Results 11 to 20 of about 2,372 (180)
Oncomodulin: The Enigmatic Parvalbumin Protein [PDF]
Frontiers in Molecular Neuroscience, 2019 EF-hand Ca2+-binding protein family members, α- and β-parvalbumins have been studied for decades. Yet, considerable information is lacking distinguishing functional differences between mammalian α-parvalbumin (PVALB) and oncomodulin (OCM), a branded β ...
Leslie K. Climer +7 more
doaj +3 more sources
Parvalbumin and parvalbumin chandelier interneurons in autism and other psychiatric disorders
Frontiers in Psychiatry, 2022 Parvalbumin (PV) is a calcium binding protein expressed by inhibitory fast-spiking interneurons in the cerebral cortex. By generating a fast stream of action potentials, PV+ interneurons provide a quick and stable inhibitory input to pyramidal neurons and contribute to the generation of gamma oscillations in the cortex.
Pablo Juarez +4 more
openaire +3 more sources
Binding of Acrylonitrile to Parvalbumin [PDF]
Toxicological Sciences, 1996 A previous study has shown that acrylonitrile (ACN) has a long half-life in rainbow trout muscle and that [14C]ACN appears to be bound to a 10,000-Da protein in muscle. The labeled protein was purified from muscle of trout exposed to [14C]ACN, separated on 20% SDS-PAGE, and digested for amino acid analysis and sequence analysis. These studies indicated
J J, Lech +4 more
openaire +2 more sources
Advanced Proteomic and Bioinformatic Tools for Predictive Analysis of Allergens in Novel Foods
Biology, 2023 In recent years, novel food is becoming an emerging trend increasingly more demanding in developed countries. Food proteins from vegetables (pulses, legumes, cereals), fungi, bacteria and insects are being researched to introduce them in meat ...
María López-Pedrouso +4 more
doaj +1 more source
Biomolecules, 2022 Parvalbumin (PA) is a small, acidic, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily. Structural and physical properties of PA are well studied but recently two highly conserved structural motifs consisting of three amino acids each (clusters I and II), which contribute to the hydrophobic core of the EF-hand domains, have been revealed.
Eugene A. Permyakov, Vladimir N. Uversky
openaire +4 more sources
Peculiarities of the development, course and diagnostic principles of food anaphylaxis in toddlers
Zdorovʹe Rebenka, 2021 Food anaphylaxis at an early age can be characterized by a development of nonspecific symptoms, including a child’s persistent crying, drowsiness, tearing of the eyes, sore throat, anxiety, numbness in the limbs, and impaired swallowing and speech. It is
L.V. Besh, O.I. Matsyura
doaj +1 more source
Engineering parvalbumin for the heart: optimizing the Mg2+ binding properties of rat β-parvalbumin [PDF]
Frontiers in Physiology, 2011 Parvalbumin (PV), an EF-hand protein family member, is a delayed calcium buffer that exchanges magnesium for calcium to facilitate fast skeletal muscle relaxation. Genetic approaches that express parvalbumin in the heart also enhance relaxation and show promise of being therapeutic against various cardiac diseases where relaxation is compromised ...
Zhang, Jianchao +8 more
openaire +2 more sources
Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin
Allergology International, 2004 Background: Parvalbumin is the major and cross-reactive allergen in fish. Sufficient amounts of IgE-reactive recombinant fish parvalbumin are needed for diagnosis and immunotherapy of fish allergy.
Yuki Hamada +5 more
doaj +1 more source
Fish allergens at a glance: Variable allergenicity of parvalbumins, the major fish allergens
Frontiers in Immunology, 2014 Fish is a common trigger of severe, food-allergic reactions. Only a limited number of proteins induce specific IgE-mediated immune reactions. The major fish allergens are the parvalbumins.
Annette eKuehn +5 more
doaj +1 more source
Parvalbumin in rat kidney [PDF]
FEBS Letters, 1986 The Ca2+‐binding parvalbumin has been purified for the first time from rat kidney. Its biochemical and immunological properties were indistinguishable from the muscle counterpart. By immunohistochemical methods parvalbumin was localized in part of the distal tubule and proximal collecting duct, similar to the vitamin D‐dependent Ca2+‐binding protein ...
Schneeberger, Peter R. +1 more
openaire +2 more sources