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Anthony L. Albiston

Researcher at University of Melbourne

Publications -  65
Citations -  4938

Anthony L. Albiston is an academic researcher from University of Melbourne. The author has contributed to research in topics: Angiotensin II & Receptor. The author has an hindex of 35, co-authored 65 publications receiving 4747 citations. Previous affiliations of Anthony L. Albiston include Prince Henry's Institute of Medical Research & Florey Institute of Neuroscience and Mental Health.

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Journal ArticleDOI

Cloning and tissue distribution of the human 1 lβ-hydroxysteroid dehydrogenase type 2 enzyme

TL;DR: The 11β-hydroxysteroid dehydrogenase (11βHSD) as mentioned in this paper was found to protect the nonselective mineralocorticoid receptor from occupation by glucocorticity, and to modulate access of glucoc Corticoid to glucoc corticoid receptors resulting in protection of the fetus and gonads.
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The brain renin-angiotensin system: location and physiological roles

TL;DR: Immunohistochemical and neuropharmacological studies suggest that angiotensinergic neural pathways and angiotENSin peptides are important in neural function and may have important homeostatic roles, particularly related to cardiovascular function, osmoregulation and thermoregulating.
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Evidence That the Angiotensin IV (AT4) Receptor Is the Enzyme Insulin-regulated Aminopeptidase

TL;DR: It is demonstrated that the AT4ceptor is IRAP and proposed that AT4 receptor ligands may exert their effects by inhibiting the catalytic activity of IRAP thereby extending the half-life of its neuropeptide substrates.
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The angiotensin IV/AT4 receptor.

TL;DR: Three hypotheses for the memory-potentiating effects of the AT(4) receptor/IRAP ligands, Ang IV and LVV-hemorphin 7, are proposed: acting as potent inhibitors of IRAP, they may prolong the action of endogenous promnestic peptides, and they may modulate glucose uptake by modulating trafficking of GLUT4.
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Receptor activity modifying proteins.

TL;DR: A review of the current state of knowledge of the mechanisms underlying RAMP function examines the role of G protein-coupled receptor interaction with the CT receptor (CTR) gene product.