메뉴 건너뛰기




Volumn 6, Issue 4, 1999, Pages 221-230

The role of copper in neurodegenerative disease

Author keywords

Aceruloplasminemia; Alzheimer's disease; Amyotrophic lateral sclerosis; Copper; Menkes disease; Prion disease; Wilson disease

Indexed keywords

ALPHA AMIDATING ENZYME; CERULOPLASMIN; COPPER; CYTOCHROME C OXIDASE; DOPAMINE BETA MONOOXYGENASE; MONOPHENOL MONOOXYGENASE; PROTEIN LYSINE 6 OXIDASE; SUPEROXIDE DISMUTASE;

EID: 0032887626     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1006/nbdi.1999.0250     Document Type: Review
Times cited : (818)

References (98)
  • 2
    • 0028058038 scopus 로고
    • The FET3 gene of S. Cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith C., Eide D., VanHo A., Bernard P. S., Li L., Davis-Kaplan S., Sipe D. M., Kaplan J. The FET3 gene of S. Cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell. 76:1994;403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Vanho, A.3    Bernard, P.S.4    Li, L.5    Davis-Kaplan, S.6    Sipe, D.M.7    Kaplan, J.8
  • 6
    • 0028813380 scopus 로고
    • Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function
    • Borchelt D. R., Guarnieri M., Wong P. C., Lee M. K., Slunt H. A., Xu Z.-S., Sisodia S. S., Price D. L., Cleveland D. W. Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J. Biol. Chem. 270:1995;3234-3238.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3234-3238
    • Borchelt, D.R.1    Guarnieri, M.2    Wong, P.C.3    Lee, M.K.4    Slunt, H.A.5    Xu, Z.-S.6    Sisodia, S.S.7    Price, D.L.8    Cleveland, D.W.9
  • 9
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • Brown D. R., Besinger A. Prion protein expression and superoxide dismutase activity. Biochem. J. 334:1998;423-429.
    • (1998) Biochem. J. , vol.334 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 10
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
    • Bruijn L. I., Beal M. F., Becher M. W., Schulz J. B., Wong P. C., Price D. L., Cleveland D. W. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl. Acad. Sci. USA. 94:1997;7606-7611.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7606-7611
    • Bruijn, L.I.1    Beal, M.F.2    Becher, M.W.3    Schulz, J.B.4    Wong, P.C.5    Price, D.L.6    Cleveland, D.W.7
  • 13
    • 0027452091 scopus 로고
    • The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene
    • Bull P. C., Thomas G. R., Rommens J. M., Forbes J. R., Cox D. W. The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nat. Genet. 5:1993;327-337.
    • (1993) Nat. Genet. , vol.5 , pp. 327-337
    • Bull, P.C.1    Thomas, G.R.2    Rommens, J.M.3    Forbes, J.R.4    Cox, D.W.5
  • 14
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
    • Casareno R. L. B., Waggoner D., Gitlin J. D. The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J. Biol. Chem. 273:1998;23625-23628.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23625-23628
    • Casareno, R.L.B.1    Waggoner, D.2    Gitlin, J.D.3
  • 16
    • 0032568546 scopus 로고    scopus 로고
    • Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants
    • Corson L. B., Strain J. J., Culotta V. C., Cleveland D. W. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants. Proc. Natl. Acad. Sci. USA. 95:1998;6301-6366.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6301-6366
    • Corson, L.B.1    Strain, J.J.2    Culotta, V.C.3    Cleveland, D.W.4
  • 17
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow J. P., Sampson J. B., Zhuang Y., Beckman J. S. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69:1997;1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Beckman, J.S.4
  • 23
    • 0024852150 scopus 로고
    • Wilson's disease: Psychiatric symptoms in 195 cases
    • Dening T. R., Berrios G. E. Wilson's disease: Psychiatric symptoms in 195 cases. Arch. Gen. Psychiatry. 46:1989;1126-1134.
    • (1989) Arch. Gen. Psychiatry , vol.46 , pp. 1126-1134
    • Dening, T.R.1    Berrios, G.E.2
  • 24
    • 0026704075 scopus 로고
    • Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative disease affecting the basal ganglia
    • Dexter D. T., Jenner P. Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative disease affecting the basal ganglia. Ann. Neurol. 32:1992;S94-S100.
    • (1992) Ann. Neurol. , vol.32
    • Dexter, D.T.1    Jenner, P.2
  • 25
    • 0031455381 scopus 로고    scopus 로고
    • Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B)
    • DiDonato M., Narindrasorasak S., Forbes J. R., Cox D. W., Sarkar B. Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B). J. Biol. Chem. 272:1997;33279-33282.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33279-33282
    • Didonato, M.1    Narindrasorasak, S.2    Forbes, J.R.3    Cox, D.W.4    Sarkar, B.5
  • 27
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:1995;97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 28
    • 0030712294 scopus 로고    scopus 로고
    • Early neuroradiologic evidence of degeneration in Menkes disease
    • Geller T. J., Pan Y., Martin D. S. Early neuroradiologic evidence of degeneration in Menkes disease. Pediatr. Neurol. 17:1997;255-258.
    • (1997) Pediatr. Neurol. , vol.17 , pp. 255-258
    • Geller, T.J.1    Pan, Y.2    Martin, D.S.3
  • 31
    • 0030014701 scopus 로고
    • Familial dementia due to a frameshift mutation in the caeruloplasmin gene
    • Harris Z. L., Migas M. D., Hughes A. E., Logan J. I., Gitlin J. D. Familial dementia due to a frameshift mutation in the caeruloplasmin gene. Q. J. Med. 89:1995b;355-359.
    • (1995) Q. J. Med. , vol.89 , pp. 355-359
    • Harris, Z.L.1    Migas, M.D.2    Hughes, A.E.3    Logan, J.I.4    Gitlin, J.D.5
  • 32
    • 15844384254 scopus 로고    scopus 로고
    • Genetic and molecular basis for copper toxicity
    • Harris Z. L., Gitlin J. D. Genetic and molecular basis for copper toxicity. Am. J. Clin. Nutr. 63:1996;836S-841S.
    • (1996) Am. J. Clin. Nutr. , vol.63
    • Harris, Z.L.1    Gitlin, J.D.2
  • 33
    • 0031981976 scopus 로고    scopus 로고
    • Aceruloplasminemia: An inherited neurodegenerative disease with impaired iron homeostasis
    • Harris Z. L., Klomp L. W., Gitlin J. D. Aceruloplasminemia: An inherited neurodegenerative disease with impaired iron homeostasis. Am. J. Clin. Nutr. 67:1998;972S-977S.
    • (1998) Am. J. Clin. Nutr. , vol.67
    • Harris, Z.L.1    Klomp, L.W.2    Gitlin, J.D.3
  • 34
    • 0028177269 scopus 로고
    • The βa4 amyloid precursor protein binding to copper
    • Hesse L., Beher D., Masters C. L., Multhaup G. The βA4 amyloid precursor protein binding to copper. FEBS Lett. 349:1994;109-116.
    • (1994) FEBS Lett. , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 35
    • 0032571387 scopus 로고    scopus 로고
    • Reduced fertility in female mice lacking copper-zinc superoxide dismutase
    • Ho Y. S., Gargano M., Cao J., Bronson R. T., Heimler I., Hutz R. J. Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J. Biol. Chem. 273:1998;7765-7769.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7765-7769
    • Ho, Y.S.1    Gargano, M.2    Cao, J.3    Bronson, R.T.4    Heimler, I.5    Hutz, R.J.6
  • 36
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • Hornshaw M. P., McDermott J. R., Candy J. M. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207:1995;621-629.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 37
    • 0030862630 scopus 로고    scopus 로고
    • The copper chelator d-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Hottinger A. F., Fine E. G., Gurney M. E., Zurn A. D., Aebischer P. The copper chelator d-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis. Eur. J. Neurosci. 9:1997;1548-1551.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1548-1551
    • Hottinger, A.F.1    Fine, E.G.2    Gurney, M.E.3    Zurn, A.D.4    Aebischer, P.5
  • 38
    • 0030803730 scopus 로고    scopus 로고
    • Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae
    • Hung I. H., Suzuki M., Yamaguchi Y., Yuan D. S., Klausner R. D., Gitlin J. D. Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 272:1997;21461-21466.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21461-21466
    • Hung, I.H.1    Suzuki, M.2    Yamaguchi, Y.3    Yuan, D.S.4    Klausner, R.D.5    Gitlin, J.D.6
  • 39
    • 0016193449 scopus 로고
    • A comparison of the biochemical changes induced in mouse brain cuprizone toxicity and by scrapie infection
    • Kimberlin R. H. A comparison of the biochemical changes induced in mouse brain cuprizone toxicity and by scrapie infection. J. Comp. Pathol. 84:1974;263-270.
    • (1974) J. Comp. Pathol. , vol.84 , pp. 263-270
    • Kimberlin, R.H.1
  • 40
  • 41
    • 0029800745 scopus 로고    scopus 로고
    • Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia
    • Klomp L. W. J., Gitlin J. D. Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia. Hum. Mol. Genet. 5:1996b;1989-1996.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1989-1996
    • Klomp, L.W.J.1    Gitlin, J.D.2
  • 44
    • 0031768025 scopus 로고    scopus 로고
    • Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Liu R., Althaus J. S., Ellerbrock B. R., Becker D. A., Gurney M. E. Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis. Ann. Neurol. 44:1998;763-770.
    • (1998) Ann. Neurol. , vol.44 , pp. 763-770
    • Liu, R.1    Althaus, J.S.2    Ellerbrock, B.R.3    Becker, D.A.4    Gurney, M.E.5
  • 46
    • 0030839796 scopus 로고    scopus 로고
    • N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat
    • Lutsenko S., Petrukhin K., Cooper M. J., Gilliam C. T., Kaplan J. H. N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J. Biol. Chem. 272:1997;18939-18944.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18939-18944
    • Lutsenko, S.1    Petrukhin, K.2    Cooper, M.J.3    Gilliam, C.T.4    Kaplan, J.H.5
  • 48
    • 0031760436 scopus 로고    scopus 로고
    • Ovarian function in superoxide dismutase 1 and 2 knockout mice
    • Matzuk M. M., Dionne L., Guo Q., Kumar T. R., Lebovitz R. M. Ovarian function in superoxide dismutase 1 and 2 knockout mice. Endocrinology. 139:1998;4008-4011.
    • (1998) Endocrinology , vol.139 , pp. 4008-4011
    • Matzuk, M.M.1    Dionne, L.2    Guo, Q.3    Kumar, T.R.4    Lebovitz, R.M.5
  • 50
    • 0345339836 scopus 로고    scopus 로고
    • Disorders of copper metabolism
    • R. N. Rosenberg, S. B. Prosiner, S. DiMauro, & R. L. Barchi. Boston: Butterworth-Heinemann
    • Menkes J. H. Disorders of copper metabolism. Rosenberg R. N., Prosiner S. B., DiMauro S., Barchi R. L. The Molecular and Genetic Basis of Neurological Disease. 1997;1273-1290 Butterworth-Heinemann, Boston.
    • (1997) The Molecular and Genetic Basis of Neurological Disease , pp. 1273-1290
    • Menkes, J.H.1
  • 52
    • 0030569412 scopus 로고    scopus 로고
    • Metal-dependent α-helix formation promoted by the glycine-rich octapeptide region of prion protein
    • Miura T., Hori I-A., Takeuchi H. Metal-dependent α-helix formation promoted by the glycine-rich octapeptide region of prion protein. FEBS Lett. 396:1996;248-252.
    • (1996) FEBS Lett. , vol.396 , pp. 248-252
    • Miura, T.1    Hori, I.-A.2    Takeuchi, H.3
  • 53
    • 0023240051 scopus 로고
    • Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration
    • Miyajima H., Nishimura Y., Mizoguchi K., Sakamoto M., Shimizu T., Honda N. Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration. Neurology. 37:1987;761-767.
    • (1987) Neurology , vol.37 , pp. 761-767
    • Miyajima, H.1    Nishimura, Y.2    Mizoguchi, K.3    Sakamoto, M.4    Shimizu, T.5    Honda, N.6
  • 55
    • 0031907553 scopus 로고    scopus 로고
    • Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia
    • Miyajima H., Adachi J., Tatsuno Y., Takahashi Y., Fujimoto M., Kaneko E., Gitlin J. D. Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia. Neurology. 50:1998;130-136.
    • (1998) Neurology , vol.50 , pp. 130-136
    • Miyajima, H.1    Adachi, J.2    Tatsuno, Y.3    Takahashi, Y.4    Fujimoto, M.5    Kaneko, E.6    Gitlin, J.D.7
  • 56
  • 57
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • Multhaup G., Schlicksupp A., Hesse L., Beher D., Ruppert T., Masters C. L., Beyreuther K. The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I). Science. 271:1996;1406-1509.
    • (1996) Science , vol.271 , pp. 1406-1509
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 58
    • 0032546577 scopus 로고    scopus 로고
    • Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide
    • Multhaup G., Ruppert T., Schlicksupp A., Hesse L., Bill E., Pipkorn R., Masters C. L., Beyreuther K. Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide. Biochemistry. 37:1998;7224-7230.
    • (1998) Biochemistry , vol.37 , pp. 7224-7230
    • Multhaup, G.1    Ruppert, T.2    Schlicksupp, A.3    Hesse, L.4    Bill, E.5    Pipkorn, R.6    Masters, C.L.7    Beyreuther, K.8
  • 60
    • 0032430185 scopus 로고    scopus 로고
    • Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase
    • Pasinelli P., Borchelt D. R., Houseweart M. K., Cleveland D. W., Brown R. H. Jr. Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase. Proc. Natl. Acad. Sci. USA. 95:1998;15763-15768.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15763-15768
    • Pasinelli, P.1    Borchelt, D.R.2    Houseweart, M.K.3    Cleveland, D.W.4    Brown R.H., Jr.5
  • 61
    • 0030856558 scopus 로고    scopus 로고
    • A novel glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes
    • Patel B. N., David S. A novel glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes. J. Biol. Chem. 272:1997;20185-20190.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20185-20190
    • Patel, B.N.1    David, S.2
  • 62
    • 0015090051 scopus 로고
    • Clinical and histological observations on cuprizone toxicity and scrapie in mice
    • Pattison I. H., Jebbett J. N. Clinical and histological observations on cuprizone toxicity and scrapie in mice. Res. Vet. Sci. 12:1971;378-380.
    • (1971) Res. Vet. Sci. , vol.12 , pp. 378-380
    • Pattison, I.H.1    Jebbett, J.N.2
  • 63
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P. C., Harris D. A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273:1998;33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 64
    • 0032488829 scopus 로고    scopus 로고
    • Functional expression of the Menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases
    • Payne A. S., Gitlin J. D. Functional expression of the Menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases. J Biol. Chem. 273:1998;3765-3770.
    • (1998) J Biol. Chem. , vol.273 , pp. 3765-3770
    • Payne, A.S.1    Gitlin, J.D.2
  • 65
    • 0032167856 scopus 로고    scopus 로고
    • Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation
    • Payne A. S., Kelly E. J., Gitlin J. D. Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation. Proc. Natl. Acad. Sci. USA. 95:1998;10854-10859.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10854-10859
    • Payne, A.S.1    Kelly, E.J.2    Gitlin, J.D.3
  • 66
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris M. J., Mercer J. F. B., Culvenor J. G., Lockhart P., Gleeson P. A., Camakaris J. Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking. EMBO J. 15:1996;6084-6095.
    • (1996) EMBO J. , vol.15 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.B.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 67
    • 0031730641 scopus 로고    scopus 로고
    • A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network
    • Petris M. J., Camakaris J., Greenough M., LaFontaine S., Mercer J. F. B. A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network. Hum. Mol. Genet. 7:1998;2063-2071.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 2063-2071
    • Petris, M.J.1    Camakaris, J.2    Greenough, M.3    Lafontaine, S.4    Mercer, J.F.B.5
  • 68
    • 0028040512 scopus 로고
    • Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: Genomic organization, alternative splicing, and structure/function predicting
    • Petrukhin K., Lutsenko S., Chernov L., Ross B. M., Kaplan J. H., Gilliam T. C. Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: Genomic organization, alternative splicing, and structure/function predicting. Hum. Mol. Genet. 3:1994;1647-1656.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1647-1656
    • Petrukhin, K.1    Lutsenko, S.2    Chernov, L.3    Ross, B.M.4    Kaplan, J.H.5    Gilliam, T.C.6
  • 69
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic mice
    • Price D. L., Sisodia S. S. Mutant genes in familial Alzheimer's disease and transgenic mice. Annu. Rev. Neurosci. 21:1998;479-505.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 70
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner S. B. Prion diseases and the BSE crisis. Science. 278:1997;245-251.
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 71
    • 0028915976 scopus 로고
    • Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neural cells
    • Rabizadeh S., Gralla E. B., Borchelt D. R., Gwinn R., Valentine J. S., Sisodia S., Wong P., Lee M., Hahn H., Bredesen D. E. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA. 92:1995;3024-3028.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1    Gralla, E.B.2    Borchelt, D.R.3    Gwinn, R.4    Valentine, J.S.5    Sisodia, S.6    Wong, P.7    Lee, M.8    Hahn, H.9    Bredesen, D.E.10
  • 73
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps M. E., Huntley G. W., Hof P. R., Morrison J. H., Gordon J. W. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA. 92:1995;689-693.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 76
    • 0032532332 scopus 로고    scopus 로고
    • Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin
    • Salzer J. L., Lovejoy L., Linder M. C., Rosen C. Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin. J. Neurosci. Res. 54:1998;147-157.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 147-157
    • Salzer, J.L.1    Lovejoy, L.2    Linder, M.C.3    Rosen, C.4
  • 77
    • 0025729544 scopus 로고
    • Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin
    • Sato M., Gitlin J. D. Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin. J. Biol. Chem. 266:1991;5128-5134.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5128-5134
    • Sato, M.1    Gitlin, J.D.2
  • 78
    • 0032932229 scopus 로고    scopus 로고
    • Genetic disorders of membrane transport IV. Wilson's disease and Menkes disease
    • Schaefer M., Gitlin J. D. Genetic disorders of membrane transport IV. Wilson's disease and Menkes disease. Am. J. Physiol. 276:1999;G311-G314.
    • (1999) Am. J. Physiol. , vol.276
    • Schaefer, M.1    Gitlin, J.D.2
  • 79
    • 0032920935 scopus 로고    scopus 로고
    • Hepatocyte-specific localization, copper-dependent trafficking and developmental expression of the Wilson disease protein in the liver
    • Schaefer M., Hopkins R. G., Failla M. L., Gitlin J. D. Hepatocyte-specific localization, copper-dependent trafficking and developmental expression of the Wilson disease protein in the liver. Am J Physiol. 1999.
    • (1999) Am J Physiol.
    • Schaefer, M.1    Hopkins, R.G.2    Failla, M.L.3    Gitlin, J.D.4
  • 80
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid protein and prescinillin in Alzheimer's disease
    • Selkoe D. J. The cell biology of beta-amyloid protein and prescinillin in Alzheimer's disease. Trends Cell Biol. 8:1998;447-453.
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 83
    • 0030027565 scopus 로고    scopus 로고
    • Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease
    • Takahashi Y., Miyajima H., Shirabe S., Nagataki S., Suenaga A., Gitlin J. D. Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease. Hum. Mol. Genet. 5:1996;81-84.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 81-84
    • Takahashi, Y.1    Miyajima, H.2    Shirabe, S.3    Nagataki, S.4    Suenaga, A.5    Gitlin, J.D.6
  • 85
    • 0030671295 scopus 로고    scopus 로고
    • Delivering copper inside yeast and human cells
    • Valentine J. S., Gralla E. B. Delivering copper inside yeast and human cells. Science. 278:1997;817-818.
    • (1997) Science , vol.278 , pp. 817-818
    • Valentine, J.S.1    Gralla, E.B.2
  • 86
    • 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., Gitschier J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat. Genet. 3:1993;7-13.
    • (1993) Nat. Genet. , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 88
    • 0024368990 scopus 로고
    • Wilson's disease presenting with features of hepatic dysfunction: A clinical analysis of eighty-seven patients
    • Walshe J. M. Wilson's disease presenting with features of hepatic dysfunction: A clinical analysis of eighty-seven patients. Q. J. Med. 70:1989;253-263.
    • (1989) Q. J. Med. , vol.70 , pp. 253-263
    • Walshe, J.M.1
  • 90
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons
    • Williamson T. L., Cleveland D. W. Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nat. Neurosci. 2:1999;50-56.
    • (1999) Nat. Neurosci. , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 91
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P. C., Pardo C. A., Borchelt D. R., Lee M. K., Copeland N. G., Jenkins N. A., Sisodia S. S., Cleveland D. W., Price D. L. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron. 14:1995;1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 92
    • 0031672857 scopus 로고    scopus 로고
    • The genetic and molecular mechanisms of motor neuron disease
    • Wong P. C., Rothstein J. D., Price D. L. The genetic and molecular mechanisms of motor neuron disease. Curr. Opin. Neurobiol. 8:1998;791-799.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 791-799
    • Wong, P.C.1    Rothstein, J.D.2    Price, D.L.3
  • 93
    • 0027431996 scopus 로고
    • Isolation and characterization of a human liver cDNA as a candidate gene for Wilson disease
    • Yamaguchi Y., Heiny M. E., Gitlin J. D. Isolation and characterization of a human liver cDNA as a candidate gene for Wilson disease. Biochem. Biophys. Res. Commun. 197:1993;271-277.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 271-277
    • Yamaguchi, Y.1    Heiny, M.E.2    Gitlin, J.D.3
  • 95
    • 0028916909 scopus 로고
    • The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake
    • Yuan D. S., Stearman R., Dancis A., Dunn T., Beeler T., Klausner R. D. The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc. Natl. Acad. Sci. USA. 92:1995;2632-2636.
    • (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
  • 96
    • 0030820818 scopus 로고    scopus 로고
    • Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway
    • Yuan D. S., Dancis A., Klausner R. D. Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway. J. Biol. Chem. 272:1997;25787-25793.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25787-25793
    • Yuan, D.S.1    Dancis, A.2    Klausner, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.