메뉴 건너뛰기




Volumn 25, Issue 2, 2012, Pages 361-372

Cooperative folding of tau peptide by coordination of group IIB metal cations during heparin-induced aggregation

Author keywords

Aggregation; Conformation; Coordination; Group IIB metals; Tau protein

Indexed keywords

CADMIUM; CYSTEINE; HEPARIN; MERCURY; MICROTUBULE PROTEIN; MUTANT PROTEIN; PEPTIDE; PEPTIDE R2; POLYANION; PROTEIN C291A; TAU PROTEIN; THIOL GROUP; UNCLASSIFIED DRUG; ZINC;

EID: 84862767745     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-011-9505-7     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0021287299 scopus 로고
    • 2+ from brain tissue during activity
    • Assaf SY, Chung SH (1984) Release of endogenous Zn2+ from brain tissue during activity. Nature 308:734-736 (Pubitemid 14127670)
    • (1984) Nature , vol.308 , Issue.5961 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 2
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • DOI 10.1021/bi026469j
    • Barghorn S, Mandelkow E (2002) Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41:14885-14896 (Pubitemid 35470667)
    • (2002) Biochemistry , vol.41 , Issue.50 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 3
    • 33750185145 scopus 로고    scopus 로고
    • Spectroscopic approaches to the conformation of tau protein in solution and in paired helical filaments
    • DOI 10.1159/000095257
    • Bergen M, Barghorn S, Jeganathan S, Mandelkow EM, Mandelkow E (2006) Spectroscopic approaches to the conformation of tau protein in solution and in paired helical filaments. Neurodegenerative Dis 3:197-206 (Pubitemid 44600305)
    • (2006) Neurodegenerative Diseases , vol.3 , Issue.4-5 , pp. 197-206
    • Von Bergen, M.1    Barghorn, S.2    Jeganathan, S.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 6
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • DOI 10.1074/jbc.271.51.32789
    • Carmel G, Mager EM, Binder LI, Kuret J (1996) The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J Biol Chem 271:32789-32795 (Pubitemid 27008707)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.51 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 7
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • DOI 10.1021/bi980537d
    • Friedhoff P, Schneider A, Mandelkow EM, Mandelkow E (1998) Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry 37: 10223-10230 (Pubitemid 28366378)
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.-M.3    Mandelkow, E.4
  • 9
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • DOI 10.1006/abio.1996.0084
    • Greenfield NJ (1996) Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal Biochem 235:1-10 (Pubitemid 26065191)
    • (1996) Analytical Biochemistry , vol.235 , Issue.1 , pp. 1-10
    • Greenfield, N.J.1
  • 11
    • 53349144370 scopus 로고    scopus 로고
    • The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments
    • Jeganathan S, von Bergen M, Mandelkow EM, Mandelkow E (2008) The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments. Biochemistry 47:10526-10539
    • (2008) Biochemistry , vol.47 , pp. 10526-10539
    • Jeganathan, S.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 12
    • 36249000541 scopus 로고    scopus 로고
    • Impacts of Cd(II) on the conformation and self-aggregation of Alzheimer's tau fragment corresponding to the third repeat of microtubule-binding domain
    • DOI 10.1016/j.bbapap.2007.08.014, PII S1570963907002026
    • Jiang LF, Yao TM, Zhu ZL, Wang C, Ji LN (2007) Impacts of Cd(II) on the conformation and self-aggregation of Alzheimer's tau fragment corresponding to the third repeat of microtubule-binding domain. Biochim Biophys Acta 1774:1414-1421 (Pubitemid 350123204)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.11 , pp. 1414-1421
    • Jiang, L.-F.1    Yao, T.-M.2    Zhu, Z.-L.3    Wang, C.4    Ji, L.-N.5
  • 13
    • 0034954474 scopus 로고    scopus 로고
    • Gradual micronutrient accumulation and depletion in Alzheimer's disease
    • DOI 10.1054/mehy.2000.1301
    • Johnson S (2001) Gradual micronutrient accumulation and depletion in Alzheimer's disease. Med Hypotheses 56: 595-597 (Pubitemid 32588204)
    • (2001) Medical Hypotheses , vol.56 , Issue.6 , pp. 595-597
    • Johnson, S.1
  • 17
    • 0842265772 scopus 로고    scopus 로고
    • Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain
    • DOI 10.1046/j.1432-1033.2003.03956.x
    • Minoura K, Yao TM, Tomoo K, Sumida M, Sasaki M, Taniguchi T, Ishida T (2004) Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain. Eur J Biochem 271:545-552 (Pubitemid 38183628)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.3 , pp. 545-552
    • Minoura, K.1    Yao, T.-M.2    Tomoo, K.3    Sumida, M.4    Sasaki, M.5    Taniguchi, T.6    Ishida, T.7
  • 18
    • 71749113077 scopus 로고    scopus 로고
    • Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322
    • Mo ZY, Zhu YZ, Zhu HL, Fan JB, Chen J, Liang Y (2009) Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322. J Biol Chem 284:34648-34657
    • (2009) J Biol Chem , vol.284 , pp. 34648-34657
    • Mo, Z.Y.1    Zhu, Y.Z.2    Zhu, H.L.3    Fan, J.B.4    Chen, J.5    Liang, Y.6
  • 19
    • 4544219703 scopus 로고    scopus 로고
    • Alzheimer disease: Mercury as pathogenetic factor and apolipoprotein E as a moderator
    • Mutter J, Naumann J, Sadaghiani C, Schneider R, Walach H (2004) Alzheimer disease: mercury as pathogenetic factor and apolipoprotein E as a moderator. Neuro Endocrinol Lett 25:331-339 (Pubitemid 39619299)
    • (2004) Neuroendocrinology Letters , vol.25 , Issue.5 , pp. 331-339
    • Mutter, J.1    Naumann, J.2    Sadaghiani, C.3    Schneider, R.4    Walach, H.5
  • 22
    • 70450255079 scopus 로고    scopus 로고
    • Thermodynamics of the complexation of Hg(II) by cysteinyl peptide ligands using isothermal titration calorimetry
    • Ngu-Schwemlein M, Merle JK, Healy P, Schwemlein S, Rhodes S (2009) Thermodynamics of the complexation of Hg(II) by cysteinyl peptide ligands using isothermal titration calorimetry. Thermochimica Acta 496:129-135
    • (2009) Thermochimica Acta , vol.496 , pp. 129-135
    • Ngu-Schwemlein, M.1    Merle, J.K.2    Healy, P.3    Schwemlein, S.4    Rhodes, S.5
  • 23
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • DOI 10.1046/j.1471-4159.2000.0740270.x
    • Sayre LM, Perry G, Harris PLR, Liu Y, Schubert KA, Smith MA (2000) In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J Neurochem 74:270-279 (Pubitemid 30012778)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.1 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.R.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 27
    • 28244439145 scopus 로고    scopus 로고
    • Possible role of each repeat structure of the microtubule-binding domain of the tau protein in in vitro aggregation
    • DOI 10.1093/jb/mvi142
    • Tomoo K, Yao TM, Minoura K, Hiraoka S, Sumida M, Taniguchi T, Ishida T (2005) Possible role of each repeat structure of the microtubule-binding domain of the tau protein in in vitro aggregation. J Biochem 138:413-423 (Pubitemid 41703693)
    • (2005) Journal of Biochemistry , vol.138 , Issue.4 , pp. 413-423
    • Tomoo, K.1    Yao, T.-M.2    Minoura, K.3    Hiraoka, S.4    Sumida, M.5    Taniguchi, T.6    Ishida, T.7
  • 28
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK 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 NK 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
  • 29
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H, Drewes G, Biernat J, Mandelkow EM, Mandelkow E (1992) Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 118:573-584
    • (1992) J Cell Biol , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 30
    • 40749117651 scopus 로고    scopus 로고
    • The environment, epigenetics and amyloidogenesis
    • DOI 10.1007/s12031-007-0009-4
    • Wu JF, Basha MR, Zawia NH (2008) The environment, epigenetics and amyloidogenesis. J Mol Neurosci 34:1-7 (Pubitemid 351378089)
    • (2008) Journal of Molecular Neuroscience , vol.34 , Issue.1 , pp. 1-7
    • Wu, J.1    Basha, Md.R.2    Zawia, N.H.3
  • 31
    • 0036724204 scopus 로고    scopus 로고
    • Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: Implications in the formation of neurofibrillary tangles of Alzheimer's disease
    • DOI 10.1046/j.1471-4159.2002.01061.x
    • Yamamoto A, Shin RW, Hasegawa K, Naiki H, Sato H, Yoshimasu F, Kitamoto T (2002) Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease. J Neurochem 82:1137-1147 (Pubitemid 34966626)
    • (2002) Journal of Neurochemistry , vol.82 , Issue.5 , pp. 1137-1147
    • Yamamoto, A.1    Shin, R.-W.2    Hasegawa, K.3    Naiki, H.4    Sato, H.5    Yoshimasu, F.6    Kitamoto, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.