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Volumn 954, Issue 1, 2002, Pages 115-122

Presence of hydroxysteroid dehydrogenase type 10 in amyloid plaques (APs) of Hsiao's APP-Sw transgenic mouse brains, but absence in APs of Alzheimer's disease brains

Author keywords

Alzheimer's disease; ERAB; Hsiao's APP Sw transgenic mouse (Tg2576); Hydroxysteroid dehydrogenase; Mitochondria; SCHAD

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; ENDOPLASMIC RETICULUM ASSOCIATED AMYLOID BETA PEPTIDE BINDING PROTEIN; ENZYME; HYDROXYSTEROID DEHYDROGENASE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 4G8; MONOCLONAL ANTIBODY 5F3; MONOCLONAL ANTIBODY 6E10; POLYCLONAL ANTIBODY; PROTEIN; SHORT CHAIN LEVO 3 HYDROXYACYL COA DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0036839598     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(02)03354-1     Document Type: Article
Times cited : (16)

References (24)
  • 1
    • 0010983211 scopus 로고
    • Die Silberimpregnation der neurofibrillen
    • Bielschowsky M. Die Silberimpregnation der neurofibrillen. J. Psycholo-Neurol. 3:1904;169-188.
    • (1904) J. Psycholo-Neurol. , vol.3 , pp. 169-188
    • Bielschowsky, M.1
  • 2
    • 0035854582 scopus 로고    scopus 로고
    • Deposition of Alzheimer's vascular amyloid-β is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB)
    • Frackowiak J., Mazur-Kolecka B., Kaczmarski W., Dickson D. Deposition of Alzheimer's vascular amyloid-β is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB). Brain Res. 907:2001;44-53.
    • (2001) Brain Res. , vol.907 , pp. 44-53
    • Frackowiak, J.1    Mazur-Kolecka, B.2    Kaczmarski, W.3    Dickson, D.4
  • 3
    • 0034791854 scopus 로고    scopus 로고
    • Characterization and localization of human type 10 17β-hydroxysteroid dehydrogenase
    • He X.Y., Merz G., Yang Y.Z., Mehta P., Schulz H., Yang S.Y. Characterization and localization of human type 10 17β-hydroxysteroid dehydrogenase. Eur. J. Biochem. 268:2001;4899-4907.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4899-4907
    • He, X.Y.1    Merz, G.2    Yang, Y.Z.3    Mehta, P.4    Schulz, H.5    Yang, S.Y.6
  • 5
    • 0034630485 scopus 로고    scopus 로고
    • Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism
    • He X.Y., Merz G., Yang Y.Z., Pullarkat R., Mehta P., Schulz H., Yang S.Y. Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism. Biochim. Biophys. Acta. 1484:2000;267-277.
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 267-277
    • He, X.Y.1    Merz, G.2    Yang, Y.Z.3    Pullarkat, R.4    Mehta, P.5    Schulz, H.6    Yang, S.Y.7
  • 6
    • 0033985061 scopus 로고    scopus 로고
    • Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase
    • He X.Y., Yang Y.Z., Schulz H., Yang S.Y. Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase. Biochem. J. 345:2000;139-143.
    • (2000) Biochem. J. , vol.345 , pp. 139-143
    • He, X.Y.1    Yang, Y.Z.2    Schulz, H.3    Yang, S.Y.4
  • 7
    • 0033591454 scopus 로고    scopus 로고
    • Human brain short chain L-3-hydroxyacyl Coenzyme A dehydrogenase is a single-domain multifunctional enzyme
    • He X.Y., Merz G., Mehta P., Schulz H., Yang S.Y. Human brain short chain L-3-hydroxyacyl Coenzyme A dehydrogenase is a single-domain multifunctional enzyme. J. Biol. Chem. 274:1999;15014-15019.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15014-15019
    • He, X.Y.1    Merz, G.2    Mehta, P.3    Schulz, H.4    Yang, S.Y.5
  • 8
    • 0032562664 scopus 로고    scopus 로고
    • A human brain L-3-hydroxyacyl-coenzyme dehydrogenase is identical to an amyloid β-peptide-binding protein involved in Alzheimer's disease
    • He X.Y., Schulz H., Yang S.Y. A human brain L-3-hydroxyacyl-coenzyme dehydrogenase is identical to an amyloid β-peptide-binding protein involved in Alzheimer's disease. J. Biol. Chem. 273:1998;10741-10746.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10741-10746
    • He, X.Y.1    Schulz, H.2    Yang, S.Y.3
  • 11
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A., Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA. 91:1994;12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 12
    • 0029850692 scopus 로고    scopus 로고
    • New "Alzheimer's mouse" produced
    • Marx J. New "Alzheimer's mouse" produced. Science. 274:1996;177-178.
    • (1996) Science , vol.274 , pp. 177-178
    • Marx, J.1
  • 14
    • 0028085516 scopus 로고
    • Estrogen deficiency and risk of Alzheimer's disease in women
    • Paganini-Hill A., Henderson V.W. Estrogen deficiency and risk of Alzheimer's disease in women. Am. J. Epidemiol. 140:1994;256-261.
    • (1994) Am. J. Epidemiol. , vol.140 , pp. 256-261
    • Paganini-Hill, A.1    Henderson, V.W.2
  • 15
    • 0023691704 scopus 로고
    • Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA
    • Peltoketo H., Isomaa V., Maentausta O., Vihko R. Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett. 239:1988;73-77.
    • (1988) FEBS Lett. , vol.239 , pp. 73-77
    • Peltoketo, H.1    Isomaa, V.2    Maentausta, O.3    Vihko, R.4
  • 16
    • 0023107655 scopus 로고
    • Chromosome 21q21 sublocalisation of gene encoding beta-amyloid peptide in cerebral vessels and neuritic (senile) plaques of people with Alzheimer disease and Down syndrome
    • Robakis N.K., Wisniewski H.M., Jenkins E.C., Devine-Cage E.A., Houck G.E., Yao X.L., Ramakrishna N., Wolfe G., Silverman W.P., Brown W.T. Chromosome 21q21 sublocalisation of gene encoding beta-amyloid peptide in cerebral vessels and neuritic (senile) plaques of people with Alzheimer disease and Down syndrome. Lancet. 1:(8529):1987;384-385.
    • (1987) Lancet , vol.1 , Issue.8529 , pp. 384-385
    • Robakis, N.K.1    Wisniewski, H.M.2    Jenkins, E.C.3    Devine-Cage, E.A.4    Houck, G.E.5    Yao, X.L.6    Ramakrishna, N.7    Wolfe, G.8    Silverman, W.P.9    Brown, W.T.10
  • 17
    • 0021211607 scopus 로고
    • Morphology and distribution of Alzheimer neuritic (senile) and amyloid plaques in striatum and diencephalon
    • Rudelli R.D., Ambler M.W., Wisniewski H.M. Morphology and distribution of Alzheimer neuritic (senile) and amyloid plaques in striatum and diencephalon. Acta Neuropathol. (Berl.). 64:1984;273-281.
    • (1984) Acta Neuropathol. (Berl.) , vol.64 , pp. 273-281
    • Rudelli, R.D.1    Ambler, M.W.2    Wisniewski, H.M.3
  • 18
    • 0014444144 scopus 로고
    • A low viscosity epoxy resin and embedding medium for electron microscopy
    • Spurr A.R. A low viscosity epoxy resin and embedding medium for electron microscopy. J. Ultrastruct. Res. 26:1969;31-43.
    • (1969) J. Ultrastruct. Res. , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 19
    • 0011023609 scopus 로고    scopus 로고
    • Double transgenic mice overexpressing ABAD and mutAPP (V717F, K670M, N671L) show an impairment of hippocampal long-term potential
    • abstract
    • Trillar A.C., Ma J., Yan S.D., Hegde A.N., Stern D., Arancio O. Double transgenic mice overexpressing ABAD and mutAPP (V717F, K670M, N671L) show an impairment of hippocampal long-term potential. Soc. Neurosci. 26:2000;1318. abstract.
    • (2000) Soc. Neurosci. , vol.26 , pp. 1318
    • Trillar, A.C.1    Ma, J.2    Yan, S.D.3    Hegde, A.N.4    Stern, D.5    Arancio, O.6
  • 20
    • 0028023267 scopus 로고
    • Presence of non-fibrillar amyloid β protein in skin biopsies of Alzheimer's disease (AD), Down syndrome and non-AD normal persons
    • Wen G.Y., Wisniewski H.M., Blondal H., Benedikz E., Frey H., Pirttila T., Rudelli R., Kim K.S. Presence of non-fibrillar amyloid β protein in skin biopsies of Alzheimer's disease (AD), Down syndrome and non-AD normal persons. Acta Neuropathol. 88:1994;201-206.
    • (1994) Acta Neuropathol. , vol.88 , pp. 201-206
    • Wen, G.Y.1    Wisniewski, H.M.2    Blondal, H.3    Benedikz, E.4    Frey, H.5    Pirttila, T.6    Rudelli, R.7    Kim, K.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.