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Volumn 67, Issue 17, 2010, Pages 3005-3015

Enrichment of ligands with molecular dockings and subsequent characterization for human alcohol dehydrogenase 3

Author keywords

Alcohol dehydrogenase; Enzyme kinetics; Inhibitors; Molecular docking; S Nitrosoglutathione; Virtual screening

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE 3; CHOLIC ACID; FATTY ACID DERIVATIVE; GLUTATHIONE DERIVATIVE; UNCLASSIFIED DRUG; ADH1C PROTEIN, HUMAN; LIGAND; PROTEIN BINDING;

EID: 77956750158     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0370-2     Document Type: Article
Times cited : (8)

References (39)
  • 1
    • 0035139107 scopus 로고    scopus 로고
    • Mammalian alcohol dehydrogenase-functional and structural implications
    • 10.1007/BF02255973 11173978
    • J-O Höög JJ Hedberg P Strömberg S Svensson 2001 Mammalian alcohol dehydrogenase-functional and structural implications J Biomed Sci 8 71 76 10.1007/BF02255973 11173978
    • (2001) J Biomed Sci , vol.8 , pp. 71-76
    • Höög, J.-O.1    Hedberg, J.J.2    Strömberg, P.3    Svensson, S.4
  • 2
    • 0026778829 scopus 로고
    • "Enzymogenesis": Classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line
    • 10.1073/pnas.89.19.9247 1:CAS:528:DyaK3sXltlCht74%3D 1409630
    • O Danielsson H Jörnvall 1992 "Enzymogenesis": classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line Proc Natl Acad Sci USA 89 9247 9251 10.1073/pnas.89.19.9247 1:CAS:528:DyaK3sXltlCht74%3D 1409630
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9247-9251
    • Danielsson, O.1    Jörnvall, H.2
  • 3
    • 0024422072 scopus 로고
    • Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase
    • DOI 10.1016/0014-5793(89)81797-1
    • M Koivusalo M Baumann L Uotila 1989 Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase FEBS Lett 257 105 109 10.1016/0014-5793(89)81797-1 1:CAS:528:DyaK3cXjt1Oi 2806555 (Pubitemid 19261773)
    • (1989) FEBS Letters , vol.257 , Issue.1 , pp. 105-109
    • Koivusalo, M.1    Baumann, M.2    Uotila, L.3
  • 4
    • 0032522535 scopus 로고    scopus 로고
    • S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • 1:CAS:528:DyaK1cXivV2it7w%3D 9531510
    • DE Jensen GK Belka GC Du Bois 1998 S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme Biochem J 331 659 668 1:CAS:528:DyaK1cXivV2it7w%3D 9531510
    • (1998) Biochem J , vol.331 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du Bois, G.C.3
  • 5
    • 58149141583 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: Dual functions of alcohol dehydrogenase 3: Implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities
    • 10.1007/s00018-008-8592-2 1:CAS:528:DC%2BD1cXhsFCgs7nI 19011746
    • CA Staab M Hellgren J-O Höög 2008 Medium- and short-chain dehydrogenase/reductase gene and protein families: dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities Cell Mol Life Sci 65 3950 3960 10.1007/s00018-008-8592-2 1:CAS:528:DC%2BD1cXhsFCgs7nI 19011746
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3950-3960
    • Staab, C.A.1    Hellgren, M.2    Höög, J.-O.3
  • 6
    • 0039699818 scopus 로고    scopus 로고
    • SDR and MDR: Completed genome sequences show these protein families to be large, of old origin, and of complex nature
    • DOI 10.1016/S0014-5793(99)00130-1, PII S0014579399001301
    • H Jörnvall J-O Höög B Persson 1999 SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature FEBS Lett 445 261 264 10.1016/S0014-5793(99)00130-1 10094468 (Pubitemid 29117223)
    • (1999) FEBS Letters , vol.445 , Issue.2-3 , pp. 261-264
    • Jornvall, H.1    Hoog, J.-O.2    Persson, B.3
  • 7
    • 0038018534 scopus 로고    scopus 로고
    • The metabolic role of human ADH3 functioning as ethanol dehydrogenase
    • DOI 10.1016/S0014-5793(03)00492-7
    • SL Lee MF Wang AI Lee SJ Yin 2003 The metabolic role of human ADH3 functioning as ethanol dehydrogenase FEBS Lett 544 143 147 10.1016/S0014- 5793(03)00492-7 1:CAS:528:DC%2BD3sXktFWlurg%3D 12782305 (Pubitemid 36628051)
    • (2003) FEBS Letters , vol.544 , Issue.1-3 , pp. 143-147
    • Lee, S.-L.1    Wang, M.-F.2    Lee, A.-I.3    Yin, S.-J.4
  • 8
    • 0033694699 scopus 로고    scopus 로고
    • Expression of alcohol dehydrogenase 3 in tissue and cultured cells from human oral mucosa
    • 1:CAS:528:DC%2BD3cXosFyhsLs%3D 11073833
    • JJ Hedberg J-O Höög JA Nilsson Z Xi Å Elfwing RC Grafström 2000 Expression of alcohol dehydrogenase 3 in tissue and cultured cells from human oral mucosa Am J Pathol 157 1745 1755 1:CAS:528: DC%2BD3cXosFyhsLs%3D 11073833
    • (2000) Am J Pathol , vol.157 , pp. 1745-1755
    • Hedberg, J.J.1    Höög, J.-O.2    Nilsson, J.A.3    Xi, Z.4    Elfwing, Å.5    Grafström, R.C.6
  • 11
    • 0346654056 scopus 로고    scopus 로고
    • The role of a formaldehyde dehydrogenase-glutathione pathway in protein S-nitrosation in mammalian cells
    • DOI 10.1016/j.niox.2003.11.003
    • AS Haqqani SK Do HC Birnboim 2003 The role of a formaldehyde dehydrogenase-glutathione pathway in protein S-nitrosation in mammalian cells Nitric Oxide 9 172 181 10.1016/j.niox.2003.11.003 1:CAS:528: DC%2BD2cXkvFOqug%3D%3D 14732341 (Pubitemid 38077278)
    • (2003) Nitric Oxide - Biology and Chemistry , vol.9 , Issue.3 , pp. 172-181
    • Haqqani, A.S.1    Do, S.K.2    Birnboim, H.C.3
  • 12
    • 48249147530 scopus 로고    scopus 로고
    • Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate alcohols via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors
    • 10.1042/BJ20071666 1:CAS:528:DC%2BD1cXosFWitbY%3D 18412547
    • CA Staab J Ålander M Brandt J Lengqvist R Morgenstern RC Grafström J-O Höög 2008 Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate alcohols via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors Biochem J 413 493 504 10.1042/BJ20071666 1:CAS:528: DC%2BD1cXosFWitbY%3D 18412547
    • (2008) Biochem J , vol.413 , pp. 493-504
    • Staab, C.A.1    Ålander, J.2    Brandt, M.3    Lengqvist, J.4    Morgenstern, R.5    Grafström, R.C.6    Höög, J.-O.7
  • 13
    • 67650848555 scopus 로고    scopus 로고
    • S-nitrosoglutathione reductase: An important regulator in human asthma
    • 10.1164/rccm.200901-0158OC 1:CAS:528:DC%2BD1MXhtVKrt7nM 19395503
    • LG Que Z Yang JS Stamler NL Lugogo M Kraft 2009 S-nitrosoglutathione reductase: an important regulator in human asthma Am J Respir Crit Care Med 180 226 231 10.1164/rccm.200901-0158OC 1:CAS:528:DC%2BD1MXhtVKrt7nM 19395503
    • (2009) Am J Respir Crit Care Med , vol.180 , pp. 226-231
    • Que, L.G.1    Yang, Z.2    Stamler, J.S.3    Lugogo, N.L.4    Kraft, M.5
  • 14
    • 0026464881 scopus 로고
    • Immunocytochemical and biochemical demonstration of formaldehyde dehydrogenase (class III alcohol dehydrogenase) in the nucleus
    • 1:CAS:528:DyaK3sXnslKhug%3D%3D 1453005
    • FJ Iborra J Renau-Piqueras M Portoles MD Boleda C Guerri X Parés 1992 Immunocytochemical and biochemical demonstration of formaldehyde dehydrogenase (class III alcohol dehydrogenase) in the nucleus J Histochem Cytochem 40 1865 1878 1:CAS:528:DyaK3sXnslKhug%3D%3D 1453005
    • (1992) J Histochem Cytochem , vol.40 , pp. 1865-1878
    • Iborra, F.J.1    Renau-Piqueras, J.2    Portoles, M.3    Boleda, M.D.4    Guerri, C.5    Parés, X.6
  • 15
    • 67349222284 scopus 로고    scopus 로고
    • Medium-chain fatty acids and glutathione derivatives as inhibitors of S-nitrosoglutathione reduction mediated by alcohol dehydrogenase 3
    • 10.1016/j.cbi.2009.01.008 1:CAS:528:DC%2BD1MXltlels7s%3D 19428350
    • CA Staab M Hellgren RC Grafström J-O Höög 2009 Medium-chain fatty acids and glutathione derivatives as inhibitors of S-nitrosoglutathione reduction mediated by alcohol dehydrogenase 3 Chem Biol Interact 180 113 118 10.1016/j.cbi.2009.01.008 1:CAS:528:DC%2BD1MXltlels7s%3D 19428350
    • (2009) Chem Biol Interact , vol.180 , pp. 113-118
    • Staab, C.A.1    Hellgren, M.2    Grafström, R.C.3    Höög, J.-O.4
  • 16
    • 69949182737 scopus 로고    scopus 로고
    • Kinetic and cellular characterization of novel inhibitors of S-nitrosoglutathione reductase
    • 10.1074/jbc.M109.019919 1:CAS:528:DC%2BD1MXhtVGgsrzF 19596685
    • PC Sanghani WI Davis SL Fears SL Green L Zhai Y Tang E Martin NS Bryan SP Sanghani 2009 Kinetic and cellular characterization of novel inhibitors of S-nitrosoglutathione reductase J Biol Chem 284 24354 24362 10.1074/jbc.M109. 019919 1:CAS:528:DC%2BD1MXhtVGgsrzF 19596685
    • (2009) J Biol Chem , vol.284 , pp. 24354-24362
    • Sanghani, P.C.1    Davis, W.I.2    Fears, S.L.3    Green, S.L.4    Zhai, L.5    Tang, Y.6    Martin, E.7    Bryan, N.S.8    Sanghani, S.P.9
  • 17
    • 0035416126 scopus 로고    scopus 로고
    • High-throughput docking for lead generation
    • DOI 10.1016/S1367-5931(00)00217-9
    • M Totrov R Abagyan 2001 High-throughput docking for lead generation Curr Opin Chem Biol 5 375 382 10.1016/S1367-5931(00)00217-9 11470599 (Pubitemid 32900508)
    • (2001) Current Opinion in Chemical Biology , vol.5 , Issue.4 , pp. 375-382
    • Abagyan, R.1    Totrov, M.2
  • 18
    • 42949174603 scopus 로고    scopus 로고
    • Combining docking, molecular dynamics and the linear interaction energy method to predict binding modes and affinities for non-nucleoside inhibitors to HIV-1 reverse transcriptase
    • DOI 10.1021/jm7012198
    • J Carlsson L Boukharta J Åqvist 2008 Combining docking, molecular dynamics and the linear interaction energy method to predict binding modes and affinities for non-nucleoside inhibitors to HIV-1 reverse transcriptase J Med Chem 51 2648 2656 10.1021/jm7012198 1:CAS:528:DC%2BD1cXksFyktLs%3D 18410085 (Pubitemid 351620786)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.9 , pp. 2648-2656
    • Carlsson, J.1    Boukharta, L.2    Aqvist, J.3
  • 19
    • 65249124122 scopus 로고    scopus 로고
    • Computations of standard binding free energies with molecular dynamics simulations
    • 10.1021/jp807701h 1:CAS:528:DC%2BD1MXlvFOqtA%3D%3D 19146384
    • Y Deng B Roux 2009 Computations of standard binding free energies with molecular dynamics simulations J Phys Chem B 113 2234 2246 10.1021/jp807701h 1:CAS:528:DC%2BD1MXlvFOqtA%3D%3D 19146384
    • (2009) J Phys Chem B , vol.113 , pp. 2234-2246
    • Deng, Y.1    Roux, B.2
  • 20
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • DOI 10.1006/jmbi.1994.1052
    • R Abagyan M Totrov 1994 Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins J Mol Biol 235 983 1002 10.1006/jmbi.1994.1052 1:CAS:528:DyaK2cXhsFyis7k%3D 8289329 (Pubitemid 24047836)
    • (1994) Journal of Molecular Biology , vol.235 , Issue.3 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 21
    • 1842431537 scopus 로고    scopus 로고
    • Comparative study of several algorithms for flexible ligand docking
    • DOI 10.1023/B:JCAM.0000017496.76572.6f
    • BD Bursulaya M Totrov R Abagyan CL Brooks 2003 3rd Comparative study of several algorithms for flexible compound docking J Comput Aided Mol Des 17 755 763 10.1023/B:JCAM.0000017496.76572.6f 1:CAS:528:DC%2BD2cXhsFOhtL0%3D 15072435 (Pubitemid 38418287)
    • (2003) Journal of Computer-Aided Molecular Design , vol.17 , Issue.11 , pp. 755-763
    • Bursulaya, B.D.1    Totrov, M.2    Abagyan, R.3    Brooks III, C.L.4
  • 22
    • 67650097331 scopus 로고    scopus 로고
    • Comparison of several molecular docking programs: Pose prediction and virtual screening accuracy
    • 10.1021/ci900056c 1:CAS:528:DC%2BD1MXmsVOmt7g%3D 19476350
    • JB Cross DC Thompson BK Rai JC Baber KY Fan Y Hu C Humblet 2009 Comparison of several molecular docking programs: pose prediction and virtual screening accuracy J Chem Inf Model 49 1455 1474 10.1021/ci900056c 1:CAS:528:DC%2BD1MXmsVOmt7g%3D 19476350
    • (2009) J Chem Inf Model , vol.49 , pp. 1455-1474
    • Cross, J.B.1    Thompson, D.C.2    Rai, B.K.3    Baber, J.C.4    Fan, K.Y.5    Hu, Y.6    Humblet, C.7
  • 23
    • 84986522918 scopus 로고
    • ICM-A new method for protein modeling and design. Applications to docking and structure prediction from the distorted native conformation
    • 10.1002/jcc.540150503 1:CAS:528:DyaK2MXhtVWisA%3D%3D
    • R Abagyan M Totrov DN Kuznetsov 1994 ICM-a new method for protein modeling and design. Applications to docking and structure prediction from the distorted native conformation J Comput Chem 15 488 506 10.1002/jcc.540150503 1:CAS:528:DyaK2MXhtVWisA%3D%3D
    • (1994) J Comput Chem , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.N.3
  • 24
    • 0001731773 scopus 로고
    • Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides
    • 10.1021/j100194a068 1:CAS:528:DyaK38XkvFSktrg%3D
    • G Nemethy KD Gibson KA Palmer CN Yoon G Paterlini A Zagari S Rumsey HA Scheraga 1992 Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides J Phys Chem 96 6472 6484 10.1021/j100194a068 1:CAS:528:DyaK38XkvFSktrg%3D
    • (1992) J Phys Chem , vol.96 , pp. 6472-6484
    • Nemethy, G.1    Gibson, K.D.2    Palmer, K.A.3    Yoon, C.N.4    Paterlini, G.5    Zagari, A.6    Rumsey, S.7    Scheraga, H.A.8
  • 26
    • 54949110209 scopus 로고    scopus 로고
    • Developing and validating predictive decision tree models from mining chemical structural fingerprints and high-throughput screening data in PubChem
    • 10.1186/1471-2105-9-401
    • L Han Y Wang SH Bryant 2008 Developing and validating predictive decision tree models from mining chemical structural fingerprints and high-throughput screening data in PubChem BMC Bioinform 9 401 10.1186/1471-2105-9-401
    • (2008) BMC Bioinform , vol.9 , pp. 401
    • Han, L.1    Wang, Y.2    Bryant, S.H.3
  • 27
    • 4744365803 scopus 로고    scopus 로고
    • Soft docking and multiple receptor conformations in virtual screening
    • DOI 10.1021/jm049756p
    • AM Ferrari BQ Wei L Costantino BK Shoichet 2004 Soft Docking and multiple receptor conformation in virtual screening J Med Chem 47 5076 5084 10.1021/jm049756p 1:CAS:528:DC%2BD2cXnt12gt74%3D 15456251 (Pubitemid 39314905)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.21 , pp. 5076-5084
    • Ferrari, A.M.1    Wei, B.Q.2    Costantino, L.3    Shoichet, B.K.4
  • 28
    • 0031302358 scopus 로고    scopus 로고
    • Flexible protein-compound docking by global energy optimization in internal coordinates
    • Totrov M, Abagyan R (1997) Flexible protein-compound docking by global energy optimization in internal coordinates. Proteins (Suppl 1):215-220
    • (1997) Proteins , Issue.SUPPL 1 , pp. 215-220
    • Totrov, M.1    Abagyan, R.2
  • 29
    • 0025167380 scopus 로고
    • Comparison of three classes of human liver alcohol dehydrogenase. Emphasis on different substrate binding pockets
    • 10.1111/j.1432-1033.1990.tb19337.x 1:CAS:528:DyaK3MXitVWisg%3D%3D 2226453
    • H Eklund P Müller-Wille E Horjales O Futer B Holmquist BL Vallee J-O Höög R Kaiser H Jörnvall 1990 Comparison of three classes of human liver alcohol dehydrogenase. Emphasis on different substrate binding pockets Eur J Biochem 193 303 310 10.1111/j.1432-1033.1990.tb19337.x 1:CAS:528:DyaK3MXitVWisg%3D%3D 2226453
    • (1990) Eur J Biochem , vol.193 , pp. 303-310
    • Eklund, H.1    Müller-Wille, P.2    Horjales, E.3    Futer, O.4    Holmquist, B.5    Vallee, B.L.6    Höög, J.-O.7    Kaiser, R.8    Jörnvall, H.9
  • 30
    • 0034863617 scopus 로고    scopus 로고
    • Rapid boundary element solvation electrostatics calculations in folding simulations: Successful folding of a 23-residue peptide
    • DOI 10.1002/1097-0282(2001)60:2<124::AID-BIP1008>3.0.CO;2-S
    • M Totrov R Abagyan 2001 Rapid boundary element solvation electrostatics calculations in folding simulations: successful folding of a 23-residue peptide Biopolymers 60 124 133 10.1002/1097-0282(2001)60:2<124::AID-BIP1008>3.0. CO;2-S 1:CAS:528:DC%2BD3MXlvVGgtbs%3D 11455546 (Pubitemid 32743529)
    • (2001) Biopolymers - Peptide Science Section , vol.60 , Issue.2 , pp. 124-133
    • Totrov, M.1    Abagyan, R.2
  • 31
    • 0026504082 scopus 로고
    • A single-residue exchange gives human recombinant ββ alcohol dehydrogenase γγ isozyme properties
    • 10.1111/j.1432-1033.1992.tb16808.x 1572355
    • J-O Höög H Eklund H Jörnvall 1992 A single-residue exchange gives human recombinant ββ alcohol dehydrogenase γγ isozyme properties Eur J Biochem 205 519 526 10.1111/j.1432-1033. 1992.tb16808.x 1572355
    • (1992) Eur J Biochem , vol.205 , pp. 519-526
    • Höög, J.-O.1    Eklund, H.2    Jörnvall, H.3
  • 32
    • 0037168478 scopus 로고    scopus 로고
    • Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation
    • DOI 10.1021/bi026705q
    • PC Sanghani WF Bosron TD Hurley 2002 Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation Biochemistry 41 15189 15194 10.1021/bi026705q 1:CAS:528: DC%2BD38XovFCnsr0%3D 12484756 (Pubitemid 36008127)
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15189-15194
    • Sanghani, P.C.1    Bosron, W.F.2    Hurley, T.D.3
  • 33
    • 0028641612 scopus 로고
    • Residues specific for class III alcohol dehydrogenase. Site-directed mutagenesis of the human enzyme
    • 10.1021/bi00254a017 1:CAS:528:DyaK2cXmvFGqsrY%3D 7999766
    • M Estonius J-O Höög O Danielsson H Jörnvall 1994 Residues specific for class III alcohol dehydrogenase. Site-directed mutagenesis of the human enzyme Biochemistry 33 15080 15085 10.1021/bi00254a017 1:CAS:528:DyaK2cXmvFGqsrY%3D 7999766
    • (1994) Biochemistry , vol.33 , pp. 15080-15085
    • Estonius, M.1    Höög, J.-O.2    Danielsson, O.3    Jörnvall, H.4
  • 35
    • 0028348480 scopus 로고
    • Interference by doxorubicin with DNA unwinding in MCF-7 breast tumor cells
    • 1:CAS:528:DyaK2cXivV2lsL8%3D 8183243
    • FA Fornari JK Randolph JC Yalowich MK Ritke DA Gewirtz 1994 Interference by doxorubicin with DNA unwinding in MCF-7 breast tumor cells Mol Pharmacol 45 649 656 1:CAS:528:DyaK2cXivV2lsL8%3D 8183243
    • (1994) Mol Pharmacol , vol.45 , pp. 649-656
    • Fornari, F.A.1    Randolph, J.K.2    Yalowich, J.C.3    Ritke, M.K.4    Gewirtz, D.A.5
  • 36
    • 43049158125 scopus 로고    scopus 로고
    • Designing transient binding drugs: A new concept for drug discovery
    • 10.1016/j.drudis.2008.02.001 1:CAS:528:DC%2BD1cXlvVWntLk%3D 18468561
    • S Ohlson 2008 Designing transient binding drugs: a new concept for drug discovery Drug Discov Today 13 433 439 10.1016/j.drudis.2008.02.001 1:CAS:528:DC%2BD1cXlvVWntLk%3D 18468561
    • (2008) Drug Discov Today , vol.13 , pp. 433-439
    • Ohlson, S.1
  • 37
    • 0034024574 scopus 로고    scopus 로고
    • Human liver class i alcohol dehydrogenase γγ isozyme: The sole cytosolic 3β-hydroxysteroid dehydrogenase of iso-bile acids
    • 10.1053/he.2000.5720 1:CAS:528:DC%2BD3cXis1Cks7Y%3D 10733557
    • H-U Marschall UCT Opperman S Svensson E Nordling B Persson J-O Höög H Jörnvall 2000 Human liver class I alcohol dehydrogenase γγ isozyme: the sole cytosolic 3β-hydroxysteroid dehydrogenase of iso-bile acids Hepatology 31 990 996 10.1053/he.2000.5720 1:CAS:528:DC%2BD3cXis1Cks7Y%3D 10733557
    • (2000) Hepatology , vol.31 , pp. 990-996
    • Marschall, H.-U.1    Opperman, U.C.T.2    Svensson, S.3    Nordling, E.4    Persson, B.5    Höög, J.-O.6    Jörnvall, H.7
  • 38
    • 0032566627 scopus 로고    scopus 로고
    • An attempt to transform class characteristics within the alcohol dehydrogenase family
    • DOI 10.1016/S0014-5793(98)01100-4, PII S0014579398011004
    • JJ Hedberg P Strömberg J-O Höög 1998 An attempt to transform class characteristics within the alcohol dehydrogenase family FEBS Lett 436 67 70 10.1016/S0014-5793(98)01100-4 1:CAS:528:DyaK1cXmt1emu7s%3D 9771895 (Pubitemid 28454608)
    • (1998) FEBS Letters , vol.436 , Issue.1 , pp. 67-70
    • Hedberg, J.J.1    Stromberg, P.2    Hoog, J.-O.3
  • 39
    • 0037351726 scopus 로고    scopus 로고
    • Reduction of S-nitrosoglutathione by human alcohol dehydrogenase 3 is an irreversible reaction as analysed by electrospray mass spectrometry
    • DOI 10.1046/j.1432-1033.2003.03486.x
    • JJ Hedberg WJ Griffiths SJ Nilsson J-O Höög 2003 Reduction of S-nitrosoglutathione by human alcohol dehydrogenase 3 is an irreversible reaction as analysed by electrospray mass spectrometry Eur J Biochem 270 1249 1256 10.1046/j.1432-1033.2003.03486.x 1:CAS:528:DC%2BD3sXivVSktLo%3D 12631283 (Pubitemid 36388743)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1249-1256
    • Hedberg, J.J.1    Griffiths, W.J.2    Nilsson, S.J.F.3    Hoog, J.-O.4


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