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Volumn 1349, Issue , 2010, Pages 90-96

Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease

Author keywords

endoplasmic reticulum stress; misfolded protein; tau

Indexed keywords

NITRIC OXIDE; PROTEIN DISULFIDE ISOMERASE;

EID: 77955653927     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2010.06.016     Document Type: Article
Times cited : (65)

References (36)
  • 1
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • A.D. Alonso, I. Grundke-Iqbal, H.S. Barra, and K. Iqbal Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau Proc. Natl. Acad. Sci. U. S. A. 94 1997 298 303
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 298-303
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Barra, H.S.3    Iqbal, K.4
  • 2
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • A.C. Alonso, B. Li, I. Grundke-Iqbal, and K. Iqbal Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity Proc. Natl. Acad. Sci. U. S. A. 103 2006 8864 8869
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8864-8869
    • Alonso, A.C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 3
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • J.D. Atkin, M.A. Farg, A.K. Walker, C. McLean, D. Tomas, and M.K. Horne Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis Neurobiol. Dis. 30 2008 400 407
    • (2008) Neurobiol. Dis. , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5    Horne, M.K.6
  • 4
    • 0029877684 scopus 로고    scopus 로고
    • Correlations between mental state and quantitative neuropathology in the Vienna Longitudinal Study on Dementia
    • C. Bancher, K. Jellinger, H. Lassmann, P. Fischer, and F. Leblhuber Correlations between mental state and quantitative neuropathology in the Vienna Longitudinal Study on Dementia Eur. Arch. Psychiatry Clin. Neurosci. 246 1996 137 146
    • (1996) Eur. Arch. Psychiatry Clin. Neurosci. , vol.246 , pp. 137-146
    • Bancher, C.1    Jellinger, K.2    Lassmann, H.3    Fischer, P.4    Leblhuber, F.5
  • 5
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • H. Braak, and E. Braak Neuropathological stageing of Alzheimer-related changes Acta Neuropathol. 82 1991 239 259
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 6
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • D.H. Cho, T. Nakamura, J. Fang, P. Cieplak, A. Godzik, Z. Gu, and S.A. Lipton S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury Science 324 2009 102 105
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 10
    • 0033501744 scopus 로고    scopus 로고
    • Behavioral disturbances in transgenic mice overexpressing the V717F beta-amyloid precursor protein
    • J.C. Dodart, H. Meziane, C. Mathis, K.R. Bales, S.M. Paul, and A. Ungerer Behavioral disturbances in transgenic mice overexpressing the V717F beta-amyloid precursor protein Behav. Neurosci. 113 1999 982 990
    • (1999) Behav. Neurosci. , vol.113 , pp. 982-990
    • Dodart, J.C.1    Meziane, H.2    Mathis, C.3    Bales, K.R.4    Paul, S.M.5    Ungerer, A.6
  • 11
    • 0035031135 scopus 로고    scopus 로고
    • Parkinson's disease and other alpha-synucleinopathies
    • M. Goedert Parkinson's disease and other alpha-synucleinopathies Clin. Chem. Lab. Med. 39 2001 308 312
    • (2001) Clin. Chem. Lab. Med. , vol.39 , pp. 308-312
    • Goedert, M.1
  • 12
    • 0038326624 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment
    • A.L. Guillozet, S. Weintraub, D.C. Mash, and M.M. Mesulam Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment Arch. Neurol. 60 2003 729 736
    • (2003) Arch. Neurol. , vol.60 , pp. 729-736
    • Guillozet, A.L.1    Weintraub, S.2    Mash, D.C.3    Mesulam, M.M.4
  • 14
    • 0035104180 scopus 로고    scopus 로고
    • P39 immunoreactivity in glial cytoplasmic inclusions in brains with multiple system atrophy
    • Y. Honjyo, Y. Kawamoto, S. Nakamura, S. Nakano, and I. Akiguchi P39 immunoreactivity in glial cytoplasmic inclusions in brains with multiple system atrophy Acta Neuropathol. 101 2001 190 194
    • (2001) Acta Neuropathol. , vol.101 , pp. 190-194
    • Honjyo, Y.1    Kawamoto, Y.2    Nakamura, S.3    Nakano, S.4    Akiguchi, I.5
  • 15
    • 33846781122 scopus 로고    scopus 로고
    • Accumulation of Hsc70 and Hsp70 in glial cytoplasmic inclusions in patients with multiple system atrophy
    • Y. Kawamoto, I. Akiguchi, Y. Shirakashi, Y. Honjo, H. Tomimoto, R. Takahashi, and H. Budka Accumulation of Hsc70 and Hsp70 in glial cytoplasmic inclusions in patients with multiple system atrophy Brain Res. 1136 2007 219 227
    • (2007) Brain Res. , vol.1136 , pp. 219-227
    • Kawamoto, Y.1    Akiguchi, I.2    Shirakashi, Y.3    Honjo, Y.4    Tomimoto, H.5    Takahashi, R.6    Budka, H.7
  • 18
    • 2942720981 scopus 로고    scopus 로고
    • Functional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins
    • T. Kimura, A. Nishida, N. Ohara, D. Yamagishi, T. Horibe, and M. Kikuchi Functional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins Biochem. J. 382 2004 169 176
    • (2004) Biochem. J. , vol.382 , pp. 169-176
    • Kimura, T.1    Nishida, A.2    Ohara, N.3    Yamagishi, D.4    Horibe, T.5    Kikuchi, M.6
  • 21
    • 0033969730 scopus 로고    scopus 로고
    • Involvement of alpha-synuclein in Parkinson's disease and other neurodegenerative disorders
    • R. Krüger, T. Müller, and O. Riess Involvement of alpha-synuclein in Parkinson's disease and other neurodegenerative disorders J. Neural Transm. 107 2000 31 40
    • (2000) J. Neural Transm. , vol.107 , pp. 31-40
    • Krüger, R.1    Müller, T.2    Riess, O.3
  • 22
    • 0024836809 scopus 로고
    • Dystrophic neuropeptidergic neurites in senile plaques of Alzheimer's disease precede formation of paired helical filaments
    • M.B. Lenders, M.C. Peers, G. Tramu, A. Delacourte, A. Defossez, H. Petit, and M. Mazzuca Dystrophic neuropeptidergic neurites in senile plaques of Alzheimer's disease precede formation of paired helical filaments Acta Neurol. Belg. 89 1989 279 285 (Pubitemid 20317825)
    • (1989) Acta Psychiatrica Belgica , vol.89 , Issue.3-4 , pp. 279-285
    • Lenders, M.B.1    Peers, M.C.2    Tramu, G.3    Delacourte, A.4    Defossez, A.5    Petit, H.6    Mazzuca, M.7
  • 24
    • 34447506680 scopus 로고    scopus 로고
    • Transgenic mice with human mutant genes causing Parkinson's disease and amyotrophic lateral sclerosis provide common insight into mechanisms of motor neuron selective vulnerability to degeneration
    • L.J. Martin Transgenic mice with human mutant genes causing Parkinson's disease and amyotrophic lateral sclerosis provide common insight into mechanisms of motor neuron selective vulnerability to degeneration Rev. Neurosci. 18 2007 115 136
    • (2007) Rev. Neurosci. , vol.18 , pp. 115-136
    • Martin, L.J.1
  • 25
    • 0029813177 scopus 로고    scopus 로고
    • Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F beta-amyloid precursor protein and Alzheimer's disease
    • E. Masliah, A. Sisk, M. Mallory, L. Mucke, D. Schenk, and D. Games Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F beta-amyloid precursor protein and Alzheimer's disease J. Neurosci. 16 1996 5795 5811
    • (1996) J. Neurosci. , vol.16 , pp. 5795-5811
    • Masliah, E.1    Sisk, A.2    Mallory, M.3    Mucke, L.4    Schenk, D.5    Games, D.6
  • 26
    • 0037010285 scopus 로고    scopus 로고
    • Alzheimer's disease: Beta-Amyloid protein and tau
    • M. Morishima-Kawashima, and Y. Ihara Alzheimer's disease: beta-Amyloid protein and tau J. Neurosci. Res. 70 2002 392 401
    • (2002) J. Neurosci. Res. , vol.70 , pp. 392-401
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 27
    • 62449244004 scopus 로고    scopus 로고
    • Cell death: Protein misfolding and neurodegenerative diseases
    • T. Nakamura, and S.A. Lipton Cell death: protein misfolding and neurodegenerative diseases Apoptosis 14 2009 455 468
    • (2009) Apoptosis , vol.14 , pp. 455-468
    • Nakamura, T.1    Lipton, S.A.2
  • 28
    • 0026731788 scopus 로고
    • Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum
    • R. Noiva, and W.J. Lennarz Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum J. Biol. Chem. 267 1992 3553 3556
    • (1992) J. Biol. Chem. , vol.267 , pp. 3553-3556
    • Noiva, R.1    Lennarz, W.J.2
  • 30
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • B. Tsai, C. Rodighiero, W.I. Lencer, and T.A. Rapoport Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin Cell 104 2001 937 948
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 31
    • 0034920989 scopus 로고    scopus 로고
    • Evolution from pretangle neurons to neurofibrillary tangles monitored by thiazin red combined with Gallyas method and double immunofluorescence
    • T. Uchihara, A. Nakamura, M. Yamazaki, and O. Mori Evolution from pretangle neurons to neurofibrillary tangles monitored by thiazin red combined with Gallyas method and double immunofluorescence Acta Neuropathol. 101 2001 535 539 (Pubitemid 32684750)
    • (2001) Acta Neuropathologica , vol.101 , Issue.6 , pp. 535-539
    • Uchihara, T.1    Nakamura, A.2    Yamazaki, M.3    Mori, O.4
  • 32
  • 34
    • 74249084267 scopus 로고    scopus 로고
    • Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis
    • A.K. Walker, M.A. Farg, C.R. Bye, C.A. McLean, M.K. Horne, and J.D. Atkin Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis Brain 133 2010 105 116
    • (2010) Brain , vol.133 , pp. 105-116
    • Walker, A.K.1    Farg, M.A.2    Bye, C.R.3    McLean, C.A.4    Horne, M.K.5    Atkin, J.D.6
  • 35
    • 54249100481 scopus 로고    scopus 로고
    • TDP-43: An emerging new player in neurodegenerative diseases
    • I.F. Wang, L.S. Wu, and C.K. Shen TDP-43: an emerging new player in neurodegenerative diseases Trends Mol. Med. 14 2008 479 485
    • (2008) Trends Mol. Med. , vol.14 , pp. 479-485
    • Wang, I.F.1    Wu, L.S.2    Shen, C.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.