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K A Wreggett

Showing results (1-10 of 17) with videos related to

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The Biochemical Journal|August 15, 1992
Inositol monophosphatase is a highly conserved enzyme having localized structural similarity to both glycerol 3-phosphate dehydrogenase and haemoglobinK A Wreggett
Journal of Receptor Research|January 1, 1986
Bacterial toxins and the role of ADP-ribosylationK A Wreggett
Biochemical and Biophysical Research Communications|September 30, 1987
Alkylation of the bovine anterior pituitary D2-dopamine receptor: inconsistency with predictions of the ternary complex modelK A Wreggett
Molecular Pharmacology|January 1, 1984
Agonist high- and low-affinity states of the D2-dopamine receptor in calf brain. Partial conversion by guanine nucleotideK A Wreggett, P Seeman
The Biochemical Journal|August 1, 1987
A rapid separation method for inositol phosphates and their isomersK A Wreggett, R F Irvine
Molecular Pharmacology|September 1, 1984
The ternary complex model. Its properties and application to ligand interactions with the D2-dopamine receptor of the anterior pituitary glandK A Wreggett, A De Léan
The Biochemical Journal|September 15, 1989
Automated isocratic high-performance liquid chromatography of inositol phosphate isomersK A Wreggett, R F Irvine
Biochemical and Biophysical Research Communications|June 30, 1993
Evidence for receptor-specific regulation of the metabolism of the second messenger, inositol trisphosphate, in human endothelial cellsK A Wreggett, R F Irvine
The Journal of Biological Chemistry|September 22, 1995
Cooperativity manifest in the binding properties of purified cardiac muscarinic receptorsK A Wreggett, J W Wells
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience|July 1, 1982
Striatal binding of 2-amino-6,7-[3H]dihydroxy-1,2,3,4-tetrahydronaphthalene to two dopaminergic sites distinguished by their low and high affinity for neurolepticsS J List, K A Wreggett, P Seeman
Pageof 2

Showing results (1-10 of 17) with videos related to

Sort By:
Pageof 2
The Biochemical Journal|August 15, 1992
Inositol monophosphatase is a highly conserved enzyme having localized structural similarity to both glycerol 3-phosphate dehydrogenase and haemoglobinK A Wreggett
Journal of Receptor Research|January 1, 1986
Bacterial toxins and the role of ADP-ribosylationK A Wreggett
Biochemical and Biophysical Research Communications|September 30, 1987
Alkylation of the bovine anterior pituitary D2-dopamine receptor: inconsistency with predictions of the ternary complex modelK A Wreggett
Molecular Pharmacology|January 1, 1984
Agonist high- and low-affinity states of the D2-dopamine receptor in calf brain. Partial conversion by guanine nucleotideK A Wreggett, P Seeman
The Biochemical Journal|August 1, 1987
A rapid separation method for inositol phosphates and their isomersK A Wreggett, R F Irvine
Molecular Pharmacology|September 1, 1984
The ternary complex model. Its properties and application to ligand interactions with the D2-dopamine receptor of the anterior pituitary glandK A Wreggett, A De Léan
The Biochemical Journal|September 15, 1989
Automated isocratic high-performance liquid chromatography of inositol phosphate isomersK A Wreggett, R F Irvine
Biochemical and Biophysical Research Communications|June 30, 1993
Evidence for receptor-specific regulation of the metabolism of the second messenger, inositol trisphosphate, in human endothelial cellsK A Wreggett, R F Irvine
The Journal of Biological Chemistry|September 22, 1995
Cooperativity manifest in the binding properties of purified cardiac muscarinic receptorsK A Wreggett, J W Wells
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience|July 1, 1982
Striatal binding of 2-amino-6,7-[3H]dihydroxy-1,2,3,4-tetrahydronaphthalene to two dopaminergic sites distinguished by their low and high affinity for neurolepticsS J List, K A Wreggett, P Seeman
Pageof 2