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Published in 2021 at "Experimental eye research"
DOI: 10.1016/j.exer.2021.108707
Abstract: The nuclear region of the lens is metabolically quiescent, but it is far from inert chemically. Without cellular renewal and with decades of environmental exposures, the lens proteome, lipidome, and metabolome change. The lens crystallins…
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Keywords:
chemistry lens;
system cysteines;
redox chemistry;
chemistry ... See more keywords
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Published in 2020 at "Accounts of chemical research"
DOI: 10.1021/acs.accounts.0c00014
Abstract: ConspectusCrystallins are transparent, refractive proteins that contribute to the focusing power of the vertebrate eye lens. These proteins are extremely soluble and resist aggregation for decades, even under crowded conditions. Crystallins have evolved to avoid…
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Keywords:
aggregation;
function aggregation;
lens crystallins;
eye lens ... See more keywords
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Published in 2023 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.2c13397
Abstract: Cataracts are caused by high-molecular-weight aggregates of human eye lens proteins that scatter light, causing lens opacity. Metal ions have emerged as important potential players in the etiology of cataract disease, as human lens γ-crystallins…
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Keywords:
human lens;
lens crystallins;
chemistry;
radical chemistry ... See more keywords
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Published in 2022 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1073/pnas.2212051119
Abstract: Significance One common feature conserved across living systems is the presence of a high concentration of crystallin proteins packed within the eye lens. The polydispersity of crystallins in the vertebrate lens is one factor that…
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Keywords:
manipulating polydispersity;
crystallins using;
lens crystallins;
divalent cations ... See more keywords