RLBP1 Antibody

1. RLBP1 gene geographical area-related mutation is associated with retinitis punctata albescens. PMID: 28764803
2. we provide evidence for an allosteric modulation of the enzymatic activity by 11-cis retinoids. This regulation is independent from cellular retinaldehyde-binding protein (CRALBP), the major cis-retinoid binding protein. PMID: 28096191
3. These results show that joint tests of main effects and gene-gene interaction reveal associations at some novel loci that were missed when considering main effects alone. PMID: 28813576
4. Different mutations in RLBP1 are correlated with quite different morphological and functional characteristics outlines the complexity of the protein. PMID: 25429852
5. RLBP1 gene is upregulated in patients with reactive retinal astrocytic tumors. PMID: 24921169
6. Patients with retinitis punctata albescens (RPA) show variable degrees of foveal cone death, even at an early stage. This finding has implications for future treatment. PMID: 23929416
7. The two RLBP1 genotypes presented a phenotypical and electrophysiological expression of progressive retinal disease similar to that previously described in homozygotes for the c.700C>T (p.R234W) RLBP1 mutation. PMID: 22551409
8. The clinical characteristics of a Japanese patient with a homozygous R234W mutation in RLBP1 are very similar to that of Swedish patients with Bothnia dystrophy. PMID: 22171637
9. Identification of autoantibodies specific for two retinal antigens (CRALBP and S-Ag) supports the concept of an autoimmunological origin of the disease. PMID: 21904838
10. The R234W mutation reveals impaired 11-cis-retinal release through stabilization of the ligand complex. PMID: 22183382
11. mutations in RLBP1 are responsible for fundus albipunctatus in the affected individuals of these consanguineous Pakistani families. PMID: 21447491
12. In the RLBP1-Bothnia dystrophy phenotype, a loss of function and thinning of the central macula are found, indicating early damage of the cone photoreceptors in this disease of the visual cycle. PMID: 20696998
13. Newfoundland rod-cone dystrophy, an early-onset retinal dystrophy, is caused by splice-junction mutations in RLBP1 PMID: 11868161
14. the M225K mutation abolishes and the R233W mutation tightens retinoid binding and both impair CRALBP function in the visual cycle as an 11-cis-retinol acceptor and as a substrate carrier. PMID: 12536144
15. Trp-165, Met-208, Met-222, Met-225, and Trp-244 are components of the CRALBP ligand binding cavity. PMID: 12536149
16. Patients with a clinical presentation of RPA (retinitis punctata albescens) can have genetically different mutations. PMID: 14718298
17. Only eight RLBP1 mutations have been reported to date, and here we describe two novel mutations. PMID: 15234312
18. Cellular retinaldehyde binding protein 1 (CRALBP) inhibits the reduction of 11-cis-retinal stronger than the oxidation of 11-cis-retinol, in accord with its higher affinity for 11-cis-retinal. PMID: 15865448
19. A novel mutation in RLBP1 gene was found in a Japanese patient with retinitis punctata albescens. Degenerative changes of the outer retina were detected by optical coherence tomography PMID: 15953459
20. Because of the high density of Alu elements in RLBP1, a systematic search should be made for deletions in this gene when one or both alleles lack point mutations, in the case of RPA or flecked retinal dystrophy. PMID: 17065479
21. analysis of CRALBP ligand and protein interactions PMID: 17249612
22. CRALBP transcripts in retinal pigment epithelium cells contain a noncoding exon in addition to a newly described promoter and, by definition, an additional intron PMID: 17652763
23. The presence of CRALBP autoantibodies in 54% of tested uveitis patients supports CRALBP as a possible autoantigen in human autoimmune uveitis PMID: 18317528
24. Bothnia dystrophy is caused by the loss of CRALBP function due to changed physical features and impaired activity of retinoid binding. PMID: 18344446
25. These results reveal an unanticipated domino-like structural transition causing Bothnia-type retinal dystrophy by the impaired release of 11-cis-retinal from R234W. PMID: 19846785
26. Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia PMID: 19165527

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HGNC: 10024

OMIM: 136880

KEGG: hsa:6017

STRING: 9606.ENSP00000268125

UniGene: Hs.1933