메뉴 건너뛰기




Volumn 22, Issue 1, 2009, Pages 159-175

Can copper binding to the prion protein generate a misfolded form of the protein?

Author keywords

cleavage; Copper binding; Density functional theory; Molecular dynamics; Oxidative damage; Prion protein; Protein misfolding

Indexed keywords

COPPER; GLYCINE; HISTIDINE; PRION PROTEIN; PROTEIN; TRYPTOPHAN;

EID: 59449085625     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-008-9196-x     Document Type: Conference Paper
Times cited : (18)

References (81)
  • 1
    • 41649121724 scopus 로고    scopus 로고
    • Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation
    • 10.1110/ps.073249008
    • K Antwi M Mahar R Srikanth MR Olbris JF Tyson RW Vachet 2008 Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation Protein Sci 17 748 759 10.1110/ps.073249008
    • (2008) Protein Sci , vol.17 , pp. 748-759
    • Antwi, K.1    Mahar, M.2    Srikanth, R.3    Olbris, M.R.4    Tyson, J.F.5    Vachet, R.W.6
  • 3
    • 34548317095 scopus 로고    scopus 로고
    • Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126
    • A-L Bergström J Chabry L Bastholm PMH Heegaard 2007 Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126 Biochim Biophys Acta 1774 1118 1127
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1118-1127
    • Bergström, A.-L.1    Chabry, J.2    Bastholm, L.3    Heegaard, P.M.H.4
  • 4
    • 0034680507 scopus 로고    scopus 로고
    • Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study
    • RP Bonomo G Imperllizzeri G Pappalardo E Rizzarelli G Tabbì 2000 Copper(II) binding modes in the prion octapeptide PHGGGWGQ: a spectroscopic and voltammetric study Chemistry (Easton) 6 4195 4202
    • (2000) Chemistry (Easton) , vol.6 , pp. 4195-4202
    • Bonomo, R.P.1    Imperllizzeri, G.2    Pappalardo, G.3    Rizzarelli, E.4    Tabbì, G.5
  • 8
    • 0141849856 scopus 로고    scopus 로고
    • Prion protein conversions: Insight into mechanisms, TSE transmission barriers and strains
    • 10.1093/bmb/66.1.109
    • B Caughey 2003 Prion protein conversions: insight into mechanisms, TSE transmission barriers and strains Br Med Bull 66 109 120 10.1093/bmb/66.1.109
    • (2003) Br Med Bull , vol.66 , pp. 109-120
    • Caughey, B.1
  • 10
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators
    • 10.1016/S0166-2236(02)02263-4
    • F Checler B Vincent 2002 Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators Trends Neurosci 25 616 620 10.1016/S0166-2236(02)02263-4
    • (2002) Trends Neurosci , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 11
    • 0029027854 scopus 로고
    • Truncated forms of the human prion protein in normal brain and in prion diseases
    • 10.1074/jbc.270.32.19173
    • SG Chen DB Teplow P Parchi JK Teller P Gambetti L Autilio-Gambetti 1995 Truncated forms of the human prion protein in normal brain and in prion diseases J Biol Chem 270 19173 19180 10.1074/jbc.270.32.19173
    • (1995) J Biol Chem , vol.270 , pp. 19173-19180
    • Chen, S.G.1    Teplow, D.B.2    Parchi, P.3    Teller, J.K.4    Gambetti, P.5    Autilio-Gambetti, L.6
  • 13
    • 0024474822 scopus 로고
    • Diagnosis of Gerstmann-Sträussler syndrome in familial dementia with prion protein gene analysis
    • 10.1016/S0140-6736(89)90256-0
    • J Collinge AE Harding F Owen M Poulter R Lofthouse AM Boughey T Shah TJ Crow 1989 Diagnosis of Gerstmann-Sträussler syndrome in familial dementia with prion protein gene analysis Lancet 2 15 17 10.1016/S0140-6736(89)90256-0
    • (1989) Lancet , vol.2 , pp. 15-17
    • Collinge, J.1    Harding, A.E.2    Owen, F.3    Poulter, M.4    Lofthouse, R.5    Boughey, A.M.6    Shah, T.7    Crow, T.J.8
  • 16
    • 39449113042 scopus 로고    scopus 로고
    • A place for thioether chemistry in cellular copper ion recognition and trafficking
    • 10.1038/nchembio0308-148
    • AV Davis TV O'Halloran 2008 A place for thioether chemistry in cellular copper ion recognition and trafficking Nat Chem Biol 4 148 151 10.1038/nchembio0308-148
    • (2008) Nat Chem Biol , vol.4 , pp. 148-151
    • Davis, A.V.1    O'Halloran, T.V.2
  • 19
    • 0001070937 scopus 로고
    • Theoretical analysis of the photophysical properties of indole, the ondolyl radical, and the indole radical cation
    • 10.1021/j100535a006
    • EM Evleth O Chalvet P Bamlère 1977 Theoretical analysis of the photophysical properties of indole, the ondolyl radical, and the indole radical cation J Phys Chem 81 1913 1917 10.1021/j100535a006
    • (1977) J Phys Chem , vol.81 , pp. 1913-1917
    • Evleth, E.M.1    Chalvet, O.2    Bamlère, P.3
  • 20
    • 0033695126 scopus 로고    scopus 로고
    • Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice
    • 10.1016/S0896-6273(00)00046-5
    • E Flechsig D Shmerling I Hegyi AJ Raeber M Fischer A Cozzio C von Mering A Aguzzi C Weissmann 2000 Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice Neuron 27 399 408 10.1016/S0896-6273(00)00046-5
    • (2000) Neuron , vol.27 , pp. 399-408
    • Flechsig, E.1    Shmerling, D.2    Hegyi, I.3    Raeber, A.J.4    Fischer, M.5    Cozzio, A.6    Von Mering, C.7    Aguzzi, A.8    Weissmann, C.9
  • 21
    • 33645530594 scopus 로고    scopus 로고
    • A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat.
    • doi: 10.1039/b511553a
    • Garnett AP, Jones CE, Viles JH (2006) A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat. J Chem Soc Dalton Trans 509-518. doi: 10.1039/b511553a
    • (2006) J Chem Soc Dalton Trans , pp. 509-518
    • Garnett, A.P.1    Jones, C.E.2    Viles, J.H.3
  • 23
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: Where are we now?
    • 10.1111/j.1471-4159.2006.03907.x
    • B Halliwell 2006 Oxidative stress and neurodegeneration: where are we now? J Neurochem 97 1634 1658 10.1111/j.1471-4159.2006.03907.x
    • (2006) J Neurochem , vol.97 , pp. 1634-1658
    • Halliwell, B.1
  • 24
    • 0000406389 scopus 로고    scopus 로고
    • Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: Metal binding, DNA cleavage, and other properties
    • 10.1021/ar9501535
    • C Harford B Sarkar 1997 Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: metal binding, DNA cleavage, and other properties Acc Chem Res 30 123 130 10.1021/ar9501535
    • (1997) Acc Chem Res , vol.30 , pp. 123-130
    • Harford, C.1    Sarkar, B.2
  • 25
    • 0023748491 scopus 로고
    • Evidence for release of copper in the brain: Depolarization-induced release of newly taken-up 67copper
    • 10.1002/syn.890020408
    • DE Hartter A Barnea 1988 Evidence for release of copper in the brain: depolarization-induced release of newly taken-up 67copper Synapse 2 412 415 10.1002/syn.890020408
    • (1988) Synapse , vol.2 , pp. 412-415
    • Hartter, D.E.1    Barnea, A.2
  • 27
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • 10.1006/bbrc.1995.1233
    • MP Hornshaw JR McDermott JM Candy 1995 Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein Biochem Biophys Res Commun 207 621 629 10.1006/bbrc.1995.1233
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 28
    • 4344678284 scopus 로고    scopus 로고
    • Structure and reactions of the peroxy radicals of glycine and alanine in peptides: An ab initio study
    • 10.1002/poc.794
    • ML Huang A Rauk 2004 Structure and reactions of the peroxy radicals of glycine and alanine in peptides: an ab initio study J Phys Org Chem 17 777 786 10.1002/poc.794
    • (2004) J Phys Org Chem , vol.17 , pp. 777-786
    • Huang, M.L.1    Rauk, A.2
  • 29
    • 1842504323 scopus 로고    scopus 로고
    • Redox-active metals, oxidative stress, and Alzheimer's disease pathology
    • 10.1196/annals.1306.012
    • X Huang RD Moir RE Tanzi AI Bush JT Rogers 2004 Redox-active metals, oxidative stress, and Alzheimer's disease pathology Ann N Y Acad Sci 1012 153 163 10.1196/annals.1306.012
    • (2004) Ann N y Acad Sci , vol.1012 , pp. 153-163
    • Huang, X.1    Moir, R.D.2    Tanzi, R.E.3    Bush, A.I.4    Rogers, J.T.5
  • 30
    • 0031765769 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues
    • A Jiménez-Huete PM Lievens R Vidal P Piccardo B Ghetti F Tagliavini B Frangione F Prelli 1998 Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues Am J Pathol 153 1561 1572
    • (1998) Am J Pathol , vol.153 , pp. 1561-1572
    • Jiménez-Huete, A.1    Lievens, P.M.2    Vidal, R.3    Piccardo, P.4    Ghetti, B.5    Tagliavini, F.6    Frangione, B.7    Prelli, F.8
  • 31
    • 3542999252 scopus 로고    scopus 로고
    • 2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein
    • 10.1074/jbc.M403467200
    • 2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein J Biol Chem 279 32018 32027 10.1074/jbc.M403467200
    • (2004) J Biol Chem , vol.279 , pp. 32018-32027
    • Jones, C.E.1    Abdelraheim, S.R.2    Brown, D.R.3    Viles, J.H.4
  • 34
    • 0032722354 scopus 로고    scopus 로고
    • Prominent psychiatric features and early onset in an inherited prion disease with a new insertional mutation in the prion protein gene
    • 10.1093/brain/122.12.2375
    • JL Laplanche KH Hachimi I Durieux P Thuillet L Defebvre N Delasnerie-Laupretre K Peoc'h JF Foncin A Destee 1999 Prominent psychiatric features and early onset in an inherited prion disease with a new insertional mutation in the prion protein gene Brain 122 2375 2386 10.1093/brain/122.12.2375
    • (1999) Brain , vol.122 , pp. 2375-2386
    • Laplanche, J.L.1    Hachimi, K.H.2    Durieux, I.3    Thuillet, P.4    Defebvre, L.5    Delasnerie-Laupretre, N.6    Peoc'H, K.7    Foncin, J.F.8    Destee, A.9
  • 35
    • 33645639813 scopus 로고    scopus 로고
    • The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions
    • 10.1074/jbc.M510606200
    • SR Leliveld RT Dame GJ Wuite L Stitz C Korth 2006 The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions J Biol Chem 281 3268 3275 10.1074/jbc.M510606200
    • (2006) J Biol Chem , vol.281 , pp. 3268-3275
    • Leliveld, S.R.1    Dame, R.T.2    Wuite, G.J.3    Stitz, L.4    Korth, C.5
  • 36
    • 44949123779 scopus 로고    scopus 로고
    • Expansion of the octarepeat domain alters the misfolding pathway but not the folding pathway of the prion protein
    • 10.1021/bi800253c
    • SR Leliveld L Stitz C Korth 2008 Expansion of the octarepeat domain alters the misfolding pathway but not the folding pathway of the prion protein Biochemistry 47 6267 6278 10.1021/bi800253c
    • (2008) Biochemistry , vol.47 , pp. 6267-6278
    • Leliveld, S.R.1    Stitz, L.2    Korth, C.3
  • 37
    • 1642410070 scopus 로고    scopus 로고
    • Alpha- and beta-cleavages of the amino-terminus of the cellular prion protein
    • 10.1016/j.biolcel.2003.11.007
    • A Mangé F Béranger K Peoc'h T Onodera Y Frobert S Lehmann 2004 Alpha- and beta-cleavages of the amino-terminus of the cellular prion protein Biol Cell 96 125 132 10.1016/j.biolcel.2003.11.007
    • (2004) Biol Cell , vol.96 , pp. 125-132
    • Mangé, A.1    Béranger, F.2    Peoc'H, K.3    Onodera, T.4    Frobert, Y.5    Lehmann, S.6
  • 38
    • 0035910498 scopus 로고    scopus 로고
    • Cleavage of the amino terminus of the prion protein by reactive oxygen species
    • 10.1074/jbc.M007243200
    • HE McMahon A Mange N Nishida C Creminon D Casanova S Lehmann 2001 Cleavage of the amino terminus of the prion protein by reactive oxygen species J Biol Chem 276 2286 2291 10.1074/jbc.M007243200
    • (2001) J Biol Chem , vol.276 , pp. 2286-2291
    • McMahon, H.E.1    Mange, A.2    Nishida, N.3    Creminon, C.4    Casanova, D.5    Lehmann, S.6
  • 39
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • 10.1146/annurev.physchem.58.032806.104657
    • GL Millhauser 2007 Copper and the prion protein: methods, structures, function, and disease Annu Rev Phys Chem 58 299 320 10.1146/annurev.physchem.58. 032806.104657
    • (2007) Annu Rev Phys Chem , vol.58 , pp. 299-320
    • Millhauser, G.L.1
  • 41
    • 20544450600 scopus 로고    scopus 로고
    • Copper reduction by the octapeptide repeat region of prion protein: PH dependence and implications in cellular copper uptake
    • 10.1021/bi0501784
    • T Miura S Sasaki A Toyama H Takeuchi 2005 Copper reduction by the octapeptide repeat region of prion protein: pH dependence and implications in cellular copper uptake Biochemistry 44 8712 8720 10.1021/bi0501784
    • (2005) Biochemistry , vol.44 , pp. 8712-8720
    • Miura, T.1    Sasaki, S.2    Toyama, A.3    Takeuchi, H.4
  • 43
    • 0037355742 scopus 로고    scopus 로고
    • Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
    • 10.1023/A:1020795422185
    • C Opazo MI Barría FH Ruiz NC Inestrosa 2003 Copper reduction by copper binding proteins and its relation to neurodegenerative diseases Biometals 16 91 98 10.1023/A:1020795422185
    • (2003) Biometals , vol.16 , pp. 91-98
    • Opazo, C.1    Barría, M.I.2    Ruiz, F.H.3    Inestrosa, N.C.4
  • 44
    • 34548315721 scopus 로고    scopus 로고
    • Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: Speciation, stability constants and binding details
    • 10.1002/chem.200601568
    • K Osz Z Nagy G Pappalardo G Di Natale D Sanna G Micera E Rizzarelli I Sóvágó 2007 Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details Chemistry 13 7129 7143 10.1002/chem.200601568
    • (2007) Chemistry , vol.13 , pp. 7129-7143
    • Osz, K.1    Nagy, Z.2    Pappalardo, G.3    Di Natale, G.4    Sanna, D.5    Micera, G.6    Rizzarelli, E.7    Sóvágó, I.8
  • 48
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • 10.1074/jbc.273.50.33107
    • PC Pauly DA Harris 1998 Copper stimulates endocytosis of the prion protein J Biol Chem 273 33107 33110 10.1074/jbc.273.50.33107
    • (1998) J Biol Chem , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 49
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • 10.1016/S0960-9822(01)00147-6
    • WS Perera NM Hooper 2001 Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region Curr Biol 11 519 523 10.1016/S0960-9822(01)00147-6
    • (2001) Curr Biol , vol.11 , pp. 519-523
    • Perera, W.S.1    Hooper, N.M.2
  • 50
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • 10.1126/science.1675487
    • SB Prusiner 1991 Molecular biology of prion diseases Science 252 1515 1522 10.1126/science.1675487
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 51
    • 0037254403 scopus 로고    scopus 로고
    • Computational studies of Cu(II)[peptide] binding motifs: Cu[HGGG] and Cu[HG] as models for Cu(II) binding to the prion protein octarepeat region
    • 10.1007/s00775-002-0386-7
    • MJ Pushie A Rauk 2003 Computational studies of Cu(II)[peptide] binding motifs: Cu[HGGG] and Cu[HG] as models for Cu(II) binding to the prion protein octarepeat region J Biol Inorg Chem 8 53 65 10.1007/s00775-002-0386-7
    • (2003) J Biol Inorg Chem , vol.8 , pp. 53-65
    • Pushie, M.J.1    Rauk, A.2
  • 52
    • 36849038380 scopus 로고    scopus 로고
    • 2+-bound and metal-free forms
    • 10.1529/biophysj.107.109512
    • 2+-bound and metal-free forms Biophys J 93 3762 3774 10.1529/biophysj.107.109512
    • (2007) Biophys J , vol.93 , pp. 3762-3774
    • Pushie, M.J.1    Vogel, H.J.2
  • 53
    • 58149332705 scopus 로고    scopus 로고
    • 2+-mediated β-cleavage
    • 10.1529/biophysj.108.139568
    • 2+-mediated β-cleavage Biophys J 95 5084 5091 10.1529/biophysj.108.139568
    • (2008) Biophys J , vol.95 , pp. 5084-5091
    • Pushie, M.J.1    Vogel, H.J.2
  • 54
    • 69849104508 scopus 로고    scopus 로고
    • 2+ reduction, β-cleavage and β-sheet initiation within the N-terminal domain of the prion protein: Insights from density functional theory and molecular dynamics calculations
    • 2+ reduction, β-cleavage and β-sheet initiation within the N-terminal domain of the prion protein: insights from density functional theory and molecular dynamics calculations. J Toxicol Environ Health A (in press)
    • (2009) J Toxicol Environ Health A (In Press)
    • Pushie, M.J.1    Vogel, H.J.2
  • 55
    • 34547824101 scopus 로고    scopus 로고
    • Mass spectrometric determination of the coordination geometry of potential copper(II) surrogates for the mammalian prion protein octarepeat region
    • 10.1021/ac070312l
    • MJ Pushie ARS Ross HJ Vogel 2007 Mass spectrometric determination of the coordination geometry of potential copper(II) surrogates for the mammalian prion protein octarepeat region Anal Chem 79 5659 6767 10.1021/ac070312l
    • (2007) Anal Chem , vol.79 , pp. 5659-6767
    • Pushie, M.J.1    Ross, A.R.S.2    Vogel, H.J.3
  • 56
    • 39749196738 scopus 로고    scopus 로고
    • Why is the amyloid beta peptide of Alzheimer's disease neurotoxic?
    • doi: 10.1039/b718601k
    • Rauk A (2008) Why is the amyloid beta peptide of Alzheimer's disease neurotoxic? J Chem Soc Dalton Trans 1273-1282. doi: 10.1039/b718601k
    • (2008) J Chem Soc Dalton Trans , pp. 1273-1282
    • Rauk, A.1
  • 57
    • 0033551437 scopus 로고    scopus 로고
    • Effects of structure on αc-H bond enthalpies of amino acid residues: Relevance to H transfers in enzyme mechanisms and in protein oxidation
    • A Rauk D Yu J Taylor GV Shustov DA Block DA Armstrong 1999 Effects of structure on αC-H bond enthalpies of amino acid residues: relevance to H transfers in enzyme mechanisms and in protein oxidation Biochemistry 38 9089 9096
    • (1999) Biochemistry , vol.38 , pp. 9089-9096
    • Rauk, A.1    Yu, D.2    Taylor, J.3    Shustov, G.V.4    Block, D.A.5    Armstrong, D.A.6
  • 59
    • 0034673578 scopus 로고    scopus 로고
    • The N-terminal tandem repeat region of human prion protein reduces copper: Role of tryptophan residues
    • 10.1006/bbrc.2000.2270
    • FH Ruiz E Silva NC Inestrosa 2000 The N-terminal tandem repeat region of human prion protein reduces copper: role of tryptophan residues Biochem Biophys Res Commun 269 491 495 10.1006/bbrc.2000.2270
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 491-495
    • Ruiz, F.H.1    Silva, E.2    Inestrosa, N.C.3
  • 61
    • 33847125254 scopus 로고    scopus 로고
    • The copper(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox-active at physiological pH
    • 10.1021/ic061236s
    • J Shearer P Soh 2007 The copper(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox-active at physiological pH Inorg Chem 46 710 719 10.1021/ic061236s
    • (2007) Inorg Chem , vol.46 , pp. 710-719
    • Shearer, J.1    Soh, P.2
  • 62
    • 55349126038 scopus 로고    scopus 로고
    • Both Met(109) and Met(112) are utilized for Cu(II) coordination by the amyloidogenic fragment of the human prion protein at physiological pH
    • 10.1016/j.jinorgbio.2008.07.016
    • J Shearer P Soh S Lentz 2008 Both Met(109) and Met(112) are utilized for Cu(II) coordination by the amyloidogenic fragment of the human prion protein at physiological pH J Inorg Biochem 102 2103 2113 10.1016/j.jinorgbio.2008.07.016
    • (2008) J Inorg Biochem , vol.102 , pp. 2103-2113
    • Shearer, J.1    Soh, P.2    Lentz, S.3
  • 65
    • 50849129564 scopus 로고    scopus 로고
    • Identification of the copper(II) coordinating residues in the prion protein by metal-catalyzed oxidation mass spectrometry: Evidence for multiple isomers at low copper(II) loadings
    • 10.1021/bi800970m
    • R Srikanth J Wilson CS Burns RW Vachet 2008 Identification of the copper(II) coordinating residues in the prion protein by metal-catalyzed oxidation mass spectrometry: evidence for multiple isomers at low copper(II) loadings Biochemistry 47 9258 9268 10.1021/bi800970m
    • (2008) Biochemistry , vol.47 , pp. 9258-9268
    • Srikanth, R.1    Wilson, J.2    Burns, C.S.3    Vachet, R.W.4
  • 67
    • 53149101680 scopus 로고    scopus 로고
    • Absence of the cellular prion protein exacerbates and prolongs neuroinflammation in experimental autoimmune encephalomyelitis
    • 10.2353/ajpath.2008.071062
    • S Tsutsui JN Hahn TA Johnson Z Ali FR Jirik 2008 Absence of the cellular prion protein exacerbates and prolongs neuroinflammation in experimental autoimmune encephalomyelitis Am J Pathol 173 1029 1041 10.2353/ajpath.2008. 071062
    • (2008) Am J Pathol , vol.173 , pp. 1029-1041
    • Tsutsui, S.1    Hahn, J.N.2    Johnson, T.A.3    Ali, Z.4    Jirik, F.R.5
  • 68
    • 0029598460 scopus 로고
    • Hypokinesia and presenile dementia in a Dutch family with a novel insertion in the prion protein gene
    • 10.1093/brain/118.6.1565
    • WA van Gool GW Hensels EM Hoogerwaard JH Wiezer P Wesseling PA Bolhuis 1995 Hypokinesia and presenile dementia in a Dutch family with a novel insertion in the prion protein gene Brain 118 1565 1571 10.1093/brain/118.6.1565
    • (1995) Brain , vol.118 , pp. 1565-1571
    • Van Gool, W.A.1    Hensels, G.W.2    Hoogerwaard, E.M.3    Wiezer, J.H.4    Wesseling, P.5    Bolhuis, P.A.6
  • 69
    • 0041302374 scopus 로고    scopus 로고
    • Cellular prion protein function in copper homeostasis and redox signalling at the synapse
    • 10.1046/j.1471-4159.2003.01882.x
    • N Vassallo J Herms 2003 Cellular prion protein function in copper homeostasis and redox signalling at the synapse J Neurochem 86 538 544 10.1046/j.1471-4159.2003.01882.x
    • (2003) J Neurochem , vol.86 , pp. 538-544
    • Vassallo, N.1    Herms, J.2
  • 71
    • 27844566750 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS)-mediated β-cleavage of the prion protein in the mechanism of the cellular response to oxidative stress
    • 10.1042/BST20051123
    • NT Watt NM Hooper 2005 Reactive oxygen species (ROS)-mediated β-cleavage of the prion protein in the mechanism of the cellular response to oxidative stress Biochem Soc Trans 33 1123 1125 10.1042/BST20051123
    • (2005) Biochem Soc Trans , vol.33 , pp. 1123-1125
    • Watt, N.T.1    Hooper, N.M.2
  • 72
    • 0141738255 scopus 로고    scopus 로고
    • PrP knock-out and PrP transgenic mice in prion research
    • 10.1093/bmb/66.1.43
    • C Weissmann E Flechsig 2003 PrP knock-out and PrP transgenic mice in prion research Br Med Bull 66 43 60 10.1093/bmb/66.1.43
    • (2003) Br Med Bull , vol.66 , pp. 43-60
    • Weissmann, C.1    Flechsig, E.2
  • 74
    • 33750534538 scopus 로고    scopus 로고
    • Multiple forms of copper (II) coordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4
    • 10.1042/BJ20060721
    • MA Wells C Jelinska LLP Hosszu CJ Craven AR Clarke J Collinge JP Waltho GS Jackson 2006 Multiple forms of copper (II) coordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4 Biochem J 400 501 510 10.1042/BJ20060721
    • (2006) Biochem J , vol.400 , pp. 501-510
    • Wells, M.A.1    Jelinska, C.2    Hosszu, L.L.P.3    Craven, C.J.4    Clarke, A.R.5    Collinge, J.6    Waltho, J.P.7    Jackson, G.S.8
  • 76
    • 33748774117 scopus 로고    scopus 로고
    • Effect of side chains on competing pathways for β-scission reactions of peptide-backbone alkoxyl radicals
    • 10.1021/jp062916j
    • GPF Wood CJ Easton A Rauk MJ Davies L Radom 2006 Effect of side chains on competing pathways for β-scission reactions of peptide-backbone alkoxyl radicals J Phys Chem A 110 10316 10323 10.1021/jp062916j
    • (2006) J Phys Chem A , vol.110 , pp. 10316-10323
    • Wood, G.P.F.1    Easton, C.J.2    Rauk, A.3    Davies, M.J.4    Radom, L.5
  • 77
    • 0344326239 scopus 로고    scopus 로고
    • Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein
    • 10.1006/jmbi.1999.2831
    • F Wopfner G Weidenhöfer R Schneider A von Brunn S Gilch TF Schwarz T Werner HM Schätzl 1999 Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein J Mol Biol 289 1163 1178 10.1006/jmbi.1999.2831
    • (1999) J Mol Biol , vol.289 , pp. 1163-1178
    • Wopfner, F.1    Weidenhöfer, G.2    Schneider, R.3    Von Brunn, A.4    Gilch, S.5    Schwarz, T.F.6    Werner, T.7    Schätzl, H.M.8
  • 78
    • 33744959528 scopus 로고    scopus 로고
    • Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack
    • 10.1074/jbc.M511819200
    • S Yin S Yu C Li P Wong B Chang F Xiao SC Kang H Yan G Xiao J Grassi P Tien MS Sy 2006 Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack J Biol Chem 281 10698 10705 10.1074/jbc.M511819200
    • (2006) J Biol Chem , vol.281 , pp. 10698-10705
    • Yin, S.1    Yu, S.2    Li, C.3    Wong, P.4    Chang, B.5    Xiao, F.6    Kang, S.C.7    Yan, H.8    Xiao, G.9    Grassi, J.10    Tien, P.11    Sy, M.S.12
  • 81
    • 39749155839 scopus 로고    scopus 로고
    • Raman optical activity and circular dichroism reveal dramatic differences in the influence of divalent copper and manganese ions on prion protein folding
    • F Zhu P Davies AR Thompsett SM Kelly GE Tranter L Hecht NW Isaacs DR Brown LD Barron 2008 Raman optical activity and circular dichroism reveal dramatic differences in the influence of divalent copper and manganese ions on prion protein folding Biochemistry 47 2510 2517
    • (2008) Biochemistry , vol.47 , pp. 2510-2517
    • Zhu, F.1    Davies, P.2    Thompsett, A.R.3    Kelly, S.M.4    Tranter, G.E.5    Hecht, L.6    Isaacs, N.W.7    Brown, D.R.8    Barron, L.D.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.