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Five Members of a Novel Ca2+-binding Protein (CABP) Subfamily with Similarity to Calmodulin*
TLDR
Five members of a novel Ca2+-binding protein subfamily (CaBP), with 46–58% sequence similarity to calmodulin (CaM), were identified in the vertebrate retina, suggesting that these novel CaBPs are an important component of Ca2-mediated cellular signal transduction in the central nervous system where they may augment or substitute for CaM.
Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function
TLDR
Observations indicate that CaBP4 is important for normal synaptic function, probably through regulation of Ca2+ influx and neurotransmitter release in photoreceptor synaptic terminals.
Molecular Characterization of a Novel Short-chain Dehydrogenase/Reductase That Reduces All-trans-retinal*
TLDR
The cloning of a dehydrogen enzyme, retSDR1, that belongs to the short-chain dehydrogenase/reductase superfamily and localizes predominantly in cone photoreceptors is reported.
Dual-substrate Specificity Short Chain Retinol Dehydrogenases from the Vertebrate Retina* 210
TLDR
Three enzymes from a novel subfamily of four retinol dehydrogenases (RDH11–14) that display dual-substrate specificity are described, uniquely metabolizing all-trans- andcis-retinols with C15 pro-Rspecificity.
Differential modulation of Cav2.1 channels by calmodulin and Ca2+-binding protein 1
TLDR
It is reported that the neuronal Ca2+-binding protein 1 (CaBP1) modulates Cav2.1 channels in a manner that is markedly different from modulation by CaM, and may regulate Ca2-dependent forms of synaptic plasticity by inhibiting Ca2+.
A comparison of immunocytochemical markers to identify bipolar cell types in human and monkey retina
TLDR
The results support the use of macaque monkey retina as a model for human, but caution against the assumption that all labeling patterns are identical in the two primates.
Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1.
TLDR
This work reports that the neuronal Ca2+-binding protein 1 (CaBP1) modulates Ca(v)2.1 channels in a manner that is markedly different from modulation by CaM.
Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca2+ release channels
TLDR
CaBP/caldendrin, a subfamily of the EF-hand-containing neuronal calcium sensor family of calmodulin-related proteins, bind specifically to the InsP3-binding region of all three InsP2+ channel isoforms with high affinity, activating single-channel gating as efficaciously as InsP 3, dependent on functional EF-hands in CaBP.
Ca2+‐binding proteins tune Ca2+‐feedback to Cav1.3 channels in mouse auditory hair cells
TLDR
It is demonstrated that CaBPs differentially modify Ca2+ feedback to Cav1.3 channels in transfected cells and implicate CaBP1 rather than CaBP4 in conferring the anomalous slow inactivation of Cav 1.3.
Rod and cone visual cycle consequences of a null mutation in the 11-cis-retinol dehydrogenase gene in man
TLDR
In vivo visual consequences of this null mutation showed complex kinetics of dark adaptation of rod and cone resensitization and the causative novel RDH5 mutation, Arg157Trp, that replaces an amino acid residue conserved among short-chain alcohol dehydrogenases.
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