Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Michele A. McGuirl"'
Autor:
Michele A. McGuirl, Xu Qi
Publikováno v:
Biochemical and Biophysical Research Communications. 503:32-37
Conversion of prion protein (PrP) from its α-helical form to a β-sheet rich scrapie form constitutes the key event of the etiology of prion diseases. Fundamental questions remain concerning the functions of prion protein and the mechanisms leading
Autor:
Michele A. McGuirl, Xu Qi
Publikováno v:
Biochemical and biophysical research communications. 504(1)
Publikováno v:
Biochemistry. 46:4850-4860
Two conformational isomers of recombinant hamster prion protein (residues 90-232) have been probed by reaction with two tyrosine nitration reagents, peroxynitrite and tetranitromethane. Two conserved tyrosine residues (tyrosines 149 and 150) are not
Publikováno v:
Analytical Biochemistry. 362:89-97
The ability to adsorb proteins and enzymes on electrode surfaces enhances opportunities for studying enzyme activity and redox-based catalysis. Proteins may be bound in a chosen orientation on surfaces so that specific sites within them may be prefer
Publikováno v:
Biochemistry. 45:12240-12252
The formation of the unique catalytic tetranuclear copper cluster (CuZ) of nitrous oxide reductase, N2OR, requires the coexpression of a multiprotein assembly apparatus encoded by the nosDFYL operon. NosL, one of the proteins encoded by this transcri
Publikováno v:
Protein Expression and Purification. 47:162-170
We report here the development of a robust recombinant expression system for Drosophila melanogaster tyramine beta-monooxygenase (TbetaM), the insect analog of mammalian dopamine beta-monooxygenase. Recombinant TbetaM is rapidly purified from the hos
Autor:
Harry B. Gray, John H. Richards, Michele A. McGuirl, Chalita Thanyakoop, Jay R. Winkler, Jennifer C. Lee, Julia G. Lyubovitsky
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1619:23-28
The cytochrome (cyt) c', cyt c(556), and cyt c(2) genes from Rhodopseudomonas palustris have been cloned; recombinant cyt c' and cyt c(556) have been expressed, purified, and characterized. Unlike mitochondrial cyt c, these two proteins are structura
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 6:189-195
NosL, one of the accessory proteins of the nos (nitrous oxide reductase) gene cluster, has been heterologously expressed, purified, and characterized. NosL is a monomeric protein of 18,540 MW that specifically and stoichiometrically binds Cu(I). The
Autor:
Michele A. McGuirl, David M. Dooley
Publikováno v:
Current Opinion in Chemical Biology. 3:138-144
Major advances have been made during 1997 and 1998 toward understanding the structure/function relationships of the active sites in copper-containing oxidases. Central to this progress has been the elucidation of crystal structures for many of these
Publikováno v:
Journal of Inorganic Biochemistry. 70:155-169
The nitrous oxide (N2O) reductase (nos) gene cluster from Achromobacter cycloclastes has been cloned and sequenced. Seven protein coding regions corresponding to nosR, nosZ (structural N2O reductase gene), nosD, nosF, nosY, nosL, and nosX are detecte