%PDF-1.3
%
1 0 obj
<<
/Names 2 0 R
/Outlines 3 0 R
/Metadata 4 0 R
/Pages 5 0 R
/Type/Catalog
/PageLabels 6 0 R
>>
endobj
2 0 obj
<<
/Dests 8 0 R
>>
endobj
3 0 obj
<<
/First 9 0 R
/Count 1
/Last 9 0 R
>>
endobj
4 0 obj
<<
/Subtype/XML
/Length 1973
/Type/Metadata
>>
stream
Arbortext Advanced Print Publisher 10.0.1465/W Unicode
2018-05-08T15:34:36+05:01
2019-01-18T08:03:43+00:00
application/pdf
S0033583518000045jrv 1..5
Not for further distribution unless allowed by the License or with the express written permission of Cambridge University Press.
https://doi.org/10.1017/S0033583518000045
Chalmers Tekniska Högskola
Downloaded from https://www.cambridge.org/core. Chalmers Tekniska Högskola, on 18 Jan 2019 at 08:03:43, subject to the Cambridge Core terms of use, available at https://www.cambridge.org/core/terms.
Acrobat Distiller 8.1.0 (Windows)
uuid:91045170-ecf3-4ba2-88d4-b88d9fc12cec
uuid:0e6b3314-2d74-4982-92c0-ea0535762891
endstream
endobj
5 0 obj
<<
/Count 6
/Type/Pages
/Kids[264 0 R 10 0 R 11 0 R 12 0 R 13 0 R 14 0 R]
>>
endobj
6 0 obj
<<
/Nums[0 15 0 R]
>>
endobj
7 0 obj
<<
/CreationDate(D:20180508153436+05'30')
/Creator(Arbortext Advanced Print Publisher 10.0.1465/W Unicode)
/Producer(PDFsharp 1.50.5147 \(www.pdfsharp.com\) \(Original: Chalmers Tekniska Hgskola\))
/ModDate(D:20240328101654+00'00')
/Title(Copper chaperone blocks amyloid formation via ternary complex)
/Author(Horvath, I., Werner, T., Kumar, R. et al)
/Keywords(copper chaperone, protein misfolding, Alpha-synuclein, amyloids, metal transport, Atox1, )
/Subject(Protein misfolding in cells is avoided by a network of protein chaperones that detect misfolded or partially folded species. When proteins escape these control systems, misfolding may result in protein aggregation and amyloid formation. We here show that aggregation of the amyloidogenic protein alpha-synuclein \(alpha S\), the key player in Parkinson's disease, is controlled by the copper transport protein Atox1 in vitro. Copper ions are not freely available in the cellular environment, but when provided by Atox1, the resulting copper-dependent ternary complex blocks aS aggregation. Because the same inhibition was found for a truncated version of alpha S, lacking the C-terminal part, it appears that Atox1 interacts with the N-terminal copper site in alpha S. Metal-dependent chaperoning may be yet another manner in which cells control its proteome.)
>>
endobj
8 0 obj
<<
/Kids[16 0 R]
>>
endobj
9 0 obj
<<
/First 17 0 R
/Parent 3 0 R
/Dest
/Count -5
/Last 18 0 R
/Title
>>
endobj
10 0 obj
<<
/CropBox[0 0 595.276 793.701]
/Annots[19 0 R 20 0 R 21 0 R 22 0 R 23 0 R 24 0 R 25 0 R 26 0 R 27 0 R 28 0 R 29 0 R 30 0 R 31 0 R 32 0 R 33 0 R 34 0 R 35 0 R 36 0 R 37 0 R 38 0 R 39 0 R 40 0 R 41 0 R 42 0 R 43 0 R 44 0 R 45 0 R 46 0 R 47 0 R 48 0 R 49 0 R 50 0 R 51 0 R 52 0 R 53 0 R 54 0 R 55 0 R]
/Parent 5 0 R
/Contents[56 0 R 57 0 R 58 0 R 59 0 R 60 0 R 61 0 R 62 0 R 63 0 R 64 0 R 65 0 R]
/Rotate 0
/MediaBox[0 0 595.276 793.701]
/Resources 66 0 R
/Type/Page
/Group
<<
/CS/DeviceRGB
/S/Transparency
>>
>>
endobj
11 0 obj
<<
/CropBox[0 0 595.276 793.701]
/Annots[67 0 R 68 0 R 69 0 R 70 0 R 71 0 R 72 0 R 73 0 R 74 0 R 75 0 R 76 0 R]
/Parent 5 0 R
/Contents[77 0 R 78 0 R 79 0 R]
/Rotate 0
/MediaBox[0 0 595.276 793.701]
/Resources 80 0 R
/Type/Page
/Group
<<
/CS/DeviceRGB
/S/Transparency
>>
>>
endobj
12 0 obj
<<
/CropBox[0 0 595.276 793.701]
/Annots[81 0 R 82 0 R 83 0 R 84 0 R 85 0 R 86 0 R 87 0 R]
/Parent 5 0 R
/Contents[88 0 R 89 0 R 90 0 R]
/Rotate 0
/MediaBox[0 0 595.276 793.701]
/Resources 91 0 R
/Type/Page
/Group
<<
/CS/DeviceRGB
/S/Transparency
>>
>>
endobj
13 0 obj
<<
/CropBox[0 0 595.276 793.701]
/Annots[92 0 R 93 0 R 94 0 R 95 0 R 96 0 R 97 0 R 98 0 R 99 0 R 100 0 R 101 0 R 102 0 R 103 0 R 104 0 R 105 0 R 106 0 R 107 0 R]
/Parent 5 0 R
/Contents[108 0 R 109 0 R 110 0 R]
/Rotate 0
/MediaBox[0 0 595.276 793.701]
/Resources 111 0 R
/Type/Page
/Group
<<
/CS/DeviceRGB
/S/Transparency
>>
>>
endobj
14 0 obj
<<
/CropBox[0 0 595.276 793.701]
/Annots[112 0 R 113 0 R 114 0 R 115 0 R 116 0 R 117 0 R 118 0 R 119 0 R 120 0 R]
/Parent 5 0 R
/Contents[121 0 R 122 0 R 123 0 R]
/Rotate 0
/MediaBox[0 0 595.276 793.701]
/Resources 124 0 R
/Type/Page
/Group
<<
/CS/DeviceRGB
/S/Transparency
>>
>>
endobj
15 0 obj
<<
/S/D
>>
endobj
16 0 obj
<<
/Limits[]
/Names[125 0 R126 0 R127 0 R128 0 R129 0 R130 0 R131 0 R132 0 R133 0 R134 0 R135 0 R136 0 R137 0 R138 0 R139 0 R140 0 R141 0 R142 0 R143 0 R144 0 R145 0 R146 0 R147 0 R148 0 R149 0 R150 0 R151 0 R152 0 R153 0 R154 0 R155 0 R156 0 R157 0 R158 0 R159 0 R160 0 R161 0 R162 0 R163 0 R164 0 R165 0 R166 0 R167 0 R168 0 R169 0 R170 0 R171 0 R172 0 R173 0 R174 0 R175 0 R176 0 R177 0 R178 0 R179 0 R]
>>
endobj
17 0 obj
<<
/Parent 9 0 R
/Next 180 0 R
/Dest
/Title
>>
endobj
18 0 obj
<<
/Parent 9 0 R
/Dest
/Prev 181 0 R
/Title
>>
endobj
19 0 obj
<<
/Rect[42.52 701.915 117.468 710.872]
/Subtype/Link
/A
<<
/URI(https://www.cambridge.org/qrb)
/S/URI
>>
/Border[0 0 0]
/Type/Annot
>>
endobj
20 0 obj
<<
/Rect[42.52 597.827 175.294 605.083]
/Subtype/Link
/A
<<
/URI(https://doi.org/10.1017/S0033583518000045)
/S/URI
>>
/Border[0 0 0]
/Type/Annot
>>
endobj
21 0 obj
<<
/Rect[133.852 491.357 158.683 498.614]
/Subtype/Link
/A
<<
/URI(mailto:pernilla.wittung@chalmers.se)
/S/URI
>>
/Border[0 0 0]
/Type/Annot
>>
endobj
22 0 obj
<<
/Rect[42.52 482.343 107.943 489.6]
/Subtype/Link
/A
<<
/URI(mailto:pernilla.wittung@chalmers.se)
/S/URI
>>
/Border[0 0 0]
/Type/Annot
>>
endobj
23 0 obj
<<
/Rect[351.212 453.94 369.411 463.408]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
24 0 obj
<<
/Rect[502.016 409.946 520.214 419.414]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
25 0 obj
<<
/Rect[219.175 398.948 237.373 408.416]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
26 0 obj
<<
/Rect[477.411 387.95 495.666 397.417]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
27 0 obj
<<
/Rect[493.682 376.951 511.88 386.419]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
28 0 obj
<<
/Rect[289.077 365.953 307.332 375.42]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
29 0 obj
<<
/Rect[428.201 365.953 446.457 375.42]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
30 0 obj
<<
/Rect[505.587 365.953 523.842 375.42]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
31 0 obj
<<
/Rect[279.836 343.956 298.091 353.424]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
32 0 obj
<<
/Rect[365.272 343.956 387.666 353.424]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
33 0 obj
<<
/Rect[394.923 321.902 413.178 331.427]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
34 0 obj
<<
/Rect[418.734 321.902 436.989 331.427]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
35 0 obj
<<
/Rect[520.838 321.902 539.093 331.427]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
36 0 obj
<<
/Rect[243.609 310.904 266.003 320.428]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
37 0 obj
<<
/Rect[274.167 310.904 300.076 320.428]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
38 0 obj
<<
/Rect[423.496 299.905 441.694 309.43]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
39 0 obj
<<
/Rect[497.48 299.905 515.735 309.43]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
40 0 obj
<<
/Rect[358.072 266.91 376.327 276.435]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
41 0 obj
<<
/Rect[259.313 244.913 282.331 254.438]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
42 0 obj
<<
/Rect[290.721 222.917 308.976 232.441]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
43 0 obj
<<
/Rect[198.425 211.918 216.68 221.443]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
44 0 obj
<<
/Rect[271.162 211.918 289.361 221.443]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
45 0 obj
<<
/Rect[353.48 211.918 371.735 221.443]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
46 0 obj
<<
/Rect[305.461 189.921 323.66 199.446]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
47 0 obj
<<
/Rect[463.011 167.924 489.713 177.449]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
48 0 obj
<<
/Rect[248.201 145.928 266.4 155.452]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
49 0 obj
<<
/Rect[374.457 123.931 392.655 133.398]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
50 0 obj
<<
/Rect[198.425 101.934 216.68 111.402]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
51 0 obj
<<
/Rect[468.113 90.935 486.368 100.403]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
52 0 obj
<<
/Rect[198.425 79.937 216.68 89.405]
/Subtype/Link
/Border[0 0 0]
/Dest
/Type/Annot
>>
endobj
53 0 obj
<<
/Type/Annot
/Subtype/Link
/Rect[17.16 15.849609 128.682 23.774414]
/Border[0 0 0]
/A 182 0 R
>>
endobj
54 0 obj
<<
/Type/Annot
/Subtype/Link
/Rect[131.85 15.849609 257.67 23.774414]
/Border[0 0 0]
/A 183 0 R
>>
endobj
55 0 obj
<<
/Type/Annot
/Subtype/Link
/Rect[69.804 23.774414 162.582 31.699219]
/Border[0 0 0]
/A 184 0 R
>>
endobj
56 0 obj
<<
/Filter/FlateDecode
/Length 10
>>
stream
x+ |
endstream
endobj
57 0 obj
<<
/Length 1251
/Filter/FlateDecode
>>
stream
H|VrF+p\征U.8Wd)d
@#ezvA}Lbq1g Bze;[|%aF*ǭ36K4yl=sʜ,q\o%xD&u2D'sn(a};[,y1_>|,qH20@ ]v7[/~o:̍Go;8K @r㽏Q0$$K¿,}HcE?V}ε