Zobrazeno 1 - 10
of 96
pro vyhledávání: '"Graeme B. Cox"'
Publikováno v:
Molecular microbiology. 10(2)
At least four genes are known to affect formation of the cytochrome bd-type terminal oxidase of Escherichia coli. In addition to the genes (cydA and cydB) encoding the two constituent subunits of this complex, a further two genes (cydC and cydD) map
Publikováno v:
Antimicrobial Agents and Chemotherapy. 48:2325-2330
We report that the amiloride analogues 5-( N , N -hexamethylene)amiloride and 5-( N , N -dimethyl)amiloride inhibit, at micromolar concentrations, the replication of human immunodeficiency virus type 1 (HIV-1) in cultured human blood monocyte-derived
Publikováno v:
European Biophysics Journal. 31:26-35
The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels and enhances the process of virion budding and release. Mutagenesis studies have shown that the N-terminal transmembrane domain primarily controls both of thes
Publikováno v:
Genetica. 108:239-252
The white, scarlet, and browngenes of Drosophila melanogasterencode ABC transporters involved with the uptake and storage of metabolic precursors to the red and brown eye colour pigments. It has generally been assumed that these proteins are localise
Autor:
Gary Ewart, A. J. Howells, Susan M. Mackenzie, Michael R. Brooker, Graeme B. Cox, Timothy R. Gill
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1419(2):173-185
The white , brown and scarlet genes of Drosophila melanogaster encode proteins which transport guanine or tryptophan (precursors of the red and brown eye colour pigments) and belong to the ABC transporter superfamily. Current models envisage that the
Publikováno v:
Journal of Virology. 73:4230-4238
We have previously reported that the accessory protein Vpr from human immunodeficiency virus type 1 forms cation-selective ion channels in planar lipid bilayers and is able to depolarize intact cultured neurons by causing an inward sodium current, re
Publikováno v:
ResearcherID
The role of glutamate-219 in the a-subunit of the Escherichia coli F0F1-ATPase was examined using site-directed mutagenesis. The replacement of Glu-219 by lysine, alanine or glycine resulted in a partially functional F0F1-ATPase. Combining any of the
Publikováno v:
Synapse. 26:324-327
The effects on the functional properties of the alpha 1 beta 1 GABAA receptor when the 5' (alpha 1 Val260; beta 1 Ile255) hydrophobic amino acids in the second transmembrane (M2) region were changed to threonine were examined. In response to a satura
Publikováno v:
Journal of Membrane Biology. 155:157-166
Functional properties of the alpha1beta1 GABAA receptor changes in a subunit-specific manner when a threonine residue in the M2 region at the 12' position was mutated to glutamine. The rate and extent of desensitization increased in all mutants but t
Autor:
Susan M. Howitt, J D Clements, Bryndis Birnir, Peter W. Gage, M L Tierney, N P Pillai, Graeme B. Cox
Publikováno v:
Journal of Membrane Biology. 154:11-21
The conserved leucine residues at the 9' positions in the M2 segments of alpha1 (L264) and beta1 (L259) subunits of the human GABAA receptor were replaced with threonine. Normal or mutant alpha1 subunits were co-expressed with normal or mutant beta1