Results 121 to 130 of about 2,372 (180)

Parvalbumin: as a fish-allergen

Frontiers in Immunology, 2013
openaire   +1 more source

Thalamic cells and pathway for social memory processing and storage. [PDF]

Neuron
Gao WJ.
europepmc   +1 more source

Anaphylaxis Following Fish Ingestion in a Military Member. [PDF]

Cureus
Klein AP, Howell JL, Coop C.
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Parvalbumin Neurons in the Basal Forebrain Projecting to the Mammillary Nucleus Ameliorate Age-Related Cognitive Decline. [PDF]

Int J Mol Sci
Sun T, Li Q, Liu B, Chen J, Li A, Jiang T, Gong H, Li X.   +7 more
europepmc   +1 more source

Hominoid-specific calretinin-immunopositivity of the optic radiation (geniculocalcarine tract). [PDF]

Anat Rec (Hoboken)
Santana NNM, Swiegers J, Bertelsen MF, Sherwood CC, Cavalcanti JRLP, Manger PR.   +5 more
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A proper excitatory/inhibitory ratio is required to develop synchronized network activity in mouse cortical cultures. [PDF]

Stem Cell Reports
Crocco E, Iannello L, Tonelli F, Lagani G, Pandolfini L, Ferro M, Amato G, Di Garbo A, Cremisi F.   +8 more
europepmc   +1 more source

<i>Quasipaa spinosa-Derived Parvalbumin</i> Attenuates Exercise-Induced Fatigue via Calcium Homeostasis and Oxidative Stress Modulation in Exhaustively Trained Mice. [PDF]

Nutrients
Sang K, Lu C, Zhang Y, Chen Q.
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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
J P Capony, J F Pechere
exaly   +3 more sources

Parvalbumin in Human Brain

Journal of Neurochemistry, 1985
Abstract: Parvalbumin was isolated from human cerebral cortex and biceps and triceps muscles by HPLC. The immunological properties of the human protein and the mobility in two‐dimensional polyacrylamide gels were similar to that of parvalbumin isolated from the muscles of rat, mouse, rabbit, and chicken.
M W, Berchtold, M R, Celio, C W, Heizmann   +2 more
openaire   +2 more sources