메뉴 건너뛰기




Volumn 143, Issue , 2014, Pages 460-472

Roles of 17β-hydroxysteroid dehydrogenase type 10 in neurodegenerative disorders

Author keywords

ABAD; Alzheimer'; Developmental intellectual disabilities; HSD17B10 gene; Metabolism of allopregnanolone; Mitochondria; Multifunctional protein; Neuroactive steroids; s disease

Indexed keywords

17BETA HYDROXYSTEROID DEHYDROGENASE TYPE 10; 3ALPHA HYDROXY 5ALPHA PREGNAN 20 ONE; ALCOHOL DEHYDROGENASE; CYTOCHROME C; ISOLEUCINE; TESTOSTERONE 17BETA DEHYDROGENASE; UNCLASSIFIED DRUG; 3 (OR 17)-BETA-HYDROXYSTEROID DEHYDROGENASE; HYDROXYSTEROID DEHYDROGENASE;

EID: 84904635377     PISSN: 09600760     EISSN: 18791220     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2014.07.001     Document Type: Review
Times cited : (63)

References (105)
  • 1
    • 34548401303 scopus 로고    scopus 로고
    • HSD17B10: A gene involved in cognitive function through metabolism of isoleucine and neuroactive steroids
    • DOI 10.1016/j.ymgme.2007.06.001, PII S1096719207001953
    • S.Y. Yang, X.Y. He, and D. Miller HSD17B10: a gene involved in cognitive function through metabolism of isoleucine and neuroactive steroids Mol. Genet. Metab. 92 2007 36 42 (Pubitemid 47361893)
    • (2007) Molecular Genetics and Metabolism , vol.92 , Issue.1-2 , pp. 36-42
    • Yang, S.-Y.1    He, X.-Y.2    Miller, D.3
  • 2
    • 0032562664 scopus 로고    scopus 로고
    • A human brain L-3-hydroxyacyl-coenzyme a dehydrogenase is identical to an amyloid β-peptide-binding protein involved in Alzheimer's disease
    • DOI 10.1074/jbc.273.17.10741
    • X.Y. He, H. Schulz, and S.Y. Yang A human brain l-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease J. Biol. Chem. 273 1998 10741 10746 (Pubitemid 28227690)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10741-10746
    • He, X.-Y.1    Schulz, H.2    Yang, S.-Y.3
  • 4
    • 0033591454 scopus 로고    scopus 로고
    • Human brain short chain l-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase
    • X.Y. He, G. Merz, P. Mehta, H. Schulz, and S.Y. Yang Human brain short chain l-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase 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
  • 5
    • 0033985061 scopus 로고    scopus 로고
    • Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase
    • DOI 10.1042/0264-6021:3450139
    • X.Y. He, Y.Z. Yang, H. Schulz, and S.Y. Yang Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain l-3-hydroxyacyl-CoA dehydrogenase Biochem. J. 345 Pt 1 2000 139 143 (Pubitemid 30060114)
    • (2000) Biochemical Journal , vol.345 , Issue.1 , pp. 139-143
    • He, X.-Y.1    Yang, Y.-Z.2    Schulz, H.3    Yang, S.-Y.4
  • 7
    • 26244465858 scopus 로고    scopus 로고
    • 3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease
    • DOI 10.1111/j.1742-4658.2005.04911.x
    • S.Y. Yang, X.Y. He, and H. Schulz 3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease FEBS J. 272 2005 4874 4883 (Pubitemid 41415112)
    • (2005) FEBS Journal , vol.272 , Issue.19 , pp. 4874-4883
    • Yang, S.-Y.1    He, X.-Y.2    Schulz, H.3
  • 9
    • 0034692926 scopus 로고    scopus 로고
    • Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD)
    • A.J. Powell, J.A. Read, M.J. Banfield, F. Gunn-Moore, S.D. Yan, J. Lustbader, A.R. Stern, D.M. Stern, and R.L. Brady Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD) J. Mol. Biol. 303 2000 311 327
    • (2000) J. Mol. Biol. , vol.303 , pp. 311-327
    • Powell, A.J.1    Read, J.A.2    Banfield, M.J.3    Gunn-Moore, F.4    Yan, S.D.5    Lustbader, J.6    Stern, A.R.7    Stern, D.M.8    Brady, R.L.9
  • 10
    • 16244392645 scopus 로고    scopus 로고
    • Multiple functions of type 10 17β-hydroxysteroid dehydrogenase
    • DOI 10.1016/j.tem.2005.03.006
    • S.Y. Yang, X.Y. He, and H. Schulz Multiple functions of type 10 17beta-hydroxysteroid dehydrogenase Trends Endocrinol. Metab. 16 2005 167 175 (Pubitemid 40603096)
    • (2005) Trends in Endocrinology and Metabolism , vol.16 , Issue.4 , pp. 167-175
    • Yang, S.-Y.1    He, X.-Y.2    Schulz, H.3
  • 11
    • 0344741467 scopus 로고    scopus 로고
    • Expanded substrate screenings of human and Drosophila type 10 17 β-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: Characterization of multifunctional 3α/7α/7β/17β/20β/21-HSD
    • DOI 10.1042/BJ20030877
    • N. Shafqat, H.U. Marschall, C. Filling, E. Nordling, X.Q. Wu, L. Bjork, J. Thyberg, E. Martensson, S. Salim, H. Jornvall, and U. Oppermann Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/ 17beta/20beta/21-HSD Biochem. J. 376 2003 49 60 (Pubitemid 37492899)
    • (2003) Biochemical Journal , vol.376 , Issue.1 , pp. 49-60
    • Shafqat, N.1    Marschall, H.-U.2    Filling, C.3    Nordling, E.4    Wu, X.-Q.5    Bjork, L.6    Thyberg, J.7    Martensson, E.8    Salim, S.9    Jornvall, H.10    Oppermann, U.11
  • 12
    • 10944225224 scopus 로고    scopus 로고
    • Type 10 17beta-hydroxysteroid dehydrogenase catalyzing the oxidation of steroid modulators of γ-aminobutyric acid type a receptors
    • DOI 10.1016/j.mce.2004.08.011, PII S0303720704003363
    • X.Y. He, J. Wegiel, Y.Z. Yang, R. Pullarkat, H. Schulz, and S.Y. Yang Type 10 17beta-hydroxysteroid dehydrogenase catalyzing the oxidation of steroid modulators of gamma-aminobutyric acid type A receptors Mol. Cell. Endocrinol. 229 2005 111 117 (Pubitemid 40018089)
    • (2005) Molecular and Cellular Endocrinology , vol.229 , Issue.1-2 , pp. 111-117
    • He, X.-Y.1    Wegiel, J.2    Yang, Y.-Z.3    Pullarkat, R.4    Schulz, H.5    Yang, S.-Y.6
  • 13
    • 33646046210 scopus 로고    scopus 로고
    • Roles of type 10 17beta-hydroxysteroid dehydrogenase in intracrinology and metabolism of isoleucine and fatty acids
    • X.Y. He, and S.Y. Yang Roles of type 10 17beta-hydroxysteroid dehydrogenase in intracrinology and metabolism of isoleucine and fatty acids Endocr. Metab. Immune Disord. Drug Targets 6 2006 95 102
    • (2006) Endocr. Metab. Immune Disord. Drug Targets , vol.6 , pp. 95-102
    • He, X.Y.1    Yang, S.Y.2
  • 14
    • 78650528416 scopus 로고    scopus 로고
    • (-)-CHANA, a fluorogenic probe for detecting amyloid binding alcohol dehydrogenase HSD10 activity in living cells
    • K.E. Muirhead, M. Froemming, X. Li, K. Musilek, S.J. Conway, D. Sames, and F.J. Gunn-Moore (-)-CHANA, a fluorogenic probe for detecting amyloid binding alcohol dehydrogenase HSD10 activity in living cells ACS Chem. Biol. 5 2010 1105 1114
    • (2010) ACS Chem. Biol. , vol.5 , pp. 1105-1114
    • Muirhead, K.E.1    Froemming, M.2    Li, X.3    Musilek, K.4    Conway, S.J.5    Sames, D.6    Gunn-Moore, F.J.7
  • 16
    • 60249089957 scopus 로고    scopus 로고
    • Integrated view on 17beta-hydroxysteroid dehydrogenases
    • G. Moeller, and J. Adamski Integrated view on 17beta-hydroxysteroid dehydrogenases Mol. Cell. Endocrinol. 301 2009 7 19
    • (2009) Mol. Cell. Endocrinol. , vol.301 , pp. 7-19
    • Moeller, G.1    Adamski, J.2
  • 18
    • 0034791854 scopus 로고    scopus 로고
    • Characterization and localization of human type 10 17β- hydroxysteroid dehydrogenase
    • DOI 10.1046/j.0014-2956.2001.02421.2421.x
    • X.Y. He, G. Merz, Y.Z. Yang, P. Mehta, H. Schulz, and S.Y. Yang Characterization and localization of human type10 17beta-hydroxysteroid dehydrogenase Eur. J. Biochem. 268 2001 4899 4907 (Pubitemid 32953806)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.18 , pp. 4899-4907
    • He, X.-Y.1    Merz, G.2    Yang, Y.-Z.3    Mehta, P.4    Schulz, H.5    Yang, S.-Y.6
  • 19
    • 0034994142 scopus 로고    scopus 로고
    • Role of type 10 17beta-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer's disease
    • S.Y. Yang, and X.Y. He Role of type 10 17beta-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer's disease Adv. Exp. Med. Biol. 487 2001 101 110
    • (2001) Adv. Exp. Med. Biol. , vol.487 , pp. 101-110
    • Yang, S.Y.1    He, X.Y.2
  • 20
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • J. Holzmann, P. Frank, E. Loffler, K.L. Bennett, C. Gerner, and W. Rossmanith RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme Cell 135 2008 462 474
    • (2008) Cell , vol.135 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loffler, E.3    Bennett, K.L.4    Gerner, C.5    Rossmanith, W.6
  • 21
    • 65649153354 scopus 로고    scopus 로고
    • Estrogen receptor alpha interacts with 17beta-hydroxysteroid dehydrogenase type 10 in mitochondria
    • V. Jazbutyte, F. Kehl, L. Neyses, and T. Pelzer Estrogen receptor alpha interacts with 17beta-hydroxysteroid dehydrogenase type 10 in mitochondria Biochem. Biophys. Res. Commun. 384 2009 450 454
    • (2009) Biochem. Biophys. Res. Commun. , vol.384 , pp. 450-454
    • Jazbutyte, V.1    Kehl, F.2    Neyses, L.3    Pelzer, T.4
  • 22
    • 0033046060 scopus 로고    scopus 로고
    • Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): Regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease
    • DOI 10.1016/S0014-5793(99)00586-4, PII S0014579399005864
    • U.C. Oppermann, S. Salim, L.O. Tjernberg, L. Terenius, and H. Jornvall Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease FEBS Lett. 451 1999 238 242 (Pubitemid 29243784)
    • (1999) FEBS Letters , vol.451 , Issue.3 , pp. 238-242
    • Oppermann, U.C.T.1    Salim, S.2    Tjernberg, L.O.3    Terenius, L.4    Jornvall, H.5
  • 24
    • 0030711713 scopus 로고    scopus 로고
    • Alzheimer's disease: The ins and outs of amyloid-β
    • DOI 10.1038/39479
    • K. Beyreuther, and C.L. Masters Alzheimer's disease. The ins and outs of amyloid-beta Nature 389 1997 677 678 (Pubitemid 27458939)
    • (1997) Nature , vol.389 , Issue.6652 , pp. 677-678
    • Beyreuther, K.1    Masters, C.L.2
  • 25
    • 0035931260 scopus 로고    scopus 로고
    • Molecular cloning, modeling, and localization of rat type 10 17β-hydroxysteroid dehydrogenase
    • DOI 10.1016/S0303-7207(00)00391-9, PII S0303720700003919
    • X.Y. He, G. Merz, C.H. Chu, D. Lin, Y.Z. Yang, P. Mehta, H. Schulz, and S.Y. Yang Molecular cloning, modeling, and localization of rat type 10 17beta-hydroxysteroid dehydrogenase Mol. Cell. Endocrinol. 171 2001 89 98 (Pubitemid 32098202)
    • (2001) Molecular and Cellular Endocrinology , vol.171 , Issue.1-2 , pp. 89-98
    • He, X.-Y.1    Merz, G.2    Chu, C.-H.3    Lin, D.4    Yang, Y.-Z.5    Mehta, P.6    Schulz, H.7    Yang, S.-Y.8
  • 26
    • 0037186457 scopus 로고    scopus 로고
    • Abundant type 10 17β-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer's disease model
    • DOI 10.1016/S0169-328X(02)00102-X, PII S0169328X0200102X
    • X.Y. He, G.Y. Wen, G. Merz, D. Lin, Y.Z. Yang, P. Mehta, H. Schulz, and S.Y. Yang Abundant type 10 17 beta-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer's disease model Brain Res. Mol. Brain Res. 99 2002 46 53 (Pubitemid 34178500)
    • (2002) Molecular Brain Research , vol.99 , Issue.1 , pp. 46-53
    • He, X.-Y.1    Wen, G.-Y.2    Merz, G.3    Lin, D.4    Yang, Y.-Z.5    Mehta, P.6    Schulz, H.7    Yang, S.-Y.8
  • 29
    • 78651384511 scopus 로고    scopus 로고
    • Does the HSD17B10 gene escape from X-inactivation?
    • X.Y. He, C. Dobkin, and S.Y. Yang Does the HSD17B10 gene escape from X-inactivation? Eur. J. Hum. Genet. 19 2011 123 124
    • (2011) Eur. J. Hum. Genet. , vol.19 , pp. 123-124
    • He, X.Y.1    Dobkin, C.2    Yang, S.Y.3
  • 30
    • 80051572799 scopus 로고    scopus 로고
    • Hydroxysteroid (17beta) dehydrogenase X in human health and disease
    • S.Y. Yang, X.Y. He, and D. Miller Hydroxysteroid (17beta) dehydrogenase X in human health and disease Mol. Cell. Endocrinol. 343 2011 1 6
    • (2011) Mol. Cell. Endocrinol. , vol.343 , pp. 1-6
    • Yang, S.Y.1    He, X.Y.2    Miller, D.3
  • 31
    • 0033667891 scopus 로고    scopus 로고
    • Progressive infantile neurodegeneration caused by 2-methyl-3- hydroxybutyryl-CoA dehydrogenase deficiency: A novel inborn error of branched-chain fatty acid and isoleucine metabolism
    • J. Zschocke, J.P. Ruiter, J. Brand, M. Lindner, G.F. Hoffmann, R.J. Wanders, and E. Mayatepek Progressive infantile neurodegeneration caused by 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: a novel inborn error of branched-chain fatty acid and isoleucine metabolism Pediatr. Res. 48 2000 852 855
    • (2000) Pediatr. Res. , vol.48 , pp. 852-855
    • Zschocke, J.1    Ruiter, J.P.2    Brand, J.3    Lindner, M.4    Hoffmann, G.F.5    Wanders, R.J.6    Mayatepek, E.7
  • 32
    • 84872485986 scopus 로고    scopus 로고
    • A 5-methylcytosine hotspot responsible for the prevalent HSD17B10 mutation
    • S.Y. Yang, C. Dobkin, X.Y. He, M. Philipp, and W.T. Brown A 5-methylcytosine hotspot responsible for the prevalent HSD17B10 mutation Gene 515 2013 380 384
    • (2013) Gene , vol.515 , pp. 380-384
    • Yang, S.Y.1    Dobkin, C.2    He, X.Y.3    Philipp, M.4    Brown, W.T.5
  • 34
    • 81555212293 scopus 로고    scopus 로고
    • A novel mutation in the HSD17B10 gene of a 10-year-old boy with refractory epilepsy, choreoathetosis and learning disability
    • L.H. Seaver, X.Y. He, K. Abe, T. Cowan, G.M. Enns, L. Sweetman, M. Philipp, S. Lee, M. Malik, and S.Y. Yang A novel mutation in the HSD17B10 gene of a 10-year-old boy with refractory epilepsy, choreoathetosis and learning disability PLoS One 6 2011 e27348
    • (2011) PLoS One , vol.6 , pp. 27348
    • Seaver, L.H.1    He, X.Y.2    Abe, K.3    Cowan, T.4    Enns, G.M.5    Sweetman, L.6    Philipp, M.7    Lee, S.8    Malik, M.9    Yang, S.Y.10
  • 36
    • 34247122413 scopus 로고    scopus 로고
    • Neuroimage Findings in 2-Methyl-3-Hydroxybutyryl-CoA Dehydrogenase Deficiency
    • DOI 10.1016/j.pediatrneurol.2006.11.014, PII S088789940600717X
    • M.R. Cazorla, A. Verdu, C. Perez-Cerda, and A. Ribes Neuroimage findings in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency Pediatr. Neurol. 36 2007 264 267 (Pubitemid 46601346)
    • (2007) Pediatric Neurology , vol.36 , Issue.4 , pp. 264-267
    • Cazorla, M.R.1    Verdu, A.2    Perez-Cerda, C.3    Ribes, A.4
  • 37
    • 24344497374 scopus 로고    scopus 로고
    • 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: An X-linked inborn error of isoleucine metabolism that may mimic a mitochondrial disease
    • DOI 10.1203/01.pdr.0000176916.94328.cd
    • C. Perez-Cerda, J. Garcia-Villoria, R. Ofman, P.R. Sala, B. Merinero, J. Ramos, M.T. Garcia-Silva, B. Beseler, J. Dalmau, R.J. Wanders, M. Ugarte, and A. Ribes 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: an X-linked inborn error of isoleucine metabolism that may mimic a mitochondrial disease Pediatr. Res. 58 2005 488 491 (Pubitemid 41254512)
    • (2005) Pediatric Research , vol.58 , Issue.3 , pp. 488-491
    • Garcia-Villoria, J.1    Ofman, R.2    Sala, P.R.3    Merinero, B.4    Ramos, J.5    Garcia-Silva, M.T.6    Beseler, B.7    Dalmau, J.8    Wanders, R.J.A.9    Ugarte, M.10    Ribes, A.11
  • 42
    • 84863322665 scopus 로고    scopus 로고
    • HSD10 disease: Clinical consequences of mutations in the HSD17B10 gene
    • J. Zschocke HSD10 disease: clinical consequences of mutations in the HSD17B10 gene J. Inherit. Metab. Dis. 35 2012 81 89
    • (2012) J. Inherit. Metab. Dis. , vol.35 , pp. 81-89
    • Zschocke, J.1
  • 44
    • 80052266362 scopus 로고    scopus 로고
    • Neurosteroid and GABA-A receptor alterations in Alzheimer's disease, Parkinson's disease and multiple sclerosis
    • S. Luchetti, I. Huitinga, and D.F. Swaab Neurosteroid and GABA-A receptor alterations in Alzheimer's disease, Parkinson's disease and multiple sclerosis Neuroscience 191 2011 6 21
    • (2011) Neuroscience , vol.191 , pp. 6-21
    • Luchetti, S.1    Huitinga, I.2    Swaab, D.F.3
  • 45
    • 33751314737 scopus 로고    scopus 로고
    • A receptors through two discrete transmembrane sites
    • DOI 10.1038/nature05324, PII NATURE05324
    • A.M. Hosie, M.E. Wilkins, H.M. da Silva, and T.G. Smart Endogenous neurosteroids regulate GABAA receptors through two discrete transmembrane sites Nature 444 2006 486 489 (Pubitemid 44809065)
    • (2006) Nature , vol.444 , Issue.7118 , pp. 486-489
    • Hosie, A.M.1    Wilkins, M.E.2    Da Silva, H.M.A.3    Smart, T.G.4
  • 46
    • 0037069355 scopus 로고    scopus 로고
    • Kinetics of allopregnanolone formation catalyzed by human 3α-hydroxysteroid dehydrogenase type III (AKR1C2)
    • DOI 10.1021/bi026109w
    • J.W. Trauger, A. Jiang, B.A. Stearns, and P.V. LoGrasso Kinetics of allopregnanolone formation catalyzed by human 3 alpha-hydroxysteroid dehydrogenase type III (AKR1C2) Biochemistry 41 2002 13451 13459 (Pubitemid 35303905)
    • (2002) Biochemistry , vol.41 , Issue.45 , pp. 13451-13459
    • Trauger, J.W.1    Jiang, A.2    Stearns, B.A.3    LoGrasso, P.V.4
  • 47
    • 0023117765 scopus 로고
    • +] in mouse pancreatic islets, and nutrient-induced insulin secretion
    • C.J. Hedeskov, K. Capito, and P. Thams Cytosolic ratios of free [NADPH]/[NADP+] and [NADH]/[NAD+] in mouse pancreatic islets, and nutrient-induced insulin secretion Biochem. J. 241 1987 161 167 (Pubitemid 17004725)
    • (1987) Biochemical Journal , vol.241 , Issue.1 , pp. 161-167
    • Hedeskov, C.J.1    Capito, K.2    Thams, P.3
  • 48
    • 16244423717 scopus 로고    scopus 로고
    • Intracellular oxidation of allopregnanolone by human brain type 10 17beta-hydroxysteroid dehydrogenase
    • DOI 10.1016/j.brainres.2005.01.022
    • X.Y. He, J. Wegiel, and S.Y. Yang Intracellular oxidation of allopregnanolone by human brain type 10 17beta-hydroxysteroid dehydrogenase Brain Res. 1040 2005 29 35 (Pubitemid 40459618)
    • (2005) Brain Research , vol.1040 , Issue.1-2 , pp. 29-35
    • He, X.-Y.1    Wegiel, J.2    Yang, S.-Y.3
  • 51
    • 84904685505 scopus 로고    scopus 로고
    • Possible alteration of amyloid-beta protein precursor metabolism or trafficking in a 17beta-hydroxysteroid dehydrogenase X deficiency patient
    • X.Y. He, D. Miller, and S.Y. Yang Possible alteration of amyloid-beta protein precursor metabolism or trafficking in a 17beta-hydroxysteroid dehydrogenase X deficiency patient J. Alzheimer's Dis. 2011 http://j-alz.com/ letteresditor/index.html#December2011
    • (2011) J. Alzheimer's Dis.
    • He, X.Y.1    Miller, D.2    Yang, S.Y.3
  • 52
    • 0004287714 scopus 로고
    • 10th ed. Merk & Co., Inc. Rahway, NJ
    • M. Windholz The Merk Index 10th ed. 1983 Merk & Co., Inc. Rahway, NJ 970
    • (1983) The Merk Index , pp. 970
    • Windholz, M.1
  • 53
    • 34047273223 scopus 로고    scopus 로고
    • HSD17B10 replaces HADH2 as the approved designation for the gene mutated in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency
    • DOI 10.1016/j.ymgme.2007.01.001, PII S1096719207000042
    • S.H. Korman, and S.Y. Yang HSD17B10 replaces HADH2 as the approved designation for the gene mutated in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency Mol. Genet. Metab. 91 2007 115 (Pubitemid 46550921)
    • (2007) Molecular Genetics and Metabolism , vol.91 , Issue.1 , pp. 115
    • Korman, S.H.1    Yang, S.-Y.2
  • 55
    • 34250211094 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential cause of metabolic dysfunction in Alzheimer's disease
    • DOI 10.1080/15216540601047767, PII 768588523
    • X. Chen, and S.D. Yan Mitochondrial Abeta: a potential cause of metabolic dysfunction in Alzheimer's disease IUBMB Life 58 2006 686 694 (Pubitemid 46895569)
    • (2006) IUBMB Life , vol.58 , Issue.12 , pp. 686-694
    • Chen, X.1    Yan, S.D.2
  • 56
    • 77951931900 scopus 로고    scopus 로고
    • The consequences of mitochondrial amyloid beta-peptide in Alzheimer's disease
    • K.E. Muirhead, E. Borger, L. Aitken, S.J. Conway, and F.J. Gunn-Moore The consequences of mitochondrial amyloid beta-peptide in Alzheimer's disease Biochem. J. 426 2010 255 270
    • (2010) Biochem. J. , vol.426 , pp. 255-270
    • Muirhead, K.E.1    Borger, E.2    Aitken, L.3    Conway, S.J.4    Gunn-Moore, F.J.5
  • 58
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: Role of amyloid-β peptide alcohol dehydrogenase (ABAD)
    • DOI 10.1111/j.0959-9673.2005.00427.x
    • S.D. Yan, and D.M. Stern Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD) Int. J. Exp. Pathol. 86 2005 161 171 (Pubitemid 40813912)
    • (2005) International Journal of Experimental Pathology , vol.86 , Issue.3 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 61
    • 79951548587 scopus 로고    scopus 로고
    • Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease
    • J. Yao, H. Du, S. Yan, F. Fang, C. Wang, L.F. Lue, L. Guo, D. Chen, D.M. Stern, F.J. Gunn Moore, J. Xi Chen, O. Arancio, and S.S. Yan Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease J. Neurosci. 31 2011 2313 2320
    • (2011) J. Neurosci. , vol.31 , pp. 2313-2320
    • Yao, J.1    Du, H.2    Yan, S.3    Fang, F.4    Wang, C.5    Lue, L.F.6    Guo, L.7    Chen, D.8    Stern, D.M.9    Gunn Moore, F.J.10    Xi Chen, J.11    Arancio, O.12    Yan, S.S.13
  • 62
    • 84882445921 scopus 로고    scopus 로고
    • Is amyloid binding alcohol dehydrogenase a drug target for treating Alzheimer's disease?
    • E. Borger, L. Aitken, H. Du, W. Zhang, F.J. Gunn-Moore, and S.S. Yan Is amyloid binding alcohol dehydrogenase a drug target for treating Alzheimer's disease? Curr. Alzheimer Res. 10 2013 21 29
    • (2013) Curr. Alzheimer Res. , vol.10 , pp. 21-29
    • Borger, E.1    Aitken, L.2    Du, H.3    Zhang, W.4    Gunn-Moore, F.J.5    Yan, S.S.6
  • 63
    • 84872334320 scopus 로고    scopus 로고
    • Structure-based design and synthesis of benzothiazole phosphonate analogues with inhibitors of human ABAD-Abeta for treatment of Alzheimer's disease
    • K.R. Valasani, G. Hu, M.O. Chaney, and S.S. Yan Structure-based design and synthesis of benzothiazole phosphonate analogues with inhibitors of human ABAD-Abeta for treatment of Alzheimer's disease Chem. Biol. Drug Des. 81 2013 238 249
    • (2013) Chem. Biol. Drug Des. , vol.81 , pp. 238-249
    • Valasani, K.R.1    Hu, G.2    Chaney, M.O.3    Yan, S.S.4
  • 64
    • 0029915707 scopus 로고    scopus 로고
    • Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain
    • K. Kuwabara, M. Matsumoto, J. Ikeda, O. Hori, S. Ogawa, Y. Maeda, K. Kitagawa, N. Imuta, T. Kinoshita, D.M. Stern, H. Yanagi, and T. Kamada Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain J. Biol. Chem. 271 1996 5025 5032
    • (1996) J. Biol. Chem. , vol.271 , pp. 5025-5032
    • Kuwabara, K.1    Matsumoto, M.2    Ikeda, J.3    Hori, O.4    Ogawa, S.5    Maeda, Y.6    Kitagawa, K.7    Imuta, N.8    Kinoshita, T.9    Stern, D.M.10    Yanagi, H.11    Kamada, T.12
  • 65
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • X. Wang, R. Sato, M.S. Brown, X. Hua, and J.L. Goldstein SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis Cell 77 1994 53 62
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 66
    • 33748344899 scopus 로고    scopus 로고
    • Comparative evolutionary genomics of the HADH2 gene encoding Abeta-binding alcohol dehydrogenase/17beta-hydroxysteroid dehydrogenase type 10 (ABAD/HSD10)
    • A.T. Marques, A. Antunes, P.A. Fernandes, and M.J. Ramos Comparative evolutionary genomics of the HADH2 gene encoding Abeta-binding alcohol dehydrogenase/17beta-hydroxysteroid dehydrogenase type 10 (ABAD/HSD10) BMC Genomics 7 2006 202
    • (2006) BMC Genomics , vol.7 , pp. 202
    • Marques, A.T.1    Antunes, A.2    Fernandes, P.A.3    Ramos, M.J.4
  • 67
    • 0031750831 scopus 로고    scopus 로고
    • Scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-β peptide- binding protein
    • DOI 10.1083/jcb.141.4.1009
    • L. Torroja, D. Ortuno-Sahagun, A. Ferrus, B. Hammerle, and J.A. Barbas scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II l-3-hydroxyacyl-CoA dehydrogenase/amyloid-beta peptide-binding protein J. Cell Biol. 141 1998 1009 1017 (Pubitemid 28243967)
    • (1998) Journal of Cell Biology , vol.141 , Issue.4 , pp. 1009-1017
    • Torroja, L.1    Ortuno-Sahagun, D.2    Ferrus, A.3    Hammerle, B.4    Barbas, J.A.5
  • 68
    • 70349303780 scopus 로고    scopus 로고
    • Enhanced levels of mitochondrial enzyme 17beta-hydroxysteroid dehydrogenase type 10 in patients with Alzheimer disease and multiple sclerosis
    • Z. Kristofikova, M. Bockova, K. Hegnerova, A. Bartos, J. Klaschka, J. Ricny, D. Ripova, and J. Homola Enhanced levels of mitochondrial enzyme 17beta-hydroxysteroid dehydrogenase type 10 in patients with Alzheimer disease and multiple sclerosis Mol. Biosyst. 5 2009 1174 1179
    • (2009) Mol. Biosyst. , vol.5 , pp. 1174-1179
    • Kristofikova, Z.1    Bockova, M.2    Hegnerova, K.3    Bartos, A.4    Klaschka, J.5    Ricny, J.6    Ripova, D.7    Homola, J.8
  • 69
    • 33847051684 scopus 로고    scopus 로고
    • Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction
    • Y. Yan, Y. Liu, M. Sorci, G. Belfort, J.W. Lustbader, S.S. Yan, and C. Wang Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction Biochemistry 46 2007 1724 1731
    • (2007) Biochemistry , vol.46 , pp. 1724-1731
    • Yan, Y.1    Liu, Y.2    Sorci, M.3    Belfort, G.4    Lustbader, J.W.5    Yan, S.S.6    Wang, C.7
  • 70
    • 34248532398 scopus 로고    scopus 로고
    • 3-hydroxyacyl-CoA dehydrogenase (HAD) deficiency replaces short-chain hydroxyacyl-CoA dehydrogenase (SCHAD) deficiency as well as medium- and short-chain hydroxyacyl-CoA dehydrogenase (M/SCHAD) deficiency as the consensus name of this fatty acid oxidation disorder
    • X.Y. He, and S.Y. Yang 3-hydroxyacyl-CoA dehydrogenase (HAD) deficiency replaces short-chain hydroxyacyl-CoA dehydrogenase (SCHAD) deficiency as well as medium- and short-chain hydroxyacyl-CoA dehydrogenase (M/SCHAD) deficiency as the consensus name of this fatty acid oxidation disorder Mol. Genet. Metab. 91 2007 205 206
    • (2007) Mol. Genet. Metab. , vol.91 , pp. 205-206
    • He, X.Y.1    Yang, S.Y.2
  • 71
    • 84876419130 scopus 로고    scopus 로고
    • Changes of the HSD17B10 gene expression levels in ulcerative colitis
    • X.Y. He, Y.X. Yang, and S.Y. Yang Changes of the HSD17B10 gene expression levels in ulcerative colitis Inflamm. Bowel Dis. 19 2013 E23 E24
    • (2013) Inflamm. Bowel Dis. , vol.19
    • He, X.Y.1    Yang, Y.X.2    Yang, S.Y.3
  • 72
    • 84899753548 scopus 로고    scopus 로고
    • Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate
    • Y. Xu, H. Li, Y.H. Jin, J. Fan, and F. Sun Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate PLoS One 9 2014 e95965
    • (2014) PLoS One , vol.9 , pp. 95965
    • Xu, Y.1    Li, H.2    Jin, Y.H.3    Fan, J.4    Sun, F.5
  • 73
    • 34247853439 scopus 로고    scopus 로고
    • Formation of an enolate intermediate is required for the reaction catalyzed by 3-hydroxyacyl-CoA dehydrogenase
    • DOI 10.1016/j.bmcl.2007.03.023, PII S0960894X07003150
    • X. Liu, G. Deng, X. Chu, N. Li, L. Wu, and D. Li Formation of an enolate intermediate is required for the reaction catalyzed by 3-hydroxyacyl-CoA dehydrogenase Bioorg. Med. Chem. Lett. 17 2007 3187 3190 (Pubitemid 46702609)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.11 , pp. 3187-3190
    • Liu, X.1    Deng, G.2    Chu, X.3    Li, N.4    Wu, L.5    Li, D.6
  • 76
    • 0030018017 scopus 로고    scopus 로고
    • Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells
    • DOI 10.1021/bi952807n
    • D. Green, A.R. Marks, S. Fleischer, and J.O. McIntyre Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells Biochemistry 35 1996 8158 8165 (Pubitemid 26234915)
    • (1996) Biochemistry , vol.35 , Issue.25 , pp. 8158-8165
    • Green, D.1    Marks, A.R.2    Fleischer, S.3    McIntyre, J.O.4
  • 77
    • 19444376784 scopus 로고    scopus 로고
    • Cerebral ketone body metabolism
    • DOI 10.1007/s10545-005-5518-0
    • A.A. Morris Cerebral ketone body metabolism J. Inherit. Metab. Dis. 28 2005 109 121 (Pubitemid 40723878)
    • (2005) Journal of Inherited Metabolic Disease , vol.28 , Issue.2 , pp. 109-121
    • Morris, A.A.M.1
  • 78
    • 57749102902 scopus 로고    scopus 로고
    • Cytoprotective role of mitochondrial amyloid beta peptide-binding alcohol dehydrogenase against a cytotoxic aldehyde
    • Y. Murakami, I. Ohsawa, T. Kasahara, and S. Ohta Cytoprotective role of mitochondrial amyloid beta peptide-binding alcohol dehydrogenase against a cytotoxic aldehyde Neurobiol. Aging 30 2009 325 329
    • (2009) Neurobiol. Aging , vol.30 , pp. 325-329
    • Murakami, Y.1    Ohsawa, I.2    Kasahara, T.3    Ohta, S.4
  • 80
    • 48249156188 scopus 로고    scopus 로고
    • Mitochondrial disorders in the nervous system
    • S. DiMauro, and E.A. Schon Mitochondrial disorders in the nervous system Annu. Rev. Neurosci. 31 2008 91 123
    • (2008) Annu. Rev. Neurosci. , vol.31 , pp. 91-123
    • Dimauro, S.1    Schon, E.A.2
  • 81
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • M.T. Lin, and M.F. Beal Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 443 2006 787 795 (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 82
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of alzheimer amyloidosis
    • D. Pratico, K. Uryu, S. Leight, J.Q. Trojanoswki, and V.M. Lee Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis J. Neurosci. 21 2001 4183 4187 (Pubitemid 32538543)
    • (2001) Journal of Neuroscience , vol.21 , Issue.12 , pp. 4183-4187
    • Pratico, D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.-Y.5
  • 83
    • 61849137768 scopus 로고    scopus 로고
    • Direct inhibition of the mitochondrial permeability transition pore: A possible mechanism for better neuroprotective effects of allopregnanolone over progesterone
    • I. Sayeed, S. Parvez, B. Wali, D. Siemen, and D.G. Stein Direct inhibition of the mitochondrial permeability transition pore: a possible mechanism for better neuroprotective effects of allopregnanolone over progesterone Brain Res. 1263 2009 165 173
    • (2009) Brain Res. , vol.1263 , pp. 165-173
    • Sayeed, I.1    Parvez, S.2    Wali, B.3    Siemen, D.4    Stein, D.G.5
  • 84
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • X. Wang, B. Su, S.L. Siedlak, P.I. Moreira, H. Fujioka, Y. Wang, G. Casadesus, and X. Zhu Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins Proc. Natl. Acad. Sci. U. S. A. 105 2008 19318 19323
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 86
    • 84891906038 scopus 로고    scopus 로고
    • Presynaptic mitochondrial morphology in monkey prefrontal cortex correlates with working memory and is improved with estrogen treatment
    • Y. Hara, F. Yuk, R. Puri, W.G. Janssen, P.R. Rapp, and J.H. Morrison Presynaptic mitochondrial morphology in monkey prefrontal cortex correlates with working memory and is improved with estrogen treatment Proc. Natl. Acad. Sci. U. S. A. 111 2014 486 491
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 486-491
    • Hara, Y.1    Yuk, F.2    Puri, R.3    Janssen, W.G.4    Rapp, P.R.5    Morrison, J.H.6
  • 89
    • 84861337338 scopus 로고    scopus 로고
    • Impaired butyrate oxidation in ulcerative colitis is due to decreased butyrate uptake and a defect in the oxidation pathway
    • V. De Preter, I. Arijs, K. Windey, W. Vanhove, S. Vermeire, F. Schuit, P. Rutgeerts, and K. Verbeke Impaired butyrate oxidation in ulcerative colitis is due to decreased butyrate uptake and a defect in the oxidation pathway Inflamm. Bowel Dis. 18 2012 1127 1136
    • (2012) Inflamm. Bowel Dis. , vol.18 , pp. 1127-1136
    • De Preter, V.1    Arijs, I.2    Windey, K.3    Vanhove, W.4    Vermeire, S.5    Schuit, F.6    Rutgeerts, P.7    Verbeke, K.8
  • 90
    • 77957258218 scopus 로고    scopus 로고
    • Type 10 17beta-hydroxysteroid dehydrogenase expression is regulated by C/EBPbeta in HepG2 cells
    • M. Rotinen, J. Villar, J. Celay, and I. Encio Type 10 17beta-hydroxysteroid dehydrogenase expression is regulated by C/EBPbeta in HepG2 cells J. Steroid Biochem. Mol. Biol. 122 2010 164 171
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.122 , pp. 164-171
    • Rotinen, M.1    Villar, J.2    Celay, J.3    Encio, I.4
  • 91
    • 84879828505 scopus 로고    scopus 로고
    • Transcription start sites and epigenetic analysis of the HSD17B10 proximal promoter
    • S.Y. Yang, C. Dobkin, X.Y. He, and W.T. Brown Transcription start sites and epigenetic analysis of the HSD17B10 proximal promoter BMC Biochem. 14 2013 17
    • (2013) BMC Biochem. , vol.14 , pp. 17
    • Yang, S.Y.1    Dobkin, C.2    He, X.Y.3    Brown, W.T.4
  • 92
    • 34249720583 scopus 로고    scopus 로고
    • Interaction of amyloid binding alcohol dehydrogenase/Aβ mediates up-regulation of peroxiredoxin II in the brains of Alzheimer's disease patients and a transgenic Alzheimer's disease mouse model
    • DOI 10.1016/j.mcn.2007.03.013, PII S104474310700084X
    • J. Yao, M. Taylor, F. Davey, Y. Ren, J. Aiton, P. Coote, F. Fang, J.X. Chen, S.D. Yan, and F.J. Gunn-Moore Interaction of amyloid binding alcohol dehydrogenase/Abeta mediates up-regulation of peroxiredoxin II in the brains of Alzheimer's disease patients and a transgenic Alzheimer's disease mouse model Mol. Cell. Neurosci. 35 2007 377 382 (Pubitemid 46843572)
    • (2007) Molecular and Cellular Neuroscience , vol.35 , Issue.2 , pp. 377-382
    • Yao, J.1    Taylor, M.2    Davey, F.3    Ren, Y.4    Aiton, J.5    Coote, P.6    Fang, F.7    Chen, J.X.8    Yan, S.D.9    Gunn-Moore, F.J.10
  • 94
    • 84878749549 scopus 로고    scopus 로고
    • The amyloid-beta-SDR5C1(ABAD) interaction does not mediate a specific inhibition of mitochondrial RNase P
    • E. Vilardo, and W. Rossmanith The amyloid-beta-SDR5C1(ABAD) interaction does not mediate a specific inhibition of mitochondrial RNase P PLoS One 8 2013 e65609
    • (2013) PLoS One , vol.8 , pp. 65609
    • Vilardo, E.1    Rossmanith, W.2
  • 96
    • 43849097891 scopus 로고    scopus 로고
    • Increased expression of Abeta degrading enzyme IDE in the cortex of transgenic mice with Alzheimer's disease-like neuropathology
    • S. Vepsalainen, M. Hiltunen, S. Helisalmi, J. Wang, T. van Groen, H. Tanila, and H. Soininen Increased expression of Abeta degrading enzyme IDE in the cortex of transgenic mice with Alzheimer's disease-like neuropathology Neurosci. Lett. 438 2008 216 220
    • (2008) Neurosci. Lett. , vol.438 , pp. 216-220
    • Vepsalainen, S.1    Hiltunen, M.2    Helisalmi, S.3    Wang, J.4    Van Groen, T.5    Tanila, H.6    Soininen, H.7
  • 97
    • 84860848937 scopus 로고    scopus 로고
    • Sex hormones, aging, and Alzheimer's disease
    • A.M. Barron, and C.J. Pike Sex hormones, aging, and Alzheimer's disease Front Biosci. (Elite Ed) 4 2012 976 997
    • (2012) Front Biosci. (Elite Ed) , vol.4 , pp. 976-997
    • Barron, A.M.1    Pike, C.J.2
  • 98
    • 0033302775 scopus 로고    scopus 로고
    • Estradiol: A protective and trophic factor in the brain
    • D.B. Dubal, M.E. Wilson, and P.M. Wise Estradiol: a protective and trophic factor in the brain J. Alzheimers Dis. 1 1999 265 274
    • (1999) J. Alzheimers Dis. , vol.1 , pp. 265-274
    • Dubal, D.B.1    Wilson, M.E.2    Wise, P.M.3
  • 100
    • 3142774112 scopus 로고    scopus 로고
    • Niemann-Pick type C disease involves disrupted neurosteroidogenesis and responds to allopregnanolone
    • DOI 10.1038/nm1073
    • L.D. Griffin, W. Gong, L. Verot, and S.H. Mellon Niemann-Pick type C disease involves disrupted neurosteroidogenesis and responds to allopregnanolone Nat. Med. 10 2004 704 711 (Pubitemid 38937635)
    • (2004) Nature Medicine , vol.10 , Issue.7 , pp. 704-711
    • Griffin, L.D.1    Gong, W.2    Verot, L.3    Mellon, S.H.4
  • 103
    • 84862868568 scopus 로고    scopus 로고
    • Identification of a 17beta-hydroxysteroid dehydrogenase type 10 steroidal inhibitor: A tool to investigate the role of type 10 in Alzheimer's disease and prostate cancer
    • D. Ayan, R. Maltais, and D. Poirier Identification of a 17beta-hydroxysteroid dehydrogenase type 10 steroidal inhibitor: a tool to investigate the role of type 10 in Alzheimer's disease and prostate cancer ChemMedChem 7 2012 1181 1184
    • (2012) ChemMedChem , vol.7 , pp. 1181-1184
    • Ayan, D.1    Maltais, R.2    Poirier, D.3
  • 104
    • 0017085714 scopus 로고
    • Demonstration of a new mammalian isoleucine catabolic pathway yielding an R series of metabolites
    • O.A. Mamer, S.S. Tjoa, C.R. Scriver, and G.A. Klassen Demonstration of a new mammalian isoleucine catabolic pathway yielding an R series of metabolites Biochem. J. 160 1976 417 426
    • (1976) Biochem. J. , vol.160 , pp. 417-426
    • Mamer, O.A.1    Tjoa, S.S.2    Scriver, C.R.3    Klassen, G.A.4
  • 105
    • 0027211907 scopus 로고
    • Early lipid intermediates in glycosyl-phosphatidylinositol anchor assembly are synthesized in the ER and located in the cytoplasmic leaflet of the ER membrane bilayer
    • DOI 10.1083/jcb.121.5.987
    • J. Vidugiriene, and A.K. Menon Early lipid intermediates in glycosyl-phosphatidylinositol anchor assembly are synthesized in the ER and located in the cytoplasmic leaflet of the ER membrane bilayer J. Cell Biol. 121 1993 987 996 (Pubitemid 23154260)
    • (1993) Journal of Cell Biology , vol.121 , Issue.5 , pp. 987-996
    • Vidugiriene, J.1    Menon, A.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.