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Volumn 1758, Issue 8, 2006, Pages 1142-1156

Modulating the expression of aquaporin genes in planta: A key to understand their physiological functions?

Author keywords

Aquaporin; Hydraulic conductivity; Membrane permeability; Water relation

Indexed keywords

AQUAPORIN; ISOPROTEIN; PROTEIN; RNA; VEGETABLE PROTEIN;

EID: 33748563984     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.02.017     Document Type: Review
Times cited : (125)

References (110)
  • 2
    • 0034267133 scopus 로고    scopus 로고
    • Sensitivity of growth of roots versus leaves to water stress: biophysical analysis and relation to water transport
    • Hsiao T.C., and Xu L.K. Sensitivity of growth of roots versus leaves to water stress: biophysical analysis and relation to water transport. J. Exp. Bot. 51 (2000) 1595-1616
    • (2000) J. Exp. Bot. , vol.51 , pp. 1595-1616
    • Hsiao, T.C.1    Xu, L.K.2
  • 3
    • 0031957443 scopus 로고    scopus 로고
    • How does water get trough roots?
    • Steudle E., and Peterson C.A. How does water get trough roots?. J. Exp. Bot. 49 (1998) 775-788
    • (1998) J. Exp. Bot. , vol.49 , pp. 775-788
    • Steudle, E.1    Peterson, C.A.2
  • 4
    • 0034492268 scopus 로고    scopus 로고
    • Water uptake by plant roots: an integration of views
    • Steudle E. Water uptake by plant roots: an integration of views. Plant Soil 226 (2000) 45-56
    • (2000) Plant Soil , vol.226 , pp. 45-56
    • Steudle, E.1
  • 5
    • 2442446269 scopus 로고    scopus 로고
    • Development of the Casparian strip in primary roots of maize under salt stress
    • Karahara I., Ikeda A., Kondo T., and Uetake Y. Development of the Casparian strip in primary roots of maize under salt stress. Planta 219 (2004) 41-47
    • (2004) Planta , vol.219 , pp. 41-47
    • Karahara, I.1    Ikeda, A.2    Kondo, T.3    Uetake, Y.4
  • 6
    • 0036713490 scopus 로고    scopus 로고
    • The role of aquaporins in root water uptake
    • Javot H., and Maurel C. The role of aquaporins in root water uptake. Ann. Bot. (London) 90 (2002) 301-313
    • (2002) Ann. Bot. (London) , vol.90 , pp. 301-313
    • Javot, H.1    Maurel, C.2
  • 7
    • 0000751219 scopus 로고
    • Location of the major barriers to water and ion movement in young roots of Zea-Mays L
    • Peterson C.A., Murrmann M., and Steudle E. Location of the major barriers to water and ion movement in young roots of Zea-Mays L. Planta 190 (1993) 127-136
    • (1993) Planta , vol.190 , pp. 127-136
    • Peterson, C.A.1    Murrmann, M.2    Steudle, E.3
  • 9
    • 0033958958 scopus 로고    scopus 로고
    • Chemical composition of apoplastic transport barriers in relation to radial hydraulic conductivity of corn roots (Zea mays L.)
    • Zimmermann H.M., Hartmann K., Schreiber L., and Steudle E. Chemical composition of apoplastic transport barriers in relation to radial hydraulic conductivity of corn roots (Zea mays L.). Planta 210 (2000) 302-311
    • (2000) Planta , vol.210 , pp. 302-311
    • Zimmermann, H.M.1    Hartmann, K.2    Schreiber, L.3    Steudle, E.4
  • 10
    • 0344316017 scopus 로고    scopus 로고
    • Aquaporin function, structure, and expression: are there more surprises to surface in water relations?
    • Schaffner A.R. Aquaporin function, structure, and expression: are there more surprises to surface in water relations?. Planta 204 (1998) 131-139
    • (1998) Planta , vol.204 , pp. 131-139
    • Schaffner, A.R.1
  • 11
    • 0033894575 scopus 로고    scopus 로고
    • Cell-specific expression of the mercury-insensitive plasma-membrane aquaporin NtAQP1 from Nicotiana tabacum
    • Otto B., and Kaldenhoff R. Cell-specific expression of the mercury-insensitive plasma-membrane aquaporin NtAQP1 from Nicotiana tabacum. Planta 211 (2000) 167-172
    • (2000) Planta , vol.211 , pp. 167-172
    • Otto, B.1    Kaldenhoff, R.2
  • 14
    • 0842291747 scopus 로고    scopus 로고
    • Interactions between plasma membrane aquaporins modulate their water channel activity
    • Fetter K., Van Wilder V., Moshelion M., and Chaumont F. Interactions between plasma membrane aquaporins modulate their water channel activity. Plant Cell 16 (2004) 215-228
    • (2004) Plant Cell , vol.16 , pp. 215-228
    • Fetter, K.1    Van Wilder, V.2    Moshelion, M.3    Chaumont, F.4
  • 15
    • 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., and Jung R. Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiol. 125 (2001) 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
  • 16
    • 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., Johannson I., Gustavsson S., Sjovall S., Fraysse L., Weig A.R., and Kjellbom P. 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 (2001) 1358-1369
    • (2001) Plant Physiol. , vol.126 , pp. 1358-1369
    • Johanson, U.1    Karlsson, M.2    Johannson, I.3    Gustavsson, S.4    Sjovall, S.5    Fraysse, L.6    Weig, A.R.7    Kjellbom, P.8
  • 17
    • 26444617525 scopus 로고    scopus 로고
    • Identification of 33 rice aquaporin genes and analysis of their expression and function
    • Sakurai J., Ishikawa F., Yamaguchi T., Uemura M., and Maeshima M. Identification of 33 rice aquaporin genes and analysis of their expression and function. Plant Cell Physiol. 46 (2005) 1568-1577
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1568-1577
    • Sakurai, J.1    Ishikawa, F.2    Yamaguchi, T.3    Uemura, M.4    Maeshima, M.5
  • 18
    • 0027192036 scopus 로고
    • The vacuolar membrane protein gamma-TIP creates water specific channels in Xenopus oocytes
    • Maurel C., Reizer J., Schroeder J.I., and Chrispeels M.J. The vacuolar membrane protein gamma-TIP creates water specific channels in Xenopus oocytes. EMBO J. 12 (1993) 2241-2247
    • (1993) EMBO J. , vol.12 , pp. 2241-2247
    • Maurel, C.1    Reizer, J.2    Schroeder, J.I.3    Chrispeels, M.J.4
  • 19
    • 0036187202 scopus 로고    scopus 로고
    • Plant aquaporins: multifunctional water and solute channels with expanding roles
    • Tyerman S.D., Niemietz C.M., and Bramley H. Plant aquaporins: multifunctional water and solute channels with expanding roles. Plant Cell Environ. 25 (2002) 173-194
    • (2002) Plant Cell Environ. , vol.25 , pp. 173-194
    • Tyerman, S.D.1    Niemietz, C.M.2    Bramley, H.3
  • 20
    • 26944462019 scopus 로고    scopus 로고
    • Regulation of plant aquaporin activity
    • Chaumont F., Moshelion M., and Daniels M.J. Regulation of plant aquaporin activity. Biol. Cell 97 (2005) 749-764
    • (2005) Biol. Cell , vol.97 , pp. 749-764
    • Chaumont, F.1    Moshelion, M.2    Daniels, M.J.3
  • 21
    • 12444298048 scopus 로고    scopus 로고
    • Aquaporins in a challenging environment: molecular gears for adjusting plant water status
    • Luu D.T., and Maurel C. Aquaporins in a challenging environment: molecular gears for adjusting plant water status. Plant Cell Environ. 28 (2005) 85-96
    • (2005) Plant Cell Environ. , vol.28 , pp. 85-96
    • Luu, D.T.1    Maurel, C.2
  • 22
    • 0001222337 scopus 로고
    • Tonoplast-bound protein-kinase phosphorylates tonoplast intrinsic protein
    • Johnson K.D., and Chrispeels M.J. Tonoplast-bound protein-kinase phosphorylates tonoplast intrinsic protein. Plant Physiol. 100 (1992) 1787-1795
    • (1992) Plant Physiol. , vol.100 , pp. 1787-1795
    • Johnson, K.D.1    Chrispeels, M.J.2
  • 23
    • 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., and Kjellbom P. 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 (1996) 1181-1191
    • (1996) Plant Cell , vol.8 , pp. 1181-1191
    • Johansson, I.1    Larsson, C.2    Ek, B.3    Kjellbom, P.4
  • 24
    • 0026721375 scopus 로고
    • Topology and phosphorylation of soybean nodulin-26, an intrinsic protein of the peribacteroid membrane
    • Miao G.H., Hong Z., and Verma D.P. Topology and phosphorylation of soybean nodulin-26, an intrinsic protein of the peribacteroid membrane. J. Cell Biol. 118 (1992) 481-490
    • (1992) J. Cell Biol. , vol.118 , pp. 481-490
    • Miao, G.H.1    Hong, Z.2    Verma, D.P.3
  • 25
    • 0037667409 scopus 로고    scopus 로고
    • A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots
    • Santoni V., Vinh J., Pflieger D., Sommerer N., and Maurel C. A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots. Biochem. J. 373 (2003) 289-296
    • (2003) Biochem. J. , vol.373 , pp. 289-296
    • Santoni, V.1    Vinh, J.2    Pflieger, D.3    Sommerer, N.4    Maurel, C.5
  • 26
    • 0026646048 scopus 로고
    • Determination of the site of phosphorylation of nodulin-26 by the calcium-dependent protein-kinase from soybean nodules
    • Weaver C.D., and Roberts D.M. Determination of the site of phosphorylation of nodulin-26 by the calcium-dependent protein-kinase from soybean nodules. Biochemistry 31 (1992) 8954-8959
    • (1992) Biochemistry , vol.31 , pp. 8954-8959
    • Weaver, C.D.1    Roberts, D.M.2
  • 27
    • 0028997596 scopus 로고
    • Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP
    • Maurel C., Kado R.T., Guern J., and Chrispeels M.J. Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP. EMBO J. 14 (1995) 3028-3035
    • (1995) EMBO J. , vol.14 , pp. 3028-3035
    • Maurel, C.1    Kado, R.T.2    Guern, J.3    Chrispeels, M.J.4
  • 28
    • 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., and Kjellbom P. Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. Plant Cell 10 (1998) 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
  • 29
    • 4344636281 scopus 로고    scopus 로고
    • Water channel activity of radish plasma membrane aquaporins heterologously expressed in yeast and their modification by site-directed mutagenesis
    • Suga S., and Maeshima M. Water channel activity of radish plasma membrane aquaporins heterologously expressed in yeast and their modification by site-directed mutagenesis. Plant Cell Physiol. 45 (2004) 823-830
    • (2004) Plant Cell Physiol. , vol.45 , pp. 823-830
    • Suga, S.1    Maeshima, M.2
  • 30
    • 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., and Roberts D.M. Phosphorylation of soybean nodulin 26 on serine 262 enhances water permeability and is regulated developmentally and by osmotic signals. Plant Cell 15 (2003) 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
  • 31
    • 2942711718 scopus 로고    scopus 로고
    • Phosphorylation of plasma membrane aquaporin regulates temperature-dependent opening of tulip petals
    • Azad A.K., Sawa Y., Ishikawa T., and Shibata H. Phosphorylation of plasma membrane aquaporin regulates temperature-dependent opening of tulip petals. Plant Cell Physiol. 45 (2004) 608-617
    • (2004) Plant Cell Physiol. , vol.45 , pp. 608-617
    • Azad, A.K.1    Sawa, Y.2    Ishikawa, T.3    Shibata, H.4
  • 32
    • 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., and Maurel C. The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH. Plant J. 30 (2002) 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
  • 33
    • 28044464281 scopus 로고    scopus 로고
    • Tonoplast vesicles of Beta vulgaris storage root show functional aquaporins regulated by protons
    • Sutka M., Alleva K., Parisi M., and Amodeo G. Tonoplast vesicles of Beta vulgaris storage root show functional aquaporins regulated by protons. Biol. Cell 97 (2005) 837-846
    • (2005) Biol. Cell , vol.97 , pp. 837-846
    • Sutka, M.1    Alleva, K.2    Parisi, M.3    Amodeo, G.4
  • 34
    • 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., Gout E., Gerbeau P., Luu D.T., Bligny R., and Maurel C. Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins. Nature 425 (2003) 393-397
    • (2003) Nature , vol.425 , pp. 393-397
    • Tournaire-Roux, C.1    Sutka, M.2    Javot, H.3    Gout, E.4    Gerbeau, P.5    Luu, D.T.6    Bligny, R.7    Maurel, C.8
  • 40
    • 0033579547 scopus 로고    scopus 로고
    • Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography
    • [published erratum appears in J. Mol. Biol. 2000 Mar 3;296(4):1163]
    • Daniels M.J., Chrispeels M.J., and Yeager M. Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography. [published erratum appears in J. Mol. Biol. 2000 Mar 3;296(4):1163]. J. Mol. Biol. 294 (1999) 1337-1349
    • (1999) J. Mol. Biol. , vol.294 , pp. 1337-1349
    • Daniels, M.J.1    Chrispeels, M.J.2    Yeager, M.3
  • 41
    • 0034668784 scopus 로고    scopus 로고
    • Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg(2+)-dependent and Ca(2+)-regulated kinase
    • Harvengt P., Vlerick A., Fuks B., Wattiez R., Ruysschaert J.M., and Homble F. Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg(2+)-dependent and Ca(2+)-regulated kinase. Biochem. J. 352 Pt. 1 (2000) 183-190
    • (2000) Biochem. J. , vol.352 , Issue.PART 1 , pp. 183-190
    • Harvengt, P.1    Vlerick, A.2    Fuks, B.3    Wattiez, R.4    Ruysschaert, J.M.5    Homble, F.6
  • 42
    • 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., Kanzawa N., Kuwahara M., Sasaki S., and Tsuchiya T. Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation. FEBS Lett. 579 (2005) 4417-4422
    • (2005) FEBS Lett. , vol.579 , pp. 4417-4422
    • Temmei, Y.1    Uchida, S.2    Hoshino, D.3    Kanzawa, N.4    Kuwahara, M.5    Sasaki, S.6    Tsuchiya, T.7
  • 43
    • 1142306039 scopus 로고    scopus 로고
    • A cohesion/tension mechanism explains the gating of water channels (aquaporins) in Chara internodes by high concentration
    • Ye Q., Muhr J., and Steudle E. A cohesion/tension mechanism explains the gating of water channels (aquaporins) in Chara internodes by high concentration. J. Exp. Bot. 55 (2004) 449-461
    • (2004) J. Exp. Bot. , vol.55 , pp. 449-461
    • Ye, Q.1    Muhr, J.2    Steudle, E.3
  • 44
    • 15944389916 scopus 로고    scopus 로고
    • A cohesion/tension model for the gating of aquaporins allows estimation of water channel pore volumes in Chara
    • Ye Q., Muhr J., and Steudle E. A cohesion/tension model for the gating of aquaporins allows estimation of water channel pore volumes in Chara. Plant Cell Environ. 28 (2005) 525-535
    • (2005) Plant Cell Environ. , vol.28 , pp. 525-535
    • Ye, Q.1    Muhr, J.2    Steudle, E.3
  • 45
    • 1142269645 scopus 로고    scopus 로고
    • Gating of water channels (aquaporins) in cortical cells of young corn roots by mechanical stimuli (pressure pulses): effects of ABA and of HgC12
    • Wan X., Steudle E., and Hartung W. Gating of water channels (aquaporins) in cortical cells of young corn roots by mechanical stimuli (pressure pulses): effects of ABA and of HgC12. J. Exp. Bot. 55 (2004) 411-422
    • (2004) J. Exp. Bot. , vol.55 , pp. 411-422
    • Wan, X.1    Steudle, E.2    Hartung, W.3
  • 47
    • 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., and Maurel C. Early effects of salinity on water transport in Arabidopsis roots. Molecular and cellular features of aquaporin expression. Plant Physiol. 139 (2005) 790-805
    • (2005) Plant Physiol. , vol.139 , pp. 790-805
    • Boursiac, Y.1    Chen, S.2    Luu, D.T.3    Sorieul, M.4    van den Dries, N.5    Maurel, C.6
  • 48
    • 0000179989 scopus 로고    scopus 로고
    • PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll
    • Robinson D.G., Sieber H., Kammerloher W., and Schaffner A.R. PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll. Plant Physiol. 111 (1996) 645-649
    • (1996) Plant Physiol. , vol.111 , pp. 645-649
    • Robinson, D.G.1    Sieber, H.2    Kammerloher, W.3    Schaffner, A.R.4
  • 50
    • 0032971712 scopus 로고    scopus 로고
    • Plant aquaporins: their molecular biology, biophysics and significance for plant water relations
    • Tyerman S.D., Bohnert H.J., Maurel C., Steudle E., and Smith J.A.C. Plant aquaporins: their molecular biology, biophysics and significance for plant water relations. J. Exp. Bot. 50 (1999) 1055-1071
    • (1999) J. Exp. Bot. , vol.50 , pp. 1055-1071
    • Tyerman, S.D.1    Bohnert, H.J.2    Maurel, C.3    Steudle, E.4    Smith, J.A.C.5
  • 51
    • 12444323669 scopus 로고    scopus 로고
    • An expression analysis of a gene family encoding plasma membrane aquaporins in response to abiotic stresses in Arabidopsis thaliana
    • Jang J.Y., Kim D.G., Kim Y.O., Kim J.S., and Kang H. An expression analysis of a gene family encoding plasma membrane aquaporins in response to abiotic stresses in Arabidopsis thaliana. Plant Mol. Biol. 54 (2004) 713-725
    • (2004) Plant Mol. Biol. , vol.54 , pp. 713-725
    • Jang, J.Y.1    Kim, D.G.2    Kim, Y.O.3    Kim, J.S.4    Kang, H.5
  • 52
    • 21644480409 scopus 로고    scopus 로고
    • Specific plasma membrane aquaporins of the PIP1 subfamily are expressed in sieve elements and guard cells
    • Fraysse L.C., Wells B., McCann M.C., and Kjellbom P. Specific plasma membrane aquaporins of the PIP1 subfamily are expressed in sieve elements and guard cells. Biol. Cell 97 (2005) 519-534
    • (2005) Biol. Cell , vol.97 , pp. 519-534
    • Fraysse, L.C.1    Wells, B.2    McCann, M.C.3    Kjellbom, P.4
  • 53
    • 0000785856 scopus 로고    scopus 로고
    • High expression of the tonoplast aquaporin ZmTIP1 in epidermal and conducting tissues of maize
    • Barrieu F., Chaumont F., and Chrispeels M.J. High expression of the tonoplast aquaporin ZmTIP1 in epidermal and conducting tissues of maize. Plant Physiol. 117 (1998) 1153-1163
    • (1998) Plant Physiol. , vol.117 , pp. 1153-1163
    • Barrieu, F.1    Chaumont, F.2    Chrispeels, M.J.3
  • 54
    • 0032133248 scopus 로고    scopus 로고
    • Characterization of a maize tonoplast aquaporin expressed in zones of cell division and elongation
    • Chaumont F., Barrieu F., Herman E.M., and Chrispeels M.J. Characterization of a maize tonoplast aquaporin expressed in zones of cell division and elongation. Plant Physiol. 117 (1998) 1143-1152
    • (1998) Plant Physiol. , vol.117 , pp. 1143-1152
    • Chaumont, F.1    Barrieu, F.2    Herman, E.M.3    Chrispeels, M.J.4
  • 55
    • 11444260781 scopus 로고    scopus 로고
    • PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development
    • Bots M., Feron R., Uehlein N., Waterings K., Kaldenhoff R., and Mariani T. PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development. J. Exp. Bot. 56 (2005) 113-121
    • (2005) J. Exp. Bot. , vol.56 , pp. 113-121
    • Bots, M.1    Feron, R.2    Uehlein, N.3    Waterings, K.4    Kaldenhoff, R.5    Mariani, T.6
  • 56
    • 0036009373 scopus 로고    scopus 로고
    • High expression of putative aquaporin genes in cells with transporting and nutritive functions during seed development in Norway spruce (Picea abies)
    • Hakman I., and Oliviusson P. High expression of putative aquaporin genes in cells with transporting and nutritive functions during seed development in Norway spruce (Picea abies). J. Exp. Bot. 53 (2002) 639-649
    • (2002) J. Exp. Bot. , vol.53 , pp. 639-649
    • Hakman, I.1    Oliviusson, P.2
  • 57
    • 0030918571 scopus 로고    scopus 로고
    • An aquaporin-like gene required for the Brassica self-incompatibility response
    • Ikeda S., Nasrallah J.B., Dixit R., Preiss S., and Nasrallah M.E. An aquaporin-like gene required for the Brassica self-incompatibility response. Science 276 (1997) 1564-1566
    • (1997) Science , vol.276 , pp. 1564-1566
    • Ikeda, S.1    Nasrallah, J.B.2    Dixit, R.3    Preiss, S.4    Nasrallah, M.E.5
  • 58
    • 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., and Borstlap A.C. Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies. Plant Mol. Biol. 53 (2003) 633-645
    • (2003) Plant Mol. Biol. , vol.53 , pp. 633-645
    • Schuurmans, J.A.1    van Dongen, J.T.2    Rutjens, B.P.3    Boonman, A.4    Pieterse, C.M.5    Borstlap, A.C.6
  • 59
    • 0033407429 scopus 로고    scopus 로고
    • Diurnal variations in hydraulic conductivity and root pressure can be correlated with the expression of putative aquaporins in the roots of lotus japonicus
    • Henzler T., Waterhouse R.N., Smyth A.J., Carvajal M., Cooke D.T., Schaffner A.R., Steudle E., and Clarkson D.T. Diurnal variations in hydraulic conductivity and root pressure can be correlated with the expression of putative aquaporins in the roots of lotus japonicus. Planta 210 (1999) 50-60
    • (1999) Planta , vol.210 , pp. 50-60
    • Henzler, T.1    Waterhouse, R.N.2    Smyth, A.J.3    Carvajal, M.4    Cooke, D.T.5    Schaffner, A.R.6    Steudle, E.7    Clarkson, D.T.8
  • 60
    • 0742270773 scopus 로고    scopus 로고
    • Diurnal regulation of water transport and aquaporin gene expression in maize roots: contribution of PIP2 proteins
    • Lopez M., Bousser A.S., Sissoeff I., Gaspar M., Lachaise B., Hoarau J., and Mahe A. Diurnal regulation of water transport and aquaporin gene expression in maize roots: contribution of PIP2 proteins. Plant Cell Physiol. 44 (2003) 1384-1395
    • (2003) Plant Cell Physiol. , vol.44 , pp. 1384-1395
    • Lopez, M.1    Bousser, A.S.2    Sissoeff, I.3    Gaspar, M.4    Lachaise, B.5    Hoarau, J.6    Mahe, A.7
  • 64
    • 27144525535 scopus 로고    scopus 로고
    • Differential responses of maize MIP genes to salt stress and ABA
    • Zhu C., Schraut D., Hartung W., and Schaffner A.R. Differential responses of maize MIP genes to salt stress and ABA. J. Exp. Bot. 56 (2005) 2971-2981
    • (2005) J. Exp. Bot. , vol.56 , pp. 2971-2981
    • Zhu, C.1    Schraut, D.2    Hartung, W.3    Schaffner, A.R.4
  • 66
    • 18744396394 scopus 로고    scopus 로고
    • The role of aquaporins and membrane damage in chilling and hydrogen peroxide induced changed in the hydraulic conductance of maize roots
    • Aroca R., Amodeo G., Fernandez-Illescas S., Herman E.M., Chaumont F., and Chrispeels M.J. The role of aquaporins and membrane damage in chilling and hydrogen peroxide induced changed in the hydraulic conductance of maize roots. Plant Physiol. 137 (2005) 341-353
    • (2005) Plant Physiol. , vol.137 , pp. 341-353
    • Aroca, R.1    Amodeo, G.2    Fernandez-Illescas, S.3    Herman, E.M.4    Chaumont, F.5    Chrispeels, M.J.6
  • 67
    • 0028371413 scopus 로고
    • Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel proteins
    • Fray R.G., Wallace A., Grierson D., and Lycett G.W. Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel proteins. Plant Mol. Biol. 24 (1994) 539-543
    • (1994) Plant Mol. Biol. , vol.24 , pp. 539-543
    • Fray, R.G.1    Wallace, A.2    Grierson, D.3    Lycett, G.W.4
  • 68
    • 0025463350 scopus 로고
    • Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes
    • Guerrero F.D., Jones J.T., and Mullet J.E. Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes. Plant Mol. Biol. 15 (1990) 11-26
    • (1990) Plant Mol. Biol. , vol.15 , pp. 11-26
    • Guerrero, F.D.1    Jones, J.T.2    Mullet, J.E.3
  • 69
    • 0028675651 scopus 로고
    • Isolation and expression analysis of 2 rice genes encoding the major intrinsic protein
    • Liu Q., Umeda M., and Uchimiya H. Isolation and expression analysis of 2 rice genes encoding the major intrinsic protein. Plant Mol. Biol. 26 (1994) 2003-2007
    • (1994) Plant Mol. Biol. , vol.26 , pp. 2003-2007
    • Liu, Q.1    Umeda, M.2    Uchimiya, H.3
  • 70
    • 0032438956 scopus 로고    scopus 로고
    • Desiccation- and abscisic acid-responsive genes encoding major intrinsic proteins (MIPs) from the resurrection plant Craterostigma plantagineum
    • Mariaux J.B., Bockel C., Salamini F., and Bartels D. Desiccation- and abscisic acid-responsive genes encoding major intrinsic proteins (MIPs) from the resurrection plant Craterostigma plantagineum. Plant Mol. Biol. 38 (1998) 1089-1099
    • (1998) Plant Mol. Biol. , vol.38 , pp. 1089-1099
    • Mariaux, J.B.1    Bockel, C.2    Salamini, F.3    Bartels, D.4
  • 71
    • 0032161048 scopus 로고    scopus 로고
    • Early salt-stress effects on expression of genes for aquaporin homologues in the halophyte sea aster (Aster triplium L.)
    • Uno Y., Urao T., Yamaguchi-Shinozaki K., Kanechi M., Inagaki N., Maekawa S., and Shinozaki K. Early salt-stress effects on expression of genes for aquaporin homologues in the halophyte sea aster (Aster triplium L.). J. Plant Res. 111 (1998) 411-419
    • (1998) J. Plant Res. , vol.111 , pp. 411-419
    • Uno, Y.1    Urao, T.2    Yamaguchi-Shinozaki, K.3    Kanechi, M.4    Inagaki, N.5    Maekawa, S.6    Shinozaki, K.7
  • 72
    • 0031266614 scopus 로고    scopus 로고
    • Expression of plasma membrane water channel genes under water stress in Nicotiana excelsior
    • Yamada S., Komori T., Myers P.N., Kuwata S., Kubo T., and Imaseki H. Expression of plasma membrane water channel genes under water stress in Nicotiana excelsior. Plant Cell Physiol. 38 (1997) 1226-1231
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1226-1231
    • Yamada, S.1    Komori, T.2    Myers, P.N.3    Kuwata, S.4    Kubo, T.5    Imaseki, H.6
  • 73
    • 0034657264 scopus 로고    scopus 로고
    • Molecular cloning of a novel water channel from rice: its products expression in Xenopus oocytes and involvement in chilling tolerance
    • Li L., Li S., Tao Y., and Kiatagawa Y. Molecular cloning of a novel water channel from rice: its products expression in Xenopus oocytes and involvement in chilling tolerance. Plant Sci. 154 (2000) 43-51
    • (2000) Plant Sci. , vol.154 , pp. 43-51
    • Li, L.1    Li, S.2    Tao, Y.3    Kiatagawa, Y.4
  • 74
    • 0036808135 scopus 로고    scopus 로고
    • Aquaporin isoforms responsive to salt and water stresses and phytohormones in radish seedlings
    • Suga S., Komatsu S., and Maeshima M. Aquaporin isoforms responsive to salt and water stresses and phytohormones in radish seedlings. Plant Cell Physiol. 43 (2002) 1229-1237
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1229-1237
    • Suga, S.1    Komatsu, S.2    Maeshima, M.3
  • 75
    • 0037145839 scopus 로고    scopus 로고
    • New potent inhibitors of aquaporins: silver and gold compounds inhibit aquaporins of plant and human origin
    • Niemietz C.M., and Tyerman S.D. New potent inhibitors of aquaporins: silver and gold compounds inhibit aquaporins of plant and human origin. FEBS Lett. 531 (2002) 443-447
    • (2002) FEBS Lett. , vol.531 , pp. 443-447
    • Niemietz, C.M.1    Tyerman, S.D.2
  • 76
    • 0034975415 scopus 로고    scopus 로고
    • Hydraulic conductance and mercury-sensitive water transport for roots of Opuntia acathorcarpa in relation to soil drying and rewetting
    • Martre P., North G.B., and Nobel P.S. Hydraulic conductance and mercury-sensitive water transport for roots of Opuntia acathorcarpa in relation to soil drying and rewetting. Plant Physiol. 126 (2001) 352-362
    • (2001) Plant Physiol. , vol.126 , pp. 352-362
    • Martre, P.1    North, G.B.2    Nobel, P.S.3
  • 77
    • 0028891577 scopus 로고
    • Effects of mercuric chloride on the hydraulic conductivity of tomato root systems (evidence for a channel-mediated water pathway)
    • Maggio A., and Joly R.J. Effects of mercuric chloride on the hydraulic conductivity of tomato root systems (evidence for a channel-mediated water pathway). Plant Physiol. 109 (1995) 331-335
    • (1995) Plant Physiol. , vol.109 , pp. 331-335
    • Maggio, A.1    Joly, R.J.2
  • 78
    • 0029838201 scopus 로고    scopus 로고
    • Responses of wheat plants to nutrient deprivation may involve the regulation of water-channel function
    • Carvajal M., Cooke D.T., and Clarkson D.T. Responses of wheat plants to nutrient deprivation may involve the regulation of water-channel function. Planta 199 (1996) 372-381
    • (1996) Planta , vol.199 , pp. 372-381
    • Carvajal, M.1    Cooke, D.T.2    Clarkson, D.T.3
  • 79
    • 0032918962 scopus 로고    scopus 로고
    • Physiological function of water channels as affected by salinity in roots of paprika pepper
    • Carvajal M., Martinez V., and Alcaraz C.F. Physiological function of water channels as affected by salinity in roots of paprika pepper. Physiol. Plant. 105 (1999) 95-101
    • (1999) Physiol. Plant. , vol.105 , pp. 95-101
    • Carvajal, M.1    Martinez, V.2    Alcaraz, C.F.3
  • 80
    • 0034099535 scopus 로고    scopus 로고
    • Does calcium ameliorate the negative effect of NaCl on melon root water transport by regulating aquaporin activity?
    • Carvajal M., Cerda A., and Martinez V. Does calcium ameliorate the negative effect of NaCl on melon root water transport by regulating aquaporin activity?. New Phytol. 145 (2000) 439-447
    • (2000) New Phytol. , vol.145 , pp. 439-447
    • Carvajal, M.1    Cerda, A.2    Martinez, V.3
  • 81
    • 0033009784 scopus 로고    scopus 로고
    • Radial and axial water transport in the sugar beet storage root
    • Amodeo G., Dorr R., Vallejo A., Sutka M., and Parisi M. Radial and axial water transport in the sugar beet storage root. J. Exp. Bot. 50 (1999) 509-516
    • (1999) J. Exp. Bot. , vol.50 , pp. 509-516
    • Amodeo, G.1    Dorr, R.2    Vallejo, A.3    Sutka, M.4    Parisi, M.5
  • 82
  • 83
    • 0036940134 scopus 로고    scopus 로고
    • Sensitivity of cell hydraulic conductivity to mercury is coincident with symplasmic isolation and expression of plasmalemma aquaporin genes in growing maize roots
    • Hukin D., Doering-Saad C., Thomas C.R., and Pritchard J. Sensitivity of cell hydraulic conductivity to mercury is coincident with symplasmic isolation and expression of plasmalemma aquaporin genes in growing maize roots. Planta 215 (2002) 1047-1056
    • (2002) Planta , vol.215 , pp. 1047-1056
    • Hukin, D.1    Doering-Saad, C.2    Thomas, C.R.3    Pritchard, J.4
  • 84
    • 0033677662 scopus 로고    scopus 로고
    • The high diversity of aquaporins reveals novel facets of plant membrane functions
    • Santoni V., Gerbeau P., Javot H., and Maurel C. The high diversity of aquaporins reveals novel facets of plant membrane functions. Curr. Opin. Plant Biol. 3 (2000) 476-481
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 476-481
    • Santoni, V.1    Gerbeau, P.2    Javot, H.3    Maurel, C.4
  • 85
    • 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., and Chrispeels M.J. 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 (1994) 1325-1333
    • (1994) Plant Physiol. , vol.106 , pp. 1325-1333
    • Daniels, M.J.1    Mirkov, T.E.2    Chrispeels, M.J.3
  • 86
  • 87
    • 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., and Kaldenhoff R. PIP1 plasma membrane aquaporins in tobacco: from cellular effects to function in plants. Plant Cell 14 (2002) 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
  • 88
    • 0032054595 scopus 로고    scopus 로고
    • Significance of plasmalemma aquaporins for water-transport in Arabidopsis thaliana
    • Kaldenhoff R., Grote K., Zhu J.J., and Zimmermann U. Significance of plasmalemma aquaporins for water-transport in Arabidopsis thaliana. Plant J. 14 (1998) 121-128
    • (1998) Plant J. , vol.14 , pp. 121-128
    • Kaldenhoff, R.1    Grote, K.2    Zhu, J.J.3    Zimmermann, U.4
  • 90
    • 0028486220 scopus 로고
    • Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system
    • Kammerloher W., Fischer U., Piechottka G.P., and Schaffner A.R. Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system. Plant J. 6 (1994) 187-199
    • (1994) Plant J. , vol.6 , pp. 187-199
    • Kammerloher, W.1    Fischer, U.2    Piechottka, G.P.3    Schaffner, A.R.4
  • 91
    • 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., and Chrispeels M.J. Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity. Plant Physiol. 122 (2000) 1025-1034
    • (2000) Plant Physiol. , vol.122 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Jung, R.3    Chrispeels, M.J.4
  • 93
    • 11144248492 scopus 로고    scopus 로고
    • Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death
    • Ma S., Quist T.M., Ulanov A., Joly R., and Bohnert H.J. Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death. Plant J. 40 (2004) 845-859
    • (2004) Plant J. , vol.40 , pp. 845-859
    • Ma, S.1    Quist, T.M.2    Ulanov, A.3    Joly, R.4    Bohnert, H.J.5
  • 94
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions
    • Jauh G.Y., Phillips T.E., and Rogers J.C. Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 11 (1999) 1867-1882
    • (1999) Plant Cell , vol.11 , pp. 1867-1882
    • Jauh, G.Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 96
    • 2942700260 scopus 로고    scopus 로고
    • Overexpression of the Barley aquaporin in 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., and Katsuhara M. Overexpression of the Barley aquaporin in HvPIP2;1 increases internal CO(2) conductance and CO(2) assimilation in the leaves of transgenic rice plants. Plant Cell Physiol. 45 (2004) 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
  • 97
    • 23244445986 scopus 로고    scopus 로고
    • Sense and antisense expression of plasma membrane aquaporin BnPIP1 from Brassica napus in tobacco and its effect on plant drought resistance
    • Yu Q.J., Hu Y.L., Li J.F., Wu Q., and Lin Z.P. Sense and antisense expression of plasma membrane aquaporin BnPIP1 from Brassica napus in tobacco and its effect on plant drought resistance. Plant Sci. 169 (2005) 647-656
    • (2005) Plant Sci. , vol.169 , pp. 647-656
    • Yu, Q.J.1    Hu, Y.L.2    Li, J.F.3    Wu, Q.4    Lin, Z.P.5
  • 98
    • 1242299060 scopus 로고    scopus 로고
    • Overexpression of a lily PIP1 gene in tobacco increased the osmotic water permeability of leaf cells
    • Ding X., Iwasaki I., and Kitagawa Y. Overexpression of a lily PIP1 gene in tobacco increased the osmotic water permeability of leaf cells. Plant Cell Environ. 27 (2004) 177-186
    • (2004) Plant Cell Environ. , vol.27 , pp. 177-186
    • Ding, X.1    Iwasaki, I.2    Kitagawa, Y.3
  • 99
    • 0033166563 scopus 로고    scopus 로고
    • Desiccation and osmotic stress increase the abundance of mRNA of the tonoplast aquaporin BobTIP26-1 in cauliflower cells
    • Barrieu F., Marty-Mazars D., Thomas D., Chaumont F., Charbonnier M., and Marty F. Desiccation and osmotic stress increase the abundance of mRNA of the tonoplast aquaporin BobTIP26-1 in cauliflower cells. Planta 206 (1999) 77-86
    • (1999) Planta , vol.206 , pp. 77-86
    • Barrieu, F.1    Marty-Mazars, D.2    Thomas, D.3    Chaumont, F.4    Charbonnier, M.5    Marty, F.6
  • 100
    • 0037560759 scopus 로고    scopus 로고
    • Expression of a cauliflower tonoplast aquaporin tagged with GFP in tobacco suspension cells correlates with an increase in cell size
    • Reisen D., Loborgne-Castel N., Ozalp C., Chaumont F., and Marty F. Expression of a cauliflower tonoplast aquaporin tagged with GFP in tobacco suspension cells correlates with an increase in cell size. Plant Mol. Biol. 52 (2003) 387-400
    • (2003) Plant Mol. Biol. , vol.52 , pp. 387-400
    • Reisen, D.1    Loborgne-Castel, N.2    Ozalp, C.3    Chaumont, F.4    Marty, F.5
  • 101
    • 0742305477 scopus 로고    scopus 로고
    • Overexpression of a barley aquaporin incased the shoot/root ratio and raised salt sensitivity in transgenic rice plants
    • Katsuhara M., Koshio K., Shibasaka M., Hayashi Y., Hayakawa T., and Kasamo K. Overexpression of a barley aquaporin incased the shoot/root ratio and raised salt sensitivity in transgenic rice plants. Plant Cell Physiol. 44 (2003) 1378-1383
    • (2003) Plant Cell Physiol. , vol.44 , pp. 1378-1383
    • Katsuhara, M.1    Koshio, K.2    Shibasaka, M.3    Hayashi, Y.4    Hayakawa, T.5    Kasamo, K.6
  • 102
    • 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., and Boron W.F. Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes. Am. J. Physiol., Cell Physiol. 43 (1998) C543-C548
    • (1998) Am. J. Physiol., Cell Physiol. , vol.43
    • Nakhoul, N.L.1    Davis, B.A.2    Romero, M.F.3    Boron, W.F.4
  • 103
    • 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.X., Fukuda N., van Hoek A., Matthay M.A., Ma T.H., and Verkman A.S. Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes. J. Biol. Chem. 275 (2000) 2686-2692
    • (2000) J. Biol. Chem. , vol.275 , pp. 2686-2692
    • Yang, B.X.1    Fukuda, N.2    van Hoek, A.3    Matthay, M.A.4    Ma, T.H.5    Verkman, A.S.6
  • 104
    • 0036660839 scopus 로고    scopus 로고
    • Evidence against aquaporin-1-dependent CO2 permeability in lung and kidney
    • Fang X., Yang B., Matthay M.A., and Verkman A.S. Evidence against aquaporin-1-dependent CO2 permeability in lung and kidney. J. Physiol. 542 (2002) 63-69
    • (2002) J. Physiol. , vol.542 , pp. 63-69
    • Fang, X.1    Yang, B.2    Matthay, M.A.3    Verkman, A.S.4
  • 105
    • 0142246438 scopus 로고    scopus 로고
    • The tobacco aquaporinNtAQP1 is a membrane CO2 pore with physiological functions
    • Uehlein N., Lovisolo C., Siefritz F., and Kaldenhoff R. The tobacco aquaporinNtAQP1 is a membrane CO2 pore with physiological functions. Nature 425 (2003) 734-737
    • (2003) Nature , vol.425 , pp. 734-737
    • Uehlein, N.1    Lovisolo, C.2    Siefritz, F.3    Kaldenhoff, R.4
  • 106
    • 2942700260 scopus 로고    scopus 로고
    • Overexpression of the barley aquaporinHvPIP2;1 increases internal CO2 conductance and CO2 assimilation in the leaves of transgenic rice plants
    • Hanba Y.T., Shibasaka M., Hayashi Y., Hayakawa T., Kasamo K., Terashima I., and Katsuhara M. Overexpression of the barley aquaporinHvPIP2;1 increases internal CO2 conductance and CO2 assimilation in the leaves of transgenic rice plants. Plant Cell Physiol. 45 (2004) 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
  • 107
    • 0242432461 scopus 로고    scopus 로고
    • Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but to under drought or salt stress
    • Aharon R., Shahak Y., Wininger S., Bendov R., Kapulnik Y., and Galili G. Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but to under drought or salt stress. Plant Cell 15 (2003) 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
  • 108
    • 1642441941 scopus 로고    scopus 로고
    • The plasma membrane aquaporin NtAQP1 is a key component of the leaf unfolding mechanism in tobacco
    • Siefritz F., Otto B., Bienert G.P., van der Krol A., and Kaldenhoff R. The plasma membrane aquaporin NtAQP1 is a key component of the leaf unfolding mechanism in tobacco. Plant J. 37 (2004) 147-155
    • (2004) Plant J. , vol.37 , pp. 147-155
    • Siefritz, F.1    Otto, B.2    Bienert, G.P.3    van der Krol, A.4    Kaldenhoff, R.5
  • 109
    • 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., and Mariani C. Aquaporins of the PIP2 class are required for efficient anther dehiscence in tobacco. Plant Physiol. 137 (2005) 1049-1056
    • (2005) Plant Physiol. , vol.137 , pp. 1049-1056
    • Bots, M.1    Vergeldt, F.2    Wolters-Arts, M.3    Weterings, K.4    van As, H.5    Mariani, C.6
  • 110
    • 34250095000 scopus 로고
    • A berberine-anilin blue fluorescent staining procedure for suberin, lignin, and callose in plant-tissue
    • Brundrett M.C., Enstone D.E., and Peterson C.A. A berberine-anilin blue fluorescent staining procedure for suberin, lignin, and callose in plant-tissue. Protoplasma 146 (1988) 133-142
    • (1988) Protoplasma , vol.146 , pp. 133-142
    • Brundrett, M.C.1    Enstone, D.E.2    Peterson, C.A.3


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