ArticleBiochemistry2005
Role of the second intradiscal loop of peripherin/rds in homo and hetero associations.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 48 citations in OpenAlex.
- Photoreceptor outer segment disk rim curvature relies on a tetraspanin interaction web.The Journal of biological chemistry · 2026Article
- Photoreceptor outer segment disk rim curvature relies on a tetraspanin interaction web.bioRxiv : the preprint server for biology · 2026Article
- Genotype-Phenotype Correlations inGenes · 2025Article
- The PRPH2 D2 Loop: Biochemical Insights and Implications in Disease.Advances in experimental medicine and biology · 2025Review
- Article
- ROM1 is redundant to PRPH2 as a molecular building block of photoreceptor disc rims.bioRxiv : the preprint server for biology · 2023Article
- Comparative study of PRPH2 D2 loop mutants reveals divergent disease mechanism in rods and cones.Cellular and molecular life sciences : CMLS · 2023Article
- The Role of Peripherin-2/ROM1 Complexes in Photoreceptor Outer Segment Disc Morphogenesis.Advances in experimental medicine and biology · 2023Article
- Delineating the Clinical Phenotype of Patients With the c.629C>G, p.Pro210Arg Mutation in Peripherin-2.Investigative ophthalmology & visual science · 2022Article
- ROM1 contributes to phenotypic heterogeneity in PRPH2-associated retinal disease.Human molecular genetics · 2020Article
- Genotype-phenotype associations in a large PRPH2-related retinopathy cohort.Human mutation · 2020Article
- Syntaxin 3 is essential for photoreceptor outer segment protein trafficking and survival.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Novel molecular mechanisms for Prph2-associated pattern dystrophy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Prph2 initiates outer segment morphogenesis but maturation requires Prph2/Rom1 oligomerization.Human molecular genetics · 2019Article
- Oligomerization of Prph2 and Rom1 is essential for photoreceptor outer segment formation.Human molecular genetics · 2018Article
- Peripherin-2 and Rom-1 have opposing effects on rod outer segment targeting of retinitis pigmentosa-linked peripherin-2 mutants.Scientific reports · 2017Article
- Rom1 converts Y141C-Prph2-associated pattern dystrophy to retinitis pigmentosa.Human molecular genetics · 2017Article
- Molecular basis for photoreceptor outer segment architecture.Progress in retinal and eye research · 2016Review
- PRPH2/RDS and ROM-1: Historical context, current views and future considerations.Progress in retinal and eye research · 2016Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Peripherin/rds (P/rds) is a disk rim protein that assembles into homo and hetero complexes with its nonglycosylated homologue, Rom-1, to maintain the integrity of the photoreceptor outer segment. Mutations in the rds gene have been identified in a variety of human retinal degenerative diseases. More than 70% of these mutations are located in the second intradiscal (D2) loop, highlighting the functional importance of this region. This study examines the involvement of different regions of the D2 loop in protein associations using a GST pull-down assay and a heterologous coexpression system. The pull-down assay suggests an association of the N-terminal portion (Phe(120)-Phe(187)) of the D2 loop with Rom-1 as well as with other P/rds molecules. Through peptide competition experiments, the region between Cys(165) and Asn(182) of the D2 loop has been identified as the domain for these associations. In a COS-1 cell heterologous expression system, coexpression of the D2 loop along with the intact P/rds and Rom-1 hindered the association of the two full-length proteins. In contrast to the homo association of P/rds molecules, it seems that the hetero association of P/rds with Rom-1 has a more stringent structural requirement. This work defines the crucial domain of the D2 loop, which mediates homo and hetero associations, specifically the regions that lay between Cys(165) and Asn(182). Elucidation of the molecular mechanisms behind the protein-protein associations of P/rds and its partners may reveal the pathogenic defects arising from the most common mutations in this gene.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.