Back to search

Article

Increased Association of Deamidated αA-N101D with Lens Membrane of Transgenic αAN101D vs. Wild Type αA Mice: Potential Effects on Intracellular Ionic Imbalance and Membrane Disorganization 

2020-11-20

Abstract excerpt

<title>Abstract</title> <p>We have generated two mouse models, in one by inserting the human lens αAN101D transgene in CRYαA<sub>N101D</sub> mice, and in the other by inserting human wild-type αA-transgene in CRYαA<sub>WT</sub> mice. The CRYαA<sub>N101D</sub> mice developed cortical cataract at about 7-months of age relative to CRYαA<sub>WT</sub> mice. The objective of the study was to determine the following rel...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
0a54c61a-810e-59b4-b06f-0b1ab6f63045
DOI
10.21203/rs.2.17769/v5
Open publication

Related research

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

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Increased Association of Deamidated αA-N101D with Lens Membrane of Transgenic αAN101D vs. Wild Type αA Mice: Potential Effects on Intracellular Ionic Imbalance and Membrane Disorganization&nbsp;DOI 10.21203/rs.2.17769/v5
G91-deletion in βA3/A1-crystallin induces cellular and molecular changes in mouse lenses leading to congenital cataract developmentSemantic proximity
CRYβA3/A1-Crystallin Knockout Develops Nuclear Cataract and Causes Impaired Lysosomal Cargo Clearance and Calpain Activation.Semantic proximity
Analysis of mouse lens morphological and proteomic abnormalities following depletion of βB3-crystallinSemantic proximity
Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.Semantic proximity
Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.Semantic proximity
Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.Semantic proximity
A cataract-causing Y204X mutation of CRYßB1 promotes C-terminal degradation and higher-order oligomerizationSemantic proximity
Temperature-dependent coaggregation of eye lens αB- and β-crystallins.Semantic proximity
Changes in relative histone abundance and heterochromatin in αA-crystallin and αB-crystallin knock-in mutant mouse lenses.Semantic proximity
In vivo carbamylation and acetylation of water‐soluble human lens αB‐crystallin lysine 92Semantic proximity
Dense nuclear cataract caused by the gammaB-crystallin S11R point mutation.Semantic proximity
Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Semantic proximity
Select a neighboring publication to make it the new centre.