Zobrazeno 1 - 6
of 6
pro vyhledávání: '"R A, Hallewell"'
Autor:
James R. Lepock, Peter B. Stathopulos, R. A. Hallewell, H. E. Frey, Elizabeth M. Meiering, R. A. Irani, G. A. Scholz, Jessica A.O. Rumfeldt
Publikováno v:
Proceedings of the National Academy of Sciences. 100:7021-7026
Mutations in Cu/Zn superoxide dismutase (SOD) are associated with the fatal neurodegenerative disorder amyotrophic lateral sclerosis (ALS). There is considerable evidence that mutant SOD has a gain of toxic function; however, the mechanism of this to
Publikováno v:
Journal of Biological Chemistry. 265:21612-21618
The conformational stability and reversibility of unfolding of the human dimeric enzyme Cu Zn superoxide dismutase (HSOD) and the three mutant enzymes constructed by replacement of Cys6 by Ala and Cys111 by Ser, singly and in combination, were determ
Autor:
John A. Tainer, C. L. Fisher, Yi Wang, Maurice Boissinot, L. A. Kuhn, R. A. Hallewell, Pandora Lee
Publikováno v:
Biochemical and biophysical research communications. 190(1)
In order to improve the therapeutic effectiveness of human Cu,Zn superoxide dismutase (HSOD) by targeting it to cell surfaces and increasing its circulatory half-life, we have designed and expressed a heparin-binding derivative of HSOD. This design w
Publikováno v:
Journal of Biological Chemistry. 262:14697-14701
An Escherichia coli double mutant, sodAsodB, that is deficient in both bacterial superoxide dismutases (Mn superoxide dismutase and iron superoxide dismutase) is unable to grow on minimal medium in the presence of oxygen and exhibits increased sensit
Publikováno v:
Journal of Biological Chemistry. 263:1910-1914
To establish some of the necessary steps in the toxic action of paraquat for cultured mammalian cells, we isolated paraquat-resistant HeLa cells after lethal increments in concentration of paraquat in the medium. The paraquat-resistant cells had incr
Publikováno v:
The Journal of biological chemistry. 261(22)
The specificity and reactivity of human alpha 1-proteinase inhibitor has been investigated by in vitro mutagenesis of the reactive site P1 methionine 358 residue to alanine 358 and cysteine 358. A comparison of the second-order association rates of b