Herbert Weissbach

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Cumulative oxidative damages to cell constituents are considered to contribute to aging and age-related diseases. The enzyme peptide methionine sulfoxide reductase A (MSRA) catalyzes the repair of oxidized methionine in proteins by reducing methionine sulfoxide back to methionine. However, whether MSRA plays a role in the aging process is poorly understood.(More)
The reduction of methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr). The MsrA and MsrB families can reduce free MetO and MetO within a peptide or protein context. This process is stereospecific with the S- and R-forms of MetO repaired by MsrA and MsrB, respectively. Cell extracts from an MsrA(-)B(-) knockout of Escherichia coli(More)
In 18 of 20 patients with psychosis secondary to systemic lupus erythematosus (SLE), autoantibodies to ribosomal P proteins were detected by immunoblotting and measured with a new radioimmunoassay using a synthetic peptide as antigen. The frequency of anti-P was not increased in patients with other central nervous system manifestations of SLE (3 of 20, by(More)
The demonstration of the hormone mclatonin (N-acetyl-Bmethoxytryptamine) in bovine pineal gland (1) prompted a study of the enzymes involved in its formation and metabolism. In preliminary studies (2, 3) we described an enzyme, hydroxyindole-O-methyl transferase, in the pineal gland of cows, that catalyzes the 0-methylation of N-acetyl-serotonin to(More)
Sulindac is an FDA-approved non-steroidal anti-inflammatory drug with documented anticancer activities. Our recent studies showed that sulindac selectively enhanced the killing of cancer cells exposed to oxidizing agents via production of reactive oxygen species (ROS) resulting in mitochondrial dysfunction. This effect of sulindac and oxidative stress on(More)
An enzyme that reduces methionine sulfoxide [Met(O)] residues in proteins [peptide Met(O) reductase (MsrA), EC 1.8.4.6; originally identified in Escherichia coli] was purified from bovine liver, and the cDNA encoding this enzyme was cloned and sequenced. The mammalian homologue of E. coli msrA (also called pmsR) cDNA encodes a protein of 255 amino acids(More)
An enzyme that can reduce methionine sulfoxide in proteins was first discovered in Escherichia coli about 25 years ago. It is now apparent that there is a family of enzymes, referred to as methionine sulfoxide reductases (Msr), and in recent years there has been considerable interest in one of the members of the Msr family, MsrA. This enzyme has been shown(More)
An enzyme that catalyzes the reduction of methionine sulfoxide residues in ribosomal protein L12 has been partially purified from Escherichia coli extracts. Methionine sulfoxide present in oxidize [Met]enkephalin is also reduced by the purified enzyme. The enzyme is different from a previously reported E. coli enzyme that catalyzes the reduction of(More)
Reactive oxygen and nitrogen intermediates can cause damage to many cellular components and have been implicated in a number of diseases. Cells have developed a variety of mechanisms to destroy these reactive molecules or repair the damage once it occurs. In proteins one of the amino acids most easily oxidized is methionine, which is converted to methionine(More)