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- Oliverio, Ryan; Nguyen, Peter; Kdeiss, Brianna; Ord, Sara; Daniels, Amanda J.; Nikolaidis, Nikolas
- Biochemical and biophysical research communications 2018 v.506 no.4 pp. 799-804
- adenosine triphosphate; apoptosis; calorimetry; dissociation; entropy; genes; heat shock proteins; humans; hydrolysis; luciferase; mutants; single nucleotide polymorphism; titration
- ... In this report, we investigated the effects of natural single nucleotide polymorphisms on the function of HSPA1A, the major stress-inducible Hsp70 gene in humans. We first established that all mutant proteins retain their ability to hydrolyze ATP, but three of them had a significantly lower rate of ATP hydrolysis as compared to the wild-type (WT) protein. We also used Isothermal Titration Calorime ...
- Bari, Khandekar Jishan; Sharma, Shrikant; Chary, Kandala V.R.
- Biochemical and biophysical research communications 2018 v.506 no.4 pp. 862-867
- blindness; calcium; cataract; childhood; circular dichroism spectroscopy; cortex; differential scanning calorimetry; eye lens; fluorescence; fluorescence emission spectroscopy; homeostasis; humans; mutants; mutation; proteins; titration
- ... Infantile cataracts constitute one of the most important causes of childhood blindness worldwide. Human γS-crystallin is the most abundant protein in the eye lens cortex. A missense mutant of human γS-crystallin, Y67N (abbreviated hereafter as γS-Y67N) is recently reported to be associated with dominant infantile cataracts. To understand the structural basis for γS-Y67N to cause lens opacification ...