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  • Book
    Meeta Goswami, S.R. Pandi-Perumal, Michael J. Thorpy, editors.
    Contents:
    Section I
    Etiology
    1. The Genetics of Narcolepsy
    2. Orexin (Hypocretin) and Narcolepsy
    3. Precipitants of Narcolepsy: Vaccines and Infections
    Section II
    Clinical Considerations
    4. Epidemiology of Narcolepsy
    5. Diagnostic Criteria and Delay in Diagnosis of Narcolepsy
    6. Narcolepsy in Childhood
    7. Narcolepsy in the Older Adult
    8. Hypnagogic Hallucinations and Sleep Paralysis
    9. Symptomatic Narcolepsy or Hypersomnia, with and without Hypocretin (Orexin) Deficiency
    10. Hypersomnias Other than Narcolepsy: Differential Diagnosis
    11. Narcolepsy and Other Comorbid Medical Illnesses
    12. Sleep Disorders Comorbidities in Narcolepsy and their Management
    13. Neuroimaging of Narcolepsy
    Section III
    Psychosocial Considerations
    14. Quality of Life and Psychosocial Issues in Narcolepsy: Implications for Management
    15. Narcolepsy, Intimacy and Sexuality
    16. Memory and Cognition in Narcolepsy
    17. Psychoanalysis and Narcolepsy
    18. Dreaming in Narcolepsy
    19. Narcolepsy and Mental Illness
    20. Narcolepsy, Driving and Traffic Safety
    Section IV
    Management
    21. Overview of Management of Narcolepsy
    22. Modes of Action of Drugs Related to Narcolepsy: Pharmacology of Wake-Promoting Compounds and Anticataplectics
    23. Modafinil/Armodafinil in the Treatment of Narcolepsy
    24. Sodium Oxybate in the Treatment of Narcolepsy
    25. Pregnancy and Anaesthesia in Narcolepsy
    26. Emerging Treatments for Narcolepsy
    27. Behavioral and Non-Pharmacological Management of Narcolepsy
    Section V
    Health Care Delivery and Medico-Legal Considerations
    28. Narcolepsy and Developmental Disability
    29. Succeeding in School and in the Workplace with Narcolepsy
    30. Medico-Legal Aspects of Disability in Narcolepsy
    31. The Affordable Care Act and the Future of Sleep Medicine.
    Digital Access Springer 2016
  • Article
    Hurrell JG, Smith JA, Leach SJ.
    Biochemistry. 1977 Jan 25;16(2):175-85.
    The conformational motilities of three regions of the sperm whale myoglobin molecule and of an isolated peptide of myoglobin have been examined by measuring the equilibrium constant for the native equilibrium nonnative transition. The immunological approach of Furie et al. (Furie, B., Schechter, A.N., Sachs D., and Anfinsen, C.B. (1975), J. Mol. Biol.92, 497-506) was used with convenient modifications. Antibodies specific to the nonnative conformations were used in assaying for competition between the radioactively labeled peptide and native myoglobin. Labeling was by 125I iodination of the peptide or its 3-(4-hydroxyphenyl)propionyl derivative, and separation of the immune complex from the free peptide was either by ammonium sulfate precipitation or by centrifugation of the antibodies immobilized on Agarose beads. For the antigenic regions of the sequence (1-55), the measured conformational equilibrium constant was 840 +/- 200 at 22 degrees C; the value for the C-terminal region (132-153) was 280 +/- 120 at 25 degrees C, while that for the region (66-76) adjacent to the heme group was greater than 2.5 x 10(6). Measurements on the isolated peptide (132-153) indicated that 1% of the molecules adopt native-type folding in aqueous solution at 36 degrees C.
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