메뉴 건너뛰기




Volumn 69, Issue , 2012, Pages 325-358

Pathways of Arsenic Uptake and Efflux

Author keywords

Aquaglyceroporin; Arsenate; Arsenic; Arsenite; ATPase; Metallochaperone

Indexed keywords


EID: 84867182300     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394390-3.00012-4     Document Type: Chapter
Times cited : (171)

References (137)
  • 1
    • 40949115926 scopus 로고    scopus 로고
    • Transmembrane topology of the Acr3 family arsenite transporter from Bacillus subtilis
    • Aaltonen E.K., Silow M. Transmembrane topology of the Acr3 family arsenite transporter from Bacillus subtilis. Biochimica et Biophysica Acta 2008, 1778(4):963-973.
    • (2008) Biochimica et Biophysica Acta , vol.1778 , Issue.4 , pp. 963-973
    • Aaltonen, E.K.1    Silow, M.2
  • 3
    • 33847680027 scopus 로고    scopus 로고
    • Diversity of arsenite transporter genes from arsenic-resistant soil bacteria
    • Achour A.R., Bauda P., Billard P. Diversity of arsenite transporter genes from arsenic-resistant soil bacteria. Research in Microbiology 2007, 158(2):128-137.
    • (2007) Research in Microbiology , vol.158 , Issue.2 , pp. 128-137
    • Achour, A.R.1    Bauda, P.2    Billard, P.3
  • 4
    • 23944450334 scopus 로고    scopus 로고
    • Nobel lecture. Aquaporin water channels
    • Agre P. Nobel lecture. Aquaporin water channels. Bioscience Reports 2004, 24(3):127-163.
    • (2004) Bioscience Reports , vol.24 , Issue.3 , pp. 127-163
    • Agre, P.1
  • 6
    • 0242573122 scopus 로고    scopus 로고
    • Aquaporin water channels: molecular mechanisms for human diseases
    • Agre P., Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Letters 2003, 555(1):72-78.
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 72-78
    • Agre, P.1    Kozono, D.2
  • 7
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner E.S., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. European Journal of Biochemistry 2000, 267(20):6102-6109.
    • (2000) European Journal of Biochemistry , vol.267 , Issue.20 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 8
    • 84055213176 scopus 로고    scopus 로고
    • Oral arsenic trioxide-based maintenance regimens for first complete remission of acute promyelocytic leukemia: a 10-year follow-up study
    • Au W.Y., Kumana C.R., Lee H.K., Lin S.Y., Liu H., Yeung D.Y., et al. Oral arsenic trioxide-based maintenance regimens for first complete remission of acute promyelocytic leukemia: a 10-year follow-up study. Blood 2011, 118(25):6535-6543.
    • (2011) Blood , vol.118 , Issue.25 , pp. 6535-6543
    • Au, W.Y.1    Kumana, C.R.2    Lee, H.K.3    Lin, S.Y.4    Liu, H.5    Yeung, D.Y.6
  • 9
    • 33748901612 scopus 로고    scopus 로고
    • The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae
    • Auld K.L., Hitchcock A.L., Doherty H.K., Frietze S., Huang L.S., Silver P.A. The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae. Genetics 2006, 174(1):215-227.
    • (2006) Genetics , vol.174 , Issue.1 , pp. 215-227
    • Auld, K.L.1    Hitchcock, A.L.2    Doherty, H.K.3    Frietze, S.4    Huang, L.S.5    Silver, P.A.6
  • 11
    • 0029011877 scopus 로고
    • Role of cysteinyl residues in metalloactivation of the oxyanion-translocating ArsA ATPase
    • Bhattacharjee H., Li J., Ksenzenko M.Y., Rosen B.P. Role of cysteinyl residues in metalloactivation of the oxyanion-translocating ArsA ATPase. The Journal of Biological Chemistry 1995, 270(19):11245-11250.
    • (1995) The Journal of Biological Chemistry , vol.270 , Issue.19 , pp. 11245-11250
    • Bhattacharjee, H.1    Li, J.2    Ksenzenko, M.Y.3    Rosen, B.P.4
  • 13
    • 0029661442 scopus 로고    scopus 로고
    • Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase
    • Bhattacharjee H., Rosen B.P. Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase. The Journal of Biological Chemistry 1996, 271(40):24465-24470.
    • (1996) The Journal of Biological Chemistry , vol.271 , Issue.40 , pp. 24465-24470
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 14
    • 0034470035 scopus 로고    scopus 로고
    • Role of conserved histidine residues in metalloactivation of the ArsA ATPase
    • Bhattacharjee H., Rosen B.P. Role of conserved histidine residues in metalloactivation of the ArsA ATPase. Biometals 2000, 13(4):281-288.
    • (2000) Biometals , vol.13 , Issue.4 , pp. 281-288
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 15
    • 36348997984 scopus 로고    scopus 로고
    • Arsenic metabolism in prokaryotic and eukaryotic microbes
    • Springer-Verlag, Heidelberg/New York
    • Bhattacharjee H., Rosen B.P. Arsenic metabolism in prokaryotic and eukaryotic microbes. Molecular microbiology of heavy metals 2007, Vol. 6:371-406. Springer-Verlag, Heidelberg/New York.
    • (2007) Molecular microbiology of heavy metals , vol.6 , pp. 371-406
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 17
    • 0030836016 scopus 로고    scopus 로고
    • Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae
    • Bobrowicz P., Wysocki R., Owsianik G., Goffeau A., Ulaszewski S. Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast 1997, 13(9):819-828.
    • (1997) Yeast , vol.13 , Issue.9 , pp. 819-828
    • Bobrowicz, P.1    Wysocki, R.2    Owsianik, G.3    Goffeau, A.4    Ulaszewski, S.5
  • 19
    • 0029913162 scopus 로고    scopus 로고
    • Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in Saccharomyces cerevisiae
    • Bun-ya M., Shikata K., Nakade S., Yompakdee C., Harashima S., Oshima Y. Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in Saccharomyces cerevisiae. Current Genetics 1996, 29(4):344-351.
    • (1996) Current Genetics , vol.29 , Issue.4 , pp. 344-351
    • Bun-ya, M.1    Shikata, K.2    Nakade, S.3    Yompakdee, C.4    Harashima, S.5    Oshima, Y.6
  • 21
    • 0027500261 scopus 로고
    • Arsenical-resistant trypanosomes lack an unusual adenosine transporter
    • Carter N.S., Fairlamb A.H. Arsenical-resistant trypanosomes lack an unusual adenosine transporter. Nature 1993, 361(6408):173-176.
    • (1993) Nature , vol.361 , Issue.6408 , pp. 173-176
    • Carter, N.S.1    Fairlamb, A.H.2
  • 22
    • 0023038352 scopus 로고
    • Nucleotide sequence of the structural genes for an anion pump. The plasmid-encoded arsenical resistance operon
    • Chen C.M., Misra T.K., Silver S., Rosen B.P. Nucleotide sequence of the structural genes for an anion pump. The plasmid-encoded arsenical resistance operon. The Journal of Biological Chemistry 1986, 261(32):15030-15038.
    • (1986) The Journal of Biological Chemistry , vol.261 , Issue.32 , pp. 15030-15038
    • Chen, C.M.1    Misra, T.K.2    Silver, S.3    Rosen, B.P.4
  • 23
    • 0030043666 scopus 로고    scopus 로고
    • Soft metal thiol chemistry is not involved in the transport of arsenite by the Ars pump
    • Chen Y., Dey S., Rosen B.P. Soft metal thiol chemistry is not involved in the transport of arsenite by the Ars pump. Journal of Bacteriology 1996, 178(3):911-913.
    • (1996) Journal of Bacteriology , vol.178 , Issue.3 , pp. 911-913
    • Chen, Y.1    Dey, S.2    Rosen, B.P.3
  • 25
    • 10044276808 scopus 로고    scopus 로고
    • Arsenic speciation in bile and urine following oral and intravenous exposure to inorganic and organic arsenics in rats
    • Cui X., Kobayashi Y., Hayakawa T., Hirano S. Arsenic speciation in bile and urine following oral and intravenous exposure to inorganic and organic arsenics in rats. Toxicological Sciences 2004, 82(2):478-487.
    • (2004) Toxicological Sciences , vol.82 , Issue.2 , pp. 478-487
    • Cui, X.1    Kobayashi, Y.2    Hayakawa, T.3    Hirano, S.4
  • 26
    • 0032933610 scopus 로고    scopus 로고
    • Malignant cells can be sensitized to undergo growth inhibition and apoptosis by arsenic trioxide through modulation of the glutathione redox system
    • Dai J., Weinberg R.S., Waxman S., Jing Y. Malignant cells can be sensitized to undergo growth inhibition and apoptosis by arsenic trioxide through modulation of the glutathione redox system. Blood 1999, 93(1):268-277.
    • (1999) Blood , vol.93 , Issue.1 , pp. 268-277
    • Dai, J.1    Weinberg, R.S.2    Waxman, S.3    Jing, Y.4
  • 27
    • 0028116110 scopus 로고
    • ATP-dependent arsenite transport in everted membrane vesicles of Escherichia coli
    • Dey S., Dou D., Rosen B.P. ATP-dependent arsenite transport in everted membrane vesicles of Escherichia coli. The Journal of Biological Chemistry 1994, 269(41):25442-25446.
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.41 , pp. 25442-25446
    • Dey, S.1    Dou, D.2    Rosen, B.P.3
  • 28
    • 0028309454 scopus 로고
    • Interaction of the catalytic and the membrane subunits of an oxyanion-translocating ATPase
    • Dey S., Dou D., Tisa L.S., Rosen B.P. Interaction of the catalytic and the membrane subunits of an oxyanion-translocating ATPase. Archives of Biochemistry and Biophysics 1994, 311(2):418-424.
    • (1994) Archives of Biochemistry and Biophysics , vol.311 , Issue.2 , pp. 418-424
    • Dey, S.1    Dou, D.2    Tisa, L.S.3    Rosen, B.P.4
  • 30
    • 0028796058 scopus 로고
    • Dual mode of energy coupling by the oxyanion-translocating ArsB protein
    • Dey S., Rosen B.P. Dual mode of energy coupling by the oxyanion-translocating ArsB protein. Journal of Bacteriology 1995, 177(2):385-389.
    • (1995) Journal of Bacteriology , vol.177 , Issue.2 , pp. 385-389
    • Dey, S.1    Rosen, B.P.2
  • 32
    • 84855884222 scopus 로고    scopus 로고
    • Expressing ScACR3 in rice enhanced arsenite efflux and reduced arsenic accumulation in rice grains
    • Duan G., Kamiya T., Ishikawa S., Arao T., Fujiwara T. Expressing ScACR3 in rice enhanced arsenite efflux and reduced arsenic accumulation in rice grains. Plant and Cell Physiology 2012, 53(1):154-163.
    • (2012) Plant and Cell Physiology , vol.53 , Issue.1 , pp. 154-163
    • Duan, G.1    Kamiya, T.2    Ishikawa, S.3    Arao, T.4    Fujiwara, T.5
  • 33
    • 77955414007 scopus 로고    scopus 로고
    • Arsenic trioxide-an old drug rediscovered
    • Emadi A., Gore S.D. Arsenic trioxide-an old drug rediscovered. Blood Review 2010, 24(4-5):191-199.
    • (2010) Blood Review , vol.24 , Issue.4-5 , pp. 191-199
    • Emadi, A.1    Gore, S.D.2
  • 34
    • 75349088244 scopus 로고    scopus 로고
    • Role of signature lysines in the deviant walker a motifs of the ArsA ATPase
    • Fu H.L., Ajees A.A., Rosen B.P., Bhattacharjee H. Role of signature lysines in the deviant walker a motifs of the ArsA ATPase. Biochemistry 2010, 49(2):356-364.
    • (2010) Biochemistry , vol.49 , Issue.2 , pp. 356-364
    • Fu, H.L.1    Ajees, A.A.2    Rosen, B.P.3    Bhattacharjee, H.4
  • 35
    • 67749129499 scopus 로고    scopus 로고
    • Properties of arsenite efflux permeases (Acr3) from Alkaliphilus metalliredigens and Corynebacterium glutamicum
    • Fu H.L., Meng Y., Ordonez E., Villadangos A.F., Bhattacharjee H., Gill J.A., et al. Properties of arsenite efflux permeases (Acr3) from Alkaliphilus metalliredigens and Corynebacterium glutamicum. The Journal of Biological Chemistry 2009, 284(30):19887-19895.
    • (2009) The Journal of Biological Chemistry , vol.284 , Issue.30 , pp. 19887-19895
    • Fu, H.L.1    Meng, Y.2    Ordonez, E.3    Villadangos, A.F.4    Bhattacharjee, H.5    Gill, J.A.6
  • 36
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis M.M., Komiya H.P.C., Woo D., Kornuc J.J., Rees D.C. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 1992, 257(5077):1653-1659.
    • (1992) Science , vol.257 , Issue.5077 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.P.C.2    Woo, D.3    Kornuc, J.J.4    Rees, D.C.5
  • 38
    • 0028289612 scopus 로고
    • Properties of the arsenate reductase of plasmid R773
    • Gladysheva T.B., Oden K.L., Rosen B.P. Properties of the arsenate reductase of plasmid R773. Biochemistry 1994, 33(23):7288-7293.
    • (1994) Biochemistry , vol.33 , Issue.23 , pp. 7288-7293
    • Gladysheva, T.B.1    Oden, K.L.2    Rosen, B.P.3
  • 39
    • 1242335471 scopus 로고    scopus 로고
    • The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulation
    • Haimeur A., Conseil G., Deeley R.G., Cole S.P. The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulation. Current Drug Metabolism 2004, 5(1):21-53.
    • (2004) Current Drug Metabolism , vol.5 , Issue.1 , pp. 21-53
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.4
  • 41
    • 0019195926 scopus 로고
    • Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli
    • Heller K.B., Lin E.C., Wilson T.H. Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli. Journal of Bacteriology 1980, 144(1):274-278.
    • (1980) Journal of Bacteriology , vol.144 , Issue.1 , pp. 274-278
    • Heller, K.B.1    Lin, E.C.2    Wilson, T.H.3
  • 42
    • 0024407624 scopus 로고
    • Characterization of the catalytic subunit of an anion pump
    • Hsu C.M., Rosen B.P. Characterization of the catalytic subunit of an anion pump. The Journal of Biological Chemistry 1989, 264(29):17349-17354.
    • (1989) The Journal of Biological Chemistry , vol.264 , Issue.29 , pp. 17349-17354
    • Hsu, C.M.1    Rosen, B.P.2
  • 44
    • 0037036585 scopus 로고    scopus 로고
    • Effect of arsenic on transcription factor AP-1 and NF-kappaB DNA binding activity and related gene expression
    • Hu Y., Jin X., Snow E.T. Effect of arsenic on transcription factor AP-1 and NF-kappaB DNA binding activity and related gene expression. Toxicological Letters 2002, 133(1):33-45.
    • (2002) Toxicological Letters , vol.133 , Issue.1 , pp. 33-45
    • Hu, Y.1    Jin, X.2    Snow, E.T.3
  • 45
    • 77955910648 scopus 로고    scopus 로고
    • A vacuolar arsenite transporter necessary for arsenic tolerance in the arsenic hyperaccumulating fern Pteris vittata is missing in flowering plants
    • Indriolo E., Na G., Ellis D., Salt D.E., Banks J.A. A vacuolar arsenite transporter necessary for arsenic tolerance in the arsenic hyperaccumulating fern Pteris vittata is missing in flowering plants. The Plant Cell 2010, 22(6):2045-2057.
    • (2010) The Plant Cell , vol.22 , Issue.6 , pp. 2045-2057
    • Indriolo, E.1    Na, G.2    Ellis, D.3    Salt, D.E.4    Banks, J.A.5
  • 47
    • 0033848711 scopus 로고    scopus 로고
    • Cellular localization of aquaporin 7 in the rat kidney
    • Ishibashi K., Imai M., Sasaki S. Cellular localization of aquaporin 7 in the rat kidney. Experimental Nephrology 2000, 8(4-5):252-257.
    • (2000) Experimental Nephrology , vol.8 , Issue.4-5 , pp. 252-257
    • Ishibashi, K.1    Imai, M.2    Sasaki, S.3
  • 48
    • 0030860531 scopus 로고    scopus 로고
    • Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea
    • Ishibashi K., Kuwahara M., Gu Y., Kageyama Y., Tohsaka A., Suzuki F., et al. Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea. The Journal of Biological Chemistry 1997, 272(33):20782-20786.
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20782-20786
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Kageyama, Y.4    Tohsaka, A.5    Suzuki, F.6
  • 49
    • 0032489241 scopus 로고    scopus 로고
    • Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol
    • Ishibashi K., Kuwahara M., Gu Y., Tanaka Y., Marumo F., Sasaki S. Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol. Biochemical and Biophysical Research Communications 1998, 244(1):268-274.
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , Issue.1 , pp. 268-274
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Tanaka, Y.4    Marumo, F.5    Sasaki, S.6
  • 50
    • 0037135227 scopus 로고    scopus 로고
    • Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin
    • Ishibashi K., Morinaga T., Kuwahara M., Sasaki S., Imai M. Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin. Biochimica et Biophysica Acta 2002, 1576(3):335-340.
    • (2002) Biochimica et Biophysica Acta , vol.1576 , Issue.3 , pp. 335-340
    • Ishibashi, K.1    Morinaga, T.2    Kuwahara, M.3    Sasaki, S.4    Imai, M.5
  • 52
    • 0026640112 scopus 로고
    • Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258
    • Ji G., Silver S. Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258. Proceedings of the National Academy of Sciences of the United States of America 1992, 89(20):9474-9478.
    • (1992) Proceedings of the National Academy of Sciences of the United States of America , vol.89 , Issue.20 , pp. 9474-9478
    • Ji, G.1    Silver, S.2
  • 54
    • 0034680928 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase
    • Kapahi P., Takahashi T., Natoli G., Adams S.R., Chen Y., Tsien R.Y., et al. Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase. The Journal of Biological Chemistry 2000, 275(46):36062-36066.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.46 , pp. 36062-36066
    • Kapahi, P.1    Takahashi, T.2    Natoli, G.3    Adams, S.R.4    Chen, Y.5    Tsien, R.Y.6
  • 55
    • 0025321162 scopus 로고
    • Mutagenesis of a nucleotide-binding site of an anion-translocating ATPase
    • Karkaria C.E., Chen C.M., Rosen B.P. Mutagenesis of a nucleotide-binding site of an anion-translocating ATPase. The Journal of Biological Chemistry 1990, 265(14):7832-7836.
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.14 , pp. 7832-7836
    • Karkaria, C.E.1    Chen, C.M.2    Rosen, B.P.3
  • 56
    • 0026726796 scopus 로고
    • Mutagenesis of the C-terminal nucleotide-binding site of an anion-translocating ATPase
    • Kaur P., Rosen B.P. Mutagenesis of the C-terminal nucleotide-binding site of an anion-translocating ATPase. The Journal of Biological Chemistry 1992, 267(27):19272-19277.
    • (1992) The Journal of Biological Chemistry , vol.267 , Issue.27 , pp. 19272-19277
    • Kaur, P.1    Rosen, B.P.2
  • 57
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin E.V. A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. Journal of Molecular Biology 1993, 229(4):1165-1174.
    • (1993) Journal of Molecular Biology , vol.229 , Issue.4 , pp. 1165-1174
    • Koonin, E.V.1
  • 58
    • 0031033050 scopus 로고    scopus 로고
    • Alternate energy coupling of ArsB, the membrane subunit of the Ars anion-translocating ATPase
    • Kuroda M., Dey S., Sanders O.I., Rosen B.P. Alternate energy coupling of ArsB, the membrane subunit of the Ars anion-translocating ATPase. The Journal of Biological Chemistry 1997, 272(1):326-331.
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.1 , pp. 326-331
    • Kuroda, M.1    Dey, S.2    Sanders, O.I.3    Rosen, B.P.4
  • 59
    • 0031137591 scopus 로고    scopus 로고
    • Delicious poison: arsenic trioxide for the treatment of leukemia
    • Kwong Y.L., Todd D. Delicious poison: arsenic trioxide for the treatment of leukemia. Blood 1997, 89(9):3487-3488.
    • (1997) Blood , vol.89 , Issue.9 , pp. 3487-3488
    • Kwong, Y.L.1    Todd, D.2
  • 61
    • 33846233015 scopus 로고    scopus 로고
    • Relationship of expression of aquaglyceroporin 9 with arsenic uptake and sensitivity in leukemia cells
    • Leung J., Pang A., Yuen W.H., Kwong Y.L., Tse E.W. Relationship of expression of aquaglyceroporin 9 with arsenic uptake and sensitivity in leukemia cells. Blood 2007, 109(2):740-746.
    • (2007) Blood , vol.109 , Issue.2 , pp. 740-746
    • Leung, J.1    Pang, A.2    Yuen, W.H.3    Kwong, Y.L.4    Tse, E.W.5
  • 62
    • 0029817926 scopus 로고    scopus 로고
    • Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump
    • Li J., Liu S., Rosen B.P. Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump. The Journal of Biological Chemistry 1996, 271(41):25247-25252.
    • (1996) The Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25247-25252
    • Li, J.1    Liu, S.2    Rosen, B.P.3
  • 63
    • 0033955818 scopus 로고    scopus 로고
    • The linker peptide of the ArsA ATPase
    • Li J., Rosen B.P. The linker peptide of the ArsA ATPase. Molecular Microbiology 2000, 35(2):361-367.
    • (2000) Molecular Microbiology , vol.35 , Issue.2 , pp. 361-367
    • Li, J.1    Rosen, B.P.2
  • 66
    • 34447116980 scopus 로고    scopus 로고
    • ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity
    • Lin Y.F., Yang J., Rosen B.P. ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity. The Journal of Biological Chemistry 2007, 282(23):16783-16791.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.23 , pp. 16783-16791
    • Lin, Y.F.1    Yang, J.2    Rosen, B.P.3
  • 71
  • 72
    • 0038349270 scopus 로고    scopus 로고
    • MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation
    • Lutkenhaus J., Sundaramoorthy M. MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation. Molecular Microbiology 2003, 48(2):295-303.
    • (2003) Molecular Microbiology , vol.48 , Issue.2 , pp. 295-303
    • Lutkenhaus, J.1    Sundaramoorthy, M.2
  • 74
    • 4344689976 scopus 로고    scopus 로고
    • Arsenical resistance genes in Saccharomyces douglasii and other yeast species undergo rapid evolution involving genomic rearrangements and duplications
    • Maciaszczyk E., Wysocki R., Golik P., Lazowska J., Ulaszewski S. Arsenical resistance genes in Saccharomyces douglasii and other yeast species undergo rapid evolution involving genomic rearrangements and duplications. FEMS Yeast Research 2004, 4(8):821-832.
    • (2004) FEMS Yeast Research , vol.4 , Issue.8 , pp. 821-832
    • Maciaszczyk, E.1    Wysocki, R.2    Golik, P.3    Lazowska, J.4    Ulaszewski, S.5
  • 77
    • 33846452511 scopus 로고    scopus 로고
    • The bile/arsenite/riboflavin transporter (BART) superfamily
    • Mansour N.M., Sawhney M., Tamang D.G., Vogl C., Saier M.H. The bile/arsenite/riboflavin transporter (BART) superfamily. FEBS Journal 2007, 274(3):612-629.
    • (2007) FEBS Journal , vol.274 , Issue.3 , pp. 612-629
    • Mansour, N.M.1    Sawhney, M.2    Tamang, D.G.3    Vogl, C.4    Saier, M.H.5
  • 78
    • 77950556954 scopus 로고    scopus 로고
    • High levels of human chorionic gonadotropin (hCG) correlate with increased aquaporin-9 (AQP9) expression in explants from human preeclamptic placenta
    • Marino G.I., Castro-Parodi M., Dietrich V., Damiano A.E. High levels of human chorionic gonadotropin (hCG) correlate with increased aquaporin-9 (AQP9) expression in explants from human preeclamptic placenta. Reproductive Science 2010, 17(5):444-453.
    • (2010) Reproductive Science , vol.17 , Issue.5 , pp. 444-453
    • Marino, G.I.1    Castro-Parodi, M.2    Dietrich, V.3    Damiano, A.E.4
  • 79
    • 70349272618 scopus 로고    scopus 로고
    • The structural basis of tail-anchored membrane protein recognition by Get3
    • Mateja A., Szlachcic A., Downing M.E., Dobosz M., Mariappan M., Hegde R.S., et al. The structural basis of tail-anchored membrane protein recognition by Get3. Nature 2009, 461(7262):361-366.
    • (2009) Nature , vol.461 , Issue.7262 , pp. 361-366
    • Mateja, A.1    Szlachcic, A.2    Downing, M.E.3    Dobosz, M.4    Mariappan, M.5    Hegde, R.S.6
  • 80
    • 77949425114 scopus 로고    scopus 로고
    • Pentavalent methylated arsenicals are substrates of human AQP9
    • McDermott J.R., Jiang X., Beene L.C., Rosen B.P., Liu Z. Pentavalent methylated arsenicals are substrates of human AQP9. Biometals 2010, 23(1):119-127.
    • (2010) Biometals , vol.23 , Issue.1 , pp. 119-127
    • McDermott, J.R.1    Jiang, X.2    Beene, L.C.3    Rosen, B.P.4    Liu, Z.5
  • 81
    • 2442605626 scopus 로고    scopus 로고
    • As(III) and Sb(III) uptake by GlpF and efflux by ArsB in Escherichia coli
    • Meng Y.L., Liu Z., Rosen B.P. As(III) and Sb(III) uptake by GlpF and efflux by ArsB in Escherichia coli. The Journal of Biological Chemistry 2004, 279:18334-18341.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 18334-18341
    • Meng, Y.L.1    Liu, Z.2    Rosen, B.P.3
  • 83
    • 0036802691 scopus 로고    scopus 로고
    • Arsenate reductases in prokaryotes and eukaryotes
    • Mukhopadhyay R., Rosen B.P. Arsenate reductases in prokaryotes and eukaryotes. Environmental Health Perspectives 2002, 110(Suppl. 5):745-748.
    • (2002) Environmental Health Perspectives , vol.110 , Issue.SUPPL. 5 , pp. 745-748
    • Mukhopadhyay, R.1    Rosen, B.P.2
  • 84
    • 0031769690 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase
    • Mukhopadhyay R., Rosen B.P. The Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase. FEMS Microbiology Letters 1998, 168:127-136.
    • (1998) FEMS Microbiology Letters , vol.168 , pp. 127-136
    • Mukhopadhyay, R.1    Rosen, B.P.2
  • 85
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones: an intracellular shuttle service for metal ions
    • O'Halloran T.V., Culotta V.C. Metallochaperones: an intracellular shuttle service for metal ions. The Journal of Biological Chemistry 2000, 275(33):25057-25060.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.33 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 87
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis
    • Pai E.F., Krengel U., Petsko G.A., Goody R.S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO Journal 1990, 9(8):2351-2359.
    • (1990) EMBO Journal , vol.9 , Issue.8 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 88
    • 77149134306 scopus 로고    scopus 로고
    • Aquaporin 9 expression in the developing rat epididymis is modulated by steroid hormones
    • Pastor-Soler N.M., Fisher J.S., Sharpe R., Hill E., Van Hoek A., Brown D., et al. Aquaporin 9 expression in the developing rat epididymis is modulated by steroid hormones. Reproduction 2010, 139(3):613-621.
    • (2010) Reproduction , vol.139 , Issue.3 , pp. 613-621
    • Pastor-Soler, N.M.1    Fisher, J.S.2    Sharpe, R.3    Hill, E.4    Van Hoek, A.5    Brown, D.6
  • 89
    • 36349027677 scopus 로고    scopus 로고
    • Convergent evolution of a new arsenic binding site in the ArsR/SmtB family of metalloregulators
    • Qin J., Fu H.L., Ye J., Bencze K.Z., Stemmler T.L., Rawlings D.E., et al. Convergent evolution of a new arsenic binding site in the ArsR/SmtB family of metalloregulators. The Journal of Biological Chemistry 2007, 282(47):34346-34355.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.47 , pp. 34346-34355
    • Qin, J.1    Fu, H.L.2    Ye, J.3    Bencze, K.Z.4    Stemmler, T.L.5    Rawlings, D.E.6
  • 90
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase
    • Rae T.D., Schmidt P.J., Pufahl R.A., Culotta V.C., O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 1999, 284(5415):805-808.
    • (1999) Science , vol.284 , Issue.5415 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 91
    • 0032502681 scopus 로고    scopus 로고
    • Nucleotide binding to the C-terminal nucleotide binding domain of ArsA: studies with an ATP analogue, 5' -p-fluorosulfonylbenzoyladenosine
    • Ramaswamy S., Kaur P. Nucleotide binding to the C-terminal nucleotide binding domain of ArsA: studies with an ATP analogue, 5' -p-fluorosulfonylbenzoyladenosine. The Journal of Biological Chemistry 1998, 273(15):9243-9248.
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 9243-9248
    • Ramaswamy, S.1    Kaur, P.2
  • 92
    • 11144354454 scopus 로고    scopus 로고
    • Experimental and theoretical characterization of arsenite in water: insights into the coordination environment of As-O
    • Ramírez-Solis A., Mukopadhyay R., Rosen B.P., Stemmler T.L. Experimental and theoretical characterization of arsenite in water: insights into the coordination environment of As-O. Inorganic Chemistry 2004, 43(9):2954-2959.
    • (2004) Inorganic Chemistry , vol.43 , Issue.9 , pp. 2954-2959
    • Ramírez-Solis, A.1    Mukopadhyay, R.2    Rosen, B.P.3    Stemmler, T.L.4
  • 93
    • 85067717124 scopus 로고    scopus 로고
    • Heavy metals cycles (arsenic, mercury, selenium, others)
    • Elsevier, Oxford, U.K. M. Schaechter (Ed.)
    • Rensing C., Rosen B.P. Heavy metals cycles (arsenic, mercury, selenium, others). Encyclopedia of microbiology 2009, 205-219. Elsevier, Oxford, U.K. M. Schaechter (Ed.).
    • (2009) Encyclopedia of microbiology , pp. 205-219
    • Rensing, C.1    Rosen, B.P.2
  • 94
    • 0033134885 scopus 로고    scopus 로고
    • Families of arsenic transporters
    • Rosen B.P. Families of arsenic transporters. Trends in Microbiology 1999, 7:207-212.
    • (1999) Trends in Microbiology , vol.7 , pp. 207-212
    • Rosen, B.P.1
  • 95
    • 0037010116 scopus 로고    scopus 로고
    • Biochemistry of arsenic detoxification
    • Rosen B.P. Biochemistry of arsenic detoxification. FEBS Letters 2002, 529(1):86-92.
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 86-92
    • Rosen, B.P.1
  • 96
    • 0023834869 scopus 로고
    • Molecular characterization of an anion pump. The arsA gene product is an arsenite(antimonate)-stimulated ATPase
    • Rosen B.P., Weigel U., Karkaria C., Gangola P. Molecular characterization of an anion pump. The arsA gene product is an arsenite(antimonate)-stimulated ATPase. The Journal of Biological Chemistry 1988, 263(7):3067-3070.
    • (1988) The Journal of Biological Chemistry , vol.263 , Issue.7 , pp. 3067-3070
    • Rosen, B.P.1    Weigel, U.2    Karkaria, C.3    Gangola, P.4
  • 97
    • 0017521785 scopus 로고
    • Two systems for the uptake of phosphate in Escherichia coli
    • Rosenberg H., Gerdes R.G., Chegwidden K. Two systems for the uptake of phosphate in Escherichia coli. Journal of Bacteriology 1977, 131(2):505-511.
    • (1977) Journal of Bacteriology , vol.131 , Issue.2 , pp. 505-511
    • Rosenberg, H.1    Gerdes, R.G.2    Chegwidden, K.3
  • 98
    • 37349131627 scopus 로고    scopus 로고
    • Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump
    • Ruan X., Bhattacharjee H., Rosen B.P. Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump. Molecular Microbiology 2008, 67(2):392-402.
    • (2008) Molecular Microbiology , vol.67 , Issue.2 , pp. 392-402
    • Ruan, X.1    Bhattacharjee, H.2    Rosen, B.P.3
  • 99
    • 33744508953 scopus 로고    scopus 로고
    • Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase
    • Ruan X., Bhattacharjee H., Rosen B.P. Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase. The Journal of Biological Chemistry 2006, 281(15):9925-9934.
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 9925-9934
    • Ruan, X.1    Bhattacharjee, H.2    Rosen, B.P.3
  • 100
    • 0025061168 scopus 로고
    • Identification of the metalloregulatory element of the plasmid-encoded arsenical resistance operon
    • San Francisco M.J., Hope C.L., Owolabi J.B., Tisa L.S., Rosen B.P. Identification of the metalloregulatory element of the plasmid-encoded arsenical resistance operon. Nucleic Acids Research 1990, 18(3):619-624.
    • (1990) Nucleic Acids Research , vol.18 , Issue.3 , pp. 619-624
    • San Francisco, M.J.1    Hope, C.L.2    Owolabi, J.B.3    Tisa, L.S.4    Rosen, B.P.5
  • 101
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli
    • Sanders O.I., Rensing C., Kuroda M., Mitra B., Rosen B.P. Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli. Journal of Bacteriology 1997, 179(10):3365-3367.
    • (1997) Journal of Bacteriology , vol.179 , Issue.10 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.P.5
  • 102
    • 0031896498 scopus 로고    scopus 로고
    • The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite
    • Sato T., Kobayashi Y. The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite. Journal of Bacteriology 1998, 180(7):1655-1661.
    • (1998) Journal of Bacteriology , vol.180 , Issue.7 , pp. 1655-1661
    • Sato, T.1    Kobayashi, Y.2
  • 103
    • 0030611701 scopus 로고    scopus 로고
    • Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction
    • Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C. Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 1997, 387(6631):370-376.
    • (1997) Nature , vol.387 , Issue.6631 , pp. 370-376
    • Schindelin, H.1    Kisker, C.2    Schlessman, J.L.3    Howard, J.B.4    Rees, D.C.5
  • 104
    • 0037412034 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance
    • Shen J., Hsu C.M., Kang B.K., Rosen B.P., Bhattacharjee H. The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance. Biometals 2003, 16:369-378.
    • (2003) Biometals , vol.16 , pp. 369-378
    • Shen, J.1    Hsu, C.M.2    Kang, B.K.3    Rosen, B.P.4    Bhattacharjee, H.5
  • 106
    • 0033813588 scopus 로고    scopus 로고
    • Contamination of drinking-water by arsenic in Bangladesh: a public health emergency
    • Smith A.H., Lingas E.O., Rahman M. Contamination of drinking-water by arsenic in Bangladesh: a public health emergency. Bulletin of the World Health Organization 2000, 78(9):1093-1103.
    • (2000) Bulletin of the World Health Organization , vol.78 , Issue.9 , pp. 1093-1103
    • Smith, A.H.1    Lingas, E.O.2    Rahman, M.3
  • 107
    • 0035040975 scopus 로고    scopus 로고
    • Clinical experience of arsenic trioxide in relapsed acute promyelocytic leukemia
    • Soignet S.L. Clinical experience of arsenic trioxide in relapsed acute promyelocytic leukemia. Oncologist 2001, 6(Suppl. 2):11-16.
    • (2001) Oncologist , vol.6 , Issue.SUPPL. 2 , pp. 11-16
    • Soignet, S.L.1
  • 108
    • 47249162501 scopus 로고    scopus 로고
    • Food safety. Arsenic and paddy rice: a neglected cancer risk?
    • Stone R. Food safety. Arsenic and paddy rice: a neglected cancer risk?. Science 2008, 321(5886):184-185.
    • (2008) Science , vol.321 , Issue.5886 , pp. 184-185
    • Stone, R.1
  • 109
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story R.M., Steitz T.A. Structure of the recA protein-ADP complex. Nature 1992, 355(6358):374-376.
    • (1992) Nature , vol.355 , Issue.6358 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 110
    • 0842308254 scopus 로고    scopus 로고
    • Arsenic toxicity, mutagenesis, and carcinogenesis-a health risk assessment and management approach
    • Tchounwou P.B., Centeno J.A., Patlolla A.K. Arsenic toxicity, mutagenesis, and carcinogenesis-a health risk assessment and management approach. Molecular and Cellular Biochemistry 2004, 255(1-2):47-55.
    • (2004) Molecular and Cellular Biochemistry , vol.255 , Issue.1-2 , pp. 47-55
    • Tchounwou, P.B.1    Centeno, J.A.2    Patlolla, A.K.3
  • 113
    • 0025186765 scopus 로고
    • Molecular characterization of an anion pump. The ArsB protein is the membrane anchor for the ArsA protein
    • Tisa L.S., Rosen B.P. Molecular characterization of an anion pump. The ArsB protein is the membrane anchor for the ArsA protein. The Journal of Biological Chemistry 1990, 265(1):190-194.
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.1 , pp. 190-194
    • Tisa, L.S.1    Rosen, B.P.2
  • 114
    • 60749116389 scopus 로고    scopus 로고
    • Effect of arsenic exposure during pregnancy on infant development at 7 months in rural Matlab, Bangladesh
    • Tofail F., Vahter M., Hamadani J.D., Nermell B., Huda S.N., Yunus M., et al. Effect of arsenic exposure during pregnancy on infant development at 7 months in rural Matlab, Bangladesh. Environmental Health Perspectives 2009, 117(2):288-293.
    • (2009) Environmental Health Perspectives , vol.117 , Issue.2 , pp. 288-293
    • Tofail, F.1    Vahter, M.2    Hamadani, J.D.3    Nermell, B.4    Huda, S.N.5    Yunus, M.6
  • 117
    • 36248930336 scopus 로고    scopus 로고
    • Study of interactions between arsenicals and thioredoxins (human and E. coli) using mass spectrometry
    • Wang Z., Zhang H., Li X.F., Le X.C. Study of interactions between arsenicals and thioredoxins (human and E. coli) using mass spectrometry. Rapid Communications in Mass Spectrometry 2007, 21(22):3658-3666.
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.22 , pp. 3658-3666
    • Wang, Z.1    Zhang, H.2    Li, X.F.3    Le, X.C.4
  • 119
    • 34247151719 scopus 로고    scopus 로고
    • Market basket survey shows elevated levels of As in South Central U.S. processed rice compared to California: consequences for human dietary exposure
    • Williams P.N., Raab A., Feldmann J., Meharg A.A. Market basket survey shows elevated levels of As in South Central U.S. processed rice compared to California: consequences for human dietary exposure. Environmental Science and Technology 2007, 41(7):2178-2183.
    • (2007) Environmental Science and Technology , vol.41 , Issue.7 , pp. 2178-2183
    • Williams, P.N.1    Raab, A.2    Feldmann, J.3    Meharg, A.A.4
  • 120
    • 0015577495 scopus 로고
    • Inorganic phosphate transport in Escherichia coli: involvement of two genes which play a role in alkaline phosphatase regulation
    • Willsky G.R., Bennett R.L., Malamy M.H. Inorganic phosphate transport in Escherichia coli: involvement of two genes which play a role in alkaline phosphatase regulation. Journal of Bacteriology 1973, 113(2):529-539.
    • (1973) Journal of Bacteriology , vol.113 , Issue.2 , pp. 529-539
    • Willsky, G.R.1    Bennett, R.L.2    Malamy, M.H.3
  • 121
    • 0019163171 scopus 로고
    • Effect of arsenate on inorganic phosphate transport in Escherichia coli
    • Willsky G.R., Malamy M.H. Effect of arsenate on inorganic phosphate transport in Escherichia coli. Journal of Bacteriology 1980, 144(1):366-374.
    • (1980) Journal of Bacteriology , vol.144 , Issue.1 , pp. 366-374
    • Willsky, G.R.1    Malamy, M.H.2
  • 122
    • 0026622930 scopus 로고
    • Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase
    • Wu J., Tisa L.S., Rosen B.P. Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase. The Journal of Biological Chemistry 1992, 267(18):12570-12576.
    • (1992) The Journal of Biological Chemistry , vol.267 , Issue.18 , pp. 12570-12576
    • Wu, J.1    Tisa, L.S.2    Rosen, B.P.3
  • 123
    • 0030728763 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ACR3 gene encodes a putative membrane protein involved in arsenite transport
    • Wysocki R., Bobrowicz P., Ulaszewski S. The Saccharomyces cerevisiae ACR3 gene encodes a putative membrane protein involved in arsenite transport. The Journal of Biological Chemistry 1997, 272(48):30061-30066.
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 30061-30066
    • Wysocki, R.1    Bobrowicz, P.2    Ulaszewski, S.3
  • 124
    • 0034933591 scopus 로고    scopus 로고
    • The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae
    • Wysocki R., Chery C.C., Wawrzycka D., Van Hulle M., Cornelis R., Thevelein J.M., et al. The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae. Molecular Microbiology 2001, 40(6):1391-1401.
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1391-1401
    • Wysocki, R.1    Chery, C.C.2    Wawrzycka, D.3    Van Hulle, M.4    Cornelis, R.5    Thevelein, J.M.6
  • 125
    • 57049090636 scopus 로고    scopus 로고
    • Investigation of the structure and function of a Shewanella oneidensis arsenical-resistance family transporter
    • Xia X., Postis V.L., Rahman M., Wright G.S., Roach P.C., Deacon S.E., et al. Investigation of the structure and function of a Shewanella oneidensis arsenical-resistance family transporter. Molecular Membrane Biology 2008, 25(8):691-705.
    • (2008) Molecular Membrane Biology , vol.25 , Issue.8 , pp. 691-705
    • Xia, X.1    Postis, V.L.2    Rahman, M.3    Wright, G.S.4    Roach, P.C.5    Deacon, S.E.6
  • 126
    • 26444519913 scopus 로고    scopus 로고
    • Novel pathway for arsenic detoxification in the legume symbiont Sinorhizobium meliloti
    • Yang H.C., Cheng J., Finan T.M., Rosen B.P., Bhattacharjee H. Novel pathway for arsenic detoxification in the legume symbiont Sinorhizobium meliloti. Journal of Bacteriology 2005, 187(20):6991-6997.
    • (2005) Journal of Bacteriology , vol.187 , Issue.20 , pp. 6991-6997
    • Yang, H.C.1    Cheng, J.2    Finan, T.M.3    Rosen, B.P.4    Bhattacharjee, H.5
  • 127
    • 77951679239 scopus 로고    scopus 로고
    • Arsenic binding and transfer by the ArsD As(III) metallochaperone
    • Yang J., Rawat S., Stemmler T.L., Rosen B.P. Arsenic binding and transfer by the ArsD As(III) metallochaperone. Biochemistry 2010, 49(17):3658-3666.
    • (2010) Biochemistry , vol.49 , Issue.17 , pp. 3658-3666
    • Yang, J.1    Rawat, S.2    Stemmler, T.L.3    Rosen, B.P.4
  • 128
    • 79551678402 scopus 로고    scopus 로고
    • Genetic mapping of the interface between the ArsD metallochaperone and the ArsA ATPase
    • Yang J., Salam A.A., Rosen B.P. Genetic mapping of the interface between the ArsD metallochaperone and the ArsA ATPase. Molecular Microbiology 2011, 79(4):872-881.
    • (2011) Molecular Microbiology , vol.79 , Issue.4 , pp. 872-881
    • Yang, J.1    Salam, A.A.2    Rosen, B.P.3
  • 129
    • 77953902537 scopus 로고    scopus 로고
    • The 1.4 å crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase
    • Ye J., Ajees A.A., Yang J., Rosen B.P. The 1.4 å crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase. Biochemistry 2010, 49(25):5206-5212.
    • (2010) Biochemistry , vol.49 , Issue.25 , pp. 5206-5212
    • Ye, J.1    Ajees, A.A.2    Yang, J.3    Rosen, B.P.4
  • 130
    • 79959966446 scopus 로고    scopus 로고
    • Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution
    • Ye J., He Y., Skalicky J., Rosen B.P., Stemmler T.L. Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution. Biomolecular NMR Assignments 2010, 2(3):211-219.
    • (2010) Biomolecular NMR Assignments , vol.2 , Issue.3 , pp. 211-219
    • Ye, J.1    He, Y.2    Skalicky, J.3    Rosen, B.P.4    Stemmler, T.L.5
  • 131
    • 84862776542 scopus 로고    scopus 로고
    • Arsenic biomethylation by photosynthetic organisms
    • Ye J., Rensing C., Rosen B.P., Zhu Y.G. Arsenic biomethylation by photosynthetic organisms. Trends in Plant Science 2012, 17(3):155-162.
    • (2012) Trends in Plant Science , vol.17 , Issue.3 , pp. 155-162
    • Ye, J.1    Rensing, C.2    Rosen, B.P.3    Zhu, Y.G.4
  • 132
    • 79955043823 scopus 로고    scopus 로고
    • Demethylation of methylarsonic acid by a microbial community
    • Yoshinaga M., Cai Y., Rosen B.P. Demethylation of methylarsonic acid by a microbial community. Environmental Microbiology 2011, 13(5):1205-1215.
    • (2011) Environmental Microbiology , vol.13 , Issue.5 , pp. 1205-1215
    • Yoshinaga, M.1    Cai, Y.2    Rosen, B.P.3
  • 134
    • 77952513568 scopus 로고    scopus 로고
    • Arsenic as a food chain contaminant: mechanisms of plant uptake and metabolism and mitigation strategies
    • Zhao F.J., McGrath S.P., Meharg A.A. Arsenic as a food chain contaminant: mechanisms of plant uptake and metabolism and mitigation strategies. Annual Review of Plant Biology 2010, 61:535-559.
    • (2010) Annual Review of Plant Biology , vol.61 , pp. 535-559
    • Zhao, F.J.1    McGrath, S.P.2    Meharg, A.A.3
  • 135
    • 0028864531 scopus 로고
    • Interaction of substrate and effector binding sites in the ArsA ATPase
    • Zhou T., Liu S., Rosen B.P. Interaction of substrate and effector binding sites in the ArsA ATPase. Biochemistry 1995, 34(41):13622-13626.
    • (1995) Biochemistry , vol.34 , Issue.41 , pp. 13622-13626
    • Zhou, T.1    Liu, S.2    Rosen, B.P.3
  • 136
    • 0034282542 scopus 로고    scopus 로고
    • Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
    • Zhou T., Radaev S., Rosen B.P., Gatti D.L. Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump. EMBO Journal 2000, 19(17):1-8.
    • (2000) EMBO Journal , vol.19 , Issue.17 , pp. 1-8
    • Zhou, T.1    Radaev, S.2    Rosen, B.P.3    Gatti, D.L.4
  • 137
    • 0030795417 scopus 로고    scopus 로고
    • Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase
    • Zhou T., Rosen B.P. Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase. The Journal of Biological Chemistry 1997, 272(32):19731-19737.
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.32 , pp. 19731-19737
    • Zhou, T.1    Rosen, B.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.