Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Jamie A. Ashby"'
Publikováno v:
PLoS ONE, Vol 6, Iss 1, p e15873 (2011)
Pea encodes eukaryotic translation initiation factor eIF4E (eIF4E(S)), which supports the multiplication of Pea seed-borne mosaic virus (PSbMV). In common with hosts for other potyviruses, some pea lines contain a recessive allele (sbm1) encoding a m
Externí odkaz:
https://doaj.org/article/ceb18e25cb1b408b970729468fea9a5d
Autor:
Federico Comitani, Dominic Botten, Sarah C. R. Lummis, Jamie A. Ashby, Netta Cohen, Carla Molteni
Publikováno v:
Journal of Computer-Aided Molecular Design
The resistance to dieldrin (RDL) receptor is an insect pentameric ligand-gated ion channel (pLGIC). It is activated by the neurotransmitter γ-aminobutyric acid (GABA) binding to its extracellular domain; hence elucidating the atomistic details of th
Autor:
Jamie A. Ashby, Dennis A. Dougherty, Neil J. Harrison, Darren L. Beene, Jinti Wang, Sarah C. R. Lummis, Katherine S. Millen
Publikováno v:
ACS Chemical Neuroscience
The ligand binding site of Cys-loop receptors is dominated by aromatic amino acids. In GABA(C) receptors, these are predominantly tyrosine residues, with a number of other aromatic residues located in or close to the binding pocket. Here we examine t
Autor:
Jamie A. Ashby, Kerry L. Price, Dennis A. Dougherty, Netta Cohen, Sarah C. R. Lummis, Federico Comitani, Ian McGonigle, Carla Molteni
RDL receptors are GABA-activated inhibitory Cys-loop receptors found throughout the insect CNS. They are a key target for insecticides. Here, we characterize the GABA binding site in RDL receptors using computational and electrophysiological techniqu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d72d9d152ec2067414aa3309d375e02d
https://resolver.caltech.edu/CaltechAUTHORS:20130104-082120331
https://resolver.caltech.edu/CaltechAUTHORS:20130104-082120331
Cys-loop receptor binding sites characteristically possess an “aromatic box,” where several aromatic amino acid residues surround the bound ligand. A cation-π interaction between one of these residues and the natural agonist is common, although
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9cef480db15402dfcd2eebd7c568c96
https://resolver.caltech.edu/CaltechAUTHORS:20110912-080631961
https://resolver.caltech.edu/CaltechAUTHORS:20110912-080631961
Crystallization and preliminary X-ray analysis of eukaryotic initiation factor 4E from Pisum sativum
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 65(Pt 8)
Crystals of an N-terminally truncated 20 kDa fragment of Pisum sativum eIF4E (DeltaN-eIF4E) were grown by vapour diffusion. X-ray data were recorded to a resolution of 2.2 A from a single crystal in-house. Indexing was consistent with primitive monoc