By Todd E. Feinberg
It can be the private secret of philosophy, psychology, and neuroscience: how does the mind unite to create the self, the subjective "I"? In Altered Egos, Dr. Todd Feinberg offers a brand new thought of the self, in line with his first-hand adventure as either a psychiatrist and neurologist.
Feinberg first introduces the reader to dozens of interesting situations of sufferers whose issues have ended in what he calls "altered egos": a metamorphosis within the mind that transforms the bounds of the self. He describes sufferers that suffer from "alien hand syndrome" the place one hand may well assault the patient's personal throat, sufferers with frontal lobe harm who invent remarkable tales approximately their lives, paralyzed sufferers who reject and disown one in all their limbs. Feinberg argues that the mind harm suffered by way of those humans has performed extra than just impair convinced functions--it has fragmented their feel of self. After illustrating how those sufferers offer a window into the self and the brain, the writer offers a brand new version of the self that hyperlinks the workings of the mind with precise and private good points of the brain, corresponding to which means, function, and being. Drawing on his personal and different facts, Feinberg explains how the unified self, whereas no longer positioned in a single or one other mind sector, arises out of the spectacular complexity and variety of the brain's part elements.
Lucid, insightful, jam-packed with attention-grabbing case experiences and provocative new rules, Altered Egos delivers to alter the way in which we take into consideration human attention and the production and upkeep of human identification.
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Extra resources for Altered Egos How the Brain Creates the Self
Science 332:1202–1205 Oldham ML, Chen J (2011b) Snapshots of the maltose transporter during ATP hydrolysis. Proc Natl Acad Sci USA 108:15152–15156 Oldham ML, Khare D, Quicho FA, Davidson AL, Chen J (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450:515–521 Oldham ML, Chen S, Chen J (2013) Structural basis for substrate speciﬁcity in the Escherichia coli maltose transport system. Proc Natl Acad Sci USA 110:18132–18137 Patzlaff J, van der Heide T, Poolman B (2003) The ATP/substrate stoichiometry of the ABC transporter OpuA.
2010; Erkens et al. 2011; Berntsson et al. 2012; Yu et al. 2014). The site is formed by residues in the three C-terminal helices of the S-components together with residues in the L1 and L3 loops. These residues create speciﬁc, high-afﬁnity binding sites with Kd values in the low nanomolar range (Erkens and Slotboom 2010; Zhang et al. 2010; Berntsson et al. 2012). The structure of the binding site of ThiT has been shown to be very robust, suggesting that a substantial input of energy, presumably in the form of ATP hydrolysis, is needed to accomplish conformational changes in the binding site to release its substrate (Swier et al.
The helical domains of the NBDs, as well as the coupling helices, rotate over an angle of about 30° upon closure of the MalK dimer, which allows the conformational change in the MalFG dimer. MalFGK2 has been crystallized in complex with the MBP, maltose, and ADP together with phosphate analogs VO4−, AlF4−, or BeF3−, which has provided insight into the mechanism of ATP hydrolysis within the MalK dimer (Oldham and Chen 2011b). The overall structures show the same outward-facing conformation as described above, suggesting that ATP hydrolysis does not force the transporter in a different conformation.
Altered Egos How the Brain Creates the Self by Todd E. Feinberg