International review of neurobiology. Volume 36
tarafından
 
Bradley, Ronald J.

Başlık
International review of neurobiology. Volume 36

Yazar
Bradley, Ronald J.

ISBN
9780123668363
 
9781281749277
 
9786611749279
 
9780080857701

Yayın Bilgileri
San Diego : Academic Press, 1994.

Fiziksel Tanımlama
1 online resource (viii, 444 pages) : illustrations.

Seri
International review of neurobiology ; 36
 
International review of neurobiology ; 36.

İçerik
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
 
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
 
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
 
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
 
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

Özet
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.

Konu Başlığı
Neurobiology.
 
Neurosciences.
 
Neurobiology. (OCoLC)fst01036315
 
Neurosciences. (OCoLC)fst01036509

Tür
Electronic books.

Added Author
Bradley, Ronald J.
 
Harris, R. Adron.

Elektronik Erişim
ScienceDirect http://www.sciencedirect.com/science/book/9780123668363


Yer NumarasıDemirbaş NumarasıShelf LocationShelf LocationHolding Information
RC341 .I6836 1994 EB1180275-1001Elsevier E-Kitap KoleksiyonuElsevier E-Kitap Koleksiyonu