Results 201 to 210 of about 51,781 (250)

Ferrets as a model for investigating the impact of chemical agents on cerebral cortical sulcogyrogenesis. [PDF]

Front Neurol
Sawada K.
europepmc   +1 more source

Imipenem in the Rat Brain: A Multidimensional Study on Hippocampal Behavior, GABAergic System, Astrocyte Response, and Neurogenesis. [PDF]

Antibiotics (Basel)
Araújo-Andrade L, Caetano-Mota B, Silva I, Rogeiro A, Nogueira P, Silva A, Pereira PA, Madeira MD, Cardoso A.   +8 more
europepmc   +1 more source

Methodology for human-induced pluripotent stem cell-derived excitatory and inhibitory neuron coculture with astrocytes for Alzheimer's disease modelling. [PDF]

Brain Commun
Li J, Brown LE, Rambarack N, Chan A, Prakash P, Arber C, Wray S, Ali AB.   +7 more
europepmc   +1 more source

The structure of the mouse parvalbumin gene

Mammalian Genome, 1992
Parvalbumin (PV) is a calcium-binding protein of the EF-hand family, expressed mainly in fast contracting/relaxing muscles of vertebrates. We have isolated five overlapping genomic PV clones which overall span 28 kilobase pairs (kb) around the Pva locus on mouse Chromosome (Chr) 15. The positions of four introns were determined by DNA sequencing.
Schleef, M., Zühlke, C., Jockusch, Harald, Schöffl, F.   +3 more
openaire   +4 more sources

Measuring parvalbumin levels in fish muscle tissue: Relevance of muscle locations and storage conditions

Food Chemistry, 2012
Fish is an allergenic food capable of provoking severe anaphylactic reactions. Parvalbumin is the major allergen identified in fish and frog muscles. Antibodies against fish and frog parvalbumin have been used to quantify parvalbumin levels from fish ...
Stef J Koppelman, Joseph L Baumert, Steve L Taylor   +2 more
exaly   +2 more sources

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The binding of calcium to muscular parvalbumins

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972
Abstract The binding of Ca 2+ to muscular parvalbumins from hake ( Merluccius merluccius ) and frog ( Rana esculenta ) has been measured at pH 6.7 using the 45 Ca-Chelex partition method. The results indicate that these proteins have two high affinity sites ( K d = 0.1·10 −6 –0.4·10 −6 M) and 3–6 sites with lower affinity ( K d = 2·10 −6 –9·10
G, Benzonana, J P, Capony, J F, Pechere
openaire   +2 more sources

Parvalbumin as a metal-dependent antioxidant

Cell Calcium, 2014
Parvalbumin (PA) is a Ca(2+)-binding protein of vertebrates massively expressed in tissues with high oxygen uptake and respectively elevated level of reactive oxygen species (ROS). To characterize antioxidant properties of PA, antioxidant capacity (AOC) of intact rat α-PA has been explored.
Sergei E, Permyakov, Alexey S, Kazakov, Nadezhda V, Avkhacheva, Eugene A, Permyakov   +3 more
openaire   +2 more sources

Terbium replacement of calcium in parvalbumin

Journal of Molecular Biology, 1978
Abstract Carp muscle calcium binding parvalbumin, crystallized in 2.9 m -ammonium sulfate, can bind two Tb3+ ions, which displace the two Ca2+ ions normally present. The Ca2+ co-ordinated in the loop between the E and the F α-helices is displaced at low Tb3+ concentrations; whereas the Ca2+ at the CD site is replaced only at higher Tb3 ...
J, Sowadski, G, Cornick, R H, Kretsinger
openaire   +2 more sources

Parvalbumin

1996
Abstract Parvalbumin (PV) is a soluble Ca2+-binding protein found at highest concentration in fast contracting/re/axing muscle fibers of vertebrates. In the muscle PV is believed to facilitate the transfer of Ca2+from the myofibrils to the sarcop/asmic reticulum.
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Binding of calcium by parvalbumin fragments

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978
Parvalbumin fragments from carp pI 4.47 parvalbumin corresponding to its residues 1--75 and 76--108 bind Ca2+ with affinities corresponding to Kd 0.9 . 10(-4) M and Kd 3 . 10(-3) M, respectively.
J, Derancourt, J, Haiech, J F, Pechère
openaire   +2 more sources