Cataract‐Causing Mutant R188C of βB2 Crystallin With Low Structural Stability is Sensitive to Environmental Stresses and Prone to Aggregates Formation DOI Creative Commons
Yibo Yu, Silong Chen, Ying Zhang

et al.

Exploration, Journal Year: 2025, Volume and Issue: unknown

Published: April 1, 2025

ABSTRACT This study investigated a Chinese family with congenital posterior polar cataracts linked to the βB2‐R188C mutation. βB2‐crystallin, key structural component of lens, is crucial for maintaining lens transparency and stability. We examined effects R188C mutation on βB2‐crystallin's stability resistance environmental stressors using purified proteins cellular models. The mutant showed poor tendency aggregate under physiological pathological conditions. disrupted oligomerization equilibrium, causing dissociation dimers into monomers. Molecular dynamics simulations spectroscopic experiments revealed abnormal protein folding induced by mutation, increasing susceptibility stressors. Aggregation was observed in both prokaryotic eukaryotic models normal conditions, enhanced severity Notably, lanosterol treatment or αB‐crystallin partially reversed aggregation. In summary, promotes aggregation destabilizing βB2‐crystallin disrupting potentially leading cataract formation. Targeting formation small molecules like enhancing molecular chaperone activity offers promising strategy prevention treatment.

Language: Английский

Cysteine variants in PMM2 lead to protein instability and higher sensitivity to oxidative stress in PMM2-CDG DOI

Jingmiao Sun,

Ying Zhang,

Wei Yu

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 305, P. 140865 - 140865

Published: Feb. 12, 2025

Language: Английский

Citations

0
Demonstration of the Feasibility of Mainstream Aging Theories and Intervention DOI
Baohua Huang

Published: Jan. 1, 2025

Language: Английский

Citations

0
Causality of Aging Hallmarks DOI
Baohua Huang, Xiaowen Hu

Published: Jan. 1, 2025

Citations

0
Supplementary Calcium Overcomes Nocturnal Chilling‐Induced Carbon Source‐Sink Limitations of Cyclic Electron Transport in Peanuts DOI Open Access
Di Wu,

Siwei Zhang,

Chunming Bai

et al.

Plant Cell & Environment, Journal Year: 2025, Volume and Issue: unknown

Published: March 30, 2025

ABSTRACT ‘Calcium (Ca 2+ ) priming’ is an effective strategy to restore efficient carbon assimilation with undergoing unfavourable cold stress (day/night: 25°C/8°C). However, it unclear how exogenous calcium strengthens the cyclic electron transfer (CET) attain optimal flux. To assess nutrient fortification role of Ca (15 mM) in facilitating this process for peanuts, we added antimycin (AA, 100 μM) and rotenone (R, as specific inhibitors. Our results revealed that inhibiting CET caused a negative effect on photosynthesis. The treatment accelerated turnover non‐structural carbohydrates, linear carriers while balancing photosystem I (PSI) bilateral redox potential. also strengthened PROTON GRADIENT REGULATION5 (PGR5)/PGR5‐LIKE PHOTOSYNTHETIC PHENOTYPE1 (PGRL1) NADH dehydrogenase‐like (NDH)‐mediated CET, plausible crosstalk between thioredoxin (Trx) system signalling, regulate chloroplast homoeostasis. Specifically, PGR5/PGRL1‐mediated by providing sufficient ATP adequate photoprotection during long‐term exposure; NDH‐mediated served alleviate limitations PSI acceptor side translocating protons. This study demonstrated effectiveness harnessing supply, form foliar ‐based sprays strengthen eco‐physiological resilience peanuts against stress.

Language: Английский

Citations

0
Cataract‐Causing Mutant R188C of βB2 Crystallin With Low Structural Stability is Sensitive to Environmental Stresses and Prone to Aggregates Formation DOI Creative Commons
Yibo Yu, Silong Chen, Ying Zhang

et al.

Exploration, Journal Year: 2025, Volume and Issue: unknown

Published: April 1, 2025

ABSTRACT This study investigated a Chinese family with congenital posterior polar cataracts linked to the βB2‐R188C mutation. βB2‐crystallin, key structural component of lens, is crucial for maintaining lens transparency and stability. We examined effects R188C mutation on βB2‐crystallin's stability resistance environmental stressors using purified proteins cellular models. The mutant showed poor tendency aggregate under physiological pathological conditions. disrupted oligomerization equilibrium, causing dissociation dimers into monomers. Molecular dynamics simulations spectroscopic experiments revealed abnormal protein folding induced by mutation, increasing susceptibility stressors. Aggregation was observed in both prokaryotic eukaryotic models normal conditions, enhanced severity Notably, lanosterol treatment or αB‐crystallin partially reversed aggregation. In summary, promotes aggregation destabilizing βB2‐crystallin disrupting potentially leading cataract formation. Targeting formation small molecules like enhancing molecular chaperone activity offers promising strategy prevention treatment.

Language: Английский

Citations

0