Henry Zodoc Sable

MIcrobiology Western Reserve University, Cleveland, OH, United States 
"Henry Zodoc Sable"
Mean distance: 9.25


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Carl F. Cori grad student 1950 Washington University
 (The metabolism of pentose compounds in yeast and in mammalian tissues)


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Armand J. Guarino grad student 1953 Tufts
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Ahmad TY, Morrisett JD, Pownall HJ, et al. (1990) Cyclopentanoid analogs of dipalmitoyl phosphatidic acid: effect of backbone geometry on thermotropic properties Chemistry and Physics of Lipids. 55: 231-243
Ahmad TY, Morrisett JD, Hancock AJ, et al. (1984) Dipalmitoylcyclopentano phosphatidic acid (DPCPA): Effect of head group geometry on thermotropic behavior Federation Proceedings. 43: no. 3550
Singer MA, Jain MK, Sable HZ, et al. (1983) The properties of membranes formed from cyclopentanoid analogues of phosphatidylcholine Bba - Biomembranes. 731: 373-377
Shreve DS, Holloway MP, Haggerty JC, et al. (1983) The catalytic mechanism of transketolase. Thiamin pyrophosphate-derived transition states for transketolase and pyruvate dehydrogenase are not identical. Journal of Biological Chemistry. 258: 12405-12408
Hancock AJ, Lister MD, Sable HZ. (1982) Analogs of natural lipids. VII. Synthesis of cyclopentanoid analogs of phosphatidylcholine Journal of Lipid Research. 23: 183-189
Weissman JD, Hancock AJ, MacQuarrie R, et al. (1982) DPN-linked sn-glycerol-3-phosphate dehydrogenase. Cyclopentanoid analogues mimic the active rotameric state of the natural substrate. Journal of Biological Chemistry. 257: 3618-3622
Gallo AA, Sable HZ. (1982) Conformational mobility in thiamin and related compounds studied by carbon-13 magnetic relaxation Annals of the New York Academy of Sciences. 78-90
Egan RM, Sable HZ. (1981) Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits. Journal of Biological Chemistry. 256: 4877-4883
Kremer AB, Gibby WA, Gubler CJ, et al. (1980) Synthesis and chemical properties of ethenothiamin Biochemistry. 19: 3773-3780
Kremer AB, Egan RM, Sable HZ. (1980) The active site of transketolase. Two arginine residues are essential for activity. Journal of Biological Chemistry. 255: 2405-2410
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