Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms.

Vision research - 1 Dec 2003

Janz Jay M, Farrens David L

Abstract excerpt

The stability of the retinal chromophore attachment varies between different visual pigments and may factor in some retinal disease states. Opsin appears to stabilize this Schiff base linkage by: (i) affecting the hydrolysis chemistry, (ii) shielding the retinal linkage from solvent, or (iii) acting as a kinetic trap to slow retinal release. Here we describe methods to determine Schiff base stability in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Genetic Linkage
Share to Hydrolysis
Share to Hydroxylamine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Retina

Share to Rhodopsin

Share to Schiff Bases

Share to Spectrum Analysis

Source

Identifiers

PMID: 14611935
DOI: 10.1016/j.visres.2003.08.010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms.PMID 14611935Read ↗

Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis.Semantic proximity Read ↗

Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin.Semantic proximity Read ↗

Chemical kinetic analysis of thermal decay of rhodopsin reveals unusual energetics of thermal isomerization and hydrolysis of Schiff base.Semantic proximity Read ↗

Structural role of the T94I rhodopsin mutation in congenital stationary night blindness.Semantic proximity Read ↗

Retinal Attachment Instability Is Diversified among Mammalian Melanopsins.Semantic proximity Read ↗

A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.Semantic proximity Read ↗

Time-resolved spectroscopy of the early photolysis intermediates of rhodopsin Schiff base counterion mutants.Semantic proximity Read ↗

Molecular basis for variations in the sensitivity of pathogenic rhodopsin variants to 9-cis-retinal.Semantic proximity Read ↗

G-protein activation of the dark-state conformation of the visual G protein-coupled receptor rhodopsin by releasing critical structural constraints.Semantic proximity Read ↗

Photosensitivities of rhodopsin mutants with a displaced counterion.Semantic proximity Read ↗

Molecular Basis for Variations in the Sensitivity of Pathogenic Rhodopsin Variants to 9- <i>cis</i> -RetinalSemantic proximity Read ↗

Functional analysis of two novel retinitis pigmentosa mutations reveals structural role of the third transmembrane helix in rhodopsin photoactivation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.