Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Frank Rusnak"'
Publikováno v:
Journal of Bacteriology. 186:5427-5431
Isoniazid (INH), a front-line antituberculosis agent, is activated by mycobacterial catalase-peroxidase KatG, converting INH into bactericidal reactive species. Here we investigated the requirements and the pathway of nitric oxide (NO˙) generation d
Autor:
Frank Rusnak, Tiffany A. Reiter
Publikováno v:
Biochemistry. 43:782-790
Bacteriophage lambda protein phosphatase (lambdaPP) is a member of a large superfamily of metallophosphoesterases, including serine/threonine protein phosphatases, purple acid phosphatases, 5'-nucleotidase, and DNA repair enzymes such as Mre11. Membe
Autor:
David G. Kehres, Scott W. Bearden, Carson J. La Vake, Frank Rusnak, Justin D. Radolf, Michael E. Maguire, Morgan E. La Vake, Robert D. Perry, Karsten R. O. Hazlett
Publikováno v:
Journal of Biological Chemistry. 278:20687-20694
The Treponema pallidum tro operon encodes an ABC transporter (TroABCD), a transcriptional repressor (TroR), and the essential glycolytic enzyme phosphoglycerate mutase (Gpm). The apparently discordant observations that the solute binding protein (Tro
Publikováno v:
Journal of Inorganic Biochemistry. 93:100-108
The differences in geometry at the metal centres in the two known [Fe–4S] proteins rubredoxin (Rd) and desulforedoxin (Dx) are postulated to be a result of the different spacing of the C-terminal cysteine pair in the two proteins. In order to addre
Publikováno v:
Biochemistry. 41:15404-15409
Bacteriophage lambda protein phosphatase (lambdaPP) is a member of a large family of metal-containing phosphoesterases, including purple acid phosphatase, protein serine/threonine phosphatases, 5'-nucleotidase, and DNA repair enzymes such as Mre11. l
Autor:
Frank Rusnak, Françoise Auchère
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 7:664-667
For three decades, oxidative stress and the role of reactive oxygen species in biology have been extensively studied. Recently, a new interest in these areas has emerged with the discovery of superoxide reductases, a family of familiar bacterial meta
Publikováno v:
Biochemistry. 41:1051-1059
Bacteriophage lambda protein phosphatase (lambdaPP) with Mn(2+) as the activating metal cofactor was studied using phosphatase inhibition kinetics and electron paramagnetic resonance (EPR) spectroscopy. Orthophosphate and the oxoanion analogues ortho
Publikováno v:
Biochemistry. 40:8918-8929
Bacteriophage lambda phosphoprotein phosphatase (lambdaPP) has structural similarity to the mammalian Ser/Thr phosphoprotein phosphatases (PPPs) including the immunosuppressant drug target calcineurin. PPPs possess a conserved active site containing
Autor:
Frank Rusnak, Nancy L. Wengenack
Publikováno v:
Biochemistry. 40:8990-8996
The antitubercular agent isoniazid can be activated by Mycobacterium tuberculosis KatG using either a peroxidase compound I/II or a superoxide-dependent oxyferrous pathway. The identity of activated isoniazid is unknown, but it has been suggested tha
Publikováno v:
Journal of Biological Chemistry. 276:835-843
Pneumocystis carinii is an opportunistic fungal pathogen phylogenetically related to the fission yeast Schizosaccharomyces pombe. P. carinii causes severe pneumonia in immunocompromised patients with AIDS and malignancies. Although the life cycle of