메뉴 건너뛰기




Volumn 566, Issue , 2009, Pages 109-121

Proteomic analysis of protein phosphorylation and ubiquitination in Alzheimer's disease

Author keywords

Alzheimer's disease (AD); Liquid chromatography tandem mass spectrometry (LC MS MS); Phosphorylation; Selected reaction monitoring (SRM); Tau; Ubiquitin

Indexed keywords

PROTEOME; TAU PROTEIN;

EID: 77449137513     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-562-6_8     Document Type: Article
Times cited : (23)

References (29)
  • 1
    • 0035188745 scopus 로고    scopus 로고
    • N-Methyl-daspartate receptor subunit proteins and their phosphorylation status are altered selectively in Alzheimer's disease
    • Sze C, Bi H, Kleinschmidt-DeMasters BK, Filley CM, Martin LJ. (2001) N-Methyl-daspartate receptor subunit proteins and their phosphorylation status are altered selectively in Alzheimer's disease. J Neurol Sci 182, 151-159.
    • (2001) J Neurol Sci , vol.182 , pp. 151-159
    • Sze, C.1    Bi, H.2    Kleinschmidt-DeMasters, B.K.3    Filley, C.M.4    Martin, L.J.5
  • 2
    • 14844315768 scopus 로고    scopus 로고
    • Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation
    • Zhao D, Watson JB, Xie CW. (2004) Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation. J Neurophysiol 92, 2853-2858.
    • (2004) J Neurophysiol , vol.92 , pp. 2853-2858
    • Zhao, D.1    Watson, J.B.2    Xie, C.W.3
  • 3
    • 27144530643 scopus 로고    scopus 로고
    • Vulnerability of dentate granule cells to disruption of arc expression in human amyloid precursor protein transgenic mice
    • Palop JJ, Chin J, Bien-Ly N, et al. (2005) Vulnerability of dentate granule cells to disruption of arc expression in human amyloid precursor protein transgenic mice. J Neurosci 25, 9686-9693.
    • (2005) J Neurosci , vol.25 , pp. 9686-9693
    • Palop, J.J.1    Chin, J.2    Bien-Ly, N.3
  • 4
    • 0028210962 scopus 로고
    • Abnormally phosphorylated tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat
    • Braak H, Braak E, Strothjohann M. (1994) Abnormally phosphorylated tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat. Neurosci Lett 171, 1-4.
    • (1994) Neurosci Lett , vol.171 , pp. 1-4
    • Braak, H.1    Braak, E.2    Strothjohann, M.3
  • 5
    • 10944246574 scopus 로고    scopus 로고
    • Pinning down phosphorylated tau and tauopathies
    • Lim J, Lu KP. (2005) Pinning down phosphorylated tau and tauopathies. Biochim Biophys Acta 1739, 311-322.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 311-322
    • Lim, J.1    Lu, K.P.2
  • 6
    • 18544390506 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein in Alzheimer's disease
    • Gong CX, Liu F, Grundke-Iqbal I, Iqbal K. (2005) Post-translational modifications of tau protein in Alzheimer's disease. J Neural Transm 112, 813-838.
    • (2005) J Neural Transm , vol.112 , pp. 813-838
    • Gong, C.X.1    Liu, F.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 7
    • 12144288564 scopus 로고    scopus 로고
    • Phosphorylation of tau by fyn: Implications for Alzheimer's disease
    • Lee G, Thangavel R, Sharma VM, et al. (2004) Phosphorylation of tau by fyn: Implications for Alzheimer's disease. J Neurosci 24, 2304-2312.
    • (2004) J Neurosci , vol.24 , pp. 2304-2312
    • Lee, G.1    Thangavel, R.2    Sharma, V.M.3
  • 8
    • 0345096631 scopus 로고    scopus 로고
    • Phosphorylation of tau protein to sites found in Alzheimer's disease brain is catalyzed by Ca2+/calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry
    • Yoshimura Y, Ichinose T, Yamauchi T. (2003) Phosphorylation of tau protein to sites found in Alzheimer's disease brain is catalyzed by Ca2+/calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry. Neurosci Lett 353, 185-188.
    • (2003) Neurosci Lett , vol.353 , pp. 185-188
    • Yoshimura, Y.1    Ichinose, T.2    Yamauchi, T.3
  • 9
    • 0037070224 scopus 로고    scopus 로고
    • Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease
    • Liu F, Zaidi T, Iqbal K, et al. (2002) Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease. FEBS Lett 512, 101-106.
    • (2002) FEBS Lett , vol.512 , pp. 101-106
    • Liu, F.1    Zaidi, T.2    Iqbal, K.3
  • 11
    • 0029917884 scopus 로고    scopus 로고
    • Regulation of tau phosphorylation in Alzheimer's disease
    • Lee VM. (1996) Regulation of tau phosphorylation in Alzheimer's disease. Ann N Y Acad Sci 777, 107-113.
    • (1996) Ann N Y Acad Sci , vol.777 , pp. 107-113
    • Lee, V.M.1
  • 12
    • 0028090656 scopus 로고
    • Abnormally phosphorylated tau protein in Alzheimer's disease: Heterogeneity of individual regional distribution and relationship to clinical severity
    • Holzer M, Holzapfel HP, Zedlick D, Bruckner MK, Arendt T. (1994) Abnormally phosphorylated tau protein in Alzheimer's disease: Heterogeneity of individual regional distribution and relationship to clinical severity. Neuroscience 63, 499-516.
    • (1994) Neuroscience , vol.63 , pp. 499-516
    • Holzer, M.1    Holzapfel, H.P.2    Zedlick, D.3    Bruckner, M.K.4    Arendt, T.5
  • 13
    • 0027420369 scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • Goedert M. (1993) Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci 16, 460-465.
    • (1993) Trends Neurosci , vol.16 , pp. 460-465
    • Goedert, M.1
  • 14
    • 20844432024 scopus 로고    scopus 로고
    • Correlation of cerebrospinal fluid levels of tau protein phosphorylated at threonine 231 with rates of hippocampal atrophy in Alzheimer disease
    • Hampel H, Burger K, Pruessner JC, et al. (2005) Correlation of cerebrospinal fluid levels of tau protein phosphorylated at threonine 231 with rates of hippocampal atrophy in Alzheimer disease. Arch Neurol 62, 770-773.
    • (2005) Arch Neurol , vol.62 , pp. 770-773
    • Hampel, H.1    Burger, K.2    Pruessner, J.C.3
  • 15
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack JC, Schneider A, Mandelkow EM, Hyman BT. (2002) Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol (Berl) 103, 26-35.
    • (2002) Acta Neuropathol (Berl) , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 16
    • 9744222883 scopus 로고    scopus 로고
    • Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
    • de Vrij FM, Fischer DF, van Leeuwen FW, Hol EM. (2004) Protein quality control in Alzheimer's disease by the ubiquitin proteasome system. Prog Neurobiol 74, 249-270.
    • (2004) Prog Neurobiol , vol.74 , pp. 249-270
    • De Vrij, F.M.1    Fischer, D.F.2    Van Leeuwen, F.W.3    Hol, E.M.4
  • 17
    • 17644416738 scopus 로고    scopus 로고
    • Microtubule-associated protein tau is a substrate of ATP/Mg(2+)-dependent proteasome protease system
    • Zhang JY, Liu SJ, Li HL, Wang JZ. (2005) Microtubule-associated protein tau is a substrate of ATP/Mg(2+)-dependent proteasome protease system. J Neural Transm 112, 547-555.
    • (2005) J Neural Transm , vol.112 , pp. 547-555
    • Zhang, J.Y.1    Liu, S.J.2    Li, H.L.3    Wang, J.Z.4
  • 18
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H, Schwartz D, Gygi SP, Kosik KS. (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J Biol Chem 279, 4869-4876.
    • (2004) J Biol Chem , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 19
    • 0026298636 scopus 로고
    • Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease
    • Iqbal K, Grundke-Iqbal I. (1991) Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease. Mol Neurobiol 5, 399-410.
    • (1991) Mol Neurobiol , vol.5 , pp. 399-410
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 20
    • 0034733918 scopus 로고    scopus 로고
    • Detection of tau phosphorylated at threonine 231 in cerebrospinal fluid of Alzheimer's disease patients
    • Kohnken R, Buerger K, Zinkowski R, et al. (2000) Detection of tau phosphorylated at threonine 231 in cerebrospinal fluid of Alzheimer's disease patients. Neurosci Lett 287, 187-190.
    • (2000) Neurosci Lett , vol.287 , pp. 187-190
    • Kohnken, R.1    Buerger, K.2    Zinkowski, R.3
  • 21
    • 0035066999 scopus 로고    scopus 로고
    • Tracking of Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231
    • Hampel H, Buerger K, Kohnken R, et al. (2001) Tracking of Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231. Ann Neurol 49, 545-546.
    • (2001) Ann Neurol , vol.49 , pp. 545-546
    • Hampel, H.1    Buerger, K.2    Kohnken, R.3
  • 22
    • 0037183481 scopus 로고    scopus 로고
    • CSF tau protein phosphorylated at threonine 231 correlates with cognitive decline in MCI subjects
    • Buerger K, Teipel SJ, Zinkowski R, et al. (2002) CSF tau protein phosphorylated at threonine 231 correlates with cognitive decline in MCI subjects. Neurology 59, 627-629.
    • (2002) Neurology , vol.59 , pp. 627-629
    • Buerger, K.1    Teipel, S.J.2    Zinkowski, R.3
  • 23
    • 0036338203 scopus 로고    scopus 로고
    • Differential diagnosis of Alzheimer disease with cerebrospinal fluid levels of tau protein phosphorylated at threonine 231
    • Buerger K, Zinkowski R, Teipel SJ, et al. (2002) Differential diagnosis of Alzheimer disease with cerebrospinal fluid levels of tau protein phosphorylated at threonine 231. Arch Neurol 59, 1267-1272.
    • (2002) Arch Neurol , vol.59 , pp. 1267-1272
    • Buerger, K.1    Zinkowski, R.2    Teipel, S.J.3
  • 24
    • 33744950091 scopus 로고    scopus 로고
    • Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation
    • Cripps D, Thomas SN, Jeng Y, et al. (2006) Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. J Biol Chem 281, 10825-10838.
    • (2006) J Biol Chem , vol.281 , pp. 10825-10838
    • Cripps, D.1    Thomas, S.N.2    Jeng, Y.3
  • 25
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer's disease
    • Weaver CL, Espinoza M, Kress Y, Davies P. (2000) Conformational change as one of the earliest alterations of tau in Alzheimer's disease. Neurobiol Aging 21, 719-727.
    • (2000) Neurobiol Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 26
    • 0031685160 scopus 로고    scopus 로고
    • Mitotic phosphoepitopes precede paired helical filaments in Alzheimer's disease
    • Vincent I, Zheng JH, Dickson DW, Kress Y, Davies P. (1998) Mitotic phosphoepitopes precede paired helical filaments in Alzheimer's disease. Neurobiol Aging 19, 287-296.
    • (1998) Neurobiol Aging , vol.19 , pp. 287-296
    • Vincent, I.1    Zheng, J.H.2    Dickson, D.W.3    Kress, Y.4    Davies, P.5
  • 27
    • 14944346000 scopus 로고    scopus 로고
    • Systematic comparison of a two-dimensional ion trap and a three-dimensional ion trap mass spectrometer in proteomics
    • Mayya V, Rezaul K, Cong YS, Han D. (2005) Systematic comparison of a two-dimensional ion trap and a three-dimensional ion trap mass spectrometer in proteomics. Mol Cell Proteomics 4, 214-223.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 214-223
    • Mayya, V.1    Rezaul, K.2    Cong, Y.S.3    Han, D.4
  • 28
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 100, 6940-6945.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 29
    • 34547232157 scopus 로고    scopus 로고
    • Optimization of mass spectrometry-compatible surfactants for shotgun proteomics
    • Chen EI, Cociorva D, Norris JL, Yates JR, III. (2007) Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. J Proteome Res 6, 2529-2538.
    • (2007) J Proteome Res , vol.6 , pp. 2529-2538
    • Chen, E.I.1    Cociorva, D.2    Norris, J.L.3    Yates III, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.