By Robert M. Sapolsky
Publish yr note: First released in 1997
From the writer of the generally acclaimed Why Zebras Don't Get Ulcers, an enlightening standpoint at the unusual drives and intrinsic wishes underlying human habit, and the way they hyperlink us to -- and separate us from -- the remainder of the animal kingdom.
In this wide-ranging number of witty essays, Robert M. Sapolsky brings a marginally of humor and compassion to the area of state of the art technological know-how. His matters diversity from motives of the neurological bases of human individuality to discussions in regards to the philosophical and political implications of contemporary findings in organic study. eventually, Sapolsky confirms that humans are -- with unnerving frequency -- simply one other form of primate.
"Sapolsky is among the top scientist/writers of our time....What emerges in those incredible, wide-ranging essays is a wealthy photograph of human individuality and the way it truly is either limited and liberated through organic fate". -- Oliver Sacks, M.D.
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Extra info for The Trouble with Testosterone: And Other Essays On the Biology of the Human Predicament
R. H. (1972) Effect of gamma-hydroxybutyrate on dopamine and dopamine metabolites in the rat striatum. Biochem. Pharmacol. 21, 2111–21. P. E. (1956) Effects of fatty acid anions on electroencephalogram of unanesthetized rabbits. Am. J. Physiol . 186, 271–78. D. E. (1965) Various seizure activities following γhydroxybutyrate. Int. J. Neuropharmacol . 4, 197–200. Xie X. G. (1992) γ-Hydroxybutyrate hyperpolarizes hippocampal neurones by activating GABAB receptors. Eur. J. Pharmacol . 212, 291–94. , et al.
2). Although receptor homodimers had previously been described for GPCRs (Hébert and Bouvier 1998; Angers et al. 2000), GABAB receptors are the first clear evidence for heterodimerization among GPCRs. The GABAB receptor dimer appears to be the basic building block for most, if not all, GABAB receptors in the brain. In situ hybridization and light microscopic immunohistochemistry revealed their co-localization in agreement with the distribution of GABAB receptor binding sites previously identified by autoradiography (Bischoff et al.
2001; Duthey et al. 2002). A new class of compounds, the positive modulators, binds to the GABAB(2) subunit (Urwyler et al. 2001). These compounds do not activate the receptor on their own; rather they potentiate the efficacy and affinity of agonists on the GABAB receptor, as observed with the benzodiazepines on the GABAA receptor. GHB is not a positive modulator of the GABAB receptor. ) a member of family 3 G protein-coupled receptors (GPGRs). The two most prominent splice variants GABAB(la) and GABAB(lb) differ in their extreme amino-terminal Part of the pharmacological actions of γ-hydroxybutyrate 39 sequence, but share ligand-binding and effector domains.
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