메뉴 건너뛰기




Volumn 187, Issue 1-2, 2006, Pages 169-176

Aquaporins in plants

Author keywords

Gas transport; Plant aquaporin; Water channel

Indexed keywords

AQUAPORIN; CARBON DIOXIDE; NODULIN;

EID: 33744792311     PISSN: 17481708     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1748-1716.2006.01563.x     Document Type: Conference Paper
Times cited : (133)

References (63)
  • 1
    • 0242432461 scopus 로고    scopus 로고
    • Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress
    • Aharon, R., Shahak, Y., Wininger, S., Bendov, R., Kapulnik, Y. Galili, G. 2003. Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress. Plant Cell 15, 439 447.
    • (2003) Plant Cell , vol.15 , pp. 439-447
    • Aharon, R.1    Shahak, Y.2    Wininger, S.3    Bendov, R.4    Kapulnik, Y.5    Galili, G.6
  • 2
    • 0033151856 scopus 로고    scopus 로고
    • The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol
    • Biela, A., Grote, K., Otto, B., Hoth, S., Hedrich, R. Kaldenhoff, R. 1999. The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol. Plant J 18, 565 570.
    • (1999) Plant J , vol.18 , pp. 565-570
    • Biela, A.1    Grote, K.2    Otto, B.3    Hoth, S.4    Hedrich, R.5    Kaldenhoff, R.6
  • 3
    • 0842324680 scopus 로고    scopus 로고
    • Functional properties of soybean nodulin 26 from a comparative three-dimensional model
    • Biswas, S. 2004. Functional properties of soybean nodulin 26 from a comparative three-dimensional model. FEBS Lett 558, 39 44.
    • (2004) FEBS Lett , vol.558 , pp. 39-44
    • Biswas, S.1
  • 4
    • 0038793590 scopus 로고    scopus 로고
    • Aquaporin-1 and HCO3(-)-Cl- transporter-mediated transport of CO2 across the human erythrocyte membrane
    • Blank, M.E. Ehmke, H. 2003. Aquaporin-1 and HCO3(-)-Cl- transporter-mediated transport of CO2 across the human erythrocyte membrane. J Physiol 550, 419 429.
    • (2003) J Physiol , vol.550 , pp. 419-429
    • Blank, M.E.1    Ehmke, H.2
  • 5
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia, M., Nielsen, S., Engel, A. Agre, P. 1999a. Cellular and molecular biology of the aquaporin water channels. Annu Rev Biochem 68, 425 458.
    • (1999) Annu Rev Biochem , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 6
    • 0033520342 scopus 로고    scopus 로고
    • Functional reconstitution and characterization of AqpZ, the E. coli water channel protein
    • Borgnia, M.J., Kozono, D., Calamita, G., Maloney, P.C. Agre, P. 1999b. Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol 291, 1169 1179.
    • (1999) J Mol Biol , vol.291 , pp. 1169-1179
    • Borgnia, M.J.1    Kozono, D.2    Calamita, G.3    Maloney, P.C.4    Agre, P.5
  • 7
    • 11444260781 scopus 로고    scopus 로고
    • PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development
    • Bots, M., Feron, R., Uehlein, N., Weterings, K., Kaldenhoff, R. Mariani, T. 2005a. PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development. J Exp Bot 56, 113 121.
    • (2005) J Exp Bot , vol.56 , pp. 113-121
    • Bots, M.1    Feron, R.2    Uehlein, N.3    Weterings, K.4    Kaldenhoff, R.5    Mariani, T.6
  • 8
    • 20444445196 scopus 로고    scopus 로고
    • Aquaporins of the PIP2 class are required for efficient anther dehiscence in tobacco
    • Bots, M., Vergeldt, F., Wolters-Arts, M., Weterings, K., Van As, H. Mariani, C. 2005b. Aquaporins of the PIP2 class are required for efficient anther dehiscence in tobacco. Plant Physiol 137, 1049 1056.
    • (2005) Plant Physiol , vol.137 , pp. 1049-1056
    • Bots, M.1    Vergeldt, F.2    Wolters-Arts, M.3    Weterings, K.4    As, V.H.5    Mariani, C.6
  • 9
    • 33644659755 scopus 로고    scopus 로고
    • Early effects of salinity on water transport in Arabidopsis roots. Molecular and cellular features of aquaporin expression
    • Boursiac, Y., Chen, S., Luu, D.T., Sorieul, M., Van Den Dries, N. Maurel, C. 2005. Early effects of salinity on water transport in Arabidopsis roots. Molecular and cellular features of aquaporin expression. Plant Physiol 139, 790 805.
    • (2005) Plant Physiol , vol.139 , pp. 790-805
    • Boursiac, Y.1    Chen, S.2    Luu, D.T.3    Sorieul, M.4    Den Dries, V.N.5    Maurel, C.6
  • 10
    • 0037404210 scopus 로고    scopus 로고
    • The ins and outs of aquaporin-2 trafficking
    • Brown, D. 2003. The ins and outs of aquaporin-2 trafficking. Am J Physiol Renal Physiol 284, F893 F901.
    • (2003) Am J Physiol Renal Physiol , vol.284
    • Brown, D.1
  • 11
    • 0033996879 scopus 로고    scopus 로고
    • Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity
    • Chaumont, F., Barrieu, F., Jung, R. Chrispeels, M.J. 2000. Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity. Plant Physiol 122, 1025 1034.
    • (2000) Plant Physiol , vol.122 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Jung, R.3    Chrispeels, M.J.4
  • 12
    • 0035106823 scopus 로고    scopus 로고
    • Aquaporins constitute a large and highly divergent protein family in maize
    • Chaumont, F., Barrieu, F., Wojcik, E., Chrispeels, M.J. Jung, R. 2001. Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiol 125, 1206 1215.
    • (2001) Plant Physiol , vol.125 , pp. 1206-1215
    • Chaumont, F.1    Barrieu, F.2    Wojcik, E.3    Chrispeels, M.J.4    Jung, R.5
  • 13
    • 26944462019 scopus 로고    scopus 로고
    • Regulation of plant aquaporin activity
    • Chaumont, F., Moshelion, M. Daniels, M.J. 2005. Regulation of plant aquaporin activity. Biol Cell 97, 749 764.
    • (2005) Biol Cell , vol.97 , pp. 749-764
    • Chaumont, F.1    Moshelion, M.2    Daniels, M.J.3
  • 14
    • 0032245776 scopus 로고    scopus 로고
    • Effect of PCMBS on CO2 permeability of Xenopus oocytes expressing aquaporin 1 or its C189S mutant
    • Cooper, G.J. Boron, W.F. 1998. Effect of PCMBS on CO2 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
  • 16
    • 0028675704 scopus 로고
    • The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP
    • Daniels, M.J., Mirkov, T.E. Chrispeels, M.J. 1994. The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP. Plant Physiol 106, 1325 1333.
    • (1994) Plant Physiol , vol.106 , pp. 1325-1333
    • Daniels, M.J.1    Mirkov, T.E.2    Chrispeels, M.J.3
  • 17
    • 0033524436 scopus 로고    scopus 로고
    • Purification and functional reconstitution of soybean nodulin 26. An aquaporin with water and glycerol transport properties
    • Dean, R.M., Rivers, R.L., Zeidel, M.L. Roberts, D.M. 1999. Purification and functional reconstitution of soybean nodulin 26. An aquaporin with water and glycerol transport properties. Biochemistry 38, 347 353.
    • (1999) Biochemistry , vol.38 , pp. 347-353
    • Dean, R.M.1    Rivers, R.L.2    Zeidel, M.L.3    Roberts, D.M.4
  • 18
    • 0023768507 scopus 로고
    • Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
    • Denker, B.M., Smith, B.L., Kuhajda, F.P. Agre, P. 1988. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J Biol Chem 263, 15634 15642.
    • (1988) J Biol Chem , vol.263 , pp. 15634-15642
    • Denker, B.M.1    Smith, B.L.2    Kuhajda, F.P.3    Agre, P.4
  • 19
    • 0033737020 scopus 로고    scopus 로고
    • Permeability and channel-mediated transport of boric acid across membrane vesicles isolated from squash roots
    • Dordas, C., Chrispeels, M.J. Brown, P.H. 2000. Permeability and channel-mediated transport of boric acid across membrane vesicles isolated from squash roots. Plant Physiol 124, 1349 1362.
    • (2000) Plant Physiol , vol.124 , pp. 1349-1362
    • Dordas, C.1    Chrispeels, M.J.2    Brown, P.H.3
  • 20
    • 0036660839 scopus 로고    scopus 로고
    • Evidence against aquaporin-1-dependent CO2 permeability in lung and kidney
    • Fang, X., Yang, B., Matthay, M.A. Verkman, A.S. 2002. Evidence against aquaporin-1-dependent CO2 permeability in lung and kidney. J Physiol 542, 63 69.
    • (2002) J Physiol , vol.542 , pp. 63-69
    • Fang, X.1    Yang, B.2    Matthay, M.A.3    Verkman, A.S.4
  • 21
    • 0141643394 scopus 로고    scopus 로고
    • Ontogeny, distribution, and possible functional implications of an unusual aquaporin, AQP8, in mouse liver
    • Ferri, D., Mazzone, A., Liquori, G.E., Cassano, G., Svelto, M. Calamita, G. 2003. Ontogeny, distribution, and possible functional implications of an unusual aquaporin, AQP8, in mouse liver. Hepatology 38, 947 957.
    • (2003) Hepatology , vol.38 , pp. 947-957
    • Ferri, D.1    Mazzone, A.2    Liquori, G.E.3    Cassano, G.4    Svelto, M.5    Calamita, G.6
  • 22
    • 0842291747 scopus 로고    scopus 로고
    • Interactions between plasma membrane aquaporins modulate their water channel activity
    • Fetter, K., Van Wilder, V., Moshelion, M. Chaumont, F. 2004. Interactions between plasma membrane aquaporins modulate their water channel activity. Plant Cell 16, 215 228.
    • (2004) Plant Cell , vol.16 , pp. 215-228
    • Fetter, K.1    Wilder, V.V.2    Moshelion, M.3    Chaumont, F.4
  • 23
    • 0023088416 scopus 로고
    • Nodulin-26, a peribacteroid membrane nodulin is expressed independently of the development of the peribacteroid compartment
    • Fortin, M.G., Morrison, N.A. Verma, D.P. 1987. Nodulin-26, a peribacteroid membrane nodulin is expressed independently of the development of the peribacteroid compartment. Nucleic Acids Res 15, 813 824.
    • (1987) Nucleic Acids Res , vol.15 , pp. 813-824
    • Fortin, M.G.1    Morrison, N.A.2    Verma, D.P.3
  • 24
    • 0039251522 scopus 로고    scopus 로고
    • Aquaporin Nt-TIPa can account for the high permeability of tobacco cell vacuolar membrane to small neutral solutes
    • Gerbeau, P., Güçlü, J., Ripoche, P. Maurel, C. 1999. Aquaporin Nt-TIPa can account for the high permeability of tobacco cell vacuolar membrane to small neutral solutes. Plant J 18, 577 587.
    • (1999) Plant J , vol.18 , pp. 577-587
    • Gerbeau, P.1    Güçlü, J.2    Ripoche, P.3    Maurel, C.4
  • 25
    • 0036011030 scopus 로고    scopus 로고
    • The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH
    • Gerbeau, P., Amodeo, G., Henzler, T., Santoni, V., Ripoche, P. Maurel, C. 2002. The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH. Plant J 30, 71 81.
    • (2002) Plant J , vol.30 , pp. 71-81
    • Gerbeau, P.1    Amodeo, G.2    Henzler, T.3    Santoni, V.4    Ripoche, P.5    Maurel, C.6
  • 26
    • 0037394367 scopus 로고    scopus 로고
    • Phosphorylation of soybean nodulin 26 on serine 262 enhances water permeability and is regulated developmentally and by osmotic signals
    • Guenther, J.F., Chanmanivone, N., Galetovic, M.P., Wallace, I.S., Cobb, J.A. Roberts, D.M. 2003. Phosphorylation of soybean nodulin 26 on serine 262 enhances water permeability and is regulated developmentally and by osmotic signals. Plant Cell 15, 981 991.
    • (2003) Plant Cell , vol.15 , pp. 981-991
    • Guenther, J.F.1    Chanmanivone, N.2    Galetovic, M.P.3    Wallace, I.S.4    Cobb, J.A.5    Roberts, D.M.6
  • 27
    • 2942700260 scopus 로고    scopus 로고
    • Overexpression of the barley aquaporin HvPIP2;1 increases internal CO(2) conductance and CO(2) assimilation in the leaves of transgenic rice plants
    • Hanba, Y.T., Shibasaka, M., Hayashi, Y., Hayakawa, T., Kasamo, K., Terashima, I. Katsuhara, M. 2004. Overexpression of the barley aquaporin HvPIP2;1 increases internal CO(2) conductance and CO(2) assimilation in the leaves of transgenic rice plants. Plant Cell Physiol 45, 521 529.
    • (2004) Plant Cell Physiol , vol.45 , pp. 521-529
    • Hanba, Y.T.1    Shibasaka, M.2    Hayashi, Y.3    Hayakawa, T.4    Kasamo, K.5    Terashima, I.6    Katsuhara, M.7
  • 28
    • 0033446707 scopus 로고    scopus 로고
    • Aquaporins: Phylogeny, structure, and physiology of water channels
    • Heymann, J.B. Engel, A. 1999. Aquaporins: phylogeny, structure, and physiology of water channels. News Physiol Sci 14, 187 193.
    • (1999) News Physiol Sci , vol.14 , pp. 187-193
    • Heymann, J.B.1    Engel, A.2
  • 30
    • 26844545473 scopus 로고    scopus 로고
    • Novel type aquaporin SIPs are mainly localized to the ER membrane and show cell-specific expression in Arabidopsis thaliana
    • Ishikawa, F., Suga, S., Uemura, T., Sato, M.H. Maeshima, M. 2005. Novel type aquaporin SIPs are mainly localized to the ER membrane and show cell-specific expression in Arabidopsis thaliana. FEBS Lett 579, 5814 5820.
    • (2005) FEBS Lett , vol.579 , pp. 5814-5820
    • Ishikawa, F.1    Suga, S.2    Uemura, T.3    Sato, M.H.4    Maeshima, M.5
  • 32
    • 0036221680 scopus 로고    scopus 로고
    • A new subfamily of major intrinsic proteins in plants
    • Johanson, U. Gustavsson, S. 2002. A new subfamily of major intrinsic proteins in plants. Mol Biol Evol 19, 456 461.
    • (2002) Mol Biol Evol , vol.19 , pp. 456-461
    • Johanson, U.1    Gustavsson, S.2
  • 33
    • 0034870819 scopus 로고    scopus 로고
    • The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants
    • Johanson, U., Karlsson, M., Johansson, I., Gustavsson, S., Sjövall, S., Fraysse, L., Weig, A.R. Kjellbom, P. 2001. The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants. Plant Physiol 126, 1358 1369.
    • (2001) Plant Physiol , vol.126 , pp. 1358-1369
    • Johanson, U.1    Karlsson, M.2    Johansson, I.3    Gustavsson, S.4    Sjövall, S.5    Fraysse, L.6    Weig, A.R.7    Kjellbom, P.8
  • 34
    • 0030199138 scopus 로고    scopus 로고
    • The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential
    • Johansson, I., Larsson, C., Ek, B. Kjellbom, P. 1996. The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential. Plant Cell 8, 1181 1191.
    • (1996) Plant Cell , vol.8 , pp. 1181-1191
    • Johansson, I.1    Larsson, C.2    Ek, B.3    Kjellbom, P.4
  • 35
    • 0032029335 scopus 로고    scopus 로고
    • Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation
    • Johansson, I., Karlsson, M., Shukla, V.K., Chrispeels, M.J., Larsson, C. Kjellbom, P. 1998. Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. Plant Cell 10, 451 459.
    • (1998) Plant Cell , vol.10 , pp. 451-459
    • Johansson, I.1    Karlsson, M.2    Shukla, V.K.3    Chrispeels, M.J.4    Larsson, C.5    Kjellbom, P.6
  • 36
    • 0037855844 scopus 로고    scopus 로고
    • Functional expression and characterization of an archaeal aquaporin. AqpM from Methanothermobacter marburgensis
    • Kozono, D., Ding, X., Iwasaki, I., Meng, X., Kamagata, Y., Agre, P. Kitagawa, Y. 2003. Functional expression and characterization of an archaeal aquaporin. AqpM from Methanothermobacter marburgensis. J Biol Chem 278, 10649 10656.
    • (2003) J Biol Chem , vol.278 , pp. 10649-10656
    • Kozono, D.1    Ding, X.2    Iwasaki, I.3    Meng, X.4    Kamagata, Y.5    Agre, P.6    Kitagawa, Y.7
  • 38
    • 0345392686 scopus 로고    scopus 로고
    • Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis
    • Liu, L.H., Ludewig, U., Gassert, B., Frommer, W.B. Von Wiren, N. 2003. Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis. Plant Physiol 133, 1220 1228.
    • (2003) Plant Physiol , vol.133 , pp. 1220-1228
    • Liu, L.H.1    Ludewig, U.2    Gassert, B.3    Frommer, W.B.4    Von Wiren, N.5
  • 39
    • 0742270773 scopus 로고    scopus 로고
    • Diurnal regulation of water transport and aquaporin gene expression in maize roots: Contribution of PIP2 proteins
    • Lopez, F., Bousser, A., Sissoeff, I., Gaspar, M., Lachaise, B., Hoarau, J., Mahe, A. 2003. Diurnal regulation of water transport and aquaporin gene expression in maize roots: contribution of PIP2 proteins. Plant Cell Physiol 44, 1384 1395.
    • (2003) Plant Cell Physiol , vol.44 , pp. 1384-1395
    • Lopez, F.1    Bousser, A.2    Sissoeff, I.3    Gaspar, M.4    Lachaise, B.5    Hoarau, J.6    Mahe, A.7
  • 40
    • 0347298563 scopus 로고    scopus 로고
    • Plasma membrane aquaporins play a significant role during recovery from water deficit
    • Martre, P., Morillon, R., Barrieu, F., North, G.B., Nobel, P.S. Chrispeels, M.J. 2002. Plasma membrane aquaporins play a significant role during recovery from water deficit. Plant Physiol 130, 2101 2110.
    • (2002) Plant Physiol , vol.130 , pp. 2101-2110
    • Martre, P.1    Morillon, R.2    Barrieu, F.3    North, G.B.4    Nobel, P.S.5    Chrispeels, M.J.6
  • 41
    • 0028997596 scopus 로고
    • Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP
    • Maurel, C., Kado, R.T., Guern, J. Chrispeels, M.J. 1995. Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP. Embo J 14, 3028 3035.
    • (1995) Embo J , vol.14 , pp. 3028-3035
    • Maurel, C.1    Kado, R.T.2    Guern, J.3    Chrispeels, M.J.4
  • 43
    • 0031888726 scopus 로고    scopus 로고
    • Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes
    • Nakhoul, N.L., Davis, B.A., Romero, M.F. Boron, W.F. 1998. Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes. Am J Physiol 274, C543 C548.
    • (1998) Am J Physiol , vol.274
    • Nakhoul, N.L.1    Davis, B.A.2    Romero, M.F.3    Boron, W.F.4
  • 45
    • 0033964857 scopus 로고    scopus 로고
    • Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules
    • Niemietz, C.M. Tyerman, S.D. 2000. Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules. FEBS Lett 465, 110 114.
    • (2000) FEBS Lett , vol.465 , pp. 110-114
    • Niemietz, C.M.1    Tyerman, S.D.2
  • 46
    • 0028070870 scopus 로고
    • Identification of a high affinity NH4+ transporter from plants
    • Ninnemann, O., Jauniaux, J.C. Frommer, W.B. 1994. Identification of a high affinity NH4+ transporter from plants. Embo J 13, 3464 3471.
    • (1994) Embo J , vol.13 , pp. 3464-3471
    • Ninnemann, O.1    Jauniaux, J.C.2    Frommer, W.B.3
  • 47
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park, J.H. Saier, M.H. Jr.. 1996. Phylogenetic characterization of the MIP family of transmembrane channel proteins. J Membr Biol 153, 171 180.
    • (1996) J Membr Biol , vol.153 , pp. 171-180
    • Park, J.H.1    Saier Jr., M.H.2
  • 48
    • 20644433762 scopus 로고    scopus 로고
    • Reconstituted aquaporin 1 water channels transport CO2 across membranes
    • Prasad, G.V., Coury, L.A., Finn, F. Zeidel, M.L. 1998. Reconstituted aquaporin 1 water channels transport CO2 across membranes. J Biol Chem 273, 33123 33126.
    • (1998) J Biol Chem , vol.273 , pp. 33123-33126
    • Prasad, G.V.1    Coury, L.A.2    Finn, F.3    Zeidel, M.L.4
  • 49
    • 0026332210 scopus 로고
    • Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family
    • Preston, G.M. Agre, P. 1991. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. Proc Natl Acad Sci USA 88, 11110 11114.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11110-11114
    • Preston, G.M.1    Agre, P.2
  • 50
    • 1942442451 scopus 로고    scopus 로고
    • Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies
    • Schuurmans, J.A., Van Dongen, J.T., Rutjens, B.P., Boonman, A., Pieterse, C.M. Borstlap, A.C. 2003. Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies. Plant Mol Biol 53, 633 645.
    • (2003) Plant Mol Biol , vol.53 , pp. 633-645
    • Schuurmans, J.A.1    Dongen, V.J.T.2    Rutjens, B.P.3    Boonman, A.4    Pieterse, C.M.5    Borstlap, A.C.6
  • 51
    • 0035999374 scopus 로고    scopus 로고
    • PIP1 plasma membrane aquaporins in tobacco: From cellular effects to function in plants
    • Siefritz, F., Tyree, M.T., Lovisolo, C., Schubert, A. Kaldenhoff, R. 2002. PIP1 plasma membrane aquaporins in tobacco: from cellular effects to function in plants. Plant Cell 14, 869 876.
    • (2002) Plant Cell , vol.14 , pp. 869-876
    • Siefritz, F.1    Tyree, M.T.2    Lovisolo, C.3    Schubert, A.4    Kaldenhoff, R.5
  • 52
    • 0035141868 scopus 로고    scopus 로고
    • Effect of AQP1 expression level on Co(2) permeability in bovine corneal endothelium
    • Sun, X.C., Allen, K.T., Xie, Q., Stamer, W.D. Bonanno, J.A. 2001. Effect of AQP1 expression level on Co(2) permeability in bovine corneal endothelium. Invest Ophthalmol Vis Sci 42, 417 423.
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 417-423
    • Sun, X.C.1    Allen, K.T.2    Xie, Q.3    Stamer, W.D.4    Bonanno, J.A.5
  • 53
    • 23644442412 scopus 로고    scopus 로고
    • Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation
    • Temmei, Y., Uchida, S., Hoshino, D., Kanzava, N., Kuvahara, M., Sasaki, S. Tsuchiya, T. 2005. Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation. FEBS Lett 579, 4417 4422.
    • (2005) FEBS Lett , vol.579 , pp. 4417-4422
    • Temmei, Y.1    Uchida, S.2    Hoshino, D.3    Kanzava, N.4    Kuvahara, M.5    Sasaki, S.6    Tsuchiya, T.7
  • 54
    • 0036008346 scopus 로고    scopus 로고
    • Effects of HgCl(2) on CO(2) dependence of leaf photosynthesis: Evidence indicating involvement of aquaporins in CO(2) diffusion across the plasma membrane
    • Terashima, I. Ono, K. 2002. Effects of HgCl(2) on CO(2) dependence of leaf photosynthesis: evidence indicating involvement of aquaporins in CO(2) diffusion across the plasma membrane. Plant Cell Physiol 43, 70 78.
    • (2002) Plant Cell Physiol , vol.43 , pp. 70-78
    • Terashima, I.1    Ono, K.2
  • 56
    • 0141484616 scopus 로고    scopus 로고
    • Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins
    • Tournaire-Roux, C., Sutka, M., Javot, H. et al. 2003. Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins. Nature 425, 393 397.
    • (2003) Nature , vol.425 , pp. 393-397
    • Tournaire-Roux, C.1    Sutka, M.2    Javot, H.3
  • 57
    • 0142246438 scopus 로고    scopus 로고
    • The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological functions
    • Uehlein, N., Lovisolo, C., Siefritz, F. Kaldenhoff, R. 2003. The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological functions. Nature 425, 734 737.
    • (2003) Nature , vol.425 , pp. 734-737
    • Uehlein, N.1    Lovisolo, C.2    Siefritz, F.3    Kaldenhoff, R.4
  • 58
    • 0036558026 scopus 로고    scopus 로고
    • Quaternary structure and function of transport proteins
    • Veenhoff, L.M., Heuberger, E.H. Poolman, B. 2002. Quaternary structure and function of transport proteins. Trends Biochem Sci 27, 242 249.
    • (2002) Trends Biochem Sci , vol.27 , pp. 242-249
    • Veenhoff, L.M.1    Heuberger, E.H.2    Poolman, B.3
  • 60
    • 3042583806 scopus 로고    scopus 로고
    • Homology modeling of representative subfamilies of Arabidopsis major intrinsic proteins. Classification based on the aromatic/arginine selectivity filter
    • Wallace, I.S. Roberts, D.M. 2004. Homology modeling of representative subfamilies of Arabidopsis major intrinsic proteins. Classification based on the aromatic/arginine selectivity filter. Plant Physiol 135, 1059 1068.
    • (2004) Plant Physiol , vol.135 , pp. 1059-1068
    • Wallace, I.S.1    Roberts, D.M.2
  • 61
    • 0026646048 scopus 로고
    • Determination of the site of phosphorylation of nodulin 26 by the calcium-dependent protein kinase from soybean nodules
    • Weaver, C.D. Roberts, D.M. 1992. Determination of the site of phosphorylation of nodulin 26 by the calcium-dependent protein kinase from soybean nodules. Biochemistry 31, 8954 8959.
    • (1992) Biochemistry , vol.31 , pp. 8954-8959
    • Weaver, C.D.1    Roberts, D.M.2
  • 62
    • 0031200862 scopus 로고    scopus 로고
    • The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group
    • Weig, A., Deswarte, C. Chrispeels, M.J. 1997. The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group. Plant Physiol 114, 1347 1357.
    • (1997) Plant Physiol , vol.114 , pp. 1347-1357
    • Weig, A.1    Deswarte, C.2    Chrispeels, M.J.3
  • 63
    • 21044445996 scopus 로고    scopus 로고
    • Phylogeny and evolution of the major intrinsic protein family
    • Zardoya, R. 2005. Phylogeny and evolution of the major intrinsic protein family. Biol Cell 97, 397 414.
    • (2005) Biol Cell , vol.97 , pp. 397-414
    • Zardoya, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.