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Volumn 1838, Issue 11, 2014, Pages 2838-2851

The pore-lining regions in cytochrome c oxidases: A computational analysis of caveolin, cholesterol and transmembrane helix contributions to proton movement

Author keywords

Caveolin; Channels; Cholesterol; COX 1; Cytochrome c oxidase; Protein topology

Indexed keywords

CAVEOLIN; CHOLESTEROL; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; CYCLOOXYGENASE 3; CYTOCHROME C OXIDASE;

EID: 84905600658     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.07.011     Document Type: Article
Times cited : (7)

References (56)
  • 1
    • 0030983047 scopus 로고    scopus 로고
    • Architecture of helix bundle membrane proteins: An analysis of cytochrome c oxidase from bovine mitochondria
    • E. Wallin, T. Tsukihara, S. Yoshikawa, G. Von Heijne, and A. Elofsson Architecture of helix bundle membrane proteins: an analysis of cytochrome c oxidase from bovine mitochondria Protein Sci. 6 1997 808 815 (Pubitemid 27154807)
    • (1997) Protein Science , vol.6 , Issue.4 , pp. 808-815
    • Wallin, E.1    Tsukihara, T.2    Yoshikawa, S.3    Von Heijne, G.4    Elofsson, A.5
  • 2
    • 0642283837 scopus 로고    scopus 로고
    • Cytochrome c oxidase - Structure, function, and physiology of a redox-driven molecular machine
    • O.-M.H. Richter, and B. Ludwig Cytochrome c oxidase - structure, function, and physiology of a redox-driven molecular machine Rev. Physiol. Biochem. Pharmacol. 147 2003 47 74
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.147 , pp. 47-74
    • Richter, O.-M.H.1    Ludwig, B.2
  • 4
    • 84886288179 scopus 로고    scopus 로고
    • Current advances in research of cytochrome c oxidase
    • D.M. Popovic Current advances in research of cytochrome c oxidase Amino Acids 45 2013 1073 1087
    • (2013) Amino Acids , vol.45 , pp. 1073-1087
    • Popovic, D.M.1
  • 5
    • 34250865041 scopus 로고    scopus 로고
    • Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure
    • DOI 10.1021/bi700548a
    • J. Stanicova, E. Sedlak, A. Musatov, and N.C. Robinson Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure Biochemistry 46 2007 7146 7152 (Pubitemid 46978203)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7146-7152
    • Stanicova, J.1    Sedlak, E.2    Musatov, A.3    Robinson, N.C.4
  • 6
    • 20444468821 scopus 로고    scopus 로고
    • The inner mitochondrial membrane has aquaporin-8 water channels and is highly permeable to water
    • DOI 10.1074/jbc.C400595200
    • G. Calamita, D. Ferri, P. Gena, G.E. Liquori, A. Cavalier, D. Thomas, and M. Svelto The inner mitochondrial membrane has aquaporin-8 water channels and is highly permeable to water J. Biol. Chem. 280 2005 17149 17153 (Pubitemid 41389180)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17149-17153
    • Calamita, G.1    Ferri, D.2    Gena, P.3    Liquori, G.E.4    Cavalier, A.5    Thomas, D.6    Svelto, M.7
  • 7
    • 0035031405 scopus 로고    scopus 로고
    • Cell-specific targeting of caveolin-1 to caveolae, secretory vesicles, cytoplasm or mitochondria
    • W.P. Li, P. Liu, B.K. Pilcher, and R.G. Anderson Cell-specific targeting of caveolin-1 to caveolae, secretory vesicles, cytoplasm or mitochondria J. Cell Sci. 114 2001 1397 1408 (Pubitemid 32409475)
    • (2001) Journal of Cell Science , vol.114 , Issue.7 , pp. 1397-1408
    • Li, W.-P.1    Liu, P.2    Pilcher, B.K.3    Anderson, R.G.W.4
  • 8
    • 80053601906 scopus 로고    scopus 로고
    • Mitochondrial cholesterol: A connection between caveolin, metabolism and disease
    • M. Bosch, M. Mari, S.P. Gross, J.C. Fernandez-Checa, and A. Pol Mitochondrial cholesterol: a connection between caveolin, metabolism and disease Traffic 12 2011 1483 1489
    • (2011) Traffic , vol.12 , pp. 1483-1489
    • Bosch, M.1    Mari, M.2    Gross, S.P.3    Fernandez-Checa, J.C.4    Pol, A.5
  • 9
    • 84868278452 scopus 로고    scopus 로고
    • Mitochondrial-localized caveolin in adaption to cellular stress and injury
    • H.N. Fridolfsson, Y. Kawaraguchi, S.S. Ali, and M. Panneerselvam Mitochondrial-localized caveolin in adaption to cellular stress and injury FASEB J. 26 2012 4637 4649
    • (2012) FASEB J. , vol.26 , pp. 4637-4649
    • Fridolfsson, H.N.1    Kawaraguchi, Y.2    Ali, S.S.3    Panneerselvam, M.4
  • 10
    • 44949272730 scopus 로고
    • A time-efficient, linear space local similarity algorithm
    • X. Huang, and W. Miller A time-efficient, linear space local similarity algorithm Adv. Appl. Math. 12 1991 337 357
    • (1991) Adv. Appl. Math. , vol.12 , pp. 337-357
    • Huang, X.1    Miller, W.2
  • 11
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405 (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 14
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • DOI 10.1016/j.jmb.2004.03.016, PII S0022283604002943
    • L. Kall, A. Krogh, and E.L.L. Sonnhammer A combined transmembrane topology and signal peptide prediction method J. Mol. Biol. 338 2004 1027 1036 (Pubitemid 38542831)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.5 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.L.3
  • 15
    • 84865484068 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction in support vector machines
    • T. Nugent, and D.T. Jones Transmembrane protein topology prediction in support vector machines BMC Bioinformatics 19 2009 874 881
    • (2009) BMC Bioinformatics , vol.19 , pp. 874-881
    • Nugent, T.1    Jones, D.T.2
  • 16
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • A. Krogh, B. Larsson, G. von Heijne, and E.L.L. Sonnhammer Predicting transmembrane protein topology with a Hidden Markov Model: application to complete genomes J. Mol. Biol. 305 2001 567 580 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 17
    • 84866158866 scopus 로고    scopus 로고
    • Detecting pore-lining regions in transmembrane protein sequences
    • T. Nugent, and D.T. Jones Detecting pore-lining regions in transmembrane protein sequences BMC Bioinformatics 13 2012 169 178
    • (2012) BMC Bioinformatics , vol.13 , pp. 169-178
    • Nugent, T.1    Jones, D.T.2
  • 18
    • 79959336987 scopus 로고    scopus 로고
    • TMKink: A method to predict transmembrane helix kinks
    • A.D. Meruelo, I. Samish, and J.U. Bowie TMKink: a method to predict transmembrane helix kinks Protein Sci. 20 2011 1256 1264
    • (2011) Protein Sci. , vol.20 , pp. 1256-1264
    • Meruelo, A.D.1    Samish, I.2    Bowie, J.U.3
  • 19
    • 68249097450 scopus 로고    scopus 로고
    • PoreWalker: A novel tool for the identification and characterization of channels in transmembrane proteins from their three-dimensional structure
    • M. Pellegrini-Calace, T. Malwald, and J.M. Thornton PoreWalker: a novel tool for the identification and characterization of channels in transmembrane proteins from their three-dimensional structure PLoS Comput. Biol. 5 2009 1 16
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1-16
    • Pellegrini-Calace, M.1    Malwald, T.2    Thornton, J.M.3
  • 20
    • 77953625243 scopus 로고    scopus 로고
    • MPRAP: An accessibility predictor for a-helical transmembrane proteins that performs well inside and outside the membrane
    • K. Illergard, S. Callegari, and A. Elofsson MPRAP: an accessibility predictor for a-helical transmembrane proteins that performs well inside and outside the membrane BMC Bioinformatics 11 2010 333 344
    • (2010) BMC Bioinformatics , vol.11 , pp. 333-344
    • Illergard, K.1    Callegari, S.2    Elofsson, A.3
  • 22
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins
    • J. Couvet, M. Sargiacomo, and M.P. Lisanti Interaction of a receptor tyrosine kinase, EGF-R, with caveolins J. Biol. Chem. 272 1997 30429 30438
    • (1997) J. Biol. Chem. , vol.272 , pp. 30429-30438
    • Couvet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 23
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • H. Li, and V. Papadopoulos Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consenous pattern Endocrinology 139 1998 4991 4997 (Pubitemid 28533447)
    • (1998) Endocrinology , vol.139 , Issue.12 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 24
    • 84860158205 scopus 로고    scopus 로고
    • Disclosure of cholesterol recognition motifs in transmembrane domains of human nicoticin acetylcholine receptor
    • doi:10.1038/srep00069
    • C.J. Baier, J. Fantini, F.J. Barrantes, Disclosure of cholesterol recognition motifs in transmembrane domains of human nicoticin acetylcholine receptor, Sci. Rep. 1, 2011, 69, http://dx.doi.org/10.1038/srep00069.
    • (2011) Sci. Rep. , vol.1 , pp. 69
    • Baier, C.J.1    Fantini, J.2    Barrantes, F.J.3
  • 25
    • 67649472570 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction using support vector machines
    • T. Nugent, and D.T. Jones Transmembrane protein topology prediction using support vector machines BMC Bioinformatics 10 2009 159 170
    • (2009) BMC Bioinformatics , vol.10 , pp. 159-170
    • Nugent, T.1    Jones, D.T.2
  • 27
    • 84874298962 scopus 로고    scopus 로고
    • Identification of cardiolipin binding sites on cytochrome c oxidase at the entrance of proton channels
    • 10.1038/srep01263
    • C. Arnarez, S.J. Marrink, and X. Periole Identification of cardiolipin binding sites on cytochrome c oxidase at the entrance of proton channels Sci. Rep. 3 2013 1263 10.1038/srep01263
    • (2013) Sci. Rep. , vol.3 , pp. 1263
    • Arnarez, C.1    Marrink, S.J.2    Periole, X.3
  • 28
    • 67349266230 scopus 로고    scopus 로고
    • Position of helical kinks in membrane protein crystal structures and the accuracy of computational prediction
    • S.E. Hall, K. Roberts, and N. Vaidehi Position of helical kinks in membrane protein crystal structures and the accuracy of computational prediction J. Mol. Graph. Model. 27 2009 944 950
    • (2009) J. Mol. Graph. Model. , vol.27 , pp. 944-950
    • Hall, S.E.1    Roberts, K.2    Vaidehi, N.3
  • 29
    • 78650702465 scopus 로고    scopus 로고
    • Improved helix and kink characterization in membrane proteins allows evaluation of kink sequence predictors
    • D.N. Langelaan, M. Wieczorek, C. Biouin, and J.K. Rainey Improved helix and kink characterization in membrane proteins allows evaluation of kink sequence predictors J. Chem. Inf. Model. 50 2010 2213 2220
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 2213-2220
    • Langelaan, D.N.1    Wieczorek, M.2    Biouin, C.3    Rainey, J.K.4
  • 30
    • 0036343993 scopus 로고    scopus 로고
    • Conformational dynamics of helix S6 from Shaker potassium channel simulation studies
    • J.N. Bright, I.H. Shrivastava, F.S. Cordes, and M.S.P. Sansom Conformational dynamics of helix S6 from Shaker potassium channel simulation studies Biopolymers 64 2002 303 313
    • (2002) Biopolymers , vol.64 , pp. 303-313
    • Bright, J.N.1    Shrivastava, I.H.2    Cordes, F.S.3    Sansom, M.S.P.4
  • 31
    • 0037174606 scopus 로고    scopus 로고
    • β2 Adrenergic receptor activation: Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • DOI 10.1074/jbc.M206801200
    • L. Shi, G. Liapakia, R. Xu, F. Guarnieri, J.A. Ballesteros, and J.A. Javich Beta 2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch J. Biol. Chem. 277 2002 40989 40996 (Pubitemid 35215688)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 32
    • 60849099626 scopus 로고    scopus 로고
    • Prediction of membrane protein structures with complex topologies using limited constraints
    • P. Barth, B. Wallner, and D. Baker Prediction of membrane protein structures with complex topologies using limited constraints Proc. Natl. Acad. Sci. U. S. A. 106 2009 1409 1414
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 1409-1414
    • Barth, P.1    Wallner, B.2    Baker, D.3
  • 33
    • 79955774472 scopus 로고    scopus 로고
    • The MEMPACK alpha-helical transmembrane protein structure prediction server
    • T. Nugent, S. Ward, and D.T. Jones The MEMPACK alpha-helical transmembrane protein structure prediction server Bioinformatics 27 2011 1438 1439
    • (2011) Bioinformatics , vol.27 , pp. 1438-1439
    • Nugent, T.1    Ward, S.2    Jones, D.T.3
  • 34
    • 39449131104 scopus 로고    scopus 로고
    • Coarse-grained simulation: A high-throughput computational approach to membrane proteins
    • DOI 10.1042/BST0360027
    • M.S. Sansom, K.A. Scott, and P.J. Bond Coarse-grained simulation: a high-throughput computational approach to membrane proteins Biochem. Soc. Trans. 36 2008 27 32 (Pubitemid 351269615)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.1 , pp. 27-32
    • Sansom, M.S.P.1    Scott, K.A.2    Bond, P.J.3
  • 36
    • 39049099153 scopus 로고    scopus 로고
    • The extracellular leucine-rich repeat superfamily; A comparative survey and analysis of evolutionary relationships and expression patterns
    • J. Dolan, K. Walshe, S. Alsbury, K. Hokamp, S. O'Keeffe, T. Okafuji, S.F. Miller, G. Tear, and K.J. Mitchell The extracellular leucine-rich repeat superfamily; a comparative survey and analysis of evolutionary relationships and expression patterns BMC Genomics 8 2007 320 344
    • (2007) BMC Genomics , vol.8 , pp. 320-344
    • Dolan, J.1    Walshe, K.2    Alsbury, S.3    Hokamp, K.4    O'Keeffe, S.5    Okafuji, T.6    Miller, S.F.7    Tear, G.8    Mitchell, K.J.9
  • 37
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • DOI 10.1074/jbc.R200020200
    • P. Liu, M. Rudick, and R.G.W. Anderson Multiple functions of caveolin-1 J. Biol. Chem. 277 2002 41295 41298 (Pubitemid 35257426)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41295-41298
    • Rudick, M.1    Anderson, R.G.W.2
  • 38
    • 84883556425 scopus 로고    scopus 로고
    • How cholesterol interacts with membrane proteins: An exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
    • J. Fantini, and F.J. Barrantes How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains Front. Physiol. 4 2013 1 9
    • (2013) Front. Physiol. , vol.4 , pp. 1-9
    • Fantini, J.1    Barrantes, F.J.2
  • 39
    • 9644281567 scopus 로고    scopus 로고
    • Caveolin scaffolding region and cholesterol-rich domains in membranes
    • DOI 10.1016/j.jmb.2004.10.064, PII S0022283604013701
    • E.M. Epand, B.G. Sayer, and R.F. Epand Caveolin scaffolding region and cholesterol-rich domains in membranes J. Mol. Biol. 345 2005 339 350 (Pubitemid 39574855)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.2 , pp. 339-350
    • Epand, R.M.1    Sayer, B.G.2    Epand, R.F.3
  • 40
    • 0023110044 scopus 로고
    • A new procedure for the purification of monodisperse highly active cytochrome c oxidase from bovine heart
    • Y. Li, A. Naqui, T.G. Frey, and B. Chance A new procedure for the purification of monodisperse highly active cytochrome c oxidase from bovine heart Biochem. J. 242 1987 417 423 (Pubitemid 17026589)
    • (1987) Biochemical Journal , vol.242 , Issue.2 , pp. 417-423
    • Li, Y.1    Naqui, A.2    Frey, T.G.3    Chance, B.4
  • 41
    • 0023968083 scopus 로고
    • Crystalline cytochrome c oxidase of bovine heart mitochondrial membrane: Composition and x-ray diffraction studies
    • S. Yoshikawa, T. Tera, Y. Takahashi, T. Tsukihara, and W.S. Caughey Crystalline cytochrome c oxidase of bovine heart mitochondrial membrane: composition and x-ray diffraction studies Proc. Natl. Acad. Sci. U. S. A. 85 1988 1354 1358
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 1354-1358
    • Yoshikawa, S.1    Tera, T.2    Takahashi, Y.3    Tsukihara, T.4    Caughey, W.S.5
  • 42
    • 0034647940 scopus 로고    scopus 로고
    • A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 c-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo
    • DOI 10.1074/jbc.M002558200
    • A. Schlegel, and M.P. Lisanti A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo J. Biol. Chem. 275 2000 21605 21617 (Pubitemid 30481867)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21605-21617
    • Schlegel, A.1    Lisanti, M.P.2
  • 43
    • 0037036135 scopus 로고    scopus 로고
    • Cell biology: A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • DOI 10.1126/science.1068886
    • R.G. Anderson, and K. Jacobson A role for lipid shell in targeting proteins to caveolae, rafts, and other lipid domains Science 296 2002 1821 1825 (Pubitemid 34596260)
    • (2002) Science , vol.296 , Issue.5574 , pp. 1821-1825
    • Anderson, R.G.W.1    Jacobson, K.2
  • 44
    • 33847738814 scopus 로고    scopus 로고
    • Lipid rafts: Structure, function and role in HIV, Alzheimer's and prion diseases
    • J. Fantini, N. Garmy, R. Mahfoud, and N. Yahi Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases Expert Rev. Mol. Med. 4 2002 1 22
    • (2002) Expert Rev. Mol. Med. , vol.4 , pp. 1-22
    • Fantini, J.1    Garmy, N.2    Mahfoud, R.3    Yahi, N.4
  • 45
    • 84865475880 scopus 로고    scopus 로고
    • Caveolin-Na/K-ATPase interactions: Role of transmembrane topology in non-genomic signal transduction
    • G.A. Morrill, A.B. Kostellow, and A. Askari Caveolin-Na/K-ATPase interactions: role of transmembrane topology in non-genomic signal transduction Steroids 77 2012 1160 1168
    • (2012) Steroids , vol.77 , pp. 1160-1168
    • Morrill, G.A.1    Kostellow, A.B.2    Askari, A.3
  • 48
    • 77955984919 scopus 로고    scopus 로고
    • Internally bridging water molecule in transmembrane α-helical link
    • M. Miyano, A. Hideo, H. Saino, T. Hori, and K. Ida Internally bridging water molecule in transmembrane α-helical link Curr. Opin. Struct. Biol. 20 2010 456 463
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 456-463
    • Miyano, M.1    Hideo, A.2    Saino, H.3    Hori, T.4    Ida, K.5
  • 49
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • L. Serrano, and A.R. Fersch Capping and α-helix stability Nature 342 1989 296 299
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersch, A.R.2
  • 50
    • 84880791416 scopus 로고    scopus 로고
    • Functions of the hydrophilic channels in protomotive cytochrome c oxidase
    • P.R. Rich, and A. Marechal Functions of the hydrophilic channels in protomotive cytochrome c oxidase J. R. Soc. Interface 10 2013 20130183
    • (2013) J. R. Soc. Interface , vol.10 , pp. 20130183
    • Rich, P.R.1    Marechal, A.2
  • 51
    • 84877835123 scopus 로고    scopus 로고
    • Redox-controlled proton gating in bovine cytochrome c oxidase
    • T. Egawa, S.-R. Yeh, and D.L. Rousseau Redox-controlled proton gating in bovine cytochrome c oxidase PLoS One 8 2013 e63669
    • (2013) PLoS One , vol.8 , pp. 63669
    • Egawa, T.1    Yeh, S.-R.2    Rousseau, D.L.3
  • 52
    • 79957707195 scopus 로고    scopus 로고
    • Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy
    • A. Marechal, and P.R. Rich Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 108 2011 8634 8638
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 8634-8638
    • Marechal, A.1    Rich, P.R.2
  • 53
    • 33748573656 scopus 로고    scopus 로고
    • Water permeability of rat liver mitochondria: A biophysical study
    • DOI 10.1016/j.bbamem.2006.07.008, PII S0005273606002707, Auquporins
    • G. Calamita, P. Gena, D. Meleleo, D. Ferri, and M. Svelto Water permeability of rat liver mitochondria: a biophysical study Biochim. Biophys. Acta 1758 2006 1018 1024 (Pubitemid 44373868)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.8 , pp. 1018-1024
    • Calamita, G.1    Gena, P.2    Meleleo, D.3    Ferri, D.4    Svelto, M.5
  • 55
    • 0025989554 scopus 로고
    • Modulation of membrane function by cholesterol
    • P.L. Yeagle Modulation of membrane function by cholesterol Biochimie 73 1991 1303 1310
    • (1991) Biochimie , vol.73 , pp. 1303-1310
    • Yeagle, P.L.1
  • 56
    • 0028067399 scopus 로고
    • Dynamical order and disorder in lipid bilayers
    • DOI 10.1016/0009-3084(94)90171-6
    • O.G. Mouritsen, and K. Jorgensen Dynamical order and disorder in lipid bilayers Chem. Phys. Lipids 73 1994 3 25 (Pubitemid 24299185)
    • (1994) Chemistry and Physics of Lipids , vol.73 , Issue.1-2 , pp. 3-25
    • Mouritsen, O.G.1    Jorgensen, K.2


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