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Volumn 6, Issue 9, 2011, Pages

Characterization of leishmania donovani aquaporins shows presence of subcellular aquaporins similar to tonoplast intrinsic proteins of plants

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AQUAPORIN; ARGININE; GLYCEROL; VALINE; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; TONOPLAST INTRINSIC PROTEIN, PLANT; VEGETABLE PROTEIN;

EID: 80053232424     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024820     Document Type: Article
Times cited : (18)

References (53)
  • 1
    • 0034451615 scopus 로고    scopus 로고
    • Failure of pentavalent antimony in visceral leishmaniasis in India: report from the center of the Indian epidemic
    • CID000236 [pii];10.1086/318121 [doi]
    • Sundar S, More DK, Singh MK, Singh VP, Sharma S, et al. (2000) Failure of pentavalent antimony in visceral leishmaniasis in India: report from the center of the Indian epidemic. Clin Infect Dis 31: 1104-1107 CID000236 [pii];10.1086/318121 [doi].
    • (2000) Clin Infect Dis , vol.31 , pp. 1104-1107
    • Sundar, S.1    More, D.K.2    Singh, M.K.3    Singh, V.P.4    Sharma, S.5
  • 2
    • 1642442461 scopus 로고    scopus 로고
    • Channels and transporters as drug targets in the Plasmodium-infected erythrocyte
    • S0001706X03002717 [pii]
    • Kirk K, (2004) Channels and transporters as drug targets in the Plasmodium-infected erythrocyte. Acta Trop 89: 285-298 S0001706X03002717 [pii].
    • (2004) Acta Trop , vol.89 , pp. 285-298
    • Kirk, K.1
  • 3
    • 21044454794 scopus 로고    scopus 로고
    • Aquaporins from pathogenic protozoan parasites: structure, function and potential for chemotherapy
    • BC20040095 [pii];10.1042/BC20040095 [doi]
    • Beitz E, (2005) Aquaporins from pathogenic protozoan parasites: structure, function and potential for chemotherapy. Biol Cell 97: 373-383 BC20040095 [pii];10.1042/BC20040095 [doi].
    • (2005) Biol Cell , vol.97 , pp. 373-383
    • Beitz, E.1
  • 4
    • 24644521470 scopus 로고    scopus 로고
    • Brain mitochondria contain aquaporin water channels: evidence for the expression of a short AQP9 isoform in the inner mitochondrial membrane
    • 19/11/1459 [pii];10.1096/fj.04-3515com [doi]
    • Amiry-Moghaddam M, Lindland H, Zelenin S, Roberg BA, Gundersen BB, et al. (2005) Brain mitochondria contain aquaporin water channels: evidence for the expression of a short AQP9 isoform in the inner mitochondrial membrane. FASEB J 19: 1459-1467 19/11/1459 [pii];10.1096/fj.04-3515com [doi].
    • (2005) FASEB J , vol.19 , pp. 1459-1467
    • Amiry-Moghaddam, M.1    Lindland, H.2    Zelenin, S.3    Roberg, B.A.4    Gundersen, B.B.5
  • 5
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • 10.1146/annurev.biochem.68.1.425 [doi]
    • Borgnia M, Nielsen S, Engel A, Agre P, (1999) Cellular and molecular biology of the aquaporin water channels. Annu Rev Biochem 68: 425-458 10.1146/annurev.biochem.68.1.425 [doi].
    • (1999) Annu Rev Biochem , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 6
    • 22244437571 scopus 로고    scopus 로고
    • The genome of the kinetoplastid parasite, Leishmania major
    • 309/5733/436 [pii];10.1126/science.1112680 [doi]
    • Ivens AC, Peacock CS, Worthey EA, Murphy L, Aggarwal G, et al. (2005) The genome of the kinetoplastid parasite, Leishmania major. Science 309: 436-442 309/5733/436 [pii];10.1126/science.1112680 [doi].
    • (2005) Science , vol.309 , pp. 436-442
    • Ivens, A.C.1    Peacock, C.S.2    Worthey, E.A.3    Murphy, L.4    Aggarwal, G.5
  • 7
    • 61449375176 scopus 로고    scopus 로고
    • Aquaglyceroporins and metalloid transport: implications in human diseases
    • 10.1007/978-3-540-79885-9_16 [doi]
    • Bhattacharjee H, Rosen BP, Mukhopadhyay R, (2009) Aquaglyceroporins and metalloid transport: implications in human diseases. Handb Exp Pharmacol pp. 309-325 10.1007/978-3-540-79885-9_16 [doi].
    • (2009) Handb Exp Pharmacol , pp. 309-325
    • Bhattacharjee, H.1    Rosen, B.P.2    Mukhopadhyay, R.3
  • 8
    • 34547665529 scopus 로고    scopus 로고
    • Biochemical characterization of Leishmania major aquaglyceroporin LmAQP1: possible role in volume regulation and osmotaxis
    • MMI5845 [pii];10.1111/j.1365-2958.2007.05845.x [doi]
    • Figarella K, Uzcategui NL, Zhou Y, LeFurgey A, Ouellette M, et al. (2007) Biochemical characterization of Leishmania major aquaglyceroporin LmAQP1: possible role in volume regulation and osmotaxis. Mol Microbiol 65: 1006-1017 MMI5845 [pii];10.1111/j.1365-2958.2007.05845.x [doi].
    • (2007) Mol Microbiol , vol.65 , pp. 1006-1017
    • Figarella, K.1    Uzcategui, N.L.2    Zhou, Y.3    LeFurgey, A.4    Ouellette, M.5
  • 9
    • 0033063643 scopus 로고    scopus 로고
    • Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation
    • Tamas MJ, Luyten K, Sutherland FC, Hernandez A, Albertyn J, et al. (1999) Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation. Mol Microbiol 31: 1087-1104.
    • (1999) Mol Microbiol , vol.31 , pp. 1087-1104
    • Tamas, M.J.1    Luyten, K.2    Sutherland, F.C.3    Hernandez, A.4    Albertyn, J.5
  • 10
    • 0037805604 scopus 로고    scopus 로고
    • Fps1p channel is the mediator of the major part of glycerol passive diffusion in Saccharomyces cerevisiae: artefacts and re-definitions
    • S000527360300138X [pii]
    • Oliveira R, Lages F, Silva-Graca M, Lucas C, (2003) Fps1p channel is the mediator of the major part of glycerol passive diffusion in Saccharomyces cerevisiae: artefacts and re-definitions. Biochim Biophys Acta 1613: 57-71 S000527360300138X [pii].
    • (2003) Biochim Biophys Acta , vol.1613 , pp. 57-71
    • Oliveira, R.1    Lages, F.2    Silva-Graca, M.3    Lucas, C.4
  • 11
    • 15244340168 scopus 로고    scopus 로고
    • Gln3p and Nil1p regulation of invertase activity and SUC2 expression in Saccharomyces cerevisiae
    • S1567-1356(04)00182-5 [pii];10.1016/j.femsyr.2004.11.011 [doi]
    • Oliveira EM, Mansure JJ, Bon EP, (2005) Gln3p and Nil1p regulation of invertase activity and SUC2 expression in Saccharomyces cerevisiae. FEMS Yeast Res 5: 605-609 S1567-1356(04)00182-5 [pii];10.1016/j.femsyr.2004.11.011 [doi].
    • (2005) FEMS Yeast Res , vol.5 , pp. 605-609
    • Oliveira, E.M.1    Mansure, J.J.2    Bon, E.P.3
  • 12
    • 5644230835 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and characterization of three aquaglyceroporins from Trypanosoma brucei
    • 10.1074/jbc.M404518200 [doi];M404518200 [pii]
    • Uzcategui NL, Szallies A, Pavlovic-Djuranovic S, Palmada M, Figarella K, et al. (2004) Cloning, heterologous expression, and characterization of three aquaglyceroporins from Trypanosoma brucei. J Biol Chem 279: 42669-42676 10.1074/jbc.M404518200 [doi];M404518200 [pii].
    • (2004) J Biol Chem , vol.279 , pp. 42669-42676
    • Uzcategui, N.L.1    Szallies, A.2    Pavlovic-Djuranovic, S.3    Palmada, M.4    Figarella, K.5
  • 13
    • 21844460489 scopus 로고    scopus 로고
    • The yeast osmosensitive mutant fps1Delta transformed by the cauliflower BobTIP1;1 aquaporin withstand a hypo-osmotic shock
    • S0014-5793(05)00706-4 [pii];10.1016/j.febslet.2005.05.076 [doi]
    • Prudent S, Marty F, Charbonnier M, (2005) The yeast osmosensitive mutant fps1Delta transformed by the cauliflower BobTIP1;1 aquaporin withstand a hypo-osmotic shock. FEBS Lett 579: 3872-3880 S0014-5793(05)00706-4 [pii];10.1016/j.febslet.2005.05.076 [doi].
    • (2005) FEBS Lett , vol.579 , pp. 3872-3880
    • Prudent, S.1    Marty, F.2    Charbonnier, M.3
  • 14
    • 0034703362 scopus 로고    scopus 로고
    • Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae
    • S0014-5793(00)02027-5 [pii]
    • Weig AR, Jakob C, (2000) Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae. FEBS Lett 481: 293-298 S0014-5793(00)02027-5 [pii].
    • (2000) FEBS Lett , vol.481 , pp. 293-298
    • Weig, A.R.1    Jakob, C.2
  • 15
    • 33747889760 scopus 로고    scopus 로고
    • Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae
    • 10.1007/s00294-006-0092-z [doi]
    • Pettersson N, Hagstrom J, Bill RM, Hohmann S, (2006) Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae. Curr Genet 50: 247-255 10.1007/s00294-006-0092-z [doi].
    • (2006) Curr Genet , vol.50 , pp. 247-255
    • Pettersson, N.1    Hagstrom, J.2    Bill, R.M.3    Hohmann, S.4
  • 16
    • 0028302033 scopus 로고
    • GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway
    • Albertyn J, Hohmann S, Thevelein JM, Prior BA, (1994) GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway. Mol Cell Biol 14: 4135-4144.
    • (1994) Mol Cell Biol , vol.14 , pp. 4135-4144
    • Albertyn, J.1    Hohmann, S.2    Thevelein, J.M.3    Prior, B.A.4
  • 17
    • 3843084085 scopus 로고    scopus 로고
    • Drug uptake and modulation of drug resistance in Leishmania by an aquaglyceroporin
    • 10.1074/jbc.M403959200 [doi];M403959200 [pii]
    • Gourbal B, Sonuc N, Bhattacharjee H, Legare D, Sundar S, et al. (2004) Drug uptake and modulation of drug resistance in Leishmania by an aquaglyceroporin. J Biol Chem 279: 31010-31017 10.1074/jbc.M403959200 [doi];M403959200 [pii].
    • (2004) J Biol Chem , vol.279 , pp. 31010-31017
    • Gourbal, B.1    Sonuc, N.2    Bhattacharjee, H.3    Legare, D.4    Sundar, S.5
  • 18
    • 77950336943 scopus 로고    scopus 로고
    • Assessing aquaglyceroporin gene status and expression profile in antimony-susceptible and -resistant clinical isolates of Leishmania donovani from India
    • dkp468 [pii];10.1093/jac/dkp468 [doi]
    • Mandal S, Maharjan M, Singh S, Chatterjee M, Madhubala R, (2010) Assessing aquaglyceroporin gene status and expression profile in antimony-susceptible and-resistant clinical isolates of Leishmania donovani from India. J Antimicrob Chemother 65: 496-507 dkp468 [pii];10.1093/jac/dkp468 [doi].
    • (2010) J Antimicrob Chemother , vol.65 , pp. 496-507
    • Mandal, S.1    Maharjan, M.2    Singh, S.3    Chatterjee, M.4    Madhubala, R.5
  • 19
    • 46849086969 scopus 로고    scopus 로고
    • Role of aquaglyceroporin (AQP1) gene and drug uptake in antimony-resistant clinical isolates of Leishmania donovani
    • 79/1/69 [pii]
    • Maharjan M, Singh S, Chatterjee M, Madhubala R, (2008) Role of aquaglyceroporin (AQP1) gene and drug uptake in antimony-resistant clinical isolates of Leishmania donovani. Am J Trop Med Hyg 79: 69-75 79/1/69 [pii].
    • (2008) Am J Trop Med Hyg , vol.79 , pp. 69-75
    • Maharjan, M.1    Singh, S.2    Chatterjee, M.3    Madhubala, R.4
  • 20
    • 33748560815 scopus 로고    scopus 로고
    • Aquaporin subfamily with unusual NPA boxes
    • S0005-2736(06)00077-0 [pii];10.1016/j.bbamem.2006.02.024 [doi]
    • Ishibashi K, (2006) Aquaporin subfamily with unusual NPA boxes. Biochim Biophys Acta 1758: 989-993 S0005-2736(06)00077-0 [pii];10.1016/j.bbamem.2006.02.024 [doi].
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 989-993
    • Ishibashi, K.1
  • 21
    • 33748556239 scopus 로고    scopus 로고
    • Aquaporin-5 water channel in lipid rafts of rat parotid glands
    • S0005-2736(06)00112-X [pii];10.1016/j.bbamem.2006.03.026 [doi]
    • Ishikawa Y, Cho G, Yuan Z, Inoue N, Nakae Y, (2006) Aquaporin-5 water channel in lipid rafts of rat parotid glands. Biochim Biophys Acta 1758: 1053-1060 S0005-2736(06)00112-X [pii];10.1016/j.bbamem.2006.03.026 [doi].
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1053-1060
    • Ishikawa, Y.1    Cho, G.2    Yuan, Z.3    Inoue, N.4    Nakae, Y.5
  • 22
  • 23
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Moller S, Croning MD, Apweiler R, (2001) Evaluation of methods for the prediction of membrane spanning regions. Bioinformatics 17: 646-653.
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Moller, S.1    Croning, M.D.2    Apweiler, R.3
  • 24
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • btn221 [pii];10.1093/bioinformatics/btn221 [doi]
    • Viklund H, Elofsson A, (2008) OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24: 1662-1668 btn221 [pii];10.1093/bioinformatics/btn221 [doi].
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 25
    • 84859917105 scopus 로고    scopus 로고
    • EMBOSS HMOMENT
    • Available:. Accessed 2011 Jan 3
    • EMBOSS HMOMENT. Available: http://inn-temp.weizmann.ac.il/cgi-bin/emboss/help/hmoment. Accessed 2011 Jan 3.
  • 26
    • 51749085388 scopus 로고    scopus 로고
    • HELIQUEST: a web server to screen sequences with specific alpha-helical properties
    • btn392 [pii];10.1093/bioinformatics/btn392 [doi]
    • Gautier R, Douguet D, Antonny B, Drin G, (2008) HELIQUEST: a web server to screen sequences with specific alpha-helical properties. Bioinformatics 24: 2101-2102 btn392 [pii];10.1093/bioinformatics/btn392 [doi].
    • (2008) Bioinformatics , vol.24 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Antonny, B.3    Drin, G.4
  • 27
    • 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: 52-6, 29.
    • (1990) J Mol Graph , vol.8
    • Vriend, G.1
  • 28
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • gkm216 [pii];10.1093/nar/gkm216 [doi]
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-W383 gkm216 [pii];10.1093/nar/gkm216 [doi].
    • (2007) Nucleic Acids Res , vol.35 , pp. 375-383
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 29
    • 68249097450 scopus 로고    scopus 로고
    • PoreWalker: a novel tool for the identification and characterization of channels in transmembrane proteins from their three-dimensional structure
    • 10.1371/journal.pcbi.1000440 [doi]
    • Pellegrini-Calace M, Maiwald T, Thornton JM, (2009) PoreWalker: a novel tool for the identification and characterization of channels in transmembrane proteins from their three-dimensional structure. PLoS Comput Biol 5: e1000440 10.1371/journal.pcbi.1000440 [doi].
    • (2009) PLoS Comput Biol , vol.5
    • Pellegrini-Calace, M.1    Maiwald, T.2    Thornton, J.M.3
  • 30
    • 0029858530 scopus 로고    scopus 로고
    • A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network
    • Alconada A, Bauer U, Hoflack B, (1996) A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network. EMBO J 15: 6096-6110.
    • (1996) EMBO J , vol.15 , pp. 6096-6110
    • Alconada, A.1    Bauer, U.2    Hoflack, B.3
  • 31
    • 33845669996 scopus 로고    scopus 로고
    • The structure of aquaporins
    • S0033583506004458 [pii];10.1017/S0033583506004458 [doi]
    • Gonen T, Walz T, (2006) The structure of aquaporins. Q Rev Biophys 39: 361-396 S0033583506004458 [pii];10.1017/S0033583506004458 [doi].
    • (2006) Q Rev Biophys , vol.39 , pp. 361-396
    • Gonen, T.1    Walz, T.2
  • 32
    • 11144248492 scopus 로고    scopus 로고
    • Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death
    • TPJ2265 [pii];10.1111/j.1365-313X.2004.02265.x [doi]
    • Ma S, Quist TM, Ulanov A, Joly R, Bohnert HJ, (2004) Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death. Plant J 40: 845-859 TPJ2265 [pii];10.1111/j.1365-313X.2004.02265.x [doi].
    • (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
  • 33
    • 48249135074 scopus 로고    scopus 로고
    • Identification of transmembrane region and orientation of aquaglyceroporin of Plasmodium falciparum
    • Wiwanitkit V, (2008) Identification of transmembrane region and orientation of aquaglyceroporin of Plasmodium falciparum. Indian J Med Microbiol 26: 246-247.
    • (2008) Indian J Med Microbiol , vol.26 , pp. 246-247
    • Wiwanitkit, V.1
  • 34
    • 33847313314 scopus 로고    scopus 로고
    • Exploring gas permeability of cellular membranes and membrane channels with molecular dynamics
    • S1047-8477(06)00378-9 [pii];10.1016/j.jsb.2006.11.008 [doi]
    • Wang Y, Cohen J, Boron WF, Schulten K, Tajkhorshid E, (2007) Exploring gas permeability of cellular membranes and membrane channels with molecular dynamics. J Struct Biol 157: 534-544 S1047-8477(06)00378-9 [pii];10.1016/j.jsb.2006.11.008 [doi].
    • (2007) J Struct Biol , vol.157 , pp. 534-544
    • Wang, Y.1    Cohen, J.2    Boron, W.F.3    Schulten, K.4    Tajkhorshid, E.5
  • 35
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F, (1991) Getting started with yeast. Methods Enzymol 194: 3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 36
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A, (1983) Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153: 163-168.
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 37
    • 0033747235 scopus 로고    scopus 로고
    • Episomal and stable expression of the luciferase reporter gene for quantifying Leishmania spp. infections in macrophages and in animal models
    • S0166-6851(00)00270-X [pii]
    • Roy G, Dumas C, Sereno D, Wu Y, Singh AK, et al. (2000) Episomal and stable expression of the luciferase reporter gene for quantifying Leishmania spp. infections in macrophages and in animal models. Mol Biochem Parasitol 110: 195-206 S0166-6851(00)00270-X [pii].
    • (2000) Mol Biochem Parasitol , vol.110 , pp. 195-206
    • Roy, G.1    Dumas, C.2    Sereno, D.3    Wu, Y.4    Singh, A.K.5
  • 38
    • 48249102000 scopus 로고    scopus 로고
    • Phylogeny.fr: robust phylogenetic analysis for the non-specialist
    • gkn180 [pii];10.1093/nar/gkn180 [doi]
    • Dereeper A, Guignon V, Blanc G, Audic S, Buffet S, et al. (2008) Phylogeny.fr: robust phylogenetic analysis for the non-specialist. Nucleic Acids Res 36: W465-W469 gkn180 [pii];10.1093/nar/gkn180 [doi].
    • (2008) Nucleic Acids Res , vol.36 , pp. 465-469
    • Dereeper, A.1    Guignon, V.2    Blanc, G.3    Audic, S.4    Buffet, S.5
  • 39
    • 0035852730 scopus 로고    scopus 로고
    • Visualization of a water-selective pore by electron crystallography in vitreous ice
    • 10.1073/pnas.041489198 [doi];041489198 [pii]
    • Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK, (2001) Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc Natl Acad Sci U S A 98: 1398-1403 10.1073/pnas.041489198 [doi];041489198 [pii].
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1398-1403
    • Ren, G.1    Reddy, V.S.2    Cheng, A.3    Melnyk, P.4    Mitra, A.K.5
  • 40
    • 67649963000 scopus 로고    scopus 로고
    • Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism
    • 10.1371/journal.pbio.1000130 [doi]
    • Fischer G, Kosinska-Eriksson U, Aponte-Santamaria C, Palmgren M, Geijer C, et al. (2009) Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism. PLoS Biol 7: e1000130 10.1371/journal.pbio.1000130 [doi].
    • (2009) PLoS Biol , vol.7
    • Fischer, G.1    Kosinska-Eriksson, U.2    Aponte-Santamaria, C.3    Palmgren, M.4    Geijer, C.5
  • 41
    • 29144521255 scopus 로고    scopus 로고
    • Implications of the aquaporin-4 structure on array formation and cell adhesion
    • S0022-2836(05)01366-5 [pii];10.1016/j.jmb.2005.10.081 [doi]
    • Hiroaki Y, Tani K, Kamegawa A, Gyobu N, Nishikawa K, et al. (2006) Implications of the aquaporin-4 structure on array formation and cell adhesion. J Mol Biol 355: 628-639 S0022-2836(05)01366-5 [pii];10.1016/j.jmb.2005.10.081 [doi].
    • (2006) J Mol Biol , vol.355 , pp. 628-639
    • Hiroaki, Y.1    Tani, K.2    Kamegawa, A.3    Gyobu, N.4    Nishikawa, K.5
  • 42
    • 32544450674 scopus 로고    scopus 로고
    • Structural mechanism of plant aquaporin gating
    • nature04316 [pii];10.1038/nature04316 [doi]
    • Tornroth-Horsefield S, Wang Y, Hedfalk K, Johanson U, Karlsson M, et al. (2006) Structural mechanism of plant aquaporin gating. Nature 439: 688-694 nature04316 [pii];10.1038/nature04316 [doi].
    • (2006) Nature , vol.439 , pp. 688-694
    • Tornroth-Horsefield, S.1    Wang, Y.2    Hedfalk, K.3    Johanson, U.4    Karlsson, M.5
  • 43
    • 44849139900 scopus 로고    scopus 로고
    • Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum
    • nsmb.1431 [pii];10.1038/nsmb.1431 [doi]
    • Newby ZE, O'Connell J III, Robles-Colmenares Y, Khademi S, Miercke LJ, et al. (2008) Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum. Nat Struct Mol Biol 15: 619-625 nsmb.1431 [pii];10.1038/nsmb.1431 [doi].
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 619-625
    • Newby, Z.E.1    O'Connell III, J.2    Robles-Colmenares, Y.3    Khademi, S.4    Miercke, L.J.5
  • 44
    • 33644850534 scopus 로고    scopus 로고
    • Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel
    • M508926200 [pii];10.1074/jbc.M508926200 [doi]
    • Jiang J, Daniels BV, Fu D, (2006) Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel. J Biol Chem 281: 454-460 M508926200 [pii];10.1074/jbc.M508926200 [doi].
    • (2006) J Biol Chem , vol.281 , pp. 454-460
    • Jiang, J.1    Daniels, B.V.2    Fu, D.3
  • 45
    • 0037134267 scopus 로고    scopus 로고
    • Control of the selectivity of the aquaporin water channel family by global orientational tuning
    • 10.1126/science.1067778 [doi];296/5567/525 [pii]
    • Tajkhorshid E, Nollert P, Jensen MO, Miercke LJ, O'Connell J, et al. (2002) Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science 296: 525-530 10.1126/science.1067778 [doi];296/5567/525 [pii].
    • (2002) Science , vol.296 , pp. 525-530
    • Tajkhorshid, E.1    Nollert, P.2    Jensen, M.O.3    Miercke, L.J.4    O'Connell, J.5
  • 46
  • 48
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • 10.1002/prot.1168 [pii]
    • Bates PA, Kelley LA, MacCallum RM, Sternberg MJ, (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins Suppl 5: 39-46 10.1002/prot.1168 [pii].
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 49
    • 49649114605 scopus 로고    scopus 로고
    • Protein structure modeling with MODELLER
    • 10.1007/978-1-60327-058-8_8 [doi]
    • Eswar N, Eramian D, Webb B, Shen MY, Sali A, (2008) Protein structure modeling with MODELLER. Methods Mol Biol 426: 145-159 10.1007/978-1-60327-058-8_8 [doi].
    • (2008) Methods Mol Biol , vol.426 , pp. 145-159
    • Eswar, N.1    Eramian, D.2    Webb, B.3    Shen, M.Y.4    Sali, A.5
  • 50
    • 84859890422 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 0.99
    • Schrödinger L, The PyMOL Molecular Graphics System, Version 0.99.
    • Schrödinger, L.1
  • 51
    • 0029119568 scopus 로고
    • RASMOL: biomolecular graphics for all
    • S0968-0004(00)89080-5 [pii]
    • Sayle RA, Milner-White EJ, (1995) RASMOL: biomolecular graphics for all. Trends Biochem Sci 20: 374 S0968-0004(00)89080-5 [pii].
    • (1995) Trends Biochem Sci , vol.20 , pp. 374
    • Sayle, R.A.1    Milner-White, E.J.2
  • 52
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins
    • gkm290 [pii];10.1093/nar/gkm290 [doi]
    • Wiederstein M, Sippl MJ, (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 35: W407-W410 gkm290 [pii];10.1093/nar/gkm290 [doi].
    • (2007) Nucleic Acids Res , vol.35 , pp. 407-410
    • Wiederstein, M.1    Sippl, M.J.2
  • 53
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D, Luthy R, Bowie JU, (1997) VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol 277: 396-404.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.