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Conformational studies on parvalbumins by circular dichroism

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
Structural variations of two parvalbumins, Whiting III and Pike III, in various denaturing conditions, have been studied by circular dichroism. CD signals are depressed from 4 urea. For Pike III, acidic pH, sodium dodecyl sulfate or complete removal of Ca2+ show little effect in the far ultraviolet region but rather strong effects in the near ...
J, Closset, C, Gerday
openaire   +2 more sources

Shining light on parvalbumin interneuron plasticity

Trends in Pharmacological Sciences
Neuronal networks rely on a balance between the activity of excitatory and inhibitory neurons, each having distinct roles in regulating the flow of activity across brain circuits and signal processing. Recent work by Selten et al. uncovers how parvalbumin (PV)-expressing interneurons adjust their inhibitory inputs in response to activity changes ...
Hommersom, M.P.   +3 more
openaire   +3 more sources

The Rat Parvalbumin Gene

1988
Parvalbumin belongs to the family of high affinity Ca2+-binding proteins (Heizmann and Berchtold 1987). In mammals, parvalbumin is synthesized in high amounts in fast contracting/relaxing muscles in a development-dependent manner (Celio and Heizmann 1982; Berchtold and Means 1985). Parvalbumin is also expressed in nonmuscle tissues such as brain (Celio
openaire   +1 more source

Reduction in IgE reactivity of Pacific mackerel parvalbumin by heat treatment

Food Chemistry, 2016
Yukihiro Kobayashi, Kazuo Shiomi
exaly  

Quantification of major allergen parvalbumin in 22 species of fish by SDS–PAGE

Food Chemistry, 2016
Yukihiro Kobayashi   +2 more
exaly  

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