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Volumn 91, Issue 3, 2006, Pages 842-848

Does CO2 permeate through aquaporin-1?

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN 1; ARGININE; CARBON DIOXIDE; ETHANOLAMINE DERIVATIVE; AQUAPORIN; CARBON; GLYCEROL; OXYGEN; WATER;

EID: 33746730535     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.081406     Document Type: Article
Times cited : (134)

References (50)
  • 1
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red-cell CHIP28 protein
    • Preston, G. M., T. P. Carroll, W. B. Guggino, and P. Agre. 1992. Appearance of water channels in Xenopus oocytes expressing red-cell CHIP28 protein. Science. 256:385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 2
    • 0026806764 scopus 로고
    • Reconstitution of functional water channels in liposomes containing purified red-cell CHIP28 protein
    • Zeidel, M. L., S. V. Ambudkar, B. L. Smith, and P. Agre. 1992. Reconstitution of functional water channels in liposomes containing purified red-cell CHIP28 protein. Biochemistry. 31:7436-7440.
    • (1992) Biochemistry , vol.31 , pp. 7436-7440
    • Zeidel, M.L.1    Ambudkar, S.V.2    Smith, B.L.3    Agre, P.4
  • 3
    • 0028200818 scopus 로고
    • Functional characterization of the Eschericia coli glycerol facilitator, GlpF, in Xenopus oocytes
    • Maurel, C., J. Reizer, J. I. Schroeder, M. J. Chrispeels, and M. H. Saier. 1994. Functional characterization of the Eschericia coli glycerol facilitator, GlpF, in Xenopus oocytes. J. Biol. Chem. 269:11869-11872.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11869-11872
    • Maurel, C.1    Reizer, J.2    Schroeder, J.I.3    Chrispeels, M.J.4    Saier, M.H.5
  • 4
    • 0032510966 scopus 로고    scopus 로고
    • The aquaporins, blueprints for cellular plumbing systems
    • Agre, P., M. Bonhivers, and M. J. Borgnia. 1998. The aquaporins, blueprints for cellular plumbing systems. J. Biol. Chem. 273:14659-14662.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14659-14662
    • Agre, P.1    Bonhivers, M.2    Borgnia, M.J.3
  • 7
    • 0036259463 scopus 로고    scopus 로고
    • Aquaporin water channels: Atomic structure molecular dynamics meet clinical medicine
    • Kozono, D., M. Yasui, L. S. King, and P. Agre. 2002. Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine. J. Clin. Invest. 109:1395-1399.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1395-1399
    • Kozono, D.1    Yasui, M.2    King, L.S.3    Agre, P.4
  • 8
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: The evolving tale of aquaporin biology
    • King, L. S., D. Kozono, and P. Agre. 2004. From structure to disease: the evolving tale of aquaporin biology. Nat. Rev. Mol. Cell Biol. 5:687-698.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 10
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui, H., B.-G. Han, J. K. Lee, P. Walian, and B. K. Jap. 2001. Structural basis of water-specific transport through the AQP1 water channel. Nature. 414:872-878.
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 12
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen, T., P. Sliz, J. Kistler, Y. Cheng, and T. Walz. 2004. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature. 429:193-197.
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 15
    • 0242405520 scopus 로고    scopus 로고
    • Selectivity and conductance among the glycerol and water conducting aquaporin family of channels
    • Stroud, R. M., D. Savage, L. J. W. Miercke, J. K. Lee, S. Khademi, and W. Harries. 2003. Selectivity and conductance among the glycerol and water conducting aquaporin family of channels. FEBS Lett. 555:79-82.
    • (2003) FEBS Lett. , vol.555 , pp. 79-82
    • Stroud, R.M.1    Savage, D.2    Miercke, L.J.W.3    Lee, J.K.4    Khademi, S.5    Harries, W.6
  • 16
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of Aquaporin-1 and GlpF
    • de Groot, B. L., and H. Grubmüller. 2001. Water permeation across biological membranes: mechanism and dynamics of Aquaporin-1 and GlpF. Science. 294:2353-2357.
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmüller, H.2
  • 18
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • de Groot, B. L., T. Frigato, V. Helms, and H. Grubmüller. 2003. The mechanism of proton exclusion in the aquaporin-1 water channel. J. Mol. Biol. 333:279-293.
    • (2003) J. Mol. Biol. , vol.333 , pp. 279-293
    • De Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmüller, H.4
  • 19
    • 1642493669 scopus 로고    scopus 로고
    • Molecular basis of proton blockage in aquaporins
    • Chakrabarti, N., E. Tajkhorshid, B. Roux, and R. Pomes. 2004. Molecular basis of proton blockage in aquaporins. Strucure. 12:65-74.
    • (2004) Strucure , vol.12 , pp. 65-74
    • Chakrabarti, N.1    Tajkhorshid, E.2    Roux, B.3    Pomes, R.4
  • 20
    • 4644308725 scopus 로고    scopus 로고
    • Structural determinants of proton blockage in aquaporins
    • Chakrabarti, N., B. Roux, and R. Pomes. 2004. Structural determinants of proton blockage in aquaporins. J. Mol. Biol. 343:493-510.
    • (2004) J. Mol. Biol. , vol.343 , pp. 493-510
    • Chakrabarti, N.1    Roux, B.2    Pomes, R.3
  • 21
    • 1842583051 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in aquaporin channels
    • Ilan, B., E. Tajkhorshid, K. Schulten, and G. A. Voth. 2004. The mechanism of proton exclusion in aquaporin channels. Proteins. 55:223-228.
    • (2004) Proteins , vol.55 , pp. 223-228
    • Ilan, B.1    Tajkhorshid, E.2    Schulten, K.3    Voth, G.A.4
  • 23
    • 0032245776 scopus 로고    scopus 로고
    • 2 permeability of Xenopus oocytes expressing aquaporin 1 or its C189S mutant
    • 2 permeability of Xenopus oocytes expressing aquaporin 1 or its C189S mutant. Am. J. Physiol. 275:C1481-C1486.
    • (1998) Am. J. Physiol. , vol.275
    • Cooper, G.J.1    Boron, W.F.2
  • 25
    • 0034723202 scopus 로고    scopus 로고
    • Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes
    • Yang, B., N. Fukuda, A. van Hoek, M. A. Matthay, T. Ma, and A. S. Verkman. 2000. Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes. J. Biol. Chem. 275:2686-2692.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2686-2692
    • Yang, B.1    Fukuda, N.2    Van Hoek, A.3    Matthay, M.A.4    Ma, T.5    Verkman, A.S.6
  • 27
    • 0036660847 scopus 로고    scopus 로고
    • Does aquaporin-1 pass gas? An opposing view
    • Verkman, A. S. 2002. Does aquaporin-1 pass gas? An opposing view. J. Physiol. 542:31.
    • (2002) J. Physiol. , vol.542 , pp. 31
    • Verkman, A.S.1
  • 29
    • 0038793590 scopus 로고    scopus 로고
    • 2 across the human erythrocyte membrane
    • 550.2
    • 2 across the human erythrocyte membrane. J. Physiol. 550.2:419-429.
    • (2003) J. Physiol. , pp. 419-429
    • Blank, M.E.1    Ehmke, H.2
  • 30
    • 0017750205 scopus 로고
    • Diffusion of carbon dioxide through lipid bilayer membranes: Effects of carbonic anhydrase, bicarbonate, and unstirred layers
    • Gutknecht, J., M. A. Bisson, and F. C. Tosteson. 1977. Diffusion of carbon dioxide through lipid bilayer membranes: effects of carbonic anhydrase, bicarbonate, and unstirred layers. J. Gen. Physiol. 69:779-794.
    • (1977) J. Gen. Physiol. , vol.69 , pp. 779-794
    • Gutknecht, J.1    Bisson, M.A.2    Tosteson, F.C.3
  • 31
    • 0028280013 scopus 로고
    • Unusual permeability properties of gastric gland cells
    • Waisbren, S. J., J. P. Geibel, I. M. Modlin, and W. F. Boron. 1994. Unusual permeability properties of gastric gland cells. Nature. 368:332-335.
    • (1994) Nature , vol.368 , pp. 332-335
    • Waisbren, S.J.1    Geibel, J.P.2    Modlin, I.M.3    Boron, W.F.4
  • 33
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. 1990. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 35
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W. L.,D. S.Maxwell, and J. Tirado-Rives. 1996.Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 36
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G. A., R. A. Friesner, J. Tirado-Rives, and W. L. Jorgensen. 2001. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105:6474-6487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 37
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger, O., O. Edholm, and F. Jähnig. 1997. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys. J. 72:2002-2013.
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jähnig, F.3
  • 38
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Internet
    • Lindahl, E., B. Hess, and D. Van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. (Online). 7:306-317 (Internet).
    • (2001) J. Mol. Model. (Online) , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 40
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N·log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 42
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • Miyamoto, S., and P. A. Kollman. 1992. SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models. J. Comput. Chem. 13:952-962.
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 45
    • 33646251373 scopus 로고    scopus 로고
    • Single-channel water permeabilities of E. coli aquaporins AqpZ and GlpF
    • Jensen, M. Ø., and O. G. Mouritsen. 2006. Single-channel water permeabilities of E. coli aquaporins AqpZ and GlpF. Biophys. J. 90:2270-2284.
    • (2006) Biophys. J. , vol.90 , pp. 2270-2284
    • Jensen, M.Ø.1    Mouritsen, O.G.2
  • 46
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar, S., D. Bouzida, R. H. Swendsen, P. A. Kollman, and J. M. Rosenberg. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 48
    • 0028175266 scopus 로고
    • Biologically active two-dimensional crystals of aquaporin CHIP
    • Walz, T., B. L. Smith, M. L. Zeidel, A. Engel, and P. Agre. 1994. Biologically active two-dimensional crystals of aquaporin CHIP. J. Biol. Chem. 269:1583-1586.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1583-1586
    • Walz, T.1    Smith, B.L.2    Zeidel, M.L.3    Engel, A.4    Agre, P.5
  • 49
    • 33644850534 scopus 로고    scopus 로고
    • Crystal structure of aquaporin Z tetramer reveals both open and closed water-conducting channels
    • Jiang, J., B. V. Daniels, and D. Fu. 2006. Crystal structure of aquaporin Z tetramer reveals both open and closed water-conducting channels. J. Biol. Chem. 281:454-460.
    • (2006) J. Biol. Chem. , vol.281 , pp. 454-460
    • Jiang, J.1    Daniels, B.V.2    Fu, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.