Biography
Dr. Ananda M. Chakrabarty serves as Senior Science Advisor of Amrita Therapeutics Limited. Dr. Chakrabarty is a Amrita’s Senior Science Mentor and Global Domain Expert relating to how bacterial proteins effectively combat cancers, parasites, and viruses in the human body. Dr. Chakrabarty serves as a Distinguished University Professor of Microbiology and Immunology at the University of Illinois College of Medicine, and advises senior officials in the U.S. and abroad on policies relating to biotechnology and related technology transfer. He is a Consultant to the United Nations. In 1980, Dr. Chakrabarty’s genetically modified Pseudomonas bacteria became the first genetically-engineered organism to gain a patent, as a result of the Supreme Court decision in Diamond vs. Chakrabarty. Dr. Chakrabarty undertook pioneering biotechnology research into the therapeutic potential for protein products of bacteria, both at the University of Illinois at Chicago (UIC) and on behalf of CDG Therapeutics, a U.S. biotechnology start-up company engaged in clinical cancer research. Dr. Chakrabarty has led path-breaking research into the therapeutic qualities of protein products of bacteria. His work includes recent studies with water-soluble products of pathogenic bacteria demonstrating significant promise for cancer therapies, effective against HIV/AIDS, malaria and perhaps even tuberculosis. Dr. Chakrabarty was a part of the Advisory Committee that resulted in creation of the International Center for Genetic Engineering and Biotechnology (ICGEB) in Trieste, Italy and rejoined the ICGEB Advisory Board. Dr. Chakrabarty has numerous publications and has received many notable awards for his contributions to biotechnology, including Padma Shri in 2007, one of the Indian Government’s highest civilian honors.
Research Interest
Cell Biology, Microbiology, Pseudomonas aeruginosa, Cancer Cells, Biotechnology, Oncology, Cancer Biology, Cancer Therapy, Pseudomonas, Malaria, Cystic Fibrosis, Genetic Engineering, Infectious Diseases, Cancer Chemotherapy, Mutation
Biography
Akira Kaji is a professor of microbiology, School of Medicine, University of Pennsylvania. He contributed to the deciphering of genetic code by his discovery of the fact that the complex of poly-U with ribosome binds specifically tRNA specific for phenylalanine. He also discovered RRF.
Research Interest
The following is a short review of Akira Kaji past work. In 1963, they discovered that specific tRNA binds to the complex of mRNA and ribosome. This finding was essential to decipher the genetic code (9). Regarding RRF, upon in vivo inactivation of RRF, the ribosome starts the unscheduled translation downstream from the termination codon. Crystal structure by X-ray crystallography as well as solution structure by NMR has revealed that RRF is a near perfect structural mimic of tRNA. Indeed, we found that RRF functionally mimics tRNA in that it moves in the inter-subunits space like tRNA does. However, the mode of RRF binding to the ribosome is different from that of tRNA. We also discovered arginyl-tRNA protein transferase in 1963(10). This enzyme is an essential for higher eukaryotes and involved in post-translational protein modification.
Biography
2006-present: Adjunct Professor of Biochemistry & Molecular Biology, Indiana University School of Medicine 1996-present: Director, WM Keck Center for Transgene Research, University of Notre Dame 1983-present: Kleiderer/Pezold Professor of Biochemistry, University of Notre Dame 1979-2002: Dean, College of Science, University of Notre Dame 1977-1983: Professor, University of Notre Dame 1974-1977: Associate Professor, University of Notre Dame 1970-1974: Assistant Professor, University of Notre Dame 1968-1970: NIH Postdoctoral Fellow, Duke University 1968: Ph.D. in Biochemistry, University of Iowa 1964: B.S. University of Scranton
Research Interest
The interests of Professor Castellino\'s laboratory involve the structure, function and activation of proteins that participate in blood coagulation and blood clot dissolution. The in vivo mechanisms of the roles of these proteins in these processes are being addressed through in vivo targeted gene-replacement approaches and corresponding in vitro structure-function studies on these genes and proteins are being studied by the most modern biophysical techniques, e.g., X-ray crystallography, NMR, etc. Most of these proteins exist in an inactive state in plasma and thus must be activated to enzymes to exhibit their functional properties. The molecular events involved in the activation and analysis of the concomitant structural changes that occur in the protein are investigated by modern biochemical techniques. Major tools of the laboratory involve cloning, mutagenesis and expression of variant recombinant proteins and individual protein domains, immunochemical studies of the proteins, as well as physical and chemical analysis of their solution structures. The properties of the proteins are then related to their functions. Another project receiving attention involves the structure-function relationships of small gamma-carboxyglutamic acid (Gla)-containing peptides from marine cone snails that target the brain NMDA receptor. These peptides inhibit the flow of calcium into neuronal cells, this latter event being responsible for the neuropathology associated with stroke, epilepsy, Alzheimer\'s Disease, ALS, etc. The biochemical, pharmacological and neurobiological mechanisms of the actions of these peptides are under study. Peptide synthesis, receptor binding, molecular biological and electrophysiological tools are currently employed in this work. To determine the biological functions of genes encoding coagulation and clot-dissolving proteins in hemostasis, cancer, inflammation, wound healing, embryonic implantation and development, metastases, and athersclerosis, gene deletion and other gene targeting experiments are being performed in mice, in conjunction with phenotyping of these animals. Such studies are expected to provide important information on the development and progression of these disease states.