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Volumn 20, Issue 9, 2012, Pages 1540-1549

β-Barrel mobility underlies closure of the voltage-dependent anion channel

Author keywords

[No Author keywords available]

Indexed keywords

VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84865760948     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.06.015     Document Type: Article
Times cited : (97)

References (62)
  • 4
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • R. Benz Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins Biochim. Biophys. Acta 1197 1994 167 196
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 5
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • R. Benz, K. Janko, W. Boos, and P. Läuger Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli Biochim. Biophys. Acta 511 1978 305 319
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Läuger, P.4
  • 6
    • 0026872512 scopus 로고
    • Studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived "porin 31HL" are similar to those of mitochondrial porins
    • R. Benz, E. Maier, F.P. Thinnes, H. Götz, and N. Hilschmann Studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived "Porin 31HL" are similar to those of mitochondrial porins Biol. Chem. Hoppe Seyler 373 1992 295 303
    • (1992) Biol. Chem. Hoppe Seyler , vol.373 , pp. 295-303
    • Benz, R.1    Maier, E.2    Thinnes, F.P.3    Götz, H.4    Hilschmann, N.5
  • 8
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • O. Berger, O. Edholm, and F. Jähnig Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys. J. 72 1997 2002 2013
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jähnig, F.3
  • 10
    • 0024458675 scopus 로고
    • Voltage gating in the mitochondrial channel, VDAC
    • M. Colombini Voltage gating in the mitochondrial channel, VDAC J. Membr. Biol. 111 1989 103 111
    • (1989) J. Membr. Biol. , vol.111 , pp. 103-111
    • Colombini, M.1
  • 11
    • 0842345400 scopus 로고    scopus 로고
    • VDAC: The channel at the interface between mitochondria and the cytosol
    • M. Colombini VDAC: the channel at the interface between mitochondria and the cytosol Mol. Cell. Biochem. 256-257 2004 107 115
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 107-115
    • Colombini, M.1
  • 13
    • 0022707338 scopus 로고
    • The selectivity filter of voltage-dependent channels formed by phosphoporin (PhoE protein) from E. coli
    • B. Dargent, W. Hofmann, F. Pattus, and J.P. Rosenbusch The selectivity filter of voltage-dependent channels formed by phosphoporin (PhoE protein) from E. coli EMBO J. 5 1986 773 778
    • (1986) EMBO J. , vol.5 , pp. 773-778
    • Dargent, B.1    Hofmann, W.2    Pattus, F.3    Rosenbusch, J.P.4
  • 14
    • 0025788323 scopus 로고
    • Peptide-specific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin
    • V. De Pinto, G. Prezioso, F. Thinnes, T.A. Link, and F. Palmieri Peptide-specific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin Biochemistry 30 1991 10191 10200
    • (1991) Biochemistry , vol.30 , pp. 10191-10200
    • De Pinto, V.1    Prezioso, G.2    Thinnes, F.3    Link, T.A.4    Palmieri, F.5
  • 15
    • 34250851879 scopus 로고    scopus 로고
    • Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore
    • V. De Pinto, F. Tomasello, A. Messina, F. Guarino, R. Benz, D. La Mendola, A. Magrì, D. Milardi, and G. Pappalardo Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore ChemBioChem 8 2007 744 756
    • (2007) ChemBioChem , vol.8 , pp. 744-756
    • De Pinto, V.1    Tomasello, F.2    Messina, A.3    Guarino, F.4    Benz, R.5    La Mendola, D.6    Magrì, A.7    Milardi, D.8    Pappalardo, G.9
  • 16
    • 52449134572 scopus 로고    scopus 로고
    • Structure of the voltage dependent anion channel: State of the art
    • V. De Pinto, S. Reina, F. Guarino, and A. Messina Structure of the voltage dependent anion channel: state of the art J. Bioenerg. Biomembr. 40 2008 139 147
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 139-147
    • De Pinto, V.1    Reina, S.2    Guarino, F.3    Messina, A.4
  • 17
    • 34748835813 scopus 로고    scopus 로고
    • High-level expression, refolding and probing the natural fold of the human voltage-dependent anion channel isoforms i and II
    • H. Engelhardt, T. Meins, M. Poynor, V. Adams, S. Nussberger, W. Welte, and K. Zeth High-level expression, refolding and probing the natural fold of the human voltage-dependent anion channel isoforms I and II J. Membr. Biol. 216 2007 93 105
    • (2007) J. Membr. Biol. , vol.216 , pp. 93-105
    • Engelhardt, H.1    Meins, T.2    Poynor, M.3    Adams, V.4    Nussberger, S.5    Welte, W.6    Zeth, K.7
  • 18
    • 0029016857 scopus 로고
    • Molecular design of the voltage-dependent, anion-selective channel in the mitochondrial outer membrane
    • X.W. Guo, P.R. Smith, B. Cognon, D. D'Arcangelis, E. Dolginova, and C.A. Mannella Molecular design of the voltage-dependent, anion-selective channel in the mitochondrial outer membrane J. Struct. Biol. 114 1995 41 59
    • (1995) J. Struct. Biol. , vol.114 , pp. 41-59
    • Guo, X.W.1    Smith, P.R.2    Cognon, B.3    D'Arcangelis, D.4    Dolginova, E.5    Mannella, C.A.6
  • 19
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • T. Haltia, and E. Freire Forces and factors that contribute to the structural stability of membrane proteins Biochim. Biophys. Acta 1241 1995 295 322
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 20
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 21
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • S. Hiller, R.G. Garces, T.J. Malia, V.Y. Orekhov, M. Colombini, and G. Wagner Solution structure of the integral human membrane protein VDAC-1 in detergent micelles Science 321 2008 1206 1210
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 23
    • 0033134460 scopus 로고    scopus 로고
    • Collective membrane motions in the mesoscopic range and their modulation by the binding of a monomolecular protein layer of streptavidin studied by dynamic light scattering
    • R. Hirn, R. Benz, and T.M. Bayerl Collective membrane motions in the mesoscopic range and their modulation by the binding of a monomolecular protein layer of streptavidin studied by dynamic light scattering Phys. Rev. E 59 5 Pt B 1999 5987 5994
    • (1999) Phys. Rev. e , vol.59 , Issue.5 PART B , pp. 5987-5994
    • Hirn, R.1    Benz, R.2    Bayerl, T.M.3
  • 24
    • 0000432697 scopus 로고    scopus 로고
    • Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy
    • M. Hohwy, C.M. Rienstra, C.P. Jaroniec, and R.G. Griffin Fivefold symmetric homonuclear dipolar recoupling in rotating solids: application to double quantum spectroscopy J. Chem. Phys. 110 1999 7983 7992
    • (1999) J. Chem. Phys. , vol.110 , pp. 7983-7992
    • Hohwy, M.1    Rienstra, C.M.2    Jaroniec, C.P.3    Griffin, R.G.4
  • 25
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • V. Hornak, R. Abel, A. Okur, B. Strockbine, A. Roitberg, and C. Simmerling Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 26
    • 49749095639 scopus 로고    scopus 로고
    • Lipids and membrane protein structures
    • C. Hunte, and S. Richers Lipids and membrane protein structures Curr. Opin. Struct. Biol. 18 2008 406 411
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 406-411
    • Hunte, C.1    Richers, S.2
  • 27
    • 80052503022 scopus 로고    scopus 로고
    • Computational electrophysiology: The molecular dynamics of ion channel permeation and selectivity in atomistic detail
    • C. Kutzner, H. Grubmüller, B.L. de Groot, and U. Zachariae Computational electrophysiology: the molecular dynamics of ion channel permeation and selectivity in atomistic detail Biophys. J. 101 2011 809 817
    • (2011) Biophys. J. , vol.101 , pp. 809-817
    • Kutzner, C.1    Grubmüller, H.2    De Groot, B.L.3    Zachariae, U.4
  • 28
    • 0024833498 scopus 로고
    • The voltage-dependent activity of Escherichia coli porins in different planar bilayer reconstitutions
    • J.H. Lakey, and F. Pattus The voltage-dependent activity of Escherichia coli porins in different planar bilayer reconstitutions Eur. J. Biochem. 186 1989 303 308
    • (1989) Eur. J. Biochem. , vol.186 , pp. 303-308
    • Lakey, J.H.1    Pattus, F.2
  • 29
    • 0029897494 scopus 로고    scopus 로고
    • Porins of Escherichia coli: Unidirectional gating by pressure
    • A.C. Le Dain, C.C. Häse, J. Tommassen, and B. Martinac Porins of Escherichia coli: unidirectional gating by pressure EMBO J. 15 1996 3524 3528
    • (1996) EMBO J. , vol.15 , pp. 3524-3528
    • Le Dain, A.C.1    Häse, C.C.2    Tommassen, J.3    Martinac, B.4
  • 30
    • 79551659527 scopus 로고    scopus 로고
    • Brownian dynamics simulations of ion transport through the VDAC
    • K.I. Lee, H. Rui, R.W. Pastor, and W. Im Brownian dynamics simulations of ion transport through the VDAC Biophys. J. 100 2011 611 619
    • (2011) Biophys. J. , vol.100 , pp. 611-619
    • Lee, K.I.1    Rui, H.2    Pastor, R.W.3    Im, W.4
  • 31
    • 0031448082 scopus 로고    scopus 로고
    • Minireview: On the structure and gating mechanism of the mitochondrial channel, VDAC
    • C.A. Mannella Minireview: on the structure and gating mechanism of the mitochondrial channel, VDAC J. Bioenerg. Biomembr. 29 1997 525 531
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 525-531
    • Mannella, C.A.1
  • 32
    • 0031857554 scopus 로고    scopus 로고
    • Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications
    • C.A. Mannella Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications J. Struct. Biol. 121 1998 207 218
    • (1998) J. Struct. Biol. , vol.121 , pp. 207-218
    • Mannella, C.A.1
  • 34
    • 80052090331 scopus 로고    scopus 로고
    • Solution NMR studies of polytopic α-helical membrane proteins
    • D. Nietlispach, and A. Gautier Solution NMR studies of polytopic α-helical membrane proteins Curr. Opin. Struct. Biol. 21 2011 497 508
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 497-508
    • Nietlispach, D.1    Gautier, A.2
  • 35
    • 0026696184 scopus 로고
    • Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel
    • discussion 131-135
    • S. Peng, E. Blachly-Dyson, M. Forte, and M. Colombini Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel Biophys. J. 62 1992 123 131 discussion 131-135
    • (1992) Biophys. J. , vol.62 , pp. 123-131
    • Peng, S.1    Blachly-Dyson, E.2    Forte, M.3    Colombini, M.4
  • 36
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • E. Perozo, D.M. Cortes, P. Sompornpisut, A. Kloda, and B. Martinac Open channel structure of MscL and the gating mechanism of mechanosensitive channels Nature 418 2002 942 948
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 37
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • R. Phillips, T. Ursell, P. Wiggins, and P. Sens Emerging roles for lipids in shaping membrane-protein function Nature 459 2009 379 385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 38
    • 76049107193 scopus 로고    scopus 로고
    • Simulations of anion transport through OprP reveal the molecular basis for high affinity and selectivity for phosphate
    • P. Pongprayoon, O. Beckstein, C.L. Wee, and M.S. Sansom Simulations of anion transport through OprP reveal the molecular basis for high affinity and selectivity for phosphate Proc. Natl. Acad. Sci. USA 106 2009 21614 21618
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21614-21618
    • Pongprayoon, P.1    Beckstein, O.2    Wee, C.L.3    Sansom, M.S.4
  • 39
    • 0029920281 scopus 로고    scopus 로고
    • The role of the N and C termini of recombinant Neurospora mitochondrial porin in channel formation and voltage-dependent gating
    • B. Popp, D.A. Court, R. Benz, W. Neupert, and R. Lill The role of the N and C termini of recombinant Neurospora mitochondrial porin in channel formation and voltage-dependent gating J. Biol. Chem. 271 1996 13593 13599
    • (1996) J. Biol. Chem. , vol.271 , pp. 13593-13599
    • Popp, B.1    Court, D.A.2    Benz, R.3    Neupert, W.4    Lill, R.5
  • 40
    • 0020476642 scopus 로고
    • Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria
    • N. Roos, R. Benz, and D. Brdiczka Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria Biochim. Biophys. Acta 686 1982 204 214
    • (1982) Biochim. Biophys. Acta , vol.686 , pp. 204-214
    • Roos, N.1    Benz, R.2    Brdiczka, D.3
  • 41
    • 33845983303 scopus 로고    scopus 로고
    • Voltage gating of VDAC is regulated by nonlamellar lipids of mitochondrial membranes
    • T.K. Rostovtseva, N. Kazemi, M. Weinrich, and S.M. Bezrukov Voltage gating of VDAC is regulated by nonlamellar lipids of mitochondrial membranes J. Biol. Chem. 281 2006 37496 37506
    • (2006) J. Biol. Chem. , vol.281 , pp. 37496-37506
    • Rostovtseva, T.K.1    Kazemi, N.2    Weinrich, M.3    Bezrukov, S.M.4
  • 42
    • 79551677025 scopus 로고    scopus 로고
    • Molecular dynamics studies of ion permeation in VDAC
    • H. Rui, K.I. Lee, R.W. Pastor, and W. Im Molecular dynamics studies of ion permeation in VDAC Biophys. J. 100 2011 602 610
    • (2011) Biophys. J. , vol.100 , pp. 602-610
    • Rui, H.1    Lee, K.I.2    Pastor, R.W.3    Im, W.4
  • 43
    • 33646155114 scopus 로고    scopus 로고
    • Deletion variants of Neurospora mitochondrial porin: Electrophysiological and spectroscopic analysis
    • G. Runke, E. Maier, W.A.T. Summers, D.C. Bay, R. Benz, and D.A. Court Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis Biophys. J. 90 2006 3155 3164
    • (2006) Biophys. J. , vol.90 , pp. 3155-3164
    • Runke, G.1    Maier, E.2    Summers, W.A.T.3    Bay, D.C.4    Benz, R.5    Court, D.A.6
  • 44
    • 0019555702 scopus 로고
    • Matrix protein in planar membranes: Clusters of channels in a native environment and their functional reassembly
    • H. Schindler, and J.P. Rosenbusch Matrix protein in planar membranes: clusters of channels in a native environment and their functional reassembly Proc. Natl. Acad. Sci. USA 78 1981 2302 2306
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2302-2306
    • Schindler, H.1    Rosenbusch, J.P.2
  • 45
    • 58049194119 scopus 로고    scopus 로고
    • Voltage-dependent K+ channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane
    • D. Schmidt, and R. MacKinnon Voltage-dependent K+ channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane Proc. Natl. Acad. Sci. USA 105 2008 19276 19281
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19276-19281
    • Schmidt, D.1    MacKinnon, R.2
  • 47
    • 74849131082 scopus 로고    scopus 로고
    • Probing molecular motion by double-quantum (13C,13C) solid-state NMR spectroscopy: Application to ubiquitin
    • R. Schneider, K. Seidel, M. Etzkorn, A. Lange, S. Becker, and M. Baldus Probing molecular motion by double-quantum (13C,13C) solid-state NMR spectroscopy: application to ubiquitin J. Am. Chem. Soc. 132 2010 223 233
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 223-233
    • Schneider, R.1    Seidel, K.2    Etzkorn, M.3    Lange, A.4    Becker, S.5    Baldus, M.6
  • 48
    • 52449116862 scopus 로고    scopus 로고
    • Uncovering the role of VDAC in the regulation of cell life and death
    • V. Shoshan-Barmatz, N. Keinan, and H. Zaid Uncovering the role of VDAC in the regulation of cell life and death J. Bioenerg. Biomembr. 40 2008 183 191
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 183-191
    • Shoshan-Barmatz, V.1    Keinan, N.2    Zaid, H.3
  • 50
    • 0031806216 scopus 로고    scopus 로고
    • The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes
    • J. Song, C. Midson, E. Blachly-Dyson, M. Forte, and M. Colombini The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes Biophys. J. 74 1998 2926 2944
    • (1998) Biophys. J. , vol.74 , pp. 2926-2944
    • Song, J.1    Midson, C.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 51
    • 0036280794 scopus 로고    scopus 로고
    • Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes
    • S. Sukharev Purification of the small mechanosensitive channel of Escherichia coli (MscS): the subunit structure, conduction, and gating characteristics in liposomes Biophys. J. 83 2002 290 298
    • (2002) Biophys. J. , vol.83 , pp. 290-298
    • Sukharev, S.1
  • 52
    • 84859488878 scopus 로고    scopus 로고
    • Affixing the N-terminal alpha helix of the voltage dependent anion channel to the channel's wall does not prevent its voltage gating
    • O. Teijido, R. Ujwal, C.O. Hillerdal, L. Kullman, T.K. Rostovtseva, and J. Abramson Affixing the N-terminal alpha helix of the voltage dependent anion channel to the channel's wall does not prevent its voltage gating J. Biol. Chem. 287 2012 11437 11445
    • (2012) J. Biol. Chem. , vol.287 , pp. 11437-11445
    • Teijido, O.1    Ujwal, R.2    Hillerdal, C.O.3    Kullman, L.4    Rostovtseva, T.K.5    Abramson, J.6
  • 53
    • 0027315863 scopus 로고
    • Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel
    • L. Thomas, E. Blachly-Dyson, M. Colombini, and M. Forte Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel Proc. Natl. Acad. Sci. USA 90 1993 5446 5449
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5446-5449
    • Thomas, L.1    Blachly-Dyson, E.2    Colombini, M.3    Forte, M.4
  • 54
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • D.P. Tieleman, and H.J. Berendsen A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer Biophys. J. 74 1998 2786 2801
    • (1998) Biophys. J. , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.2
  • 57
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • W.C. Wimley The versatile beta-barrel membrane protein Curr. Opin. Struct. Biol. 13 2003 404 411
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 58
    • 77954256616 scopus 로고    scopus 로고
    • G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • M.G. Wolf, M. Hoefling, C. Aponte-Santamaría, H. Grubmüller, and G. Groenhof g-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation J. Comput. Chem. 31 2010 2169 2174
    • (2010) J. Comput. Chem. , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaría, C.3    Grubmüller, H.4    Groenhof, G.5
  • 60
    • 33646354636 scopus 로고    scopus 로고
    • High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32
    • U. Zachariae, T. Klühspies, S. De, H. Engelhardt, and K. Zeth High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32 J. Biol. Chem. 281 2006 7413 7420
    • (2006) J. Biol. Chem. , vol.281 , pp. 7413-7420
    • Zachariae, U.1    Klühspies, T.2    De, S.3    Engelhardt, H.4    Zeth, K.5
  • 62
    • 0023041574 scopus 로고
    • Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel
    • J. Zimmerberg, and V.A. Parsegian Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel Nature 323 1986 36 39
    • (1986) Nature , vol.323 , pp. 36-39
    • Zimmerberg, J.1    Parsegian, V.A.2


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