Neuron , vol.15 , pp. 323-331
    • Beroukhim, R.1    Unwin, N.2
  • 94
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • 94. Rayment I, Holden HM, Whittaker CB, Yohn M, Lorentz M, Holmes KC, Milligan (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, C.B.3    Yohn, M.4    Lorentz, M.5    Holmes, K.C.6
  • 95
    • 0030692707 scopus 로고    scopus 로고
    • Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis
    • 95. Jontes JD, Milligan RA (1997) Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. J Cell Biol 139: 683-693
    • (1997) J Cell Biol , vol.139 , pp. 683-693
    • Jontes, J.D.1    Milligan, R.A.2
  • 96
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • 96. Holmes KC (1997) The swinging lever-arm hypothesis of muscle contraction. Curr Biol 7:R112-R118
    • (1997) Curr Biol , vol.7
    • Holmes, K.C.1
  • 97
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • 97. Geeves MA, Holmes KC (1999) Structural mechanism of muscle contraction. Annu Rev Biochem 68:687-728
    • (1999) Annu Rev Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 99
    • 0032809077 scopus 로고    scopus 로고
    • Low-resolution density maps from atomic models: How a stepping "back" can be a step "forward"
    • 99. Belnap DM, Kumar A, Folk JT, Smith TJ, Baker TS (1999) Low-resolution density maps from atomic models: how a stepping "back" can be a step "forward." J Struct Biol 125: 166-175
    • (1999) J Struct Biol , vol.125 , pp. 166-175
    • Belnap, D.M.1    Kumar, A.2    Folk, J.T.3    Smith, T.J.4    Baker, T.S.5
  • 100
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: Bridging the resolution gap between X-ray crystallography and electron microscopy
    • 100. Stewart PL, Fuller SD, Burnett RM (1993) Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J 12:2589-2599
    • (1993) EMBO J , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 101
    • 0029353191 scopus 로고
    • Wilson's disease: A new gene and an animal model for an old disease
    • 101. Cuthbert JA (1995) Wilson's disease: a new gene and an animal model for an old disease. J Investig Med 43:323-336
    • (1995) J Investig Med , vol.43 , pp. 323-336
    • Cuthbert, J.A.1
  • 102
    • 0030907484 scopus 로고    scopus 로고
    • Three-dimensional structure of the porcine gastric H, K-ATPase from negatively stained crystals
    • 102. Xian Y, Hebert H (1997) Three-dimensional structure of the porcine gastric H, K-ATPase from negatively stained crystals. J Struct Biol 118:169-1-77
    • (1997) J Struct Biol , vol.118 , pp. 169-177
    • Xian, Y.1    Hebert, H.2
  • 103
    • 0032772540 scopus 로고    scopus 로고
    • Reconstitution of detergent-solubilized Na, K-ATPase and formation of two-dimensional crystals
    • 103. Mohraz M (1999) Reconstitution of detergent-solubilized Na, K-ATPase and formation of two-dimensional crystals. J Struct Biol 125:76-85
    • (1999) J Struct Biol , vol.125 , pp. 76-85
    • Mohraz, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.