یادداشتهای مربوط به کتابنامه ، واژه نامه و نمایه های داخل اثر
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Includes bibliographical references and index.
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Front Cover; International Review of Neurobiology, Volume 36; Copyright Page; Contents; Chapter 1. Ca2+, N-Methyl-D-aspartate Receptors, and AIDS-Related Neuronal Injury; I. Introduction; II. Neuronal Loss in the CNS of AIDS Patients; III. gpl20-Induced Neuronal Injury Is Ameliorated by Calcium Channel Anotagonists; IV. Involvement of the NMDA Receptor in gpl20-Induced Neuronal Injury; V. Indirect Neuronal Injury Mediated by HIV-Infected or gp120-Stimulated Monocytic Cells; VI. Possible Involvement of Astrocytes, Oligodendrocytes, and Other HIV-1 Proteins in Neuronal Injury
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I. IntroductionII. Pharmacology of GABAB Receptors; III. Properties of GABAB Receptors; IV. Function of GABAB Receptors; V. Summary and Conclusions; References; Chapter 5.The Role of the Amygdala in Emotional Learning; I. Introduction; II. Morphology; III. Electrophysiology; IV. Anatomical Connections between the Amygdala and Brain Areas Involved in Fear and Anxiety; V. Elicitation of Fear by Electrical or Chemical Stimulation of the Amygdagdala; VI. Effects of Amygdala Lesions on Conditioned Fear; VII. Effects of Amygdala Lesions on Unconditioned Fear
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IX. Signal Transduction via Protein Phosphorylation Regulates the Relative Utilization of APP Processing PathwaysX. Beyond Aß-Amyloid: Other Molecular Factors in Amyloidogenesis and Factors Differentiating Aging-Related Cerebral Amyloidosis from Alzheimer Disease; References; Chapter 3. Molecular Neurobiology of the GABAA Receptor; I. Introduction; II. Pharmacology of the GABAA Receptor; III. Biochemistry; IV. Molecular Cloning of Receptor Subunits; V. Characterization of the Receptor Family; VI. The Future; Reference; Chapter 4. The Pharmacology and Function of Central GABAB Receptors
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V. "Alternative" Pathways of APP Metabolism Provide Clues to the Source of Aß-AmyloidVI. Aß-Amyloid Is a Normal Constituent of Body Fluids and the Conditioned Medium of Cultured Cells; VII. Evidence Suggests the Existence of an Enzyme, ß-Secretase, That Cleaves APP at the Amino Terminus of the Aß-Amyloid Domain; VIII. APP Mutations in Familial Cerebral Amyloidoses Occur within or near the Aß-Amyloid Domain, Segregate with Disease in Affected Kindreds, and Yield APP Molecules That Display Some Proamyloidogenic Properties
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VII. Overstimulation of NMDA Receptors, a Final Common PathwayVIII. Development of Clinically Tolerated NMDA Antagonists for HIV-Related Neuronal Injury; IX. Excitatory Amino Acid Antagonist Treatments on the Horizon; X. Conclusion; References; Chapter 2. Processing of Alzheimer Aß-Amyloid Precursor Protein: Cell Biology, Regulation, and Role in Alzheimer Disease; I. Introduction; II. Alzheimer Disease Is Associated with an Intracranial Amyloidosis; III. APP Structure Gives Clues to Some of Its Functions; IV. APP Is Processed via Several Distinct Enzymatic and Subcellular Pathways
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Published since 1959, this serial presents in-depth reviews on key topics in neuroscience, from molecules to behavior. The serial stays keenly attuned to recent developments in the field through the contributions offirst-class experts. Neuroscientists as well as clinicians, psychologists, physiologists, and pharmacologists will find this serial an indispensable addition to their library.