Carl C. Correll Associate Professor 2004-present Ph.D., University of Michigan, '92 American Cancer Society Fellow Yale University with T.A. Steitz, ’92-‘97 Assistant Professor, University of Chicago,'98-'04 Phone: (847) 578-8611 Fax: (847) 578 3240 Email: Carl.Correll@RosalindFranklin.edu Department of Biochemistry and Molecular Biology Rosalind Franklin University of Medicine and Science 3333 Green Bay Road North Chicago, IL 60064

Interaction between protein and RNA is central to cellular and viral processes ranging from expressing genes to directing cell mortality, yet the principles that govern protein-RNA recognition are poorly understood. RNA can fold and as a consequence can create a great variety of distinctive molecular surfaces. How do these surfaces enable protein-RNA and RNA-RNA recognition? What role do these surfaces play in the structure, function and assembly of ribonucleoprotein (RNP) complexes? Which RNP proteins mediate RNA structural rearrangements and what mechanism do they use? We aim to address these questions by combining crystallographic, energetic and kinetic studies. Current projects focus on deciphering the molecular underpinnings of essential RNA–protein interactions in ribosome biogenesis--a vital cellular process that is emerging as an unexplored target for cancer treatment.

 Last updated by Correll November 2, 2010

Carl C. Correll Associate Professor 2004-present Ph.D., University of Michigan, '92 American Cancer Society Fellow Yale University with T.A. Steitz, ’92-‘97 Assistant Professor, University of Chicago,'98-'04 Phone: (847) 578-8611 Fax: (847) 578 3240 Email: Carl.Correll@RosalindFranklin.edu Department of Biochemistry and Molecular Biology Rosalind Franklin University of Medicine and Science 3333 Green Bay Road North Chicago, IL 60064

Interaction between protein and RNA is central to cellular and viral processes ranging from expressing genes to directing cell mortality, yet the principles that govern protein-RNA recognition are poorly understood. RNA can fold and as a consequence can create a great variety of distinctive molecular surfaces. How do these surfaces enable protein-RNA and RNA-RNA recognition? What role do these surfaces play in the structure, function and assembly of ribonucleoprotein (RNP) complexes? Which RNP proteins mediate RNA structural rearrangements and what mechanism do they use? We aim to address these questions by combining crystallographic, energetic and kinetic studies. Current projects focus on deciphering the molecular underpinnings of essential RNA–protein interactions in ribosome biogenesis--a vital cellular process that is emerging as an unexplored target for cancer treatment.

 Last updated by Correll November 2, 2010