메뉴 건너뛰기




Volumn 14, Issue 8, 2009, Pages 1175-1185

Interaction of selected divalent metal ions with human ataxin-3 Q36

Author keywords

Ataxin 3; Fourier transform Raman; Metal ions; Secondary structures

Indexed keywords

APOMYOGLOBIN; ATAXIN 3; CADMIUM; COPPER ION; DIVALENT CATION; METAL ION; NICKEL; POLYGLUTAMINE; ZINC ION;

EID: 70449530587     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-009-0561-1     Document Type: Article
Times cited : (20)

References (65)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • DOI 10.1146/annurev.neuro.23.1.217
    • HY Zoghbi HT Orr 2000 Annu Rev Neurosci 23 217 247 10.1146/annurev.neuro. 23.1.217 1:CAS:528:DC%2BD3cXjs1Gmsrw%3D 10845064 (Pubitemid 30350043)
    • (2000) Annual Review of Neuroscience , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 2
    • 0034762642 scopus 로고    scopus 로고
    • Expansion explosion: New clues to the pathogenesis of repeat expansion neurodegenerative diseases
    • DOI 10.1016/S1471-4914(01)02179-7, PII S1471491401021797
    • RL Margolis CA Ross 2001 Trends Mol Med 7 479 482 10.1016/S1471-4914(01) 02179-7 1:CAS:528:DC%2BD3MXotF2qt7Y%3D 11689312 (Pubitemid 33021670)
    • (2001) Trends in Molecular Medicine , vol.7 , Issue.11 , pp. 479-482
    • Margolis, R.L.1    Ross, C.A.2
  • 3
    • 49749198315 scopus 로고
    • 10.1016/0009-8981(59)90119-6 1:CAS:528:DyaG1MXovF2itQ%3D%3D 13663253
    • H Baum KS Dodgson B Spencer 1959 Clin Chim Acta 4 453 455 10.1016/0009-8981(59)90119-6 1:CAS:528:DyaG1MXovF2itQ%3D%3D 13663253
    • (1959) Clin Chim Acta , vol.4 , pp. 453-455
    • Baum, H.1    Dodgson, K.S.2    Spencer, B.3
  • 8
    • 0035976953 scopus 로고    scopus 로고
    • 10.1074/jbc.M106575200 1:CAS:528:DC%2BD3MXovFegurY%3D 11572863
    • Y Chai L Wu JD Griffin HL Paulson 2001 J Biol Chem 276 44889 44897 10.1074/jbc.M106575200 1:CAS:528:DC%2BD3MXovFegurY%3D 11572863
    • (2001) J Biol Chem , vol.276 , pp. 44889-44897
    • Chai, Y.1    Wu, L.2    Griffin, J.D.3    Paulson, H.L.4
  • 9
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3
    • DOI 10.1016/j.jmb.2004.09.065, PII S0022283604012239
    • L Masino G Nicastro RP Menon F Dal Piaz L Calder A Pastore 2004 J Mol Biol 344 1021 1035 10.1016/j.jmb.2004.09.065 1:CAS:528:DC%2BD2cXpslWmsbY%3D 15544810 (Pubitemid 39491247)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Piaz, F.D.4    Calder, L.5    Pastore, A.6
  • 11
    • 0347481134 scopus 로고    scopus 로고
    • Temperature-Dependent, Irreversible Formation of Amyloid Fibrils by a Soluble Human Ataxin-3 Carrying a Moderately Expanded Polyglutamine Stretch (Q36)
    • DOI 10.1021/bi0352825
    • E Shehi P Fusi F Secundo S Pozzuolo A Bairati P Tortora 2003 Biochemistry 42 14626 14632 10.1021/bi0352825 1:CAS:528:DC%2BD3sXptVegsbs%3D 14661975 (Pubitemid 37532009)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14626-14632
    • Shehi, E.1    Fusi, P.2    Secundo, F.3    Pozzuolo, S.4    Bairati, A.5    Tortora, P.6
  • 12
    • 0035871295 scopus 로고    scopus 로고
    • Beyond the qs in the polyglutamine diseases
    • DOI 10.1101/gad.888401
    • HT Orr 2001 Genes Dev 15 925 932 10.1101/gad.888401 1:CAS:528: DC%2BD3MXjtVOku7w%3D 11316786 (Pubitemid 32323542)
    • (2001) Genes and Development , vol.15 , Issue.8 , pp. 925-932
    • Orr, H.T.1
  • 13
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • DOI 10.1016/S1367-5931(99)00073-3
    • AI Bush 2000 Curr Opin Chem Biol 4 184 191 10.1016/S1367-5931(99)00073-3 1:CAS:528:DC%2BD3cXisVaiu7s%3D 10742195 (Pubitemid 30189310)
    • (2000) Current Opinion in Chemical Biology , vol.4 , Issue.2 , pp. 184-191
    • Bush, A.I.1
  • 14
    • 33744748011 scopus 로고    scopus 로고
    • Aggregation/fibrillogenesis of recombinant human prion protein and Gerstmann-Straussler-Scheinker disease peptides in the presence of metal ions
    • DOI 10.1021/bi0601454
    • F Ricchelli R Buggio D Drago M Salmona G Forloni A Negro G Togon P Zatta 2006 Biochemistry 45 6724 6732 10.1021/bi0601454 1:CAS:528:DC%2BD28XktVyrtL0%3D 16716083 (Pubitemid 43825373)
    • (2006) Biochemistry , vol.45 , Issue.21 , pp. 6724-6732
    • Ricchelli, F.1    Buggio, R.2    Drago, D.3    Salmona, M.4    Forloni, G.5    Negro, A.6    Tognon, G.7    Zatta, P.8
  • 16
    • 0035941201 scopus 로고    scopus 로고
    • 10.1074/jbc.M105343200 1:CAS:528:DC%2BD3MXos12nurw%3D 11553618
    • VN Uversky J Li AL Fink 2001 J Biol Chem 276 44284 44296 10.1074/jbc.M105343200 1:CAS:528:DC%2BD3MXos12nurw%3D 11553618
    • (2001) J Biol Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 17
    • 0014109212 scopus 로고
    • 10.1021/bi00859a010 1:CAS:528:DyaF2sXksFSqtbg%3D 6049437
    • H Edelhoch 1967 Biochemistry 6 1948 1954 10.1021/bi00859a010 1:CAS:528:DyaF2sXksFSqtbg%3D 6049437
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 18
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin. Even an ordinary globular protein can assume a rogue guise if conditions are right
    • DOI 10.1038/35065514
    • M Fandrich MA Fletcher CM Dobson 2001 Nature 410 165 166 10.1038/35065514 1:CAS:528:DC%2BD3MXitVyktb4%3D 11242064 (Pubitemid 32216577)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 20
    • 70449523929 scopus 로고
    • Heyden and Sons, London
    • Clark RJH, Hester RE (1975) vol 1, Heyden and Sons, London, pp 35-97
    • (1975) , vol.1 , pp. 35-97
    • Clark, R.J.H.1    Hester, R.E.2
  • 22
    • 0022503458 scopus 로고
    • 10.1016/0076-6879(86)30016-8
    • A Williams 1985 Methods Enzymol 130 311 331 10.1016/0076-6879(86)30016-8
    • (1985) Methods Enzymol , vol.130 , pp. 311-331
    • Williams, A.1
  • 24
    • 0017491293 scopus 로고
    • 10.1366/000370277774463706 1:CAS:528:DyaE2sXktFynsLs%3D
    • RC Lord 1977 Appl Spectrosc 31 187 194 10.1366/000370277774463706 1:CAS:528:DyaE2sXktFynsLs%3D
    • (1977) Appl Spectrosc , vol.31 , pp. 187-194
    • Lord, R.C.1
  • 25
    • 0041563693 scopus 로고    scopus 로고
    • Domain architecture of the polyglutamine protein ataxin-3: A globular domain followed by a flexible tail
    • DOI 10.1016/S0014-5793(03)00748-8
    • L Masino V Musi RP Menon P Fusi G Kelly TA Frenkiel Y Trottier A Pastore 2003 FEBS Lett 549 21 25 10.1016/S0014-5793(03)00748-8 1:CAS:528: DC%2BD3sXmt1Gqsr0%3D 12914917 (Pubitemid 36959836)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 21-25
    • Masino, L.1    Musi, V.2    Menon, R.P.3    Fusi, P.4    Kelly, G.5    Frenkiel, T.A.6    Trottier, Y.7    Pastore, A.8
  • 26
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in ataxin-3 does not affect protein stability: Implications for misfolding and disease
    • DOI 10.1074/jbc.M405799200
    • MKM Chow AM Ellisdon LD Cabrita SP Bottomley 2004 J Biol Chem 279 47643 47651 10.1074/jbc.M405799200 1:CAS:528:DC%2BD2cXptl2gurg%3D 15345714 (Pubitemid 39540910)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47643-47651
    • Chow, M.K.M.1    Ellisdon, A.M.2    Cabrita, L.D.3    Bottomley, S.P.4
  • 27
    • 34147152672 scopus 로고    scopus 로고
    • Protein secondary structure and orientation in silk as revealed by Raman spectromicroscopy
    • DOI 10.1529/biophysj.106.100339
    • T Lefevre M-E Rousseau M Pezolet 2007 Biophys J 92 2885 2895 10.1529/biophysj.106.100339 1:CAS:528:DC%2BD2sXkt1Cnsrg%3D 17277183 (Pubitemid 46557862)
    • (2007) Biophysical Journal , vol.92 , Issue.8 , pp. 2885-2895
    • Lefevre, T.1    Rousseau, M.-E.2    Pezolet, M.3
  • 29
    • 1342331870 scopus 로고    scopus 로고
    • The peculiar nature of unfolding of the human prion protein
    • DOI 10.1110/ps.03457204
    • IV Baskakov G Leganme Z Gryczynski SB Prusiner 2004 Protein Sci 13 586 595 10.1110/ps.03457204 1:CAS:528:DC%2BD2cXhvVCmt7Y%3D 14767078 (Pubitemid 38252555)
    • (2004) Protein Science , vol.13 , Issue.3 , pp. 586-595
    • Baskakov, I.V.1    Legname, G.2    Gryczynski, Z.3    Prusiner, S.B.4
  • 31
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • DOI 10.1016/S0076-6879(99)09020-5
    • H LeVine 3rd 1999 Methods Enzymol 309 274 284 10.1016/S0076-6879(99) 09020-5 1:CAS:528:DC%2BD3cXksVKhuw%3D%3D 10507030 (Pubitemid 29446455)
    • (1999) Methods in Enzymology , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 33
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • DOI 10.1074/jbc.M601470200
    • AM Ellisdon B Thomas SP Bottomley 2006 J Biol Chem 281 16888 16896 10.1074/jbc.M601470200 1:CAS:528:DC%2BD28XlvVGksro%3D 16624810 (Pubitemid 43909491)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.25 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 35
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • JT Jarrett PT Lansbury Jr 1993 Cell 73 1055 1058 10.1016/0092-8674(93) 90635-4 1:CAS:528:DyaK3sXksVKnsL8%3D 8513491 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 36
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • DOI 10.1021/bi00164a008
    • JT Jarrett PT Lansbury Jr 1992 Biochemistry 31 12345 12352 10.1021/bi00164a008 1:CAS:528:DyaK38XmsV2msL4%3D 1463722 (Pubitemid 23163109)
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 39
    • 0021095444 scopus 로고
    • 10.1016/S0022-2836(83)80285-X 1:CAS:528:DyaL3sXks1Kqu7s%3D 6864791
    • A Williams 1983 J Mol Biol 166 581 603 10.1016/S0022-2836(83)80285-X 1:CAS:528:DyaL3sXks1Kqu7s%3D 6864791
    • (1983) J Mol Biol , vol.166 , pp. 581-603
    • Williams, A.1
  • 40
    • 0032478198 scopus 로고    scopus 로고
    • Uv resonance raman-selective amide vibrational enhancement: Quantitative methodology for determining protein secondary structure
    • DOI 10.1021/bi971160z
    • Z Chi XG Chen JS Holtz SA Asher 1998 Biochemistry 37 2854 2864 10.1021/bi971160z 1:CAS:528:DyaK1cXhsVektb4%3D 9485436 (Pubitemid 28145738)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 2854-2864
    • Chi, Z.1    Chen, X.G.2    Holtz, J.S.W.3    Asher, S.A.4
  • 41
    • 33749635854 scopus 로고    scopus 로고
    • Contribution of transition dipole coupling to amide coupling in IR spectra of peptide secondary structures
    • DOI 10.1016/j.vibspec.2006.04.003, PII S0924203106000592
    • J Kubelka J Kim P Bour TA Keiderling 2006 Vib Spectrosc 42 63 73 10.1016/j.vibspec.2006.04.003 1:CAS:528:DC%2BD28XhtVOrtL7I (Pubitemid 44540394)
    • (2006) Vibrational Spectroscopy , vol.42 , Issue.1 , pp. 63-73
    • Kubelka, J.1    Kim, J.2    Bour, P.3    Keiderling, T.A.4
  • 42
    • 0023910427 scopus 로고
    • 1:CAS:528:DyaL1cXhs1emt74%3D 3346247
    • SV Evans GD Brayer 1988 J Biol Chem 263 4263 4269 1:CAS:528: DyaL1cXhs1emt74%3D 3346247
    • (1988) J Biol Chem , vol.263 , pp. 4263-4269
    • Evans, S.V.1    Brayer, G.D.2
  • 44
    • 0042658237 scopus 로고    scopus 로고
    • The prion protein and neuronal zinc homeostasis
    • DOI 10.1016/S0968-0004(03)00166-X
    • NT Watt NM Hooper 2003 Trends Biochem Sci 28 406 410 10.1016/S0968- 0004(03)00166-X 1:CAS:528:DC%2BD3sXmsVGqsL0%3D 12932728 (Pubitemid 36976742)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.8 , pp. 406-410
    • Watt, N.T.1    Hooper, N.M.2
  • 47
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes
    • DOI 10.1021/bi0002479
    • T Miura K Suzuki N Kohata H Takeuchi 2000 Biochemistry 39 7024 7031 10.1021/bi0002479 1:CAS:528:DC%2BD3cXjt1emsLY%3D 10841784 (Pubitemid 30390396)
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 48
    • 0035895830 scopus 로고    scopus 로고
    • +3) and zinc in the hippocampus
    • DOI 10.1016/S0006-8993(00)03195-4, PII S0006899300031954
    • C Armstrong W Leong GJ Lees 2001 Brain Res 892 51 62 10.1016/S0006- 8993(00)03195-4 1:CAS:528:DC%2BD3MXhtFSlsrc%3D 11172748 (Pubitemid 32126566)
    • (2001) Brain Research , vol.892 , Issue.1 , pp. 51-62
    • Armstrong, C.1    Leong, W.2    Lees, G.J.3
  • 50
    • 0015913994 scopus 로고
    • 10.1126/science.180.4085.511 1:CAS:528:DyaE3sXhsFOmtbc%3D 4735595
    • DR Crapper SS Krishnan AJ Dalton 1973 Science 180 511 513 10.1126/science.180.4085.511 1:CAS:528:DyaE3sXhsFOmtbc%3D 4735595
    • (1973) Science , vol.180 , pp. 511-513
    • Crapper, D.R.1    Krishnan, S.S.2    Dalton, A.J.3
  • 51
    • 0345118103 scopus 로고    scopus 로고
    • Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: A model for misfolding in polyglutamine disease
    • DOI 10.1016/j.jmb.2003.08.064
    • MKM Chow HL Paulson SP Bottomley 2004 J Mol Biol 335 333 341 10.1016/j.jmb.2003.08.064 1:CAS:528:DC%2BD3sXpsVSnsrg%3D 14659761 (Pubitemid 37494983)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.1 , pp. 333-341
    • Chow, M.K.M.1    Paulson, H.L.2    Bottomley, S.P.3
  • 52
    • 0002737588 scopus 로고
    • 10.1063/1.1700199 1:CAS:528:DyaG38XjvVeksA%3D%3D
    • M Kasha 1952 J Chem Phys 20 71 74 10.1063/1.1700199 1:CAS:528: DyaG38XjvVeksA%3D%3D
    • (1952) J Chem Phys , vol.20 , pp. 71-74
    • Kasha, M.1
  • 53
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1'-bis(4-anilino-5- naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • DOI 10.1021/bi00190a006
    • L Shi DR Palleros AL Fink 1994 Biochemistry 33 7536 7546 10.1021/bi00190a006 1:CAS:528:DyaK2cXksFalsbY%3D 8011619 (Pubitemid 24230577)
    • (1994) Biochemistry , vol.33 , Issue.24 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 54
    • 0024963570 scopus 로고
    • 10.1021/bi00429a004 1:CAS:528:DyaL1MXntFOrtA%3D%3D 2496758
    • Y Goto AL Fink 1989 Biochemistry 28 945 952 10.1021/bi00429a004 1:CAS:528:DyaL1MXntFOrtA%3D%3D 2496758
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 58
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • DOI 10.1016/S0014-5793(01)02486-3, PII S0014579301024863
    • C Soto 2001 FEBS Lett 498 204 207 10.1016/S0014-5793(01)02486-3 1:CAS:528:DC%2BD3MXksVGksr4%3D 11412858 (Pubitemid 32539204)
    • (2001) FEBS Letters , vol.498 , Issue.2-3 , pp. 204-207
    • Soto, C.1
  • 61
    • 0033584895 scopus 로고    scopus 로고
    • 10.1016/S0166-1280(99)00119-0 1:CAS:528:DyaK1MXntVOrsb4%3D
    • BJ Smith R Liu 1999 J Mol Struct (Theochem) 491 211 222 10.1016/S0166-1280(99)00119-0 1:CAS:528:DyaK1MXntVOrsb4%3D
    • (1999) J Mol Struct (Theochem) , vol.491 , pp. 211-222
    • Smith, B.J.1    Liu, R.2
  • 63
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • CM Dobson 1999 Trends Biochem Sci 24 329 332 10.1016/S0968-0004(99)01445- 0 1:CAS:528:DyaK1MXls1ygtLg%3D 10470028 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.