چاپ صفحه |  صفحه نخست سامانه |  چکیده مقاله |  نویسندگان |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده ثبت کننده مقاله | حامد همیشه کار |
| مرحله جاری مقاله | تایید نهایی |
| دانشکده/مرکز مربوطه | مرکز تحقیقات کاربردی دارویی |
| کد مقاله | 61476 |
| عنوان فارسی مقاله | Exploring the association of rs10490924 polymorphism with age-related macular degeneration: An in silico approach |
| عنوان لاتین مقاله | Exploring the association of rs10490924 polymorphism with age-related macular degeneration: An in silico approach |
| ناشر | 2 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ | |
| عنوان نشریه (خارج از لیست فوق) | Journal of Molecular Graphics and Modelling |
| نوع مقاله | Original Article |
| نحوه ایندکس شدن مقاله | ایندکس شده سطح یک – ISI - Web of Science |
| آدرس لینک مقاله/ همایش در شبکه اینترنت | http://www.sciencedirect.com/science/article/pii/S1093326317302942 |
| The polymorphism rs10490924 (A69S) in the age-related maculopathy susceptibility 2 (ARMS2) gene is highly associated with age-related macular degeneration, which is the leading cause of blindness among the elderly population. The ARMS2 gene encodes a putative small (11 kDa) protein, which the function and localization of the ARMS2 protein remain under debate. For a better understanding of functional impacts of the A69S mutation, we performed a detailed analysis of the ARMS2 sequence with a broad set of bioinformatics tools. In silico analysis was followed to predict the tertiary structure, putative binding site regions, and binding site residues. Also, the effects of this mutation on protein stability, aggregation propensity, and homodimerization were analyzed. Next, a molecular dynamic simulation was carried out to understand the dynamic behavior of wild-type, A69S, and phosphorylated A69S structures. The results showed alterations in the putative post-translational modification sites on the ARMS2 protein, due to the mutation. Furthermore, the stability of protein and putative homodimer conformations were affected by the mutation. Molecular dynamic simulation results revealed that the A69S mutation enhances the rigidity of the ARMS2 structure and residue serine at position 69 is buried and may not be phosphorylated; however, phosphorylated serine enhances the flexibility of the ARMS2 structure. In conclusion, our study provides new insights into the deleterious effects of the A69S mutation on the ARMS2 structure. |
| نویسنده | نفر چندم مقاله |
|---|---|
| حامد همیشه کار | دوم |
| فرهاد جهانفر | اول |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| 1-s2.0-S1093326317302942-main.pdf | 1396/07/03 | 2522448 | دانلود |
