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  • Author: Jörnvall H
  • References

Author: Jörnvall H


References 29 references


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  • Jörnvall H, et al. (2003) Multiplicity of eukaryotic ADH and other MDR forms. Chem Biol Interact 143-144:255-61 PMID:12604211
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  • Persson B, et al. (2003) Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem Biol Interact 143-144:271-8 PMID:12604213
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  • Kallberg Y, et al. (2002) Short-chain dehydrogenases/reductases (SDRs). Eur J Biochem 269(18):4409-17 PMID:12230552
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  • Nordling E, et al. (2002) Differential multiplicity of MDR alcohol dehydrogenases: enzyme genes in the human genome versus those in organisms initially studied. Cell Mol Life Sci 59(6):1070-5 PMID:12169018
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  • Nordling E, et al. (2002) Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-76 PMID:12199705
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  • Jörnvall H, et al. (2001) Variations and constant patterns in eukaryotic MDR enzymes. Conclusions from novel structures and characterized genomes. Chem Biol Interact 130-132(1-3):491-8 PMID:11306070
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  • Jörnvall H, et al. (1999) SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature. FEBS Lett 445(2-3):261-4 PMID:10094468
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  • Persson B, et al. (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7 PMID:10352708
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  • Weeks CM, et al. (1999) Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution. Acta Crystallogr D Biol Crystallogr 55(Pt 1):93-102 PMID:10089399
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  • Johansson K, et al. (1998) Structure of betaine aldehyde dehydrogenase at 2.1 A resolution. Protein Sci 7(10):2106-17 PMID:9792097
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  • Stark M, et al. (1998) Phosphatidate phosphatase--a key enzyme in glycerolipid biosynthesis. Studies on the yeast enzyme. J Protein Chem 17(1):1-7 PMID:9491922
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  • Ramaswamy S, et al. (1996) Crystal structure of cod liver class I alcohol dehydrogenase: substrate pocket and structurally variable segments. Protein Sci 5(4):663-71 PMID:8845755
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  • Fernández MR, et al. (1995) Class III alcohol dehydrogenase from Saccharomyces cerevisiae: structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication. FEBS Lett 370(1-2):23-6 PMID:7649298
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  • Jörnvall H, et al. (1995) Short-chain dehydrogenases/reductases (SDR). Biochemistry 34(18):6003-13 PMID:7742302
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  • Persson B, et al. (1995) Short-chain dehydrogenases/reductases. Adv Exp Med Biol 372:383-95 PMID:7484402
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  • Persson B, et al. (1994) A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins. Eur J Biochem 226(1):15-22 PMID:7957243
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  • Persson B, et al. (1991) Functionally important regions of glucose-6-phosphate dehydrogenase defined by the Saccharomyces cerevisiae enzyme and its differences from the mammalian and insect forms. Eur J Biochem 198(2):485-91 PMID:2040308
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  • Eklund H, et al. (1985) Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry 24(27):8005-12 PMID:2936393
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  • Jeffery J, et al. (1985) Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae: characterization of a reactive lysine residue labeled with acetylsalicylic acid. Biochemistry 24(3):666-71 PMID:3922403
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  • Jörnvall H, et al. (1984) Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family. Eur J Biochem 140(1):17-23 PMID:6368230
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  • Jörnvall H, et al. (1984) Extended superfamily of short alcohol-polyol-sugar dehydrogenases: structural similarities between glucose and ribitol dehydrogenases. FEBS Lett 165(2):190-6 PMID:6420186
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  • Jörnvall H, et al. (1981) Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc Natl Acad Sci U S A 78(7):4226-30 PMID:7027257
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  • Wills C and Jörnvall H (1979) Amino acid substitutions in two functional mutants of yeast alcohol dehydrogenase. Nature 279(5715):734-6 PMID:377102
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  • Wills C and Jörnvall H (1979) The two major isozymes of yeast alcohol dehydrogenase. Eur J Biochem 99(2):323-31 PMID:387413
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  • Woenckhaus C, et al. (1979) Affinity labelling of yeast and liver alcohol dehydrogenases with the NAD analogue 4-(3-bromoacetylpyridinio)butyldiphosphoadenosine. Eur J Biochem 93(1):65-90 PMID:220046
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  • Jörnvall H, et al. (1978) Subunit conformation of yeast alcohol dehydrogenase. J Biol Chem 253(23):8414-9 PMID:361742
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  • Jörnvall H (1977) The primary structure of yeast alcohol dehydrogenase. Eur J Biochem 72(3):425-42 PMID:320000
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  • Jörnvall H, et al. (1975) Modification of alcohol dehydrogenases with two NAD-+-analogues containing reactive substituents on the functional side of the molecule. FEBS Lett 54(2):297-301 PMID:165980
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  • Jörnvall H (1973) Partial similarities between yeast and liver alcohol dehydrogenases. Proc Natl Acad Sci U S A 70(8):2295-8 PMID:4599620
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