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Calcium binding protein 4

CaBP4, calcium binding protein 4
This gene encodes a member of the CABP family of calcium binding protein characterized by four EF-hand motifs. Mutations in this gene are associated with congenital stationary night blindness type 2B. [provided by RefSeq, Mar 2010] (from NCBI)
Top mentioned proteins: ROD, CACNA1F, CAN, HAD, WAVE
Papers on CaBP4
Impact of gold nanoparticles on brain of mice infected with Schistosoma mansoni.
New
Al-Quraishy et al., Riyadh, Saudi Arabia. In Parasitol Res, Oct 2015
In addition, S. mansoni was able to disregulate the infected mice brain Cacnb4, Cabp4, Vdac3, Glrb, and Adam23 messenger RNA (mRNA).
Structural insights into activation of the retinal L-type Ca²⁺ channel (Cav1.4) by Ca²⁺-binding protein 4 (CaBP4).
Ames et al., Davis, United States. In J Biol Chem, 2014
CaBP4 modulates Ca(2+)-dependent activity of L-type voltage-gated Ca(2+) channels (Cav1.4) in retinal photoreceptor cells.
¹H, ¹⁵N, and ¹³C chemical shift assignments of murine calcium-binding protein 4.
Ames et al., Davis, United States. In Biomol Nmr Assign, 2014
Calcium-binding protein 4 (CaBP4) regulates voltage-gated Ca(2+) channels in retinal rod cells and specific mutations within CaBP4 are associated with congenital stationary night blindness type 2. We report complete NMR chemical shift assignments of the Ca(2+)-saturated form of CaBP4 with Ca(2+) bound at EF1, EF3 and EF4 (BMRB no.
Allostery in Ca²⁺ channel modulation by calcium-binding proteins.
Yue et al., Baltimore, United States. In Nat Chem Biol, 2014
Here, we devise a live-cell, holomolecule approach that reveals an allosteric mechanism for calcium channels whose CaM-mediated inactivation is eliminated by CaBP4.
Dysregulation of Ca(v)1.4 channels disrupts the maturation of photoreceptor synaptic ribbons in congenital stationary night blindness type 2.
Lee et al., Iowa City, United States. In Channels (austin), 2013
In mouse models of CSNB2 in which the voltage-dependence of Cav 1.4 activation is either enhanced (Cav 1.4I756T) or inhibited (CaBP4 KO), the initial stages of PR synaptic ribbon formation are largely unaffected.
Genotype and phenotype of 101 dutch patients with congenital stationary night blindness.
van Genderen et al., Zeist, Netherlands. In Ophthalmology, 2013
Molecular analysis was performed by direct Sanger sequencing of the entire coding regions in NYX, TRPM1, GRM6, and GPR179 in patients with CSNB1 and CACNA1F and CABP4 in patients with CSNB2.
ZRANB2 localizes to supraspliceosomes and influences the alternative splicing of multiple genes in the transcriptome.
Morris et al., Sydney, Australia. In Mol Biol Rep, 2013
At the FDR ≤1.3 significance level we found that ZRANB2 influenced the alternative splicing of primary transcripts of CENTB1, WDR78, C10orf18, CABP4, SMARCC2, SPATA13, OR4C6, ZNF263, CAPN10, SALL1, ST18 and ZP2.
Clinical characterisation of the CABP4-related retinal phenotype.
Alkuraya et al., Riyadh, Saudi Arabia. In Br J Ophthalmol, 2013
BACKGROUND: Calcium binding protein 4 (CABP4), specifically located in photoreceptor synaptic terminals, has been associated with congenital stationary night blindness based on this clinical diagnosis being made for three individuals from two Swiss families with CABP4 mutations; however, the few reported cases limit phenotype-genotype correlation.
Protein phosphatase 2A dephosphorylates CaBP4 and regulates CaBP4 function.
Lee et al., Seattle, United States. In Invest Ophthalmol Vis Sci, 2013
PURPOSE: CaBP4 is a neuronal Ca(2+)-binding protein that is expressed in the retina and in the cochlea, and is essential for normal photoreceptor synaptic function.
Complex regulation of voltage-dependent activation and inactivation properties of retinal voltage-gated Cav1.4 L-type Ca2+ channels by Ca2+-binding protein 4 (CaBP4).
Wahl-Schott et al., München, Germany. In J Biol Chem, 2012
Recent studies suggest that the activity of this channel is regulated by the Ca(2+)-binding protein 4 (CaBP4).
Homozygosity mapping in patients with cone-rod dystrophy: novel mutations and clinical characterizations.
den Hollander et al., Rotterdam, Netherlands. In Invest Ophthalmol Vis Sci, 2010
The variants were detected in the following six genes: ABCA4, CABP4, CERKL, EYS, KCNV2, and PROM1.
A null mutation in CABP4 causes Leber's congenital amaurosis-like phenotype.
GeneRIF
Alkuraya et al., Riyadh, Saudi Arabia. In Mol Vis, 2009
This report significantly expands on the phenotype associated with calcium binding protein 4 mutations.
Genotyping microarray for CSNB-associated genes.
Berger et al., Zürich, Switzerland. In Invest Ophthalmol Vis Sci, 2009
Subsequently, oligonucleotides were designed representing 126 sequence variations in RHO, CABP4, CACNA1F, CACNA2D4, GNAT1, GRM6, NYX, PDE6B, and SAG and spotted on the chip.
A novel homozygous nonsense mutation in CABP4 causes congenital cone-rod synaptic disorder.
GeneRIF
van den Born et al., Rotterdam, Netherlands. In Invest Ophthalmol Vis Sci, 2009
A novel homozygous nonsense mutation in CABP4 in two siblings resulted in a phenotype with severely reduced cone function and only negligibly reduced rod function on electroretinography and psychophysical testing.
Interaction and colocalization of CaBP4 and Unc119 (MRG4) in photoreceptors.
GeneRIF
Haeseleer, Seattle, United States. In Invest Ophthalmol Vis Sci, 2008
This study provides evidence for the interaction of CaBP4 with Unc119 at the photoreceptor synapse.
Ca2+-binding proteins tune Ca2+-feedback to Cav1.3 channels in mouse auditory hair cells.
GeneRIF
Lee et al., Atlanta, United States. In J Physiol, 2008
our results implicate CaBP1 rather than CaBP4 in conferring the anomalous slow inactivation of Ca(v)1.3 Ca(2+) currents required for auditory transmission
Phosphorylation of the Ca2+-binding protein CaBP4 by protein kinase C zeta in photoreceptors.
GeneRIF
Haeseleer et al., Atlanta, United States. In J Neurosci, 2007
These findings demonstrate how light-stimulated changes in CaBP4 phosphorylation and Ca2+ binding may regulate presynaptic Ca2+ signals in photoreceptors.
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