Rubin studies

B Rubin. Studies on the induction of antibody synthesis against sulfanilic acid in rabbits, I. Effect of the number of hapten molecules introduced in homogeneous protein on antibody synthesis against the hapten and the new antigenic determinants. Eur J Immunol 2 5, 1972. 

Random maps have been studied by a large number of different authors, including Kruskal [krus54], Rubin and Sitgreaves [rubin54], Pittel [pittel83] and Kolchin [kolc86]. 

Rubin recently disclosed the synthesis of ortho/meta-I DM 121 [74]. The molecule is formed by dimerization of deprotected 122, which in turn can be synthesized in a few steps and in sizable quantity [Eq. (5)]. The UCLA group was interested in zipping up polyacetylenic systems like 121 to prepare fullerenes (vide infra). Unfortunately, MALDl mass spectroscopic studies showed that 121... 

The importance of lipophilicity to bitterness has been well established, both directly and indirectly. The importance of partitioning effects in bitterness perception has been stressed by Rubin and coworkers, and Gardner demonstrated that the threshold concentration of bitter amino acids and peptides correlates very well with molecular connectivity (which is generally regarded as a steric parameter, but is correlated with the octanol-water partition coefficient ). Studies on the surface pressure in monolayers of lipids from bovine, circumvallate papillae also indicated that there is a very good correlation between the concentration of a bitter compound that is necessary in order to give an increase in the surface pressure with the taste threshold in humans. These results and the observations of others suggested that the ability of bitter compounds to penetrate cell membranes is an important factor in bitterness perception. 

Other early alpha spectrometry studies examined U-series disequilibria in East Pacific Rise (EPR) samples. Newman et al. (1983) measured samples from the RISE study area (21°N EPR) finding significant variations in Th/U and ( °Th)/( U) (Fig. 2B). Rubin and Macdougall (1988) measured ( °Th)/( U) and ( Ra)/( °Th) for samples from both the northern ( 10-12°isn and southern (-20-25°) EPR (Fig. 2C,D). This study was first to document large disequilibria in young MORB and interpreted the... 

R8. Rubin, C. E., Brandborg, L. L., Phelps, P. C., and Taylor, H. C., Jr., Studies of celiac disease. I. The apparent identical and specific nature of the duodenal and proximal jejunal lesion in celiac disease and idiopathic sprue. Gastroenterology 38, 28-49 (1960). 

One of the important consequences of studying catalysis by mutant enzymes in comparison with wild-type enzymes is the possibility of identifying residues involved in catalysis that are not apparent from crystal structure determinations. This has been usefully applied (Fersht et al., 1988) to the tyrosine activation step in tyrosine tRNA synthetase (47) and (49). The residues Lys-82, Arg-86, Lys-230 and Lys-233 were replaced by alanine. Each mutation was studied in turn, and comparison with the wild-type enzyme revealed that each mutant was substantially less effective in catalysing formation of tyrosyl adenylate. Kinetic studies showed that these residues interact with the transition state for formation of tyrosyl adenylate and pyrophosphate from tyrosine and ATP and have relatively minor effects on the binding of tyrosine and tyrosyl adenylate. However, the crystal structures of the tyrosine-enzyme complex (Brick and Blow, 1987) and tyrosyl adenylate complex (Rubin and Blow, 1981) show that the residues Lys-82 and Arg-86 are on one side of the substrate-binding site and Lys-230 and Lys-233 are on the opposite side. It would be concluded from the crystal structures that not all four residues could be simultaneously involved in the catalytic process. Movement of one pair of residues close to the substrate moves the other pair of residues away. It is therefore concluded from the kinetic effects observed for the mutants that, in the wild-type enzyme, formation of the transition state for the reaction involves a conformational change to a structure which differs from the enzyme structure in the complex with tyrosine or tyrosine adenylate. The induced fit to the transition-state structure must allow interaction with all four residues simultaneously. 

Richter CA, Bimbaum LS, Farabollini F, Newbold RR, Rubin BS, Talsness CE, Vandenbergh JG, Walser-Kuntz DR, vom Saal FS (2007) In vivo effects of bisphenol A in laboratory rodent studies. Reprod Toxicol 24 199-224... 

McDonald S, MeyerowitzC, SmudzinT, Rubin P. Preliminary results of a pilot study using WR-2721 before fractionated irradiation of the head and neck to reduce salivary gland dysfunction. Int J Radiat Oncol Biol Phys 1994 29 747-754. 

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