Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens.

MLA

Harsolia, Ram Swaroop, et al. “Predicted Aggregation-Prone Region (APR) in ΒB1-Crystallin Forms the Amyloid-like Structure and Induces Aggregation of Soluble Proteins Isolated from Human Cataractous Eye Lens.” International Journal of Biological Macromolecules, vol. 163, Nov. 2020, pp. 702–10. EBSCOhost, https://doi.org/10.1016/j.ijbiomac.2020.07.028.

APA

Harsolia, R. S., Kanwar, A., Gour, S., Kumar, V., Kumar, V., Bansal, R., Kumar, S., Singh, M., & Yadav, J. K. (2020). Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens. International Journal of Biological Macromolecules, 163, 702–710. https://doi.org/10.1016/j.ijbiomac.2020.07.028

Chicago

Harsolia, Ram Swaroop, Ambika Kanwar, Shalini Gour, Vijay Kumar, Vikas Kumar, Rati Bansal, Suman Kumar, Manish Singh, and Jay Kant Yadav. 2020. “Predicted Aggregation-Prone Region (APR) in ΒB1-Crystallin Forms the Amyloid-like Structure and Induces Aggregation of Soluble Proteins Isolated from Human Cataractous Eye Lens.” International Journal of Biological Macromolecules 163 (November): 702–10. doi:10.1016/j.ijbiomac.2020.07.028.