H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb13996.x/fullpdf
Reference21 articles.
1. 1. C.I. Branden, H. Jornvall, B. Furugren, and P. D Boyer (1975 ) inThe enzymes () 3rd edn , vol. 11 , pp.103 -190 , Academic Press, New York and London.
2. Zinc isotope exchange in horse liver alcohol dehydrogenase
3. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution
4. Structural relationships among class I isozymes of human liver alcohol dehydrogenase
5. Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.
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1. Medium- and short-chain dehydrogenase/reductase gene and protein families;Cellular and Molecular Life Sciences;2008-11-14
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3. On the Competition for Available Zinc;Journal of Biological Chemistry;2005-02
4. Probing the structure of the human Ca2+- and Zn2+-binding protein S100A3: spectroscopic investigations of its transition metal ion complexes, and three-dimensional structural model;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1998-12
5. Analytical Approaches to Alcohol Dehydrogenase Structures;Advances in Experimental Medicine and Biology;1995
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