Anna Marie Pyle
Anna Marie Pyle is the William Edward Gilbert Professor of Molecular, Cellular and Developmental Biology and Professor of Chemistry at Yale University. She has been a Howard Hughes Medical Institute Investigator since 1997. Dr. Pyle obtained her undergraduate degree in Chemistry from Princeton University and received her Ph.D. in Chemistry from Columbia University in 1990, where she worked with Professor Jacqueline K. Barton. Dr. Pyle was a postdoctoral fellow in the laboratory of Thomas Cech at the University of Colorado. Dr. Pyle formed her own research group in 1992 in the Department of Biochemistry and Molecular Biophysics at Columbia University Medical Center. In 2002, she moved to Yale University, where she leads a research group that specializes in structure and function of large RNA molecules and RNA remodeling enzymes. In addition to her work at Yale, Dr. Pyle is a member of the Science and Technology Steering Committee at Brookhaven National Labs and is an advisor to the NSLSII. She is the Co-Editor of Methods in Enzymology and she is the author of over 160 publications. The Pyle laboratory uses a diverse set of approaches, including crystallography, cryo-EM, cell biology and enzymology, to understand the biological function of complex RNA molecules. The Pyle laboratory has solved some of the largest RNA crystal structures, including the group II intron. She pioneered the study of RNA helicase enzymes and other RNA-stimulated ATPases that serve as translocases, RNA remodeling enzymes and sensors of pathogenic RNA. These studies are complemented by efforts to develop RNA and small molecule modulators of innate immune function and antiviral response.
Anna Marie Pyle studies RNA structure and RNA recognition by protein enzymes. Her lab uses a combination of experimental biochemistry and crystallography to study the architectural features of large RNA molecules, such as self-splicing introns and other noncoding RNAs. This is accompanied by complementary work on RNA-dependent ATPase enzymes that bind and remodel RNA structures, with an emphasis on proteins that are involved in viral replication and host innate immune response.