메뉴 건너뛰기




Volumn 4, Issue 9, 2009, Pages

Copper-triggered aggregation of ubiquitin

Author keywords

[No Author keywords available]

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; AMYLOID; COPPER; CUPRIC ION; DIMER; OLIGOMER; UBIQUITIN;

EID: 75549083286     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007052     Document Type: Article
Times cited : (52)

References (70)
  • 1
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • McClellan AJ, Tam S, Kaganovich D, Frydman J (2005) Protein quality control: chaperones culling corrupt conformations. Nat Cell Biol 7: 736-741.
    • (2005) Nat Cell Biol , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 3
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart CM, Fushman D (2004) Polyubiquitin chains: polymeric protein signals. Curr Opin Chem Biol 8: 610-616.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 4
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4: 49-60.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown DR, Qin K, Herms JW, Madlung A, Manson J, et al. (1997) The cellular prion protein binds copper in vivo. Nature 390: 684-687.
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.R.1    Qin, K.2    Herms, J.W.3    Madlung, A.4    Manson, J.5
  • 7
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Ab by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood CS, Moir RD, Huang X, Scarpa RC, Bacarra NM, et al. (1998) Dramatic aggregation of Alzheimer Ab by Cu(II) is induced by conditions representing physiological acidosis. J Biol Chem 273: 12817-12826.
    • (1998) J Biol Chem , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Moir, R.D.2    Huang, X.3    Scarpa, R.C.4    Bacarra, N.M.5
  • 8
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II)-induced self-oligomerization of alpha-synuclein
    • Paik SR, Shin HJ, Lee JH, Chang CS, Kim J (1999) Copper(II)-induced self-oligomerization of alpha-synuclein. Biochem J 340: 821-828.
    • (1999) Biochem J , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, C.S.4    Kim, J.5
  • 9
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • Morgan CJ, Gelfand M, Atreya C, Miranker AD (2001) Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. J Mol Biol 309: 339-345.
    • (2001) J Mol Biol , vol.309 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 10
    • 0036932955 scopus 로고    scopus 로고
    • Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain
    • Amici M, Forti K, Nobili C, Lupidi G, Angeletti M, et al. (2002) Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain. J Biol Inorg Chem 7: 750-756.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 750-756
    • Amici, M.1    Forti, K.2    Nobili, C.3    Lupidi, G.4    Angeletti, M.5
  • 11
    • 0023927981 scopus 로고
    • Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease
    • Lowe J, Blanchard A, Morrell K, Lennox G, Reynolds L, et al. (1988) Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease. J Pathol 155: 9-15.
    • (1988) J Pathol , vol.155 , pp. 9-15
    • Lowe, J.1    Blanchard, A.2    Morrell, K.3    Lennox, G.4    Reynolds, L.5
  • 12
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A, Brundin P (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40: 427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 13
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • Ross CA, Pickart CM (2004) The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol 14: 703-711.
    • (2004) Trends Cell Biol , vol.14 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 14
    • 28844463943 scopus 로고    scopus 로고
    • Application of ubiquitin immunohistochemistry to the diagnosis of disease
    • Lowe J, Hand N, Mayer RJ (2005) Application of ubiquitin immunohistochemistry to the diagnosis of disease. Methods Enzymol 399: 86-119.
    • (2005) Methods Enzymol , vol.399 , pp. 86-119
    • Lowe, J.1    Hand, N.2    Mayer, R.J.3
  • 15
    • 34648819365 scopus 로고    scopus 로고
    • The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates
    • Wakabayashi K, Tanji K, Mori F, Takahashi H (2007) The Lewy body in Parkinson's disease: molecules implicated in the formation and degradation of alpha-synuclein aggregates. Neuropathology 27: 494-506.
    • (2007) Neuropathology , vol.27 , pp. 494-506
    • Wakabayashi, K.1    Tanji, K.2    Mori, F.3    Takahashi, H.4
  • 16
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure
    • Uversky VN, Li J, Fink AL (2001) Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure. J Biol Chem 276: 44284-44296.
    • (2001) J Biol Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 17
    • 33746633380 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement
    • Binolfi A, Rasia RM, Bertoncini CW, Ceolin M, Zweckstetter M, et al. (2006) Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement. J Am Chem Soc 128: 9893-9901.
    • (2006) J Am Chem Soc , vol.128 , pp. 9893-9901
    • Binolfi, A.1    Rasia, R.M.2    Bertoncini, C.W.3    Ceolin, M.4    Zweckstetter, M.5
  • 18
    • 38849091518 scopus 로고    scopus 로고
    • Alpha-synuclein and its role in metal binding: Relevance to Parkinson's disease
    • Wright JA, Brown DR (2008) Alpha-synuclein and its role in metal binding: relevance to Parkinson's disease. J Neurosci Res 86: 496-503.
    • (2008) J Neurosci Res , vol.86 , pp. 496-503
    • Wright, J.A.1    Brown, D.R.2
  • 19
    • 33646716271 scopus 로고    scopus 로고
    • Ubiquitin: A small protein folding paradigm
    • Jackson SE (2006) Ubiquitin: a small protein folding paradigm. Org Biomol Chem 4: 1845-1853.
    • (2006) Org Biomol Chem , vol.4 , pp. 1845-1853
    • Jackson, S.E.1
  • 20
    • 35649018196 scopus 로고    scopus 로고
    • Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding
    • Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, et al. (2007) Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding. Angew Chem Int Ed Engl 46: 7993-7995.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 7993-7995
    • Milardi, D.1    Arnesano, F.2    Grasso, G.3    Magrì, A.4    Tabbì, G.5
  • 21
    • 33745726690 scopus 로고    scopus 로고
    • Copper homeostasis and neurodegenerative disorders (Alzheimer's, Prion, and Parkinson's diseases and Amyotrophic Lateral Sclerosis)
    • Gaggelli E, Kozlowski H, Valensin D, Valensin G (2006) Copper homeostasis and neurodegenerative disorders (Alzheimer's, Prion, and Parkinson's diseases and Amyotrophic Lateral Sclerosis). Chem Rev 106: 1995-2044.
    • (2006) Chem Rev , vol.106 , pp. 1995-2044
    • Gaggelli, E.1    Kozlowski, H.2    Valensin, D.3    Valensin, G.4
  • 22
    • 15444373250 scopus 로고    scopus 로고
    • Structural characterization of copper(II) binding to a-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
    • Rasia RM, Bertoncini CW, Marsh D, Hoyer W, Cherny D, et al. (2005) Structural characterization of copper(II) binding to a-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease. Proc Natl Acad Sci U S A 102: 4294-4299.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4294-4299
    • Rasia, R.M.1    Bertoncini, C.W.2    Marsh, D.3    Hoyer, W.4    Cherny, D.5
  • 23
    • 33845978790 scopus 로고    scopus 로고
    • Insight into the structure of amyloid fibrils from the analysis of globular proteins
    • Trovato A, Chiti F, Maritan A, Seno F (2006) Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comput Biol 2: e170.
    • (2006) PLoS Comput Biol , vol.2
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 24
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes
    • Munishkina LA, Phelan C, Uversky VN, Fink AL (2003) Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes. Biochemistry 42: 2720-2730.
    • (2003) Biochemistry , vol.42 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 25
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • Chiti F, Webster P, Taddei N, Clark A, Stefani M, et al. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci U S A 96: 3590-3594.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3590-3594
    • Chiti, F.1    Webster, P.2    Taddei, N.3    Clark, A.4    Stefani, M.5
  • 26
    • 33748943122 scopus 로고    scopus 로고
    • 2-microglobulin fragment are induced by fluorine-substituted alcohols
    • 2-microglobulin fragment are induced by fluorine-substituted alcohols. J Mol Biol 363: 279-288.
    • (2006) J Mol Biol , vol.363 , pp. 279-288
    • Yamaguchi, K.1    Naiki, H.2    Goto, Y.3
  • 27
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A, Sutter M, Jiskoot W (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25: 1487-1499.
    • (2008) Pharm Res , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 28
    • 36749079833 scopus 로고    scopus 로고
    • Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM
    • Hess S, Lindquist SL, Scheibel T (2007) Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM. EMBO Rep 8: 1196-1201.
    • (2007) EMBO Rep , vol.8 , pp. 1196-1201
    • Hess, S.1    Lindquist, S.L.2    Scheibel, T.3
  • 29
    • 0023087430 scopus 로고
    • Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system
    • Parag HA, Raboy B, Kulka RG (1987) Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system. EMBO J 6: 55-61.
    • (1987) EMBO J , vol.6 , pp. 55-61
    • Parag, H.A.1    Raboy, B.2    Kulka, R.G.3
  • 30
    • 41649088465 scopus 로고    scopus 로고
    • Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb poly-ubiquitin gene
    • Ryu KY, Garza JC, Lu XY, Barsh GS, Kopito RR (2008) Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb poly-ubiquitin gene. Proc Natl Acad Sci U S A 105: 4016-4021.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4016-4021
    • Ryu, K.Y.1    Garza, J.C.2    Lu, X.Y.3    Barsh, G.S.4    Kopito, R.R.5
  • 31
    • 56449112645 scopus 로고    scopus 로고
    • Extracellular, circulating proteasomes and ubiquitin - incidence and relevance
    • Sixt SU, Dahlmann B (2008) Extracellular, circulating proteasomes and ubiquitin - incidence and relevance. Biochim Biophys Acta 1782: 817-823.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 817-823
    • Sixt, S.U.1    Dahlmann, B.2
  • 32
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
    • Zandomeneghi G, Krebs MR, McCammon MG, Fandrich M (2004) FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Sci 13: 3314-3321.
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fandrich, M.4
  • 33
    • 9344233839 scopus 로고    scopus 로고
    • Calcium(II) selectively induces alpha-synuclein annular oligo via interaction with the C-terminal domain
    • Lowe R, Pountney DL, Jensen PH, Gai WP, Voelcker NH (2004) Calcium(II) selectively induces alpha-synuclein annular oligo via interaction with the C-terminal domain. Protein Sci 13: 3245-3252.
    • (2004) Protein Sci , vol.13 , pp. 3245-3252
    • Lowe, R.1    Pountney, D.L.2    Jensen, P.H.3    Gai, W.P.4    Voelcker, N.H.5
  • 34
    • 15744402739 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein: Helping to define the relationship between oligomers, protofibrils, and filaments
    • Cole NB, Murphy DD, Lebowitz J, Di Noto L, Levine RL, et al. (2005) Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments. J Biol Chem 280: 9678-9690.
    • (2005) J Biol Chem , vol.280 , pp. 9678-9690
    • Cole, N.B.1    Murphy, D.D.2    Lebowitz, J.3    Di Noto, L.4    Levine, R.L.5
  • 35
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5
  • 37
    • 33646126948 scopus 로고    scopus 로고
    • Membrane permeabilization: A common mechanism in protein-misfolding diseases
    • Lashuel HA (2005) Membrane permeabilization: a common mechanism in protein-misfolding diseases. Sci Aging Knowledge Environ 2005: e28.
    • (2005) Sci Aging Knowledge Environ 2005
    • Lashuel, H.A.1
  • 38
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, et al. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci U S A 97: 571-576.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5
  • 39
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway KA, Rochet JC, Bieganski RM, Lansbury PT Jr (2001) Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294: 1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr, P.T.4
  • 40
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease - Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT (2002) Neurodegenerative disease - Amyloid pores from pathogenic mutations. Nature 418: 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 42
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett EJ, Bence NF, Jayakumar R, Kopito RR (2005) Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 17: 351-365.
    • (2005) Mol Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 43
    • 44449159424 scopus 로고    scopus 로고
    • Copper(II) binding to alpha-synuclein, the Parkinson's protein
    • Lee JC, Gray HB, Winkler JR (2008) Copper(II) binding to alpha-synuclein, the Parkinson's protein. J Am Chem Soc 130: 6898-6899.
    • (2008) J Am Chem Soc , vol.130 , pp. 6898-6899
    • Lee, J.C.1    Gray, H.B.2    Winkler, J.R.3
  • 44
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å reolution
    • Vijay-Kumar S, Bugg CE, Cook WJ (1987) Structure of ubiquitin refined at 1.8 Å reolution. J Mol Biol 194: 531-544.
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 45
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • Tan JM, Wong ES, Kirkpatrick DS, Pletnikova O, Ko HS, et al. (2008) Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet 17: 431-439.
    • (2008) Hum Mol Genet , vol.17 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3    Pletnikova, O.4    Ko, H.S.5
  • 46
    • 34248662942 scopus 로고    scopus 로고
    • Copper entry into human cells: Progress and unanswered questions
    • Maryon EB, Molloy SA, Zimnicka AM, Kaplan JH (2007) Copper entry into human cells: progress and unanswered questions. Biometals 20: 355-364.
    • (2007) Biometals , vol.20 , pp. 355-364
    • Maryon, E.B.1    Molloy, S.A.2    Zimnicka, A.M.3    Kaplan, J.H.4
  • 47
    • 0037174814 scopus 로고    scopus 로고
    • Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system
    • Lee J, Petris MJ, Thiele DJ (2002) Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system. J Biol Chem 277: 40253-40259.
    • (2002) J Biol Chem , vol.277 , pp. 40253-40259
    • Lee, J.1    Petris, M.J.2    Thiele, D.J.3
  • 48
    • 53449087282 scopus 로고    scopus 로고
    • Copper is taken up efficiently from albumin and alpha2-macroglobulin by cultured human cells by more than one mechanism
    • Moriya M, Ho YH, Grana A, Nguyen L, Alvarez A, et al. (2008) Copper is taken up efficiently from albumin and alpha2-macroglobulin by cultured human cells by more than one mechanism. Am J Physiol Cell Physiol 295: C708-C721.
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Moriya, M.1    Ho, Y.H.2    Grana, A.3    Nguyen, L.4    Alvarez, A.5
  • 49
  • 50
    • 1642404510 scopus 로고    scopus 로고
    • C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: Sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking
    • Xiao Z, Loughlin F, George GN, Howlett GJ, Wedd AG (2004) C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking. J Am Chem Soc 126: 3081-3090.
    • (2004) J Am Chem Soc , vol.126 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 51
    • 23844558049 scopus 로고    scopus 로고
    • Imaging of the intracellular topography of copper with a fluorescent sensor and by synchrotron x-ray fluorescence microscopy
    • Yang L, McRae R, Henary MM, Patel R, Lai B, et al. (2005) Imaging of the intracellular topography of copper with a fluorescent sensor and by synchrotron x-ray fluorescence microscopy. Proc Natl Acad Sci U S A 102: 11179-11184.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11179-11184
    • Yang, L.1    McRae, R.2    Henary, M.M.3    Patel, R.4    Lai, B.5
  • 52
    • 49849088574 scopus 로고    scopus 로고
    • Study of Cu chemical state inside single neurons from Parkinson's disease and control substantia nigra using the micro-XANES technique
    • Chwiej J, Adamek D, Szczerbowska-Boruchowska M, Krygowska-Wajs A, Bohic S, et al. (2008) Study of Cu chemical state inside single neurons from Parkinson's disease and control substantia nigra using the micro-XANES technique. J Trace Elem Med Biol 22: 183-188.
    • (2008) J Trace Elem Med Biol , vol.22 , pp. 183-188
    • Chwiej, J.1    Adamek, D.2    Szczerbowska-Boruchowska, M.3    Krygowska-Wajs, A.4    Bohic, S.5
  • 53
    • 34547557628 scopus 로고    scopus 로고
    • Identification of a vacuole-associated metallo-reductase and its role in Ctr2-mediated intracellular copper mobilization
    • Rees EM, Thiele DJ (2007) Identification of a vacuole-associated metallo-reductase and its role in Ctr2-mediated intracellular copper mobilization. J Biol Chem 282: 21629-21638.
    • (2007) J Biol Chem , vol.282 , pp. 21629-21638
    • Rees, E.M.1    Thiele, D.J.2
  • 54
    • 0024463635 scopus 로고
    • Ubiquitin-protein conjugates accumulate in the lysosomal system of fibroblasts treated with cysteine proteinase inhibitors
    • Doherty FJ, Osborn NU, Wassell JA, Heggie PE, Laszlo L, et al. (1989) Ubiquitin-protein conjugates accumulate in the lysosomal system of fibroblasts treated with cysteine proteinase inhibitors. Biochem J 263: 47-55.
    • (1989) Biochem J , vol.263 , pp. 47-55
    • Doherty, F.J.1    Osborn, N.U.2    Wassell, J.A.3    Heggie, P.E.4    Laszlo, L.5
  • 55
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, et al. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 11: 219-225.
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5
  • 57
    • 33745004381 scopus 로고    scopus 로고
    • Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease
    • Miller LM, Wang Q, Telivala TP, Smith RJ, Lanzirotti A, et al. (2006) Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease. J Struct Biol 155: 30-37.
    • (2006) J Struct Biol , vol.155 , pp. 30-37
    • Miller, L.M.1    Wang, Q.2    Telivala, T.P.3    Smith, R.J.4    Lanzirotti, A.5
  • 58
    • 23944433977 scopus 로고    scopus 로고
    • The role of trace metallic elements in neurodegenerative disorders: Quantitative analysis using XRF and XANES spectroscopy
    • Ide-Ektessabi A, Rabionet M (2005) The role of trace metallic elements in neurodegenerative disorders: quantitative analysis using XRF and XANES spectroscopy. Anal Sci 21: 885-892.
    • (2005) Anal Sci , vol.21 , pp. 885-892
    • Ide-Ektessabi, A.1    Rabionet, M.2
  • 59
    • 0033551782 scopus 로고    scopus 로고
    • Aqueous dissolution of Alzheimer's disease Abeta amyloid deposits by biometal depletion
    • Cherny RA, Legg JT, McLean CA, Fairlie DP, Huang X, et al. (1999) Aqueous dissolution of Alzheimer's disease Abeta amyloid deposits by biometal depletion. J Biol Chem 274: 23223-23228.
    • (1999) J Biol Chem , vol.274 , pp. 23223-23228
    • Cherny, R.A.1    Legg, J.T.2    McLean, C.A.3    Fairlie, D.P.4    Huang, X.5
  • 61
    • 43049150678 scopus 로고    scopus 로고
    • Metals in Alzheimer's and Parkinson's diseases
    • Barnham KJ, Bush AI (2008) Metals in Alzheimer's and Parkinson's diseases. Curr Opin Chem Biol 12: 222-228.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 63
    • 0033669319 scopus 로고    scopus 로고
    • In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies
    • Gai WP, Yuan HX, Li XQ, Power JT, Blumbergs PC, et al. (2000) In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies. Exp Neurol 166: 324-333.
    • (2000) Exp Neurol , vol.166 , pp. 324-333
    • Gai, W.P.1    Yuan, H.X.2    Li, X.Q.3    Power, J.T.4    Blumbergs, P.C.5
  • 64
    • 0037456578 scopus 로고    scopus 로고
    • The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease
    • Sharon R, Bar-Joseph I, Frosch MP, Walsh DM, Hamilton JA, et al. (2003) The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 37: 583-595.
    • (2003) Neuron , vol.37 , pp. 583-595
    • Sharon, R.1    Bar-Joseph, I.2    Frosch, M.P.3    Walsh, D.M.4    Hamilton, J.A.5
  • 65
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: A common structural link for protein-misfolding disease
    • Quist A, Doudevski I, Lin H, Azimova R, Ng D, et al. (2005) Amyloid ion channels: a common structural link for protein-misfolding disease. Proc Natl Acad Sci U S A 102: 10427-10432.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lin, H.3    Azimova, R.4    Ng, D.5
  • 66
    • 0029317175 scopus 로고
    • Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N
    • Wang AC, Grzesiek S, Tschudin R, Lodi PJ, Bax A (1995) Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N. J Biomol NMR 5: 376-382.
    • (1995) J Biomol NMR , vol.5 , pp. 376-382
    • Wang, A.C.1    Grzesiek, S.2    Tschudin, R.3    Lodi, P.J.4    Bax, A.5
  • 68
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two dimensional heteronuclear correlation NMR spectroscopy
    • Palmer AG III, Cavanagh J, Wright PE, Rance M (1991) Sensitivity improvement in proton-detected two dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 93: 151-170.
    • (1991) J Magn Reson , vol.93 , pp. 151-170
    • Palmer III, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 69
    • 0006925492 scopus 로고
    • Pure Absorption Gradient Enhanced Heteronucler Single Quantum Correlation Spectroscopy with Improved Sensitivity
    • Kay LE, Keifer P, Saarinen T (1992) Pure Absorption Gradient Enhanced Heteronucler Single Quantum Correlation Spectroscopy with Improved Sensitivity. J Am Chem Soc 114: 10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 70
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey JH (1981) Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 117: 307-310.
    • (1981) Anal Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.