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Volumn 62, Issue 6, 1998, Pages 1258-1260

Essential cys-pro-cys motif of caenorhabditis elegans copper transport atpase

Author keywords

Caenorhabditis elegans; Copper ATPase; Cysteine residue; Menkes and Wilson diseases; Yeast CCC2 gene

Indexed keywords

ADENOSINE TRIPHOSPHATASE; COPPER; OLIGOPEPTIDE;

EID: 0032084939     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.1258     Document Type: Article
Times cited : (32)

References (14)
  • 2
    • 0001435653 scopus 로고
    • Copper and iron content of brain and liver in normal and in hepato-lenticular degeneration
    • Cumings, J. N., Copper and iron content of brain and liver in normal and in hepato-lenticular degeneration. Brain, 71, 410-415 (1948).
    • (1948) Brain , vol.71 , pp. 410-415
    • Cumings, J.N.1
  • 3
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for menkes disease and evidence that it encodes a copper-transporting atpase
    • Vulpe, C., Levinson, B., Whitney, S., Packman, S., and Gitschier, J., Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nature Genet., 3, 7-13 (1993).
    • (1993) Nature Genet. , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 4
    • 0028040512 scopus 로고
    • Characterization of the wilson disease gene encoding a p-type copper transporting atpase: Genomic organization, alternative splicing, and structure/function predictions
    • Petrukhin, K., Lutsenko, S., Chernov, I., Ross, B. M., Kaplan, J. H., and Gilliam, T. C., Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: genomic organization, alternative splicing, and structure/function predictions. Hum. Mol. Genet., 3, 1647-1656 (1994).
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1647-1656
    • Petrukhin, K.1    Lutsenko, S.2    Chernov, I.3    Ross, B.M.4    Kaplan, J.H.5    Gilliam, T.C.6
  • 5
    • 0022558845 scopus 로고
    • Two ca2+-atpase genes: Homologies and mechanistic implications of deduced amino acid sequences
    • Brandi, C. J., Green, N. M., Korczak, B., and MacLennan, D. H., Two Ca2+-ATPase genes: homologies and mechanistic implications of deduced amino acid sequences. Cell, 44, 597-607 (1986).
    • (1986) Cell , vol.44 , pp. 597-607
    • Brandi, C.J.1    Green, N.M.2    Korczak, B.3    Mac Lennan, D.H.4
  • 6
    • 0028948274 scopus 로고
    • Sequence, mapping and disruption of ccc2, a gene that cross-complements the ca2+-sensitive phenotype of csgl mutants and encodes a p-type atpase belonging to the cu2+-atpase subfamily
    • Fu, D., Beeler, T. J., and Dunn, T. M., Sequence, mapping and disruption of CCC2, a gene that cross-complements the Ca2+-sensitive phenotype of csgl mutants and encodes a P-type ATPase belonging to the Cu2+-ATPase subfamily. Yeast, 11, 283-292 (1995).
    • (1995) Yeast , vol.11 , pp. 283-292
    • Fu, D.1    Beeler, T.J.2    Dunn, T.M.3
  • 7
    • 0028916909 scopus 로고
    • The menkes/wilson disease gene homo-logue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake
    • Yuan, D. S., Stearman, R., Dancis, A., Dunn, T., Beeler, T., and Klausner, R. D., The Menkes/Wilson disease gene homo-logue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc. Natl. Acad. Sci. USA, 92, 2632-2636 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2632-2636
    • Yuan, D.S.1    Stearman, R.2    Dancis, A.3    Dunn, T.4    Beeler, T.5    Klausner, R.D.6
  • 8
    • 0030858817 scopus 로고    scopus 로고
    • Caenorhabditis elegans cdna for a menkes/wilson disease gene homologue and its function in a yeast ccc2 gene deletion mutant
    • Sambongi, Y., Wakabayashi, T., Yoshimizu, T., Omote, H., Oka, T., and Futai, M., Caenorhabditis elegans cDNA for a Menkes/Wilson disease gene homologue and its function in a yeast CCC2 gene deletion mutant. J. Biochem., 121, 1169-1175 (1997).
    • (1997) J. Biochem. , vol.121 , pp. 1169-1175
    • Sambongi, Y.1    Wakabayashi, T.2    Yoshimizu, T.3    Omote, H.4    Oka, T.M.5
  • 9
    • 0345150216 scopus 로고
    • Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the ca2+ transport activity of the ca2+-atpase expressed in cos-1 cells
    • Maruyama, K., and MacLennan, D. H., Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells. Proc. Natl. Acad. Sci. USA, 85, 3314-3318 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3314-3318
    • Maruyama, K.1    Mac Lennan, D.H.2
  • 10
    • 0024826344 scopus 로고
    • Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the ca2+-atpase of sarcoplasmic reticulum
    • Vilsen, B., Andersen, J. P., Clarke, D. M., and MacLennan, D. H., Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the Ca2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem., 264, 21024-21030 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 21024-21030
    • Vilsen, B.1    Ersen, J.P.2    Clarke, D.M.3    Mac Lennan, D.H.4
  • 11
    • 0025236388 scopus 로고
    • Functional consequences of alterations to polar amino acids located in the transmembrane domain of the ca2+-atpase of sarcoplasmic reticulum
    • Clarke, D. M., Loo, T. W., and MacLennan, D. H., Functional consequences of alterations to polar amino acids located in the transmembrane domain of the Ca2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem., 265, 6262-6267 (1989).
    • (1989) J. Biol. Chem. , vol.265 , pp. 6262-6267
    • Clarke, D.M.1    Loo, T.W.2    Mac Lennan, D.H.3
  • 12
    • 0030199612 scopus 로고    scopus 로고
    • Cpx-type atpases: A class of p-type atpases that pump heavy metals
    • Solioz, M., and Vulpe, C., CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci., 21, 237-241 (1996).
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 13
    • 0027288228 scopus 로고
    • Primary structure of two p-type atpases involved in copper homeostasis in
    • Odermatt, A., Suter, H., Krapf, R., and Solioz, M., Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem., 268, 12775-12779 (1993).
    • (1993) Enterococcus Hirae. J. Biol. Chem. , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 14
    • 0028986792 scopus 로고
    • Nucleotide sequence and mutational analysis indicate that two helicobacter pylori genes encode a p-type atpase and a cation-binding protein associated with copper transport
    • Ge, Z., Hiratsuka, K., and Taylor, D. E., Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport. Mol. Microbiol., 15, 97-106 (1995).
    • (1995) Mol. Microbiol. , vol.15 , pp. 97-106
    • Ge, Z.1    Hiratsuka, K.2    Taylor, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.