메뉴 건너뛰기




Volumn 51, Issue , 2001, Pages 39-119

Chapter 2 The aquaporin superfamily: Structure and function

Author keywords

[No Author keywords available]

Indexed keywords


EID: 35448948757     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s1063-5823(01)51004-2     Document Type: Review
Times cited : (9)

References (111)
  • 2
    • 0025333990 scopus 로고
    • Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes
    • T. Aerts J.Z. Xia H. Slegers J. de Bock J. Clauwaert Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes J. Biol. Chem. 265 1990 8675 8680
    • (1990) J. Biol. Chem. , vol.265 , pp. 8675-8680
    • Aerts, T.1    Xia, J.Z.2    Slegers, H.3    de Bock, J.4    Clauwaert, J.5
  • 3
    • 0023053025 scopus 로고
    • Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans
    • W. Baumeister M. Barth R. Hegerl R. Guckenberger M. Hahn W.O. Saxton Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans J. Mol. Biol. 187 1986 241 253
    • (1986) J. Mol. Biol. , vol.187 , pp. 241-253
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 6
    • 0020078925 scopus 로고
    • Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions
    • D. Bok J. Dockstader J. Horwitz Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions J. Cell. Biol. 92 1982 213 220
    • (1982) J. Cell. Biol. , vol.92 , pp. 213-220
    • Bok, D.1    Dockstader, J.2    Horwitz, J.3
  • 7
    • 0029739781 scopus 로고    scopus 로고
    • Liquefaction of cortical tissue in diabetic and galactosemic rat lenses defined by confocal laser scanning microscopy
    • J. Bond C. Green P. Donaldson J. Kistler Liquefaction of cortical tissue in diabetic and galactosemic rat lenses defined by confocal laser scanning microscopy Invest. Ophthalmol. Vis. Sci. 37 1996 1557 1565
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.37 , pp. 1557-1565
    • Bond, J.1    Green, C.2    Donaldson, P.3    Kistler, J.4
  • 12
    • 0030997806 scopus 로고    scopus 로고
    • Secondary structures comparison of aquaporin-1 and bacteriorhodopsin: A Fourier transform infrared spectroscopy study of two-dimensional membrane crystals
    • V. Cabiaux K.A. Oberg P. Pancoska T. Walz P. Agre A. Engel Secondary structures comparison of aquaporin-1 and bacteriorhodopsin: A Fourier transform infrared spectroscopy study of two-dimensional membrane crystals Biophys. J. 73 1 1997 406 417
    • (1997) Biophys. J. , vol.73 , Issue.1 , pp. 406-417
    • Cabiaux, V.1    Oberg, K.A.2    Pancoska, P.3    Walz, T.4    Agre, P.5    Engel, A.6
  • 13
    • 0028787084 scopus 로고
    • Molecular cloning and characterization of AgpZ, a water channel from Escherichia coli
    • G. Calamita W. Bishai G. Preston W. Guggino P. Agre Molecular cloning and characterization of AgpZ, a water channel from Escherichia coli J. Biol. Chem. 270 49 1995 29063 29066
    • (1995) J. Biol. Chem. , vol.270 , Issue.49 , pp. 29063-29066
    • Calamita, G.1    Bishai, W.2    Preston, G.3    Guggino, W.4    Agre, P.5
  • 14
    • 0032584246 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli water channel gene agpZ
    • G. Calamita B. Kempf M. Bonhivers W. Bishai E. Bremer P. Agre Regulation of the Escherichia coli water channel gene agpZ Proc. Nat. Acad. Sci. USA 95 1998 3627 3631 7
    • (1998) , pp. 3627-3631
    • Calamita, G.1    Kempf, B.2    Bonhivers, M.3    Bishai, W.4    Bremer, E.5    Agre, P.6
  • 15
    • 0030729551 scopus 로고    scopus 로고
    • Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response
    • M.C. Canfield B.K. Tamarappoo A.M. Moses A.S. Verkman E.J. Holtzman Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response Human Mol. Gen. 6 11 1997 1865 1871
    • (1997) Human Mol. Gen. , vol.6 , Issue.11 , pp. 1865-1871
    • Canfield, M.C.1    Tamarappoo, B.K.2    Moses, A.M.3    Verkman, A.S.4    Holtzman, E.J.5
  • 16
    • 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 D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel Science 282 5397 1998 2220 2226
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 18
    • 85038048643 scopus 로고    scopus 로고
    • 2D crystallization of a plant vacuole membrane aquaporin and determination of its projection structure by electron crystallography
    • M.J. Daniels M.J. Chrispeels M. Yeager 2D crystallization of a plant vacuole membrane aquaporin and determination of its projection structure by electron crystallography Biophys. J. 76 1999 A456
    • (1999) Biophys. J. , vol.76 , pp. A456
    • Daniels, M.J.1    Chrispeels, M.J.2    Yeager, M.3
  • 19
    • 0033579547 scopus 로고    scopus 로고
    • Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography
    • M.J. Daniels M.J. Chrispeels M. Yeager Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography J. Mol. Biol. 294 5 1999 1337 1349
    • (1999) J. Mol. Biol. , vol.294 , Issue.5 , pp. 1337-1349
    • Daniels, M.J.1    Chrispeels, M.J.2    Yeager, M.3
  • 20
    • 0028326794 scopus 로고
    • requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine
    • P. Deen M. Verdijk N. Knoers B. Wieringa L. Monnens C. van Os B. van Oost requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine Science 264 1994 92 95
    • (1994) Science , vol.264 , pp. 92-95
    • Deen, P.1    Verdijk, M.2    Knoers, N.3    Wieringa, B.4    Monnens, L.5    van Os, C.6    van Oost, B.7
  • 21
    • 0032580978 scopus 로고    scopus 로고
    • Thermal denaturation of ribonuclease A characterized by water 17O and 2H magnetic relaxation dispersion
    • 2H magnetic relaxation dispersion Biochem 37 1998 9595 9604
    • (1998) Biochem , vol.37 , pp. 9595-9604
    • Denisov, V.B.1    Halle, B.2
  • 24
    • 0029986047 scopus 로고    scopus 로고
    • The micelle to vesicle transition of lipids and detergents in the presence of a membrane protein: Towards a rationale for 2D crystallization
    • M. Dolder A. Engel M. Zulauf The micelle to vesicle transition of lipids and detergents in the presence of a membrane protein: Towards a rationale for 2D crystallization FEBS Letters 382 1996 203 208
    • (1996) FEBS Letters , vol.382 , pp. 203-208
    • Dolder, M.1    Engel, A.2    Zulauf, M.3
  • 25
    • 0028177302 scopus 로고
    • The prediction and orientation of helices from sequence alignments: The combined use of environment-dependent substitution tables, Fourier transform methods and helix capping rules
    • D. Donnelly J.P. Overington T.L. Blundell The prediction and orientation of helices from sequence alignments: The combined use of environment-dependent substitution tables, Fourier transform methods and helix capping rules Protein Eng. 7 5 1994 645 653
    • (1994) Protein Eng. , vol.7 , Issue.5 , pp. 645-653
    • Donnelly, D.1    Overington, J.P.2    Blundell, T.L.3
  • 28
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • D. Eisenberg E. Schwarz M. Komaromy R. Wall Analysis of membrane and surface protein sequences with the hydrophobic moment plot J. Mol. Biol. 179 1 1984 125 142
    • (1984) J. Mol. Biol. , vol.179 , Issue.1 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 29
    • 0026969052 scopus 로고
    • Assembly of 2-D membrane protein crystals—dynamics, crystal order, and fidelity of structure analysis by electron microscopy
    • A. Engel A. Hoenger A. Hefti C. Henn R.C. Ford J. Kistler M. Zulauf Assembly of 2-D membrane protein crystals—dynamics, crystal order, and fidelity of structure analysis by electron microscopy J. Struct. Biol. 109 3 1992 219 234
    • (1992) J. Struct. Biol. , vol.109 , Issue.3 , pp. 219-234
    • Engel, A.1    Hoenger, A.2    Hefti, A.3    Henn, C.4    Ford, R.C.5    Kistler, J.6    Zulauf, M.7
  • 30
    • 0033084066 scopus 로고    scopus 로고
    • Atomic force microscopy: A powerful tool to observe biomolecules at work
    • A. Engel Y.L. Lyubchenkov D.J. Müller Atomic force microscopy: A powerful tool to observe biomolecules at work Trends Cell Biol. 9 1999 77 80
    • (1999) Trends Cell Biol. , vol.9 , pp. 77-80
    • Engel, A.1    Lyubchenkov, Y.L.2    Müller, D.J.3
  • 31
    • 0010214174 scopus 로고
    • Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor
    • J. Finer-Moore R.M. Stroud Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor Proc. Nat. Acad. Sci. USA 81 1984 155 159 1
    • (1984) , pp. 155-159
    • Finer-Moore, J.1    Stroud, R.M.2
  • 32
    • 0021064311 scopus 로고
    • Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens
    • P.G Fitzgerald D. Bok J. Horwitz Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens J. Cell Biol. 97 1983 1491 1499
    • (1983) J. Cell Biol. , vol.97 , pp. 1491-1499
    • Fitzgerald, P.G1    Bok, D.2    Horwitz, J.3
  • 34
    • 0018243812 scopus 로고
    • Reconstruction of glutamine synthetase using computer averaging
    • J. Frank W. Goldfarb D. Eisenberg T.S. Baker Reconstruction of glutamine synthetase using computer averaging Ultramicroscopy 3 1978 283 290
    • (1978) Ultramicroscopy , vol.3 , pp. 283-290
    • Frank, J.1    Goldfarb, W.2    Eisenberg, D.3    Baker, T.S.4
  • 35
    • 0019802812 scopus 로고
    • Computer averaging of electron micrographs of 40S ribosomal subunits
    • J. Frank A. Verschoor M. Boublik Computer averaging of electron micrographs of 40S ribosomal subunits Science 214 1981 1353 1355
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 36
    • 0000003034 scopus 로고
    • Infrared membrane spectroscopy
    • U.P. Fringeli H.H. Günthard Infrared membrane spectroscopy E. Grell Membrane Spectroscopy 1981 Springer Verlag Berlin
    • (1981)
    • Fringeli, U.P.1    Günthard, H.H.2
  • 37
    • 0031777369 scopus 로고    scopus 로고
    • Prediction of functional residues in water channels and related proteins
    • A. Froger B. Tallur D. Thomas C. Delamarche Prediction of functional residues in water channels and related proteins Prot. Sci. 7 6 1998 1458 1468
    • (1998) Prot. Sci. , vol.7 , Issue.6 , pp. 1458-1468
    • Froger, A.1    Tallur, B.2    Thomas, D.3    Delamarche, C.4
  • 38
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Y. Fujiyoshi The structural study of membrane proteins by electron crystallography Adv. Biophys. 35 1998 25 80
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 39
    • 0031773249 scopus 로고    scopus 로고
    • Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function
    • K. Goji M. Kuwahara Y. Gu M. Matsuo F. Marumo S. Sasaki Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function J. Clin. Endocrinol. Metab. 83 9 1998 3205 3209
    • (1998) J. Clin. Endocrinol. Metab. , vol.83 , Issue.9 , pp. 3205-3209
    • Goji, K.1    Kuwahara, M.2    Gu, Y.3    Matsuo, M.4    Marumo, F.5    Sasaki, S.6
  • 40
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy
    • E. Goormaghtigh V. Cabiaux J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy Subcell. Biochem. 23 1994 329 450
    • (1994) Subcell. Biochem. , vol.23 , pp. 329-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 41
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning
    • M.B. Gorin S.B. Yancey J. Cline J.-P. Revel J. Horwitz The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning Cell 39 1984 49 59
    • (1984) Cell , vol.39 , pp. 49-59
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3    Revel, J.-P.4    Horwitz, J.5
  • 43
    • 0021693911 scopus 로고
    • Surface reliefs derived from heavy-metal-shadowed specimens—Fourier space techniques applied to periodic objects
    • R. Guckenberger Surface reliefs derived from heavy-metal-shadowed specimens—Fourier space techniques applied to periodic objects Ultramicroscopy 16 1985 357 370
    • (1985) Ultramicroscopy , vol.16 , pp. 357-370
    • Guckenberger, R.1
  • 44
    • 0031858060 scopus 로고    scopus 로고
    • 2D crystallization of membrane proteins: Rationales and examples
    • L. Hasler J.B. Heymann A. Engel J. Kistler T. Walz 2D crystallization of membrane proteins: Rationales and examples J. Struct. Biol. 121 2 1998 162 171
    • (1998) J. Struct. Biol. , vol.121 , Issue.2 , pp. 162-171
    • Hasler, L.1    Heymann, J.B.2    Engel, A.3    Kistler, J.4    Walz, T.5
  • 45
    • 0032546752 scopus 로고    scopus 로고
    • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    • L. Hasler T. Walz P. Tittmann H. Gross J. Kistler A. Engel Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution J. Mol. Biol. 279 1998 855 864
    • (1998) J. Mol. Biol. , vol.279 , pp. 855-864
    • Hasler, L.1    Walz, T.2    Tittmann, P.3    Gross, H.4    Kistler, J.5    Engel, A.6
  • 46
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson J.M. Baldwin T.A. Ceska 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
  • 47
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • R. Henderson J.M. Baldwin K.H. Downing J. Lepault F. Zemlin Structure of purple membrane from Halobacterium halobium : Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution Ultramicroscopy 19 1986 147 178
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 48
    • 0034723156 scopus 로고    scopus 로고
    • Structural clues in the sequences of the aquaporins
    • B. Heymann A. Engel Structural clues in the sequences of the aquaporins J. Mol. Biol. 295 4 2000 1039 1053
    • (2000) J. Mol. Biol. , vol.295 , Issue.4 , pp. 1039-1053
    • Heymann, B.1    Engel, A.2
  • 49
    • 0033446707 scopus 로고    scopus 로고
    • Aquaporins: Phylogeny, structure and physiology of water channels
    • J. Heymann A. Engel Aquaporins: Phylogeny, structure and physiology of water channels News Physiolog. Sci. 14 1999 187 193
    • (1999) News Physiolog. Sci. , vol.14 , pp. 187-193
    • Heymann, J.1    Engel, A.2
  • 50
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • J.H. Hoh R. Lal S.A. John J.P. Revel M.F. Arndorf Atomic force microscopy and dissection of gap junctions Science 253 1991 1405 1408
    • (1991) Science , vol.253 , pp. 1405-1408
    • Hoh, J.H.1    Lal, R.2    John, S.A.3    Revel, J.P.4    Arndorf, M.F.5
  • 51
    • 0029647451 scopus 로고
    • Structure of the osmo-regulated H2O-channel, AQP-CHIP, in projection at 3.5 Å resolution
    • 2O-channel, AQP-CHIP, in projection at 3.5 Å resolution J. Mol. Biol. 251 1995 413 420
    • (1995) J. Mol. Biol. , vol.251 , pp. 413-420
    • Jap, B.K.1    Li, H.2
  • 53
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP. The hourglass model
    • J. Jung G. Preston B. Smith W. Guggino P. Agre Molecular structure of the water channel through aquaporin CHIP. The hourglass model J. Biol. Chem. 269 20 1994 14648 14654
    • (1994) J. Biol. Chem. , vol.269 , Issue.20 , pp. 14648-14654
    • Jung, J.1    Preston, G.2    Smith, B.3    Guggino, W.4    Agre, P.5
  • 54
    • 0020559760 scopus 로고
    • Arrangement of MP26 in lens junctional membranes: Analysis with proteases and antibodies
    • P. Keeling K. Johnson D. Sas K. Klukas P. Donahue R. Johnson Arrangement of MP26 in lens junctional membranes: Analysis with proteases and antibodies J. Membr Biol. 74 1983 217 228
    • (1983) J. Membr Biol. , vol.74 , pp. 217-228
    • Keeling, P.1    Johnson, K.2    Sas, D.3    Klukas, K.4    Donahue, P.5    Johnson, R.6
  • 56
    • 0019332210 scopus 로고
    • Lens gap junctions and orthogonal arrays are unrelated
    • J. Kistler S. Bullivant Lens gap junctions and orthogonal arrays are unrelated Febs Lett. 111 1 1980 73 78
    • (1980) Febs Lett. , vol.111 , Issue.1 , pp. 73-78
    • Kistler, J.1    Bullivant, S.2
  • 57
    • 0031556944 scopus 로고    scopus 로고
    • Characterization of the major intrinsic protein (MIP) from bovine fibre membranes by electron microscopy and hydrodynamics
    • N. Koenig G.A. Zampighi P.J.G. Butler Characterization of the major intrinsic protein (MIP) from bovine fibre membranes by electron microscopy and hydrodynamics J. Mol. Biol. 265 1997 590 602
    • (1997) J. Mol. Biol. , vol.265 , pp. 590-602
    • Koenig, N.1    Zampighi, G.A.2    Butler, P.J.G.3
  • 60
    • 0030915303 scopus 로고    scopus 로고
    • Molecular design of aquaporin-1 water channel as revealed by electron crystallography
    • H. Li S. Lee B.K. Jap Molecular design of aquaporin-1 water channel as revealed by electron crystallography Nat. Struct. Biol. 4 4 1997 263 265
    • (1997) Nat. Struct. Biol. , vol.4 , Issue.4 , pp. 263-265
    • Li, H.1    Lee, S.2    Jap, B.K.3
  • 61
    • 0021331726 scopus 로고
    • Phospholipase-induced crystallization of channels in mitochondrial outer membranes
    • C.A. Mannella Phospholipase-induced crystallization of channels in mitochondrial outer membranes Science 224 1984 165 166
    • (1984) Science , vol.224 , pp. 165-166
    • Mannella, C.A.1
  • 62
    • 0028795481 scopus 로고
    • redistribution of aquaporin-2 water channels induced by vasopressin in rat kidney inner medullary collecting duct
    • D. Marples M.A. Knepper E.I. Christensen S. Nielsen redistribution of aquaporin-2 water channels induced by vasopressin in rat kidney inner medullary collecting duct Am. J. Physiot. 269 1995 C655 C664 (3 Pt 1)
    • (1995) Am. J. Physiot. , vol.269 , pp. C655-C664
    • Marples, D.1    Knepper, M.A.2    Christensen, E.I.3    Nielsen, S.4
  • 63
    • 0028200818 scopus 로고
    • Functional characterization of the Escherichia coli glycerol facilitator, GIpF, in Xenopus oocytes
    • C. Maurel J. Reizer J.I. Schroeder M.J. chrispeels M.H. Saier Jr Functional characterization of the Escherichia coli glycerol facilitator, GIpF, in Xenopus oocytes J. Biol. Chem. 269 16 1994 11869 11872
    • (1994) J. Biol. Chem. , vol.269 , Issue.16 , pp. 11869-11872
    • Maurel, C.1    Reizer, J.2    Schroeder, J.I.3    chrispeels, M.J.4    Saier, M.H.5
  • 65
  • 66
    • 0030029859 scopus 로고    scopus 로고
    • High resolution surface structure of E. coli GroES oligomer by atomic force microscopy
    • J. Mou D.M. Czajkowsky S. Sheng R. Ho Z. shao High resolution surface structure of E. coli GroES oligomer by atomic force microscopy FEBS Lett. 381 1996 161 164
    • (1996) FEBS Lett. , vol.381 , pp. 161-164
    • Mou, J.1    Czajkowsky, D.M.2    Sheng, S.3    Ho, R.4    shao, Z.5
  • 69
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • D.J. Müller A. Engel The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions Biophys. J. 73 1997 1633 1644
    • (1997) Biophys. J. , vol.73 , pp. 1633-1644
    • Müller, D.J.1    Engel, A.2
  • 70
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • D.J. Müller A. Engel Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy J. Mol. Biol. 285 4 1999 1347 1351
    • (1999) J. Mol. Biol. , vol.285 , Issue.4 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 71
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • D.J. Müller G. Büldt A. Engel Force-induced conformational change of bacteriorhodopsin J. Mol. Biol. 249 1995 239 243
    • (1995) J. Mol. Biol. , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 72
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
    • D.J. Müller D. Fotiadis S. Scheuring S.A. Müller A. Engel Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope Biophys. J. 76 1999 1101 1111
    • (1999) Biophys. J. , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 73
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • D.J. Müller H.-J. Sass S. Müller G. Büldt A. Engel Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane J. Mol. Biol. 285 5 1999 1903 1909
    • (1999) J. Mol. Biol. , vol.285 , Issue.5 , pp. 1903-1909
    • Müller, D.J.1    Sass, H.-J.2    Müller, S.3    Büldt, G.4    Engel, A.5
  • 74
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • S. Müller K.N. Goldie R. Bürki R. Häring A. Engel Factors influencing the precision of quantitative scanning transmission electron microscopy Ultramicroscopy 46 1992 317 334
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.1    Goldie, K.N.2    Bürki, R.3    Häring, R.4    Engel, A.5
  • 75
    • 0031855721 scopus 로고    scopus 로고
    • Mass measurement in the scanning transmission electron microscope: A powerful tool for studying membrane proteins
    • S.A. Müller A. Engel Mass measurement in the scanning transmission electron microscope: A powerful tool for studying membrane proteins J. Struct. Biol. 121 2 1998 219 230
    • (1998) J. Struct. Biol. , vol.121 , Issue.2 , pp. 219-230
    • Müller, S.A.1    Engel, A.2
  • 76
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • J.H. Park M.H. Saier Phylogenetic characterization of the MIP family of transmembrane channel proteins J. Membr Biol. 153 3 1996 171 180
    • (1996) J. Membr Biol. , vol.153 , Issue.3 , pp. 171-180
    • Park, J.H.1    Saier, M.H.2
  • 77
    • 0020561113 scopus 로고
    • Preparation, characterization, and localization of antisera against bovine MIP26, an integral protein from lens fiber plasma membrane
    • D.L. Paul D.A. Goodenough Preparation, characterization, and localization of antisera against bovine MIP26, an integral protein from lens fiber plasma membrane J. Cell. Biol. 96 1983 625 632
    • (1983) J. Cell. Biol. , vol.96 , pp. 625-632
    • Paul, D.L.1    Goodenough, D.A.2
  • 78
    • 0030011088 scopus 로고    scopus 로고
    • Structure and dynamics of a proton wire: A theoretical study of H+ translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel Biophys. J. 71 1 1996 19 39
    • (1996) Biophys. J. , vol.71 , Issue.1 , pp. 19-39
    • Pomès, R.1    Roux, B.2
  • 79
    • 0026332210 scopus 로고
    • Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family
    • G.M. Preston E. Agre Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family Proc. Nat. Acad. Sci. USA 88 1991 11110 11114
    • (1991) , pp. 11110-11114
    • Preston, G.M.1    Agre, E.2
  • 80
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • G.M. Preston T.P. Carroll W.B. Guggino P. Agre Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein Science 256 1992 385 387
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 81
    • 0032578454 scopus 로고    scopus 로고
    • Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord
    • J.E. Rash T. Yasumura C.S. Hudson P. Agre S. Nielsen Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord Proc. Nat. Acad. Sci. USA 95 1998 11981 11986 20 )
    • (1998) , pp. 11981-11986
    • Rash, J.E.1    Yasumura, T.2    Hudson, C.S.3    Agre, P.4    Nielsen, S.5
  • 82
  • 83
    • 0033520347 scopus 로고    scopus 로고
    • Structure of the water channel AgpZ from Escherichia coli revealed by electron crystallography
    • P. Ringler M.J. Borgnia H. Stahlberg P. Agre A. Engel Structure of the water channel AgpZ from Escherichia coli revealed by electron crystallography J. Mol. Biol. 291 1999 1181 1190
    • (1999) J. Mol. Biol. , vol.291 , pp. 1181-1190
    • Ringler, P.1    Borgnia, M.J.2    Stahlberg, H.3    Agre, P.4    Engel, A.5
  • 84
    • 0021992990 scopus 로고
    • Junctions between lens fiber cells are labeled with a monoclonal antibody shown to be specific for MP26
    • D.F. Sas J. Sas K.R. Johnson A.S. Menko R.G. Johnson Junctions between lens fiber cells are labeled with a monoclonal antibody shown to be specific for MP26 J. Cell. Biol. 100 1985 216 225
    • (1985) J. Cell. Biol. , vol.100 , pp. 216-225
    • Sas, D.F.1    Sas, J.2    Johnson, K.R.3    Menko, A.S.4    Johnson, R.G.5
  • 85
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • W.O. Saxton W. Baumeister The correlation averaging of a regularly arranged bacterial cell envelope protein J. Microsc. 127 1982 127 138
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 86
    • 0018650401 scopus 로고
    • Digital image processing: The Semper system
    • W.O. Saxton T.J. Pitt M. Horer Digital image processing: The Semper system Ultramicroscopy 4 1979 343 354
    • (1979) Ultramicroscopy , vol.4 , pp. 343-354
    • Saxton, W.O.1    Pitt, T.J.2    Horer, M.3
  • 87
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
    • F.A. Schabert A. Engel Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy Biophys. J. 67 1994 2394 2403
    • (1994) Biophys. J. , vol.67 , pp. 2394-2403
    • Schabert, F.A.1    Engel, A.2
  • 88
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • F.A. Schabert C. Henn A. Engel Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy Science 268 1995 92 94
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 89
    • 0032923225 scopus 로고    scopus 로고
    • Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscopy
    • S. Scheuring D.J. Müller P. Ringler J.B. Heymann A. Engel Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscopy J. Microsc. 193 1999 28 35
    • (1999) J. Microsc. , vol.193 , pp. 28-35
    • Scheuring, S.1    Müller, D.J.2    Ringler, P.3    Heymann, J.B.4    Engel, A.5
  • 91
    • 0028365632 scopus 로고
    • Functional independence of monomeric CHIP28 water channels revealed by expression of wild-type mutant heterodimers
    • L. Shi W. Skach A. Verkman Functional independence of monomeric CHIP28 water channels revealed by expression of wild-type mutant heterodimers J. Biol. Chem. 269 14 1994 10417 10422
    • (1994) J. Biol. Chem. , vol.269 , Issue.14 , pp. 10417-10422
    • Shi, L.1    Skach, W.2    Verkman, A.3
  • 92
    • 0025922827 scopus 로고
    • Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins
    • r 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins J. Biol. Chem. 266 10 1991 6407 6415
    • (1991) J. Biol. Chem. , vol.266 , Issue.10 , pp. 6407-6415
    • Smith, B.L.1    Agre, P.2
  • 93
    • 0017648837 scopus 로고
    • Surface reliefs computed from micrographs of heavy metal-shadowed specimens
    • P.R. Smith J. Kistler Surface reliefs computed from micrographs of heavy metal-shadowed specimens J. Ultrastruct. Res. 61 1977 124 133
    • (1977) J. Ultrastruct. Res. , vol.61 , pp. 124-133
    • Smith, P.R.1    Kistler, J.2
  • 94
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • T.D. Schneider R.M. Stephens Sequence logos: A new way to display consensus sequences Nucl. Acids Res. 18 1990 6097 6100
    • (1990) Nucl. Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 95
    • 0023067967 scopus 로고
    • A new resolution criterion based on spectral signalto-noise ratios
    • M. Unser D.L. Trus A.C. Steven A new resolution criterion based on spectral signalto-noise ratios Ultramicroscopy 23 1987 39 52
    • (1987) Ultramicroscopy , vol.23 , pp. 39-52
    • Unser, M.1    Trus, D.L.2    Steven, A.C.3
  • 96
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analysing the images of biological macromolecules
    • M. van Heel J. Frank Use of multivariate statistics in analysing the images of biological macromolecules Ultramicroscopy 6 1981 187 194
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • van Heel, M.1    Frank, J.2
  • 100
    • 0027410583 scopus 로고
    • Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator
    • R.T. Voegele G.D. Sweet W. Boos Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator J. Bacteriol. 175 4 1993 1087 1094
    • (1993) J. Bacteriol. , vol.175 , Issue.4 , pp. 1087-1094
    • Voegele, R.T.1    Sweet, G.D.2    Boos, W.3
  • 101
    • 0031877370 scopus 로고    scopus 로고
    • Electron crystallography of two-dimensional crystals of membrane proteins
    • T. Walz N. Grigorieff Electron crystallography of two-dimensional crystals of membrane proteins J. Struct. Biol. 121 2 1998 142 161
    • (1998) J. Struct. Biol. , vol.121 , Issue.2 , pp. 142-161
    • Walz, T.1    Grigorieff, N.2
  • 102
    • 0028275784 scopus 로고
    • The three-dimensional structure of human erythrocyte aquaporin CHIP
    • T. Walz B. Smith E. Agre A. Engel The three-dimensional structure of human erythrocyte aquaporin CHIP EMBO J. 13 13 1994 2985 2993
    • (1994) EMBO J. , vol.13 , Issue.13 , pp. 2985-2993
    • Walz, T.1    Smith, B.2    Agre, E.3    Engel, A.4
  • 103
    • 0028175266 scopus 로고
    • Biologically active two-dimensional crystals of aquaporin CHIP
    • T. Walz B. Smith M. Zeidel A. Engel P. Agre Biologically active two-dimensional crystals of aquaporin CHIP J. Biol. Chem. 269 3 1994 1583 1586
    • (1994) J. Biol. Chem. , vol.269 , Issue.3 , pp. 1583-1586
    • Walz, T.1    Smith, B.2    Zeidel, M.3    Engel, A.4    Agre, P.5
  • 104
    • 0029375244 scopus 로고
    • Projection map of aquaporin-1 determined by electron crystallography
    • T. Walz D. Typke B.L. Smith P. Agre A. Engel Projection map of aquaporin-1 determined by electron crystallography Nat. Struct. Biol. 2 9 1995 730 732
    • (1995) Nat. Struct. Biol. , vol.2 , Issue.9 , pp. 730-732
    • Walz, T.1    Typke, D.2    Smith, B.L.3    Agre, P.4    Engel, A.5
  • 107
    • 4244146207 scopus 로고    scopus 로고
    • Three-dimensional crystallization and preliminary characterization of human aquaporin-1
    • M.C. Wiener Three-dimensional crystallization and preliminary characterization of human aquaporin-1 Biophys. J. 76 1999 A277
    • (1999) Biophys. J. , vol.76 , pp. A277
    • Wiener, M.C.1
  • 108
    • 0025853910 scopus 로고
    • Tandem sequence repeats in transmembrane channel proteins
    • G. Wistow M. Pisano A. Chepelinsky Tandem sequence repeats in transmembrane channel proteins Trends Biochem. Sci. 16 5 1991 170 171
    • (1991) Trends Biochem. Sci. , vol.16 , Issue.5 , pp. 170-171
    • Wistow, G.1    Pisano, M.2    Chepelinsky, A.3
  • 110
    • 0024312337 scopus 로고
    • The structural organization and protein composition of lens fiber junctions
    • G.A. Zampighi J.E. Hall G.R. Ehring S.A. Simon The structural organization and protein composition of lens fiber junctions J. Cell. Biol. 108 1989 2255 2275
    • (1989) J. Cell. Biol. , vol.108 , pp. 2255-2275
    • Zampighi, G.A.1    Hall, J.E.2    Ehring, G.R.3    Simon, S.A.4
  • 111
    • 0026806764 scopus 로고
    • Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
    • M.L. Zeidel S.V. Ambudkar B.L. Smith P. Agre Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein Biochemistry 31 1992 7436 7440
    • (1992) Biochemistry , vol.31 , pp. 7436-7440
    • Zeidel, M.L.1    Ambudkar, S.V.2    Smith, B.L.3    Agre, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.