Season 2023/2024

Dr. Masaru Okabe received his PhD from Osaka University and has spent the entirety of his career researching at that institution, with the exception of 1.5 years at the National Institute of Environmental Health Sciences in Research Triangle Park, North Carolina, USA.

He served as a Professor in the Genome Information Research Center of the Research Institute for Microbial Diseases and became Director of the Animal Resource Center for Infectious Diseases at the Research Institute for Microbial Diseases, Osaka University, in 2002. He has published over 250 original articles. His general research area is reproduction, with a specific research interest in the mechanism of sperm-egg interaction. He published the first fusion factor on mouse sperm (IZUMO1) in Nature and was involved in the finding of fusion-related factor CD9 on egg, as published in Science. He believes in the power of gene-manipulated animals and utilizes many transgenic and knockout mouse lines in his research. He is also known as the scientist who demonstrated that GFP is usable in mouse by producing the first “green mice” in the world.

Ciechanover was born in Haifa, British mandate of Palestine, a year before the establishment of the State of Israel. His family had immigrated from Poland before the Second World War. He earned a master's degree in science in 1971 and graduated from Hadassah Medical School in Jerusalem in 1974. He received his doctorate in biochemistry in 1982 from the Technion (the Israel Institute of Technology), in Haifa. He is currently a Technion Distinguished Research Professor in the Ruth and Bruce Rappaport Faculty of Medicine and Research Institute at the Technion. Ciechanover is a member of the Israel Academy of Sciences and Humanities, the Pontifical Academy of Sciences, and is a foreign associate of the United States National Academy of Sciences. In 2005, he was voted the co-31st-greatest Israeli of all time, in a poll by the Israeli news website Ynet to determine whom the general public considered the 200 Greatest Israelis. As one of Israel's first Nobel Laureates in Science, he is honored in playing a central role in the history of the State of Israel and in the History of the Technion - Israel Institute of Technology. Along with Professor Guigen Li (as a Co-Director) from Texas Tech University, Professor Ciechanover is now trying to build a cross disciplinary Center in Nanjing University, where the accumulated knowledge in biology and chemistry will be translated into novel therapeutics.

Human cells receive a constant bombardment of signaling information, and they have evolved strategies to generate proper physiological responses. The cell processes this signaling information, correctly choosing which of the approximately 20,000 genes will be switched "on" or "off." Using genetic, biochemical, and biological approaches, Michael G. Rosenfeld is deciphering on a genome-wide scale how cells control gene expression through the integration of the output to these diverse signals, which is crucial to the body's development and its smooth operation. His studies have revealed surprising new strategies that precisely regulate the pattern of genes that are turned "on" and "off"—processes that are linked to other key cellular responses, such as DNA damage and repair. This knowledge is providing the backdrop to developing new treatments for diseases that occur when gene expression goes awry, such as diabetes, atherosclerosis, cancer, and growth defects in children. Rosenfeld's enthusiasm for research was initially sparked during numerous discussions he had with his father, a physical chemist, on scientific topics ranging from astronomy and mathematical models to biology and evolution. "The joy he transmitted in his love of science was very infectious," Rosenfeld says. When he entered college at the Johns Hopkins University, Rosenfeld entertained thoughts of becoming an archaeologist. But a biochemistry course taught by the renowned William McElroy, who made groundbreaking discoveries in bioluminescence and later became director of the National Science Foundation and chancellor at UC San Diego, inspired Rosenfeld with the "creative fire" to shift his major to biology and biochemistry. A number of mentors in his medical and postdoctoral training helped Rosenfeld to focus his energies on understanding the mechanisms that underlie critical aspects of mammalian development and homeostasis. Over the years, Rosenfeld has developed a comprehensive picture of cell signaling and gene transcriptional events that occur during embryonic development of the hypothalamus and pituitary gland, and an understanding of when and how these signals go wrong, resulting in disease. The hypothalamus links the nervous system to the endocrine system, and the pituitary gland secretes hormones important for metabolism, growth, homeostasis, and reproduction. These studies have served as a model for increasing the understanding of mammalian organ development and have made important contributions to comprehending the way gene expression is controlled during the development of the central nervous system and the neuroendocrine system. These lines of research have led to insights into growth defects that occur in humans. For example, Rosenfeld and his colleagues have identified the molecular basis for three forms of dwarfism, including the type based on mutations in the Prop-1 gene, the most common pituitary-based growth disorder in the world. Study of this system inevitably led the Rosenfeld laboratory to delineate new rules by which molecular mediators called transcription factors bind to DNA to activate or repress gene expression. The expression of each gene is controlled by evolutionarily conserved sequences immediately adjacent to the coding region, referred to as a "promoter," or more distant regions, referred to as "enhancers." When the correct transcription factors dock to these sequences, a process is initiated that involves the interactions between these proteins and a network of cofactors that ultimately switches genes "on" or "off." Rosenfeld also has elucidated a series of integrated molecular strategies that link cohorts of experienced genes to detection of specific signaling pathways. He is now exploring how missteps in the machinery integrating transcriptional events can lead to disease, including insulin resistance, which often develops into type 2 diabetes, and resistance to drugs used to treat several common forms of cancer. "One of the most exciting aspects of our current research efforts is to explore the vast unknown territory that links gene transcription to the architecture of the nucleus in which these events occur," says Rosenfeld. "This should provide critical insights over the next five years that have broad implications for human disease."

Michael G. Rossmann (born 1930) is a German-American physicist, microbiologist, and Hanley Distinguished Professor of Biological Sciences at Purdue University who led a team of researchers to be the first to map the structure of a human common cold virus to an atomic level. He also discovered the Rossmann fold protein motif.

Born in Frankfurt, Germany, Rossmann studied physics and mathematics at the University of London, where he received BSc and MSc degrees. He moved to Glasgow in 1953 where he taught physics in the technical college and received his Ph.D. in chemical crystallography in 1956. He attributes his initial interest in crystallography to Kathleen Lonsdale, whom he heard speak as a schoolboy.

Rossmann began his career as a crystallographer when he became a student of J. Monteath Robertson at the University of Glasgow. The title of his thesis was "A Study of Some Organic Crystal Structures".

In 1956 he and his family moved to the University of Minnesota where he worked for two years as a post-doctoral fellow with Professor William N. Lipscomb, Jr., publishing on the structure of an Iresin Diester and a terpenoid, and writing computer programs for analysing structures.

Rossmann returned to the UK and to the University of Cambridge in 1958, where he worked with Max Perutz on the structure of hemoglobin as a research associate at the MRC Laboratory of Molecular Biology.

In 1964 Rossmann joined the faculty of the Department of Biological Sciences at Purdue University as an associate professor. He directs the Purdue X-ray crystallography laboratory. He became full professor in 1967 and since 1978 has held the chair of Hanley Distinguished Professor of Biological Sciences at the university. He also holds a joint appointment in the department of biochemistry and adjunct positions in Cornell University's Division of Biological Sciences and in Indiana University's school of medicine.

In 1973 Rossmann published the description of the Rossmann fold, a nucleotide binding motif found in enzymes such as dehydrogenases or kinases that bind molecules such as adenosine triphosphate or nicotinamide adenine dinucleotide.

In 1985, he published his team's mapping, using X-ray crystallography, of a human common cold virus in the journal Nature. The breakthrough nature of this result was such that the National Science Foundation, which provided partial funding for the research, saw fit to organize a press conference, and the news travelled in the general press.

The Rossmann cluster is named for Michael Rossmann, Purdue's Hanley Distinguished Professor of Biological Sciences, who is a pioneer in employing high-performance computing in research to reveal the structure of viruses and their component protein molecules. Rossmann gained worldwide attention in 1985 by determining the structure of human rhinovirus serotype14, HRV-14, one of about 100 known cold virus strains.

Stephen Philip Jackson, FRS, FMedSci, (born 17 July 1962 in Nottingham, England) is the Frederick James Quick Professor of Biology and a Fellow of St. John's College, Cambridge. He is a Senior Group Leader and Head of Cancer Research UK Laboratories at the Gurdon Institute, and an Associate Faculty member at the Wellcome Trust Sanger Institute. He is also part-time Chief Scientific Officer for MISSION Therapeutics Ltd.

Professor Jackson was educated at the University of Leeds, graduating with a Bachelor of Science degree in Biochemistry in 1983. He then carried out his PhD research working with Jean Beggs on yeast RNA splicing at Imperial College London and Edinburgh University, earning his PhD in 1987.

Following his PhD, Jackson carried out postdoctoral research with Robert Tjian at the University of California, Berkeley, where he developed an interest in the regulation of transcription. He returned to the UK in 1991 as a Junior Group Leader at the then Wellcome-CRC Institute, now the Gurdon Institute.

In 1997 Jackson founded KuDOS Pharmaceuticals with the aim of translating knowledge of DNA damage response pathways into new treatments for cancer. KuDOS developed into a fully integrated drug-discovery and drug-development company and was acquired by AstraZeneca in 2005.

In 2011 Jackson founded MISSION Therapeutics a firm to develop drugs to improve the management of life-threatening diseases, particularly cancer.

Jackson has received various prizes, including the Biochemical Society GlaxoSmithKline Award (2008), the BBSRC Innovator of the Year Award (2009) and the Royal Society Buchanan Medal (2011), the latter in recognition of his "outstanding contributions to understanding DNA repair and DNA damage response signalling pathways". He was elected a member of the European Molecular Biology Organization (EMBO) in 1997, a Fellow of the Academy of Medical Sciences in 2001 and a Fellow of the Royal Society in 2008.

Jennifer Anne Doudna is a Professor of Chemistry and of Molecular and Cell Biology at the University of California, Berkeley. She has been an investigator with the Howard Hughes Medical Institute (HHMI) since 1997.

Doudna earned her B.A. in Chemistry from Pomona College and her Ph.D. in Biochemistry from Harvard University on ribozymes under the mentorship of Jack W. Szostak. She did her postdoctoral work with Thomas Cech at the University of Colorado, Boulder.

While in the Szostak lab, Doudna reengineered the self-splicing Group I catalytic intron into a true catalytic ribozyme that would copy RNA templates. Recognizing the limitations of not being able see the molecular mechanisms of the ribozymes. She started work to crystallize and solve the three-dimensional structure of the Tetrahymena Group I ribozyme in 1991 in the Cech Lab and continued while she started her professorship at Yale University in 1994. While the group was able to grow high-quality crystals, they struggled with the phase problem due to unspecific binding of the metal ions. One of her early graduate students and later her husband, Jamie Cate decided to soak the crystals in osmium hexamine to imitate magnesium. Using this strategy, they were able to solve the structure, the second solved folded RNA structure since tRNA. The magnesium ions would cluster at the center of the ribozyme and would serve as a core for RNA folding similar to that of a hydrophobic core of a protein.

Doudna was promoted to the position of Henry Ford II Professor of Molecular Biophysics and Biochemistry at Yale in 2000. In 2002, she accepted a faculty position at University of California, Berkeley as a Professor of Biochemistry and Molecular Biology so that she would be closer to family and the synchrotron at Lawrence Berkeley National Laboratory. This initial work to solve large RNA structures led to further structural studies on the HDV ribozyme, the IRES, and protein-RNA complexes like the Signal recognition particle. Her lab now focuses on obtaining a mechanistic understanding of biological processes involving RNA. This work is divided over three major areas, the CRISPR system, RNA interference, and translational control via MicroRNAs.

In 2012 and her colleagues generated a new discovery that would reduce the time and work on editing DNA. Their discovery relies on a protein named Cas9 found in the Streptococcus bacteria "CRISPR" immune system that works like scissors. The protein attacks its prey, the DNA of viruses, and slices it up.

Doudna was a Searle Scholar and received a 1996 Beckman Young Investigators Award, the 1999 NAS Award for Initiatives in Research and the 2000 Alan T. Waterman Award. She was elected to the National Academy of Sciences in 2002 and to the Institute of Medicine in 2010. In 2014, Doudna was awarded the Lurie Prize in Biomedical Sciences from the Foundation for the National Institutes of Health as well as the Dr. Paul Janssen Award for Biomedical Research and Breakthrough Prize in Life Sciences, both shared with Emmanuelle Charpentier. In 2015, Doudna was named one of Time Magazine's 100 most influential people in the world and received the Princess of Asturias Awards, both together with Emmanuelle Charpentier.

Joan Elaine Argetsinger Steitz (born January 26, 1941) is Sterling Professor of Molecular Biophysics and Biochemistry at Yale University and Investigator at the Howard Hughes Medical Institute. She is known for her discoveries involving RNA, including ground-breaking insights into how ribosomes interact with messenger RNA by complementary base pairing and that introns are spliced by small nuclear ribonucleic proteins (snRNPs), which occur in eukaryotes.

Steitz was born in Minneapolis, Minnesota. She grew up in Minnesota in the 1950s and 60s at a time when there were virtually no female role models in molecular biology. She attended the then all-girls Northrop College for high school.

In 1963, Steitz received her Bachelor of Science degree in chemistry from Antioch College, Ohio, where she first became interested in molecular biology at Alex Rich's Massachusetts Institute of Technology laboratory as an Antioch "coop" intern.

After completing her undergraduate degree, Steitz applied to medical school rather than graduate school since she knew of female medical doctors but not female scientists. She was accepted to Harvard Medical School, but having been excited by a summer working as a bench scientist in the laboratory of Joseph Gall at the University of Minnesota, she declined the invitation to Harvard Medical School and instead applied to Harvard's new program in biochemistry and molecular biology. There, she was the first female graduate student to join the laboratory of Nobel Laureate James Watson, with whom she first worked on bacteriophage RNA.

Steitz completed postdoctoral research at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) at the University of Cambridge (UK), where she collaborated with Francis Crick, Sydney Brenner, and Mark Bretscher. At the LMB, Steitz focused on the question of how bacteria know where to start the "reading frame" on mRNA. In the process, Steitz discovered the exact sequences on mRNA at which bacterial ribosomes bind to produce proteins. In 1969 she published a seminal paper inNature showing the nucleotide sequence of the binding start points.

In 1970, Steitz joined the faculty at Yale. In 1975, she published the research for which she is widely known, demonstrating that ribosomes use complementary base pairing to identify the start site on mRNA.

Stephen James Benkovic (born April 20, 1938) is an American chemist. He is Evan Pugh Professor and Eberly Chair in Chemistry at Penn State University.His research has focused on mechanistic enzymology and the discovery of enzyme inhibitors.He was elected to the United States National Academy of Sciences in 1985.

Benkovic was born in Orange, New Jersey. He earned his B.S. degree in chemistry and an A.B. degree in English literature from Lehigh University in 1960. He earned his Ph.D in organic chemistry from Cornell University in 1963.

Benkovic was a postdoc at University of California, Santa Barbara. There he and his advisor Thomas C. Bruice developed bioorganic textbooks that focused on enzyme catalysis. He joined the chemistry department at Penn State University in 1965. There, he uses the T4 DNA polymerase as a model system to explain the proficiency of enzymes.[5] He also uses the enzyme dihydrofolate reductase and the pathway for de novo purine biosynthesis to gain insights into enzymatic catalysis.