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  • Book
    Rommy von Bernhardi, Jaime Eugenín, Kenneth J. Muller, editors.
    Summary: A comprehensive overview of the many factors that can influence brain plasticity throughout the lifespan. Addresses perinatal plasticity, functional state plasticity, injury-induced plasticity, and stressor-induced plasticity. Because it looks at so many aspects of the field, this volume will serve as a great resource for students as well as researchers interested in expanding their knowledge. The volume comes out as an integrated view based in the expertise of Ibero American neuroscientists working in the field.

    Contents:
    1. What is neural plasticity?
    2. CREB at the crossroads of activity-dependent regulation of nervous system development and function
    3. Models of short-term synaptic plasticity
    4. Plasticity in the interoceptive system
    5. Learning as a functional state of the brain: studies in wild-type and transgenic animals
    6. Bidirectional effects of mother-young contact on the maternal and neonatal brains
    7. Prenatal stress and neurodevelopmental plasticity: relevance to psychopathology
    8. Early postnatal development of somastostatinergic systems in brainstem respiratory network
    9. Respiratory rhythm generation: the whole is greater than the sum of the parts
    10. The onset of the fetal respiratory rhythm: an emergent property triggered by chemosensory drive?
    11. Neurodevelopmental effects of serontonin on the brainstem respiratory network
    12. Neural network reconfigurations: changes of the respiratory network by hypoxia as an example
    13. Progenitors in the ependyma of the spinal cord: a potential resource for self-repair after injury
    I[subscript]KD current in cold transduction and damage-triggered cold hypersensitivity
    Index.
    Digital Access Springer 2017
  • Article
    Kodama T, Watson ID, Woledge RC.
    J Biol Chem. 1977 Nov 25;252(22):8085-7.
    A calorimetric titration method was used to study the ADP binding to the chymotryptic subfragments of myosin, heavy meromyosin (HMM) and myosin subfragment 1 (S-1), and to myosin aggregated into filaments at low ionic strength. The binding constant (K) and heat of reaction (deltaH, kiloJoules (moles of ADP bound)-1) were determined. For HMM in 0.5 M KCl, 0.01 M MgCl2, 0.02 M Tris (pH 7.8) at 12 degrees, log K = 5.92 +/- 0.13 and deltaH = -70.9 +/- 3.6 kJ mol-1. These results agree with our previous findings for myosin in 0.5 M KCl at 12 degrees. When the KCl concentration was reduced to 0.1 M, the binding constant did not change significantly (log K = 6.09 +/- 0.06) but the binding was more exothermic (deltaH = -90.1 +/- 3.3 kJ mol-1). Similar results were obtained for myosin filaments in 0.1 M KCl and also for both the isoenzymes of S-1(S-1(A1) and S-1(A2) in 0.1 M KCl. In 0.5 M KCl, the binding curves suggest that about one ADP is bound per active site, but as 0.1 M KCl, the apparent stoichiometry drops from 0.7 to 0.75. The most probable explanation is that there is some site heterogeneity which is more evident at lower ionic strength.
    Digital Access Access Options