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Luteinizing hormone response to an oestradiol challenge in 5 intersex pigs possessing ovotestes (1989)
Journal Article
Chalmers, C., Cook, B., Foxcroft, G. R., & Hunter, R. H. F. (1989). Luteinizing hormone response to an oestradiol challenge in 5 intersex pigs possessing ovotestes. Reproduction, 87(2), 455-461. https://doi.org/10.1530/jrf.0.0870455

After challenge with oestradiol benzoate, the mean maximum LH concentration in 5 XX intersex pigs possessing ovarian and testicular tissue, or only testicular tissue, was 2\m=.\10(\m=+-\0\m=.\41)ng/ml compared with 8\m=.\9ng/ml in mature domestic gil... Read More about Luteinizing hormone response to an oestradiol challenge in 5 intersex pigs possessing ovotestes.

Localization of GABAA receptor α-subunit mRNAs in relation to receptor subtypes (1989)
Journal Article
Wisden, W., Morris, B. J., Darlison, M. G., Hunt, S. P., & Barnard, E. A. (1989). Localization of GABAA receptor α-subunit mRNAs in relation to receptor subtypes. Molecular Brain Research, 5(4), 305-310. https://doi.org/10.1016/0169-328x%2889%2990065-x

The distribution of 3 {GABAA} receptor α-subunit mRNAs in various regions of bovine brain has been investigated using in situ hybridization. Whereas the α2- and α3-transcripts are of low abundance in all regions except striatum, the α1-transcript is... Read More about Localization of GABAA receptor α-subunit mRNAs in relation to receptor subtypes.

The molecular basis of muscular dystrophy in the mdx mouse: a point mutation (1989)
Journal Article
Sicinski, P., Geng, Y., Ryder-Cook, A., Barnard, E., Darlison, M., & Barnard, P. (1989). The molecular basis of muscular dystrophy in the mdx mouse: a point mutation. Science, 244(4912), 1578-1580. https://doi.org/10.1126/science.2662404

The mdx mouse is an X-linked myopathic mutant, an animal model for human Duchenne muscular dystrophy. In both mouse and man the mutations lie within the dystrophin gene, but the phenotypic differences of the disease in the two species confer much int... Read More about The molecular basis of muscular dystrophy in the mdx mouse: a point mutation.

Brain α-Neurotoxin-Binding Proteins and Nicotinic Acetylcholine Receptors (1988)
Book Chapter
Darlison, M. G., Hicks, A. A., Cockcroft, V. B., Squire, M. D., & Barnard, E. A. (1988). Brain α-Neurotoxin-Binding Proteins and Nicotinic Acetylcholine Receptors. In Cellular and Molecular Basis of Synaptic Transmission (475-492). Springer. https://doi.org/10.1007/978-3-642-73172-3_32

The study of the nicotinic acetylcholine receptor (AChR) of skeletal muscle and fish electric organ has been greatly facilitated by the application of the α-neurotoxins (postsynaptic toxins) of elapid and hydrophid snake venoms, such as α-bungarotoxi... Read More about Brain α-Neurotoxin-Binding Proteins and Nicotinic Acetylcholine Receptors.

Pharmacology, Cloning and Expression of Insect Nicotinic Acetylcholine Receptors (1988)
Book Chapter
Marshall, J., David, J. A., Darlison, M. G., Barnard, E. A., & Sattelle, D. B. (1988). Pharmacology, Cloning and Expression of Insect Nicotinic Acetylcholine Receptors. In Nicotinic Acetylcholine Receptors in the Nervous System (257-281). Springer. https://doi.org/10.1007/978-3-642-74167-8_20

There is considerable evidence that acetylcholine is an excitatory neurotransmitter at many synapses in the insect central nervous system (Sattelle 1986). Despite the acute technical difficulties of proving that a putative transmitter exerts a functi... Read More about Pharmacology, Cloning and Expression of Insect Nicotinic Acetylcholine Receptors.

Distinct GABAA receptor α subunit mRNAs show differential patterns of expression in bovine brain (1988)
Journal Article
Wisden, W., Morris, B. J., Darlison, M. G., Hunt, S. P., & Barnard, E. A. (1988). Distinct GABAA receptor α subunit mRNAs show differential patterns of expression in bovine brain. Neuron, 1(10), 937-947. https://doi.org/10.1016/0896-6273%2888%2990151-1

Specific oligonucleotide probes have been used to visualize the regional and cellular distribution of the mRNAs encoding three structurally distinct GABA A receptor α subunits in bovine brain. In situ hybridization analysis showed that these transcri... Read More about Distinct GABAA receptor α subunit mRNAs show differential patterns of expression in bovine brain.

Structural and functional basis for GABAA receptor heterogeneity (1988)
Journal Article
Levitan, E. S., Schofield, P. R., Burt, D. R., Rhee, L. M., Wisden, W., Köhler, M., Fujita, N., Rodriguez, H. F., Stephenson, A., Darlison, M. G., Barnard, E. A., & Seeburg, P. H. (1988). Structural and functional basis for GABAA receptor heterogeneity. Nature, 335(6185), 76-79. https://doi.org/10.1038/335076a0

When γ-aminobutyric acid (GABA), the major inhibitory neurotransmitter in vertebrate brain, binds to its receptor it activates a chloride channel. Neurotransmitter action at the GABAA receptor is potentiated by both benzodiazepines and barbiturates w... Read More about Structural and functional basis for GABAA receptor heterogeneity.

Molecular biology of the GABAA receptor: the receptor/channel superfamily (1987)
Journal Article
Barnard, E. A., Darlison, M. G., & Seeburg, P. (1987). Molecular biology of the GABAA receptor: the receptor/channel superfamily. Trends in Neurosciences, 10(12), 502-509. https://doi.org/10.1016/0166-2236%2887%2990130-5

Complementary DNAs encoding the two subunit types of the brain GABAA receptor have been cloned, revealing its full protein primary structure1. In another laboratory, the same point has now been reached for one of the subunits of the spinal cord glyci... Read More about Molecular biology of the GABAA receptor: the receptor/channel superfamily.

Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-family (1987)
Journal Article
Schofield, P. R., Darlison, M. G., Fujita, N., Burt, D. R., Stephenson, F. A., Rodriguez, H., Rhee, L. M., Ramachandran, J., Reale, V., Glencorse, T. A., Seeburg, P. H., & Barnard, E. A. (1987). Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-family. Nature, 328(6127), 221-227. https://doi.org/10.1038/328221a0

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-chann... Read More about Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-family.

The Molecular Biology of Acetylcholine Receptors from the Vertebrate Peripheral and Central Nervous Systems (1986)
Book Chapter
Jackson, J. F., Beeson, D. M. W., Cockcroft, V. B., Darlison, M. G., Conti-Tronconi, B. M., Bell, L. D., & Barnard, E. A. (1986). The Molecular Biology of Acetylcholine Receptors from the Vertebrate Peripheral and Central Nervous Systems. Molecular Aspects of Neurobiology (66-74). Springer. https://doi.org/10.1007/978-3-642-70690-5_13

Nicotinic acetylcholine receptors (AChR) mediate chemical communication at synapses in many parts of the vertebrate nervous system, including neuromuscular junctions, autonomic ganglia, and certain sites in the brain. This occurs through the interact... Read More about The Molecular Biology of Acetylcholine Receptors from the Vertebrate Peripheral and Central Nervous Systems.

Molecular Biology of Nicotinic Acetylcholine Receptors from Chicken Muscle and Brain (1986)
Book Chapter
Squire, M. D., Moss, S. J., Lai, F. A., Darlison, M. G., Cockcroft, V. B., Barnard, E. A., Beeson, D. M. W., Hicks, A. A., Darlison, M. G., & Ross, S. J. (1986). Molecular Biology of Nicotinic Acetylcholine Receptors from Chicken Muscle and Brain. In A. Maelicke (Ed.), Nicotinic Acetylcholine Receptor (389-415). Springer. https://doi.org/10.1007/978-3-642-71649-2_30

While it has been completely established that the AChR** as isolated from the electroplaques of electric fish is composed of four different polypeptides, such that its subunit structure is α2βγδ (as reviewed in detail elsewhere in this Volume), the e... Read More about Molecular Biology of Nicotinic Acetylcholine Receptors from Chicken Muscle and Brain.

Investigation of the substrate binding sites of elastase (1986)
Thesis
Shah, V. K. Investigation of the substrate binding sites of elastase. (Thesis). Napier College of Commerce and Technology. http://researchrepository.napier.ac.uk/id/eprint/6047

Studies of pancreatic elastase were undertaken to examine substrate binding and of human leukocyte elastase to try to gain insight into the disease, pulmonary emphysema. Porcine pancreatic elastase was inhibited by various inhibitors p-toluene sulpho... Read More about Investigation of the substrate binding sites of elastase.

Acute hypotension due to platelet serotonin-induced chemoreflexes after intravenous injection of dextran sulfate in the rabbit (1985)
Journal Article
Wiggins, R. C., Glatfelter, A., Campbell, A. M., Kunkel, R. G., & Ulevitch, R. J. (1985). Acute hypotension due to platelet serotonin-induced chemoreflexes after intravenous injection of dextran sulfate in the rabbit. Circulation Research, 57(2), 262-277. https://doi.org/10.1161/01.res.57.2.262

The hypotension and bradycardia observed after intravenous injection of dextran sulfate in rabbits was prevented by prior depletion of circulating platelets, but was not prevented by depletion of the third component of complement or Hageman factor. D... Read More about Acute hypotension due to platelet serotonin-induced chemoreflexes after intravenous injection of dextran sulfate in the rabbit.

Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase ofEscherichia coli (1984)
Journal Article
Darlison, M. G., & Guest, J. R. (1984). Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase ofEscherichia coli. Biochemical Journal, 223(2), 507-517. https://doi.org/10.1042/bj2230507

The nucleotide sequence of a 961 base-pair segment of DNA containing the sdhB gene, which encodes the iron-sulphur protein subunit of the E. coli succinate dehydrogenase, has been determined. The sdhB structural gene comprises 711 base pairs (237 cod... Read More about Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase ofEscherichia coli.

Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli (1984)
Journal Article
Wood, D., Darlison, M. G., Wilde, R. J., & Guest, J. R. (1984). Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. The biochemical journal, 222(2), 519-534. https://doi.org/10.1042/bj2220519

The nucleotide sequence of a 3614 base-pair segment of DNA containing the sdhA gene, encoding the flavoprotein subunit of succinate dehydrogenase of Escherichia coli, and two genes sdhC and sdhD, encoding small hydrophobic subunits, has been determin... Read More about Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli.

Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12 (1984)
Journal Article
Darlison, M. G., Spencer, M. E., & Guest, J. R. (1984). Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. European journal of biochemistry / FEBS, 141(2), 351-359. https://doi.org/10.1111/j.1432-1033.1984.tb08199.x

The nucleotide sequence of a 3180‐base‐pair segment of DNA, containing the sucA gene encoding the 2‐oxoglutarate dehydrogenase component (E1o) of the 2‐oxoglutarate dehydrogenase complex of Escherichia coli, has been determined by the dideoxy chain‐t... Read More about Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12.

Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase (1984)
Journal Article
Spencer, M. E., Darlison, M. G., Stephens, P. E., Duckenfield, I. K., & Guest, J. R. (1984). Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase. European journal of biochemistry / FEBS, 141(2), 361-374. https://doi.org/10.1111/j.1432-1033.1984.tb08200.x

The nucleotide sequence of the sucB gene, which encodes the dihydrolipoamide succinyltransferase component (E2o) of the 2‐oxoglutarate dehydrogenase complex of Escherichia coli K12, has been determined by the dideoxy chain‐termination method. The res... Read More about Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase.