Use of Eye Lens Protein for Estimating Age of Microtus pennsylvanicus

1983 ◽  
Vol 64 (4) ◽  
pp. 697-700 ◽  
Author(s):  
W. Q. Stump ◽  
R. G. Anthony
Keyword(s):  
Microtus Pennsylvanicus ◽  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein

Letter to the Editor: 1H, 15N and 13C resonance assignment of human ?S-crystallin, a 21�kDa eye-lens protein

2004 ◽  
Vol 30 (3) ◽  
pp. 385-386 ◽  
Author(s):  
Carine Baraguey ◽  
F�riel Skouri-Panet ◽  
Fran�ois Bontems ◽  
Annette Tardieu ◽  
G�rard Chassaing ◽  
...  
Keyword(s):  
Resonance Assignment ◽  
Eye Lens ◽  
Lens Protein ◽  
Letter To The Editor ◽  
Eye Lens Protein

scholarly journals Catalysis of cataract-associated human γD crystallin aggregation via dynamic disulfide exchange

2018 ◽  
Author(s):  
Eugene Serebryany ◽  
Shuhuai Yu ◽  
Sunia A. Trauger ◽  
Bogdan Budnik ◽  
Eugene I. Shakhnovich
Keyword(s):  
Light Scattering ◽  
Disulfide Bond ◽  
Eye Lens ◽  
Lens Protein ◽  
Biochemical Mechanism ◽  
Wild Type ◽  
Disulfide Exchange ◽  
Mechanism Of Catalysis ◽  
Eye Lens Protein

AbstractSeveral mutations in human γD-crystallin (HγD), a long-lived eye lens protein, cause misfolding and aggregation, leading to cataract. Surprisingly, wild-type HγD catalyzes aggregation of its cataract related W42Q variant while itself remaining soluble – the inverse of the classical prion-like scenario whereby misfolded polypeptides catalyze aggregation of natively folded ones. The search for a biochemical mechanism of catalysis of W42Q aggregation by WT has revealed that WT HγD can transfer a disulfide bond to the W42Q variant. The transferred disulfide kinetically traps an aggregation-prone intermediate made accessible by the W42Q mutation, facilitating light-scattering aggregation of the W42Q variant. The aggregating variant thus becomes a disulfide sink, removing the disulfides from solution. Such redox “hot potato” competitions among wild-type and mutant or modified polypeptides may be relevant for many long-lived proteins that function in oxidizing environments. In these cases aggregation may be forestalled by inhibiting disulfide flow toward damaged polypeptides.

scholarly journals e-Crystallin, a novel avian and reptilian eye lens protein

1985 ◽  
Vol 147 (1) ◽  
pp. 129-136 ◽  
Author(s):  
Steven O. STAPEL ◽  
Anneke ZWEERS ◽  
Huub J. DODEMONT ◽  
Jaap H. KAN ◽  
Wilfried W. JONG
Keyword(s):  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein

Dietary Vitamin C Delays UV-induced Eye Lens Protein Damage

1987 ◽  
Vol 498 (1 Third Confere) ◽  
pp. 460-463 ◽  
Author(s):  
J. BLONDIN ◽  
V. BARAGI ◽  
E. R. SCHWARTZ ◽  
J. A. SADOWSKI ◽  
A. TAYLOR
Keyword(s):  
Vitamin C ◽  
Protein Damage ◽  
Dietary Vitamin ◽  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein

scholarly journals Evolution of the Aldose Reductase-Related Gecko Eye Lens Protein ρB-Crystallin: A Sheep in Wolf's Clothing

2001 ◽  
Vol 52 (3) ◽  
pp. 239-248 ◽  
Author(s):  
Martinus A.M. van Boekel ◽  
Daan M.F. van Aalten ◽  
Gert-Jan Caspers ◽  
Beate Röll ◽  
Wilfried W. de Jong
Keyword(s):  
Aldose Reductase ◽  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein
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