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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.


This gene encodes a member of the recoverin family of neuronal calcium sensors. The encoded protein contains three calcium-binding EF-hand domains and may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin may be the antigen responsible for cancer-associated retinopathy. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ROD, Rhodopsin, OUT, Isl-1, HAD
Papers on Recoverin
Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF Hands.
Oprian et al., Waltham, United States. In Biochemistry, Jan 2016
Recoverin (Rv), a small Ca(2+)-binding protein that inhibits rhodopsin kinase (RK), has four EF hands, two of which are functional (EF2 and EF3).
Influence of self-assembling peptide nanofibre scaffolds on retinal differentiation potential of stem/progenitor cells derived from ciliary pigment epithelial cells.
Krishnakumar et al., India. In J Tissue Eng Regen Med, 2014
Upon differentiation of these cells in conditioned medium, the cells exhibited retinal neuronal markers such as s-Opsin, rhodopsin and Recoverin.
Isoaspartyl protein damage and repair in mouse retina.
Aswad et al., Irvine, United States. In Invest Ophthalmol Vis Sci, 2014
Recoverin may be one such protein.
Swine cone and rod precursors arise sequentially and display sequential and transient integration and differentiation potential following transplantation.
Dean et al., Louisville, United States. In Invest Ophthalmol Vis Sci, 2014
These cone progenitors are marked by expression of Islet1 (ISL1) and Recoverin (RCVRN) (at this embryonic stage, RCVRN exclusively marks these cone precursors).
Hypoxia increases the yield of photoreceptors differentiating from mouse embryonic stem cells and improves the modeling of retinogenesis in vitro.
Bhattacharya et al., Sevilla, Spain. In Stem Cells, 2013
Different populations of retinal cells are increased in number under the hypoxic conditions applied, such as Crx-positive cells, S-Opsin-positive cells, and double positive cells for Rhodopsin and Recoverin, as shown by immunofluorescence analysis.
[Paraneoplastic retinopathy].
Lei et al., Chongqing, China. In Zhonghua Yan Ke Za Zhi, 2012
Recoverin autoantibody in serum is closely related to the pathogenesis of CAR, and the inactivation of TRPM1 channel plays a key role in dysfunction of ON-bipolar cells in MAR.
Oxidation mimicking substitution of conservative cysteine in recoverin suppresses its membrane association.
Senin et al., Moscow, Russia. In Amino Acids, 2012
C39D substitution reduces alpha-helical content, decreases thermal stability and suppresses membrane association.
Conformational dynamics of recoverin's Ca2+-myristoyl switch probed by 15N NMR relaxation dispersion and chemical shift analysis.
Ames et al., Davis, United States. In Proteins, 2011
(15) N NMR relaxation data suggest that Ca(2+)-free recoverin undergoes millisecond conformational dynamics at particular amide sites throughout the protein.
Involvement of the recoverin C-terminal segment in recognition of the target enzyme rhodopsin kinase.
Koch et al., Moscow, Russia. In Biochem J, 2011
A novel rhodopsin-kinase-binding site within the C-terminal region of recoverin.
Bipolar cells of the ground squirrel retina.
Haverkamp et al., Frankfurt am Main, Germany. In J Comp Neurol, 2011
Recoverin-positive OFF bipolar cells partly overlapped with ON bipolar axon terminals at the ON/OFF border of the IPL.
Nuclear receptor Rev-erb alpha (Nr1d1) functions in concert with Nr2e3 to regulate transcriptional networks in the retina.
Haider et al., Omaha, United States. In Plos One, 2010
Several genes co-targeted by NR2E3 and NR1D1 were identified that include: Nr2c1, Recoverin, Rgr, Rarres2, Pde8a, and Nupr1.
Aberrant demethylation of the recoverin gene is involved in the aberrant expression of recoverin in cancer cells.
Philippov et al., Moscow, Russia. In Exp Dermatol, 2010
Aberrant hypomethylation of the recoverin gene region, overlapping the promoter up-stream of the first exon and the first exon itself, is involved in the aberrant expression of recoverin in tumor cells.
Two mouse models for recoverin-associated autoimmune retinopathy.
Heckenlively et al., Ann Arbor, United States. In Mol Vis, 2009
High anti-recoverin antibody levels were achieved in two mouse models, accompanied by significantly reduced scotopic and photopic responses on the electroretinograms.
Expression of synaptic and phototransduction markers during photoreceptor development in the marmoset monkey Callithrix jacchus.
Springer et al., Seattle, United States. In J Comp Neurol, 2009
Recoverin appears in cones across 70% of the retina at fetal day (Fd) 88, indicating that it is expressed shortly after photoreceptors are generated.
Immunohistochemical study of pig retinal development.
Cogliati et al., Belfast, United Kingdom. In Mol Vis, 2008
Recoverin and rhodopsin immunolabeling revealed an increase in the length of photoreceptor segments in 6 months, compared to 1 week old animals.
Early development of retinal subtypes in long-term cultures of human embryonic retina.
Ghosh et al., Lund, Sweden. In Curr Eye Res, 2008
Recoverin-labeled photoreceptors appeared in explants kept 14 days and longer.
The canine Recoverin (RCV1) gene: a candidate gene for generalized progressive retinal atrophy.
Epplen et al., Bochum, Germany. In Mol Vis, 2002
PURPOSE: We describe the cloning, sequence, and mutation analysis of the canine Recoverin (RCV1) gene, a candidate gene for generalized progressive retinal atrophy (PRA).
Recoverin and rhodopsin kinase.
Chen, Salt Lake City, United States. In Adv Exp Med Biol, 2001
Recoverin and rhodopsin kinase are expressed primarily in retinal photoreceptors and they interact with each other in a Ca2+-dependent manner.
Regulation of cGMP synthesis in photoreceptors: role in signal transduction and congenital diseases of the retina.
Dizhoor, Detroit, United States. In Cell Signal, 2000
Recoverin-like proteins, GCAP-1 and GCAP-2, interact with the intracellular portion of the cyclases and stimulate its activity through dimerization of the cyclase subunits.
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