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

Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.

Investigative ophthalmology & visual science - 1 Dec 2017

Kumari Sindhu, Gao Junyuan, Mathias Richard T, Sun Xiurong, Eswaramoorthy Amizhdini, Browne Nicholas, Zhang Nigel, Varadaraj Kulandaiappan

Abstract excerpt

Purpose: The objective of this study was to understand the molecular and physiologic mechanisms behind the lens cataract differences in Aquaporin 0-knockout-Heterozygous (AQP0-Htz) mice developed in C57 and FVB (lacks beaded filaments [BFs]) strains. Methods: Lens transparency was studied using dark field light microscopy. Water permeability (Pf) was measured in fiber cell membrane vesicles. Western...

Read the complete abstract on PubMed

Topics

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

Share to Aquaporin 1
Share to Cataract

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electric Impedance

Share to Eye Proteins

Share to Gap Junctions

Share to Intermediate Filament Proteins

Share to Lens, Crystalline

Source

Open in PubMed Open full text

Identifiers

PMID: 29196765
DOI: 10.1167/iovs.17-22153
PMCID: PMC5710632

Genes

AQP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.PMID 29196765Read ↗

Dominant cataracts result from incongruous mixing of wild-type lens connexins.Semantic proximity Read ↗

Connexin Mutants Compromise the Lens Circulation and Cause Cataracts through Biomineralization.Semantic proximity Read ↗

Optical dysfunction of the crystalline lens in aquaporin-0-deficient mice.Semantic proximity Read ↗

Disruption of the lens circulation causes calcium accumulation and precipitates in connexin mutant mice.Semantic proximity Read ↗

Focus on lens connexins.Semantic proximity Read ↗

Structural function of MIP/aquaporin 0 in the eye lens; genetic defects lead to congenital inherited cataracts.Semantic proximity Read ↗

Beta-1 integrin is important for the structural maintenance and homeostasis of differentiating fiber cells.Semantic proximity Read ↗

Connexin50D47A Decreases Levels of Fiber Cell Connexins and Impairs Lens Fiber Cell DifferentiationSemantic proximity Read ↗

Functional characterization of CatTohm, a mouse AQP0 mutation that causes oxidative stress, cytotoxicity, dominant congenital lens cataract and microphthalmia.Semantic proximity Read ↗

The cataract causing Cx50-S50P mutant inhibits Cx43 and intercellular communication in the lens epithelium.Semantic proximity Read ↗

Connexin hemichannels in the lensSemantic proximity Read ↗

The cataract-inducing S50P mutation in Cx50 dominantly alters the channel gating of wild-type lens connexins.Semantic proximity Read ↗

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