Don Straus

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We have developed a technique, called genomic subtraction, for isolating the DNA that is absent in deletion mutants. The method removes from wild-type DNA the sequences that are present in both the wild-type and the deletion mutant genomes. The DNA that corresponds to the deleted region remains. Enrichment for the deleted sequences is achieved by allowing a(More)
CTLA-4, a negative regulator of T cell function, was found to associate with the T cell receptor (TCR) complex zeta chain in primary T cells. The association of TCRzeta with CTLA-4, reconstituted in 293 transfectants, was enhanced by p56(lck)-induced tyrosine phosphorylation. Coexpression of the CTLA-4-associated tyrosine phosphatase, SHP-2, resulted in(More)
The essential catalytic base at the active site of the glycolytic enzyme triosephosphate isomerase is the carboxylate group of Glu-165, which directly abstracts either the 1-pro-R proton of dihydroxyacetone phosphate or the 2-proton of (R)-glyceraldehyde 3-phosphate to yield the cis-enediol intermediate. Using the methods of site-directed mutagenesis, we(More)
BACKGROUND The power and simplicity of visual colony counting have made it the mainstay of microbiological analysis for more than 130 years. A disadvantage of the method is the long time required to generate visible colonies from cells in a sample. New rapid testing technologies generally have failed to maintain one or more of the major advantages of(More)
  • Nigam, I M Held, Giese, J A Carton, S Nigam, Fennessy +9 others
  • 2011
1983: The influence of a critical latitude on topographically forced stationary waves in a barotropic model. On the role of sea surface temperature gradients in forcing low-level winds and convergence in the tropics. The sensitivity of stationary waves to variations in the basic state zonal flow. On the structure of variability of the observed tropospheric(More)
The essential basic residue at the active site of the glycolytic enzyme triosephosphate isomerase is Glu-165, which is responsible for the abstraction of either the 1-pro-R proton of dihydroxyacetone phosphate or of the 2-proton of D-glyceraldehyde 3-phosphate, in the enolization steps that constitute the reaction catalysed by this enzyme. We have changed(More)
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