Files and links (1)
Accepted (AM)Open Access (License Unspecified), Open
Journal article
Chemical shift assignments of retinal degeneration 3 protein (RD3)
Biomolecular NMR assignments, v 12(1), pp 167-170
01 Apr 2018
PMID: 29327102
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Retinal degeneration 3 protein (RD3) binds to retinal membrane guanylyl cyclase (RetGC) and suppresses the basal activity of RetGC in photoreceptor cells that opposes the allosteric activation of the cyclase by GCAP proteins. Mutations in RD3 that disrupt its inhibition of RetGC are implicated in human retinal degenerative disorders. Here we report both backbone and sidechain NMR assignments for the RD3 protein (BMRB accession no. 27305).
Metrics
Details
- Title
- Chemical shift assignments of retinal degeneration 3 protein (RD3)
- Creators
- Sunghyuk Lim - University of California, DavisDiana Cudia - University of California, DavisQinhong Yu - University of California, DavisIgor Peshenko - Salus UniversityAlexander M Dizhoor - Salus UniversityJames B Ames - University of California, Davis
- Publication Details
- Biomolecular NMR assignments, v 12(1), pp 167-170
- Publisher
- Springer Nature
- Grant note
- R01 EY012347 / NEI NIH HHS R01 EY011522 / NEI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy; Pennsylvania College of Optometry (PCO)
- Web of Science ID
- WOS:000428448100033
- Scopus ID
- 2-s2.0-85040326909
- Other Identifier
- 991022035113704721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biophysics
- Spectroscopy