Results 11 to 20 of about 1,689 (175)

The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association. [PDF]

open access: yesPLoS ONE, 2016
In living systems proteins are typically found in crowded environments where their effective interactions strongly depend on the surrounding medium. Yet, their association and dissociation needs to be robustly controlled in order to enable biological ...
Jiachen Wei   +3 more
doaj   +2 more sources

Interaction of βA3-Crystallin with Deamidated Mutants of αA- and αB-Crystallins.

open access: yesPLoS ONE, 2015
Interaction among crystallins is required for the maintenance of lens transparency. Deamidation is one of the most common post-translational modifications in crystallins, which results in incorrect interaction and leads to aggregate formation.
Ekta Tiwary   +4 more
doaj   +2 more sources

The Functional Significance of High Cysteine Content in Eye Lens γ-Crystallins

open access: yesBiomolecules
Cataract disease is strongly associated with progressively accumulating oxidative damage to the extremely long-lived crystallin proteins of the lens. Cysteine oxidation affects crystallin folding, interactions, and light-scattering aggregation especially
Eugene Serebryany   +2 more
doaj   +2 more sources

Therapeutic Potential of α-Crystallins in Retinal Neurodegenerative Diseases

open access: yesAntioxidants, 2021
The chaperone and anti-apoptotic activity of α-crystallins (αA- and αB-) and their derivatives has received increasing attention due to their tremendous potential in preventing cell death.
Ashutosh S. Phadte   +2 more
doaj   +1 more source

Crystalline Catalase

open access: yesScience, 1937
Sumner, James B. and Dounce, Alexander L. Crystalline Catalase, 1937 ; https://digitalcommons.rockefeller.edu/pamphlets-offprints-and-reprints/1045/thumbnail ...
Sumner, James B., Dounce, Alexander L.
openaire   +2 more sources

The human crystallin gene families

open access: yesHuman Genomics, 2012
Crystallins are the abundant, long-lived proteins of the eye lens. The major human crystallins belong to two different superfamilies: the small heat-shock proteins (α-crystallins) and the βγ-crystallins.
Wistow Graeme
doaj   +1 more source

Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro

open access: yesAdvanced Science, 2023
Positioned within the eye, the lens supports vision by transmitting and focusing light onto the retina. As an adaptive glassy material, the lens is constituted primarily by densely‐packed, polydisperse crystallin proteins that organize to resist ...
Michael R. Bergman   +4 more
doaj   +1 more source

αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregation. [PDF]

open access: yesPLoS ONE, 2011
The eye lens is composed of fiber cells that are filled with α-, β- and γ-crystallins. The primary function of crystallins is to maintain the clarity of the lens through ordered interactions as well as through the chaperone-like function of α-crystallin.
Puttur Santhoshkumar   +2 more
doaj   +1 more source

Crystalline Pepsin [PDF]

open access: yesScience, 1929
A method is described for the preparation of a crystalline protein from commercial pepsin preparations which has powerful peptic activity. The composition, optical activity, and proteolytic activity of this protein remain constant through seven successive crystallizations.
openaire   +14 more sources

Dissimilarity in the Contributions of the N‑Terminal Domain Hydrophobic Core to the Structural Stability of Lens β/γ-Crystallins

open access: yes, 2019
Vertebrate lens β/γ-crystallins share a conserved tertiary structure consisting of four Greek-key motifs divided into two globular domains. Numerous inherited mutations in β/γ-crystallins have been linked to cataractogenesis.
Wei-Jie Zhao (295923)   +7 more
core   +2 more sources

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