Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Malkaram S. Achary"'
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 26:609-623
This study embodies a detailed comparative analysis of the essential motions of the Wild type and the eight different disease mutant forms of the Human CYP1b1. The mutations considered in this study have been implicated in Primary Congenital Glaucoma
Autor:
Malkaram S. Achary, Aramati B. M. Reddy, Seyed E. Hasnain, Dorairajan Balasubramanian, Subhabrata Chakrabarti, Hampapathalu A. Nagarajaram, Niyaz Ahmed, Shirly G. Panicker, Anil K Mandal
Publikováno v:
Biophysical Journal. 91(12):4329-4339
In this communication, we report an in-depth structure-based analysis of the human CYP1b1 protein carrying disease-causing mutations that are discovered in patients suffering from primary congenital glaucoma (PCG). The “wild-type” and the PCG mut
Autor:
N. Laxman, Ahmed Kamal, P. Ramulu, M. Deepak, Malkaram S. Achary, Hampapathalu A. Nagarajaram, O. Srinivas, Tasneem Rehana, G. Ramesh
Publikováno v:
Bioorganic & Medicinal Chemistry. 12:5427-5436
Synthesis of mixed imine-amine pyrrolobenzodiazepine (PBD) dimers that are comprised of DC-81 and secondary amine (N10) of DC-81 subunits tethered to their C8 positions through alkanedioxy linkers (comprised of three and five carbons) is described. T
Publikováno v:
Journal of biosciences. 33(5)
Molecular docking has been used to compare and contrast the binding modes of oestradiol with the wild-type and some disease-associated mutant forms of the human CYP1b1 protein. The receptor structures used for docking were derived from molecular dyna
Autor:
F. Aneesa, Malkaram S. Achary, K. Sathish, R. Wasia, Hampapathalu A. Nagarajaram, Surya S. Singh, M. Sairam, Radhika V. Korupolu
Publikováno v:
International journal of biological macromolecules. 45(3)
Profilin is a cytoskeletal protein that interacts specifically with actin, phosphoinositides and poly (l-proline). Experimental results and in silico studies revealed that profilin exists as dimer and tetramer. Profilin oligomers possess weak affinit