The impact of different mutations at Arg54 on structure, chaperone-like activity and oligomerization state of human αA-crystallin: the pathomechanism underlying congenital cataract-causing mutations R54L, R54P and R54C KazemKhoshaman a , Reza Yousefi a, *, Ali Mohammad Tamaddon b , Samira Sadat Abolmaali b , Ahmad Oryan c , Ali Akbar Moosavi-Movahedi d , Boris I. Kurganov e a Protein Chemistry Laboratory (PCL), Department of Biology, Shiraz University, Shiraz, Iran b Center for Nanotechnology in Drug Delivery and School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran c Department of Pathology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran d Institute of Biochemistry and Biophysics (IBB), the University of Tehran, Tehran, Iran e Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 33, bld. 2 Leninsky Ave., Moscow 119071, Russia *Corresponding author: Dr. Reza Yousefi, Protein Chemistry Laboratory (PCL), Department of Biology, Shiraz University, Shiraz, Iran; Phone: +98 711 36137617; Fax: ++98 711 32280916; E-mail: ryousefi@shirazu.ac.ir Funding:This work was supported by theIran National Science Foundation [grant no. 92001695]andthe Russian Science Foundation [grant number 16-14-10055 to B.I.K.]. © 2017. This manuscript version is made available under the Elsevier user license http://www.elsevier.com/open-access/userlicense/1.0/