메뉴 건너뛰기




Volumn 331, Issue 3, 2003, Pages 593-604

Human 20α-hydroxysteroid dehydrogenase: Crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids

Author keywords

20 hydroxy progesterone; Aldo keto reductase; Crystal structure; Human 20 hydroxysteroid dehydrogenase; Progesterone

Indexed keywords

20ALPHA DIHYDROPROGESTERONE; 20ALPHA HYDROXYSTEROID DEHYDROGENASE; HISTIDINE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0043095539     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00762-9     Document Type: Article
Times cited : (74)

References (48)
  • 1
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenases and related enzymes
    • Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200:1991;537-543.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jornvall, H.3
  • 3
    • 0028226789 scopus 로고
    • Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities
    • Bruce N.C., Willey D.L., Coulson A.F., Jeffery J. Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities. Biochem. J. 299:1994;805-811.
    • (1994) Biochem. J. , vol.299 , pp. 805-811
    • Bruce, N.C.1    Willey, D.L.2    Coulson, A.F.3    Jeffery, J.4
  • 4
    • 0033624660 scopus 로고    scopus 로고
    • Characterization of a human 20alpha-hydroxysteroid dehydrogenase
    • Zhang Y., Dufort I., Rheault P., Luu-The V. Characterization of a human 20alpha-hydroxysteroid dehydrogenase. J. Mol. Endocrinol. 25:2000;221-228.
    • (2000) J. Mol. Endocrinol. , vol.25 , pp. 221-228
    • Zhang, Y.1    Dufort, I.2    Rheault, P.3    Luu-The, V.4
  • 5
    • 0030581692 scopus 로고    scopus 로고
    • Molecular cloning of human type 3 3 alpha-hydroxysteroid dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase by seven amino acids
    • Dufort I., Soucy P., Labrie F., Luu-The V. Molecular cloning of human type 3 3 alpha-hydroxysteroid dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase by seven amino acids. Biochem. Biophys. Res. Commun. 228:1996;474-479.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 474-479
    • Dufort, I.1    Soucy, P.2    Labrie, F.3    Luu-The, V.4
  • 6
    • 0036006774 scopus 로고    scopus 로고
    • Expression, crystallization and preliminary X-ray analysis of human and rabbit 20alpha-hydroxysteroid dehydrogenases in complex with NADP(H) and various steroid substrates
    • Couture J.F., Cantin L., Legrand P., Luu-The V., Labrie F., Breton R. Expression, crystallization and preliminary X-ray analysis of human and rabbit 20alpha-hydroxysteroid dehydrogenases in complex with NADP(H) and various steroid substrates. Acta Crystallog. sect. D. 58:2002;135-139.
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 135-139
    • Couture, J.F.1    Cantin, L.2    Legrand, P.3    Luu-The, V.4    Labrie, F.5    Breton, R.6
  • 7
    • 0035093784 scopus 로고    scopus 로고
    • Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: Differential lability and tissue distribution
    • Dufort I., Labrie F., Luu-The V. Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J. Clin. Endocrinol. Metab. 86:2001;841-846.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 841-846
    • Dufort, I.1    Labrie, F.2    Luu-The, V.3
  • 9
    • 0027158606 scopus 로고
    • CDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family
    • Stolz A., Hammond L., Lou H., Takikawa H., Ronk M., Shively J.E. cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J. Biol. Chem. 268:1993;10448-10457.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10448-10457
    • Stolz, A.1    Hammond, L.2    Lou, H.3    Takikawa, H.4    Ronk, M.5    Shively, J.E.6
  • 10
    • 0028335785 scopus 로고
    • CDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase
    • Ciaccio P.J., Tew K.D. cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. Biochim. Biophys. Acta. 1186:1994;129-132.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 129-132
    • Ciaccio, P.J.1    Tew, K.D.2
  • 11
    • 0028269192 scopus 로고
    • Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder
    • Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y., Sato K., Hara A. Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem. J. 299:1994;545-552.
    • (1994) Biochem. J. , vol.299 , pp. 545-552
    • Deyashiki, Y.1    Ogasawara, A.2    Nakayama, T.3    Nakanishi, M.4    Miyabe, Y.5    Sato, K.6    Hara, A.7
  • 12
    • 0030034858 scopus 로고    scopus 로고
    • Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells
    • Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y., Ishida N. Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem. J. 313:1996;373-376.
    • (1996) Biochem. J. , vol.313 , pp. 373-376
    • Hara, A.1    Matsuura, K.2    Tamada, Y.3    Sato, K.4    Miyabe, Y.5    Deyashiki, Y.6    Ishida, N.7
  • 13
    • 0034003544 scopus 로고    scopus 로고
    • Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes
    • Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S. Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 5:2000;111-125.
    • (2000) Genes Cells , vol.5 , pp. 111-125
    • Nishizawa, M.1    Nakajima, T.2    Yasuda, K.3    Kanzaki, H.4    Sasaguri, Y.5    Watanabe, K.6    Ito, S.7
  • 14
    • 0032510704 scopus 로고    scopus 로고
    • Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: Oxidation of trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene to the activated o-quinone metabolite benzo[a]pyrene-7,8-dione
    • Burczynski M.E., Harvey R.G., Penning T.M. Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: oxidation of trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene to the activated o-quinone metabolite benzo[a]pyrene-7,8-dione. Biochemistry. 37:1998;6781-6790.
    • (1998) Biochemistry , vol.37 , pp. 6781-6790
    • Burczynski, M.E.1    Harvey, R.G.2    Penning, T.M.3
  • 15
    • 0013874534 scopus 로고
    • Maintenance of pregnancy in spayed rats with 20a-hydroxypregn-4-ene-3-one and 20-beta-hydroxypregn-4-ene-3-one
    • Talwalker P.K., Krahenbuhl C., Desaulles P.A. Maintenance of pregnancy in spayed rats with 20a-hydroxypregn-4-ene-3-one and 20-beta-hydroxypregn-4-ene-3-one. Nature. 209:1966;86-87.
    • (1966) Nature , vol.209 , pp. 86-87
    • Talwalker, P.K.1    Krahenbuhl, C.2    Desaulles, P.A.3
  • 16
    • 0015983067 scopus 로고
    • Induction of 20 alpha-hydroxysteroid dehydrogenase in rat corpora lutea of pregnancy by prostaglandin F-2 alpha
    • Strauss J.F. III, Stambaugh R.L. Induction of 20 alpha-hydroxysteroid dehydrogenase in rat corpora lutea of pregnancy by prostaglandin F-2 alpha. Prostaglandins. 5:1974;73-85.
    • (1974) Prostaglandins , vol.5 , pp. 73-85
    • Strauss J.F. III1    Stambaugh, R.L.2
  • 17
    • 0024258307 scopus 로고
    • The endocrinology of conception cycles and implantation in women
    • Lenton E.A., Woodward A.J. The endocrinology of conception cycles and implantation in women. J. Reprod. Fertil. Suppl. 36:1988;1-15.
    • (1988) J. Reprod. Fertil. Suppl. , vol.36 , pp. 1-15
    • Lenton, E.A.1    Woodward, A.J.2
  • 18
    • 0027217863 scopus 로고
    • Dual activation of GABAA and glycine receptors by beta-alanine: Inverse modulation by progesterone and 5 alpha-pregnan-3 alpha-ol-20-one
    • Wu F.S., Gibbs T.T., Farb D.H. Dual activation of GABAA and glycine receptors by beta-alanine: inverse modulation by progesterone and 5 alpha-pregnan-3 alpha-ol-20-one. Eur. J. Pharmacol. 246:1993;239-246.
    • (1993) Eur. J. Pharmacol. , vol.246 , pp. 239-246
    • Wu, F.S.1    Gibbs, T.T.2    Farb, D.H.3
  • 19
    • 2642672840 scopus 로고    scopus 로고
    • Inhibition of oxytocin receptor function by direct binding of progesterone
    • Grazzini E., Guillon G., Mouillac B., Zingg H.H. Inhibition of oxytocin receptor function by direct binding of progesterone. Nature. 392:1998;509-512.
    • (1998) Nature , vol.392 , pp. 509-512
    • Grazzini, E.1    Guillon, G.2    Mouillac, B.3    Zingg, H.H.4
  • 20
    • 0026738827 scopus 로고
    • Progesterone modulates a neuronal nicotinic acetylcholine receptor
    • Valera S., Ballivet M., Bertrand D. Progesterone modulates a neuronal nicotinic acetylcholine receptor. Proc. Natl Acad. Sci. USA. 89:1992;9949-9953.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9949-9953
    • Valera, S.1    Ballivet, M.2    Bertrand, D.3
  • 21
    • 0022483382 scopus 로고
    • Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor
    • Majewska M.D., Harrison N.L., Schwartz R.D., Barker J.L., Paul S.M. Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor. Science. 232:1986;1004-1007.
    • (1986) Science , vol.232 , pp. 1004-1007
    • Majewska, M.D.1    Harrison, N.L.2    Schwartz, R.D.3    Barker, J.L.4    Paul, S.M.5
  • 22
    • 0025826142 scopus 로고
    • The kinetic mechanism catalysed by homogeneous rat liver 3 alpha-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs
    • Askonas L.J., Ricigliano J.W., Penning T.M. The kinetic mechanism catalysed by homogeneous rat liver 3 alpha-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs. Biochem. J. 278:1991;835-841.
    • (1991) Biochem. J. , vol.278 , pp. 835-841
    • Askonas, L.J.1    Ricigliano, J.W.2    Penning, T.M.3
  • 23
    • 0028837692 scopus 로고
    • Human aldose reductase: Rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme
    • Grimshaw C.E., Bohren K.M., Lai C.J., Gabbay K.H. Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme. Biochemistry. 34:1995;14356-14365.
    • (1995) Biochemistry , vol.34 , pp. 14356-14365
    • Grimshaw, C.E.1    Bohren, K.M.2    Lai, C.J.3    Gabbay, K.H.4
  • 24
    • 0033564742 scopus 로고    scopus 로고
    • The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3 alpha-hydroxysteroid dehydrogenase, a representative aldo-keto reductase
    • Ratnam K., Ma H., Penning T.M. The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3 alpha-hydroxysteroid dehydrogenase, a representative aldo-keto reductase. Biochemistry. 38:1999;7856-7864.
    • (1999) Biochemistry , vol.38 , pp. 7856-7864
    • Ratnam, K.1    Ma, H.2    Penning, T.M.3
  • 26
    • 0035071208 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the human type 3 3-alpha-hydroxysteroid dehydrogenase at 1.8 Å resolution
    • Zhu D.W., Cantin L., Nahoum V., Rehse P., Luu-The V., Labrie F., et al. Crystallization and preliminary X-ray crystallographic analysis of the human type 3 3-alpha-hydroxysteroid dehydrogenase at 1.8 Å resolution. Acta Crystallog. sect. D. 57:2001;589-591.
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 589-591
    • Zhu, D.W.1    Cantin, L.2    Nahoum, V.3    Rehse, P.4    Luu-The, V.5    Labrie, F.6
  • 27
    • 0035834637 scopus 로고    scopus 로고
    • Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-Å resolution
    • Nahoum V., Gangloff A., Legrand P., Zhu D.W., Cantin L., Zhorov B.S., et al. Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-Å resolution. J. Biol. Chem. 276:2001;42091-42098.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42091-42098
    • Nahoum, V.1    Gangloff, A.2    Legrand, P.3    Zhu, D.W.4    Cantin, L.5    Zhorov, B.S.6
  • 28
  • 29
    • 0035964182 scopus 로고    scopus 로고
    • Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate
    • Jin Y., Stayrook S.E., Albert R.H., Palackal N.T., Penning T.M., Lewis M. Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate. Biochemistry. 40:2001;10161-10168.
    • (2001) Biochemistry , vol.40 , pp. 10161-10168
    • Jin, Y.1    Stayrook, S.E.2    Albert, R.H.3    Palackal, N.T.4    Penning, T.M.5    Lewis, M.6
  • 31
    • 0028222097 scopus 로고
    • Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: Enzyme kinetics and crystal structure of the Y48H mutant enzyme
    • Bohren K.M., Grimshaw C.E., Lai C.J., Harrison D.H., Ringe D., Petsko G.A., Gabbay K.H. Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry. 33:1994;2021-2032.
    • (1994) Biochemistry , vol.33 , pp. 2021-2032
    • Bohren, K.M.1    Grimshaw, C.E.2    Lai, C.J.3    Harrison, D.H.4    Ringe, D.5    Petsko, G.A.6    Gabbay, K.H.7
  • 32
    • 0028274855 scopus 로고
    • Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily
    • Hoog S.S., Pawlowski J.E., Alzari P.M., Penning T.M., Lewis M. Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc. Natl Acad. Sci. USA. 91:1994;2517-2521.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2517-2521
    • Hoog, S.S.1    Pawlowski, J.E.2    Alzari, P.M.3    Penning, T.M.4    Lewis, M.5
  • 33
    • 0030907884 scopus 로고    scopus 로고
    • Identification of amino acid residues responsible for differences in substrate specificity and inhibitor sensitivity between two human liver dihydrodiol dehydrogenase isoenzymes by site-directed mutagenesis
    • Matsuura K., Deyashiki Y., Sato K., Ishida N., Miwa G., Hara A. Identification of amino acid residues responsible for differences in substrate specificity and inhibitor sensitivity between two human liver dihydrodiol dehydrogenase isoenzymes by site-directed mutagenesis. Biochem. J. 323:1997;61-64.
    • (1997) Biochem. J. , vol.323 , pp. 61-64
    • Matsuura, K.1    Deyashiki, Y.2    Sato, K.3    Ishida, N.4    Miwa, G.5    Hara, A.6
  • 34
    • 0032400498 scopus 로고    scopus 로고
    • Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: Probing with chimaeric enzymes
    • Matsuura K., Hara A., Deyashiki Y., Iwasa H., Kume T., Ishikura S., et al. Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: probing with chimaeric enzymes. Biochem. J. 336:1998;429-436.
    • (1998) Biochem. J. , vol.336 , pp. 429-436
    • Matsuura, K.1    Hara, A.2    Deyashiki, Y.3    Iwasa, H.4    Kume, T.5    Ishikura, S.6
  • 35
    • 0033612962 scopus 로고    scopus 로고
    • Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: Changing specificity from androgens to progestins
    • Ma H., Penning T.M. Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins. Proc. Natl Acad. Sci. USA. 96:1999;11161-11166.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11161-11166
    • Ma, H.1    Penning, T.M.2
  • 36
    • 0029846857 scopus 로고    scopus 로고
    • The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity
    • Barski O.A., Gabbay K.H., Bohren K.M. The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity. Biochemistry. 35:1996;14276-14280.
    • (1996) Biochemistry , vol.35 , pp. 14276-14280
    • Barski, O.A.1    Gabbay, K.H.2    Bohren, K.M.3
  • 40
    • 0029593494 scopus 로고
    • Characteristics of human types 1, 2 and 3 17 beta-hydroxysteroid dehydrogenase activities: Oxidation/reduction and inhibition
    • Luu-The V., Zhang Y., Poirier D., Labrie F. Characteristics of human types 1, 2 and 3 17 beta-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition. J. Steroid Biochem. Mol. Biol. 55:1995;581-587.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 581-587
    • Luu-The, V.1    Zhang, Y.2    Poirier, D.3    Labrie, F.4
  • 41
    • 0034287545 scopus 로고    scopus 로고
    • Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: Functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
    • Penning T.M., Burczynski M.E., Jez J.M., Hung C.F., Lin H.K., Ma H., et al. Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. Biochem. J. 351:2000;67-77.
    • (2000) Biochem. J. , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6
  • 42
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26:1993;795-800.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 43
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 44
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 46
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D. 53:1997;240-255.
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-947.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-947
    • Kraulis, P.J.1
  • 48
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.