M
Mark G. Darlison
Researcher at Edinburgh Napier University
Publications - 127
Citations - 8085
Mark G. Darlison is an academic researcher from Edinburgh Napier University. The author has contributed to research in topics: Receptor & GABAA receptor. The author has an hindex of 40, co-authored 127 publications receiving 7979 citations. Previous affiliations of Mark G. Darlison include University of Cambridge & Nottingham Trent University.
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Journal ArticleDOI
Sequence and functional expression of the GABA A receptor shows a ligand-gated receptor super-family
Peter R. Schofield,Peter R. Schofield,Mark G. Darlison,Norihisa Fujita,David R. Burt,David R. Burt,F. Anne Stephenson,Henry Rodriguez,Lucy Rhee,J. Ramachandran,V. Reale,TA Glencorse,Peter H. Seeburg,Peter H. Seeburg,Eric A. Barnard +14 more
TL;DR: Amino-acid sequences derived from complementary DMAs encoding the α- and β-subunits of the GAB A/ benzo diazepine receptor from bovine brain show homology with other ligand-gated receptor subunits, suggesting that there is a super-family of ion-channel-containing receptors.
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The molecular basis of muscular dystrophy in the mdx mouse: a point mutation
Piotr Sicinski,Yan Geng,Allan S. Ryder-Cook,Eric A. Barnard,Mark G. Darlison,Pene J. Barnard +5 more
TL;DR: Sequence analysis of the amplification products showed that the mdx mouse has a single base substitution within an exon, which causes premature termination of the polypeptide chain.
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Structural and functional basis for GABAA receptor heterogeneity.
Edwin S. Levitan,Peter R. Schofield,Peter R. Schofield,David R. Burt,Lucy Rhee,William Wisden,Martin Köhler,Henry Rodriguez,F. A. Stevenson,Mark G. Darlison,Eric A. Barnard,Peter H. Seeburg +11 more
TL;DR: Two additional cDNAs encoding two additional GABAA receptor α-subunits are isolated, confirming the heterogeneous nature of the receptor/chloride channel complex and demonstrating the molecular basis for it.
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Molecular biology of the GABAA receptor: the receptor/channel superfamily
TL;DR: Complementary DNAs encoding the two subunit types of the brain GABA A receptor have been cloned, revealing its full protein primary structure and it is illuminating to compare these sequences and those of the nicotinic acetylcholine receptor.
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The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component.
TL;DR: The nucleotide sequence of the aceF gene, which encodes the dihydrolipoamide acetyltransferase component (E2) of the pyruvate dehydrogenase complex of Escherichia coli K12, has been determined using the dideoxy chain-termination method and supports conclusions that the acetyl transferase subunit possesses two heterologous domains.