메뉴 건너뛰기




Volumn 3, Issue 9, 1997, Pages 1021-1023

Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN;

EID: 0030769092     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0997-1021     Document Type: Article
Times cited : (446)

References (20)
  • 1
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters, C.L. et al. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl. Acad. Sci. USA 82, 4245-4249 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4245-4249
    • Masters, C.L.1
  • 2
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang, J. et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325, 733-736 (1987).
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1
  • 3
    • 0028322017 scopus 로고
    • 717) mutants
    • 717) mutants. Science 264, 1336-1340 (1994).
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1
  • 4
    • 0028169925 scopus 로고
    • Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ 42(43)
    • Iwatsubo, T. et al. Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ 42(43). Neuron 13, 45-53 (1994).
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1
  • 5
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T.E., Estus, S., Younkin, L.H., Selkoe, D.J. & Younkin, S.C. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255, 728-730 (1992).
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.C.5
  • 7
    • 0029935765 scopus 로고    scopus 로고
    • Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons
    • Simons, M. et al. Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons. J. Neurosci. 16, 899-908 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 899-908
    • Simons, M.1
  • 8
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M.R., Nilsson, T. & Peterson, P.A. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9, 3153-3162 (1990).
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 9
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki forest virus glycoproteins to the cell surface
    • Saraste, J. & Kuismanen, E. Pre-and post-Golgi vacuoles operate in the transport of Semliki forest virus glycoproteins to the cell surface. Cell 38, 535-549 (1984).
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 10
    • 0028987849 scopus 로고
    • Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
    • Higaki, J., Quon, D., Zhong, Z. & Cordell, B. Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. Neuron 14, 651-659 (1995).
    • (1995) Neuron , vol.14 , pp. 651-659
    • Higaki, J.1    Quon, D.2    Zhong, Z.3    Cordell, B.4
  • 11
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • Gabuzda, D., Busciglio, J., Chen, L.B., Masudaira, P. & Yankner, B.A. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J. Biol. Chem. 269, 13623-13628 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Masudaira, P.4    Yankner, B.A.5
  • 12
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner, D. et al. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2, 864-870 (1996).
    • (1996) Nature Med. , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 13
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimers-disease-linked presenilin-1 variants elevate Abeta 1-42/1-40 ratio in-vitro and in-vivo
    • Borchelt, D.R. et al. Familial Alzheimers-disease-linked presenilin-1 variants elevate Abeta 1-42/1-40 ratio in-vitro and in-vivo. Neuron 17, 1005-1013 (1996).
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1
  • 14
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
    • Duff, K. et al. Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature 383, 710-713 (1996).
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1
  • 15
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • Lemere, C.A. et al. The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nature Med. 2, 1146-1150 (1996).
    • (1996) Nature Med. , vol.2 , pp. 1146-1150
    • Lemere, C.A.1
  • 16
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • Citron, M. et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nature Med. 3, 67-72 (1997).
    • (1997) Nature Med. , vol.3 , pp. 67-72
    • Citron, M.1
  • 17
    • 0031017795 scopus 로고    scopus 로고
    • Light and electron microscope localization of presenilin-1 in primate brain
    • Lah, J. et al. Light and electron microscope localization of presenilin-1 in primate brain. J. Neurosci. 17, 1971-1980 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 1971-1980
    • Lah, J.1
  • 18
    • 0029812077 scopus 로고    scopus 로고
    • Expression and analysis of presenilin 1 in a human neuronal system: Localization in cell bodies and dendrites
    • Cook, D.G. et al. Expression and analysis of presenilin 1 in a human neuronal system: Localization in cell bodies and dendrites. Proc. Natl. Acad. Sci. USA 93, 9223-9228 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9223-9228
    • Cook, D.G.1
  • 19
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs, D.M. et al. Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nature Med. 2, 224-229 (1996).
    • (1996) Nature Med. , vol.2 , pp. 224-229
    • Kovacs, D.M.1
  • 20
    • 0028689553 scopus 로고
    • Expression of foreign proteins in a human neuronal system
    • Cook, D.G., Lee, V.M.-Y. & Doms, R.W. Expression of foreign proteins in a human neuronal system. Methods Cell Biol. 43, 289-303 (1994).
    • (1994) Methods Cell Biol. , vol.43 , pp. 289-303
    • Cook, D.G.1    Lee, V.M.-Y.2    Doms, R.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.