Alton Meister

Affiliations: 
Biochemistry Weill Cornell Medical College, New York, NY, United States 
Area:
glutathione
Website:
http://www.asbmb.org/uploadedfiles/aboutus/asbmb_history/past_presidents/1970s/1977Meister.html
Google:
"Alton Meister"
Bio:

(1922 - 1995)
http://www.nasonline.org/member-directory/deceased-members/52647.html

Mean distance: 39813
 
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Publications

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Ye GJ, Breslow EB, Meister A, et al. (1997) The amino acid sequence of rat kidney 5-oxo-L-prolinase determined by cDNA cloning. The Journal of Biological Chemistry. 271: 32293-300
Smith TK, Ikeda Y, Fujii J, et al. (1995) Different sites of acivicin binding and inactivation of gamma-glutamyl transpeptidases. Proceedings of the National Academy of Sciences of the United States of America. 92: 2360-2364
Huang CS, He W, Meister A, et al. (1995) Amino acid sequence of rat kidney glutathione synthetase. Proceedings of the National Academy of Sciences of the United States of America. 92: 1232-6
Ikeda Y, Fujii J, Taniguchi N, et al. (1995) Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain Proceedings of the National Academy of Sciences of the United States of America. 92: 126-130
Jain A, Madsen DC, Auld PAM, et al. (1995) L-2-oxothiazolidine-4-carboxylate, a cysteine precursor, stimulates growth and normalizes tissue glutathione concentrations in rats fed a sulfur amino acid-deficient diet. Journal of Nutrition. 125: 851-856
Meister A. (1995) [1] Glutathione metabolism Methods in Enzymology. 251: 3-7
Meister A. (1995) Mitochondrial changes associated with glutathione deficiency Biochimica Et Biophysica Acta. 1271: 35-42
Meister A. (1995) [3] Glutathione biosynthesis and its inhibition Methods in Enzymology. 252: 26-30
Smith TK, Meister A. (1995) Chemical modification of active site residues in gamma-glutamyl transpeptidase. Aspartate 422 and cysteine 453. Journal of Biological Chemistry. 270: 12476-12480
Ikeda Y, Fujii J, Taniguchi N, et al. (1995) Human γ-Glutamyl Transpeptidase Mutants Involving Conserved Aspartate Residues and the Unique Cysteine Residue of the Light Subunit Journal of Biological Chemistry. 270: 12471-12475
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