Results 11 to 20 of about 51,758 (256)
Parvalbumin in rat kidney [PDF]
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
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Parvalbumin as a Pleomorphic Protein
Parvalbumin (PA) is a classical small, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily expressed in vertebrates in a tissue- and cell-specific manner, serving as a magnesium/ calcium buffer. In the last decade novel data were published on structural peculiarities of PA, likely affecting its functionality.
Permyakov, Eugene +2 more
openaire +4 more sources
The structure of the mouse parvalbumin gene
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. +3 more
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Parvalbumin and parvalbumin chandelier interneurons in autism and other psychiatric disorders
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
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Binding of Acrylonitrile to Parvalbumin [PDF]
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
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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
Parvalbumins are small molecules with important functions in Ca2+ signaling, but their sequence comparisons to date, especially in fish, have been relatively poor. We here, characterize sequence motifs that distinguish parvalbumin subfamilies across vertebrate species, as well as those that distinguish individual parvalbumins (orthologues) in fish, and
Johannes M. Dijkstra, Yasuto Kondo
openaire +3 more sources
Electrophysiological Heterogeneity of Fast-Spiking Interneurons: Chandelier versus Basket Cells [PDF]
In the prefrontal cortex, parvalbumin-positive inhibitory neurons play a prominent role in the neural circuitry that subserves working memory, and alterations in these neurons contribute to the pathophysiology of schizophrenia.
Povysheva, Nadezhda V. +16 more
core +1 more source
Removal of GABA(A) Receptor gamma 2 Subunits from Parvalbumin Neurons Causes Wide-Ranging Behavioral Alterations [PDF]
Peer ...
Sieghart Werner +46 more
core +1 more source
Lewy Bodies Are Not Associated With Neuronal or Synaptic Loss in Dementia With Lewy Bodies. [PDF]
Lewy bodies are thought to be central drivers of neurodegeneration and synaptic loss in dementia with Lewy bodies (DLB). In this article, Hawksworth, Kirkby‐Geddes et al. observe no associations between Lewy body density and loss of neurons or synaptic markers in DLB.
Hawksworth JI +7 more
europepmc +2 more sources

