For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
5
views
1
references
 Top references
cited by
0
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      15
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Correction: Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin

      correction

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The affiliation and email address for the eleventh author are incorrect. The current address for Alessandro Iannaccone should be listed as affiliation #5. Alessandro Iannaccone is affiliated with #4: Retinal Degeneration & Ophthalmic Genetics Service & Lions Visual Function Diagnostic Lab, Hamilton Eye Institute, Dept. Ophthalmology, University of Tennessee Health Science Center, Memphis, Tennessee, United States of America, and with #5: Center for Retinal Degenerations and Ophthalmic Genetic Diseases, Duke Eye Center, Dept. Ophthalmology, Duke University School of Medicine, Durham, North Carolina, United States of America. Dr. Iannaccone’s email address is alessandro.iannaccone@duke.edu.

          Related collections

          Most cited references1

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin

          James Mitchell, Fernanda Balem, Kalyan C. Tirupula … (2019)
          Mutations in the RHO gene encoding for the visual pigment protein, rhodopsin, are among the most common cause of autosomal dominant retinitis pigmentosa (ADRP). Previous studies of ADRP mutations in different domains of rhodopsin have indicated that changes that lead to more instability in rhodopsin structure are responsible for more severe disease in patients. Here, we further test this hypothesis by comparing side-by-side and therefore quantitatively two RHO mutations, N15S and P23H, both located in the N-terminal intradiscal domain. The in vitro biochemical properties of these two rhodopsin proteins, expressed in stably transfected tetracycline-inducible HEK293S cells, their UV-visible absorption, their Fourier transform infrared, circular dichroism and Metarhodopsin II fluorescence spectroscopy properties were characterized. As compared to the severely impaired P23H molecular function, N15S is only slightly defective in structure and stability. We propose that the molecular basis for these structural differences lies in the greater distance of the N15 residue as compared to P23 with respect to the predicted rhodopsin folding core. As described previously for WT rhodopsin, addition of the cytoplasmic allosteric modulator chlorin e6 stabilizes especially the P23H protein, suggesting that chlorin e6 may be generally beneficial in the rescue of those ADRP rhodopsin proteins whose stability is affected by amino acid replacement.
          Article 0 comments Cited 6 times – based on 0 reviews     Review now
            Bookmark
            All references

            Author and article information

            Journal
            Journal ID (nlm-ta): PLoS One
            Journal ID (iso-abbrev): PLoS ONE
            Journal ID (publisher-id): plos
            Journal ID (pmc): plosone
            Title: PLoS ONE
            Publisher: Public Library of Science (San Francisco, CA USA )
            ISSN (Electronic): 1932-6203
            Publication date (Electronic): 7 November 2019
            Publication date Collection: 2019
            Publication date PMC-release: 7 November 2019
            Volume: 14
            Issue: 11
            Electronic Location Identifier: e0225153
            Article
            Publisher ID: PONE-D-19-30292
            DOI: 10.1371/journal.pone.0225153
            PMC ID: 6837281
            PubMed ID: 31697785
            SO-VID: 1b5567ab-8b87-4906-bb42-e99674b4f99f
            Copyright © © 2019 Mitchell et al
            License:

            This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

            History
            Related
            Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin
            Page count
            Figures: 0, Tables: 0, Pages: 1
            Categories
            Subject: Correction

            ScienceOpen disciplines: Uncategorized
            Data availability:
            ScienceOpen disciplines: Uncategorized

            Comments

            Comment on this article