Biography
Prakash V Diwan, male Pharmacologist, obtained his PhD from Post graduate Institute of Medical Education and Research, India in 1980. He served as Assistant Professor in Medical College, India and later joined the Research and development organization, Indian Institute of Chemical Technology (CSIR) in 1983-2007. He became the Founder Director NIPER, Hyderabad in the year 2007. He was awarded with many national awards in the field of pharmacology. He is a Fellow of Royal Society of London (FRSC). To his credit he has over 160 research publication in national and international journals. He has been honored as a fellow of Indian Pharmacological Society and fellow of Andhra Pradesh Academy of Sciences. He has been a member in Indian Pharmacopeia Commission, Scientific Consultant for various reputed pharmaceutical industries. Presently he holds the responsible positions as Director and Research scientist in academia & Research and development Institutions.
Research Interest
pharmacology,biostatistics, bio standardization and Toxicology
Biography
He is completed his Postdoctoral Scholar at University of California, San Dieg and Graduate Research Assistant in University of Illinois at Urbana-Champaign. Now he is a Research Scientist in University of California, San Diego.
Research Interest
Molecular Biology, Cellular Biology, Biochemistry, and Microscopy Techniques

Sergey Suchkov
Professor and Chair
I.M. Sechenov First Moscow State Medical University
Russia
Biography
Dr Sergey Suchkov, MD, PhD. Professor in Immunology & Medicine. Chair, Dept for Personal-ized and Translational Medicine, I.M.Sechenov First Moscow State Medical Born 11 January 1957, Astrakhan, Russia; two sons. Education: MD, Astrakhan State Medical University, Russia, 1980; PhD, I.M.Sechenov First Moscow State Medical University, 1985; Doctor Degree, Na-tional Institute of Immunology, Russia, 2001. Positions held: Post Doc Research Associate, In-stitute of Medical Enzymology; Head of the Lab of Immunology, Helmholtz Eye Research Insti-tute in Moscow; Trainee, Laboratory of Immunology, NEI, Bethesda, MD, USA; Chair,, De-partment for Clinical Immunology, Moscow Clinical Research Institute; Executive Secretary-in-Chief of the Editorial Board, Biomedical Science International journal; Chairman & Director of the Department of Personalized Medicine. Honours: Secretary General, United Cultural Conven-tion, Cambridge, UK. Memberships: New York Academy of Sciences, USA; EPMA, Brussels.
Research Interest
Abs against myelin basic protein/MBP endowing with proteolytic activity (Ab-proteases) are of great value to monitor demyelination to illustrate the evolution of multiple sclerosis (MS). Anti-MBP autoAbs from MS patients and mice with EAE exhibited specific proteolytic cleavage of MBP The activity of the MBP-targeted Ab-proteases markedly differs between: (i) MS patients and healthy controls; (ii) different clinical MS courses; (iii) EDSS scales of demyelination to cor-relate with the disability of MS patients to predict the transformation prior to changes of the clin-ical course. The sequence-specificity of Ab-proteases demonstrates five sites of preferential proteolysis to be located within the immunodominant regions of MBP confirmed by the structural databanks. Two of them falling inside the sequence covering a 81-103 peptide and its 82-98 subsegment as well, with the highest encephalitogenic properties both to act as a specific inducer of EAE and to be attacked by the MBP-targeted Ab-proteases in MS patients with the most severe (progradient) clinical courses. Sites localized within the frame of 43-68 and 146-170 peptide subsegments whilst being less immunogenic happened to be EAE inducers very rare but were shown to be attacked by Ab-proteases in MS patients with moderate (remission-type) clinical courses. The activity of Ab-proteases was first registered at the subclinical stages 1-2 years prior to the clinical illness. About 24% of the direct MS-related relatives were seropositive for low-active Ab-proteases from which 38% of the seropositive relatives established were being monitored for 2 years whilst demonstrating a stable growth of the Ab-associated proteolytic activity. Registration in the evolution of highly immunogenic Ab-proteases to attack 81-103 and 82-98 sites pre-dominantly would illustrate either risks of transformation of subclinical stages into clinical ones, or risks of exacerbations to develop. The activity of Ab-proteases in combination with the sequence-specificity would confirm a high subclinical and predictive (translational) value of the tools as applicable for personalized moni-toring protocols. And close association between the proteolytic sensitivity of MBP and post-translational modifications of the latter may represent one of the key regulatory mechanisms in the epitope generation.