个人简介

Anne Baranger received a B.S. in Chemistry from the Massachusetts Institute of Technology in 1988 and a Ph.D. in Chemistry from the University of California, Berkeley, in 1993, under the direction of Professor Robert Bergman. She was a postdoctoral fellow at Yale University with Professor Alanna Schepartz from 1993-1996. Professor Baranger joined the Wesleyan University chemistry faculty in 1996 and the University of Illinois chemistry faculty in 2006. At the University of Illinois, she was Associate Head of the Department, Director of Graduate Studies, and was a Chancellor's Fellow in the I-STEM Education Initiative. She joined the University of California, Berkeley, in 2011. She is the recipient of the Rudolph Anderson Postdoctoral Fellowship (1993-95), the Donaghue Foundation Postdoctoral Fellowship (1995) and an Alfred P. Sloan Research Fellowship (2002-2004).

研究领域

RNA Recognition By Proteins and Small Molecules. Our research program seeks to understand and control the recognition of RNA by proteins and small molecules. RNA is important in all steps of gene expression and usually acts in concert with proteins. Thus, an understanding of the recognition of RNA by proteins and small molecules is necessary for a complete description of biological processes involving RNA and the development of small molecules capable of modulating these processes. One goal of our research is to determine how proteins achieve high affinity and specificity for RNA. To quantify and rationally modulate energetic contributions, we systematically modify protein sequences and RNA nucleotides. We use computational and fluorescence methods to understand and predict the contributions of energetic coupling and dynamic processes to the recognition of RNA by proteins. We have principally studied RNA recognition by proteins containing the RNA recognition motif (RRM), which is one of the most common RNA-binding domains and is found in proteins that function in nearly every step of post-transcriptional gene expression. A second goal of our research is to develop a fundamental understanding of the recognition of non-helical nucleic acid structures by small molecules. Specific, high affinity ligands for RNA would be valuable tools for probing biological processes involving RNA and could be effective drugs. We use a combination of rational design, computational docking, and high throughput screening of small molecule libraries to identify compounds that bind to RNA. Our RNA targets include RNA tetraloops that are essential for ribosome structure and function, Stem Loop 3 of Y RNA of HIV, and bulged CUG and CCUG repeat RNAs that are the cause of myotonic dystrophy. Chemical Education, Curricular Development, and Assessment. The chemistry department at the University of California, Berkeley serves a large population of undergraduate and graduate students and is a national and international leader in research. Therefore, the chemistry department is positioned to be a leader in the development of innovative programs in chemistry education that impact a large number of students. An overall goal our work is to increase the numbers of students in science, technology, engineering, and mathematics (STEM) fields and improve the scientific knowledge of both STEM students and students who do not ultimately choose to major in a STEM area. To achieve this, we are pursuing three broad topics: 1) curricular development, 2) improving the participation of underrepresented groups in our programs, and 3) developing rigorous and on-going evaluation of the program and assessment of student learning to allow an approach for educational reform based on hard data.

RNA Recognition By Proteins and Small Molecules. Our research program seeks to understand and control the recognition of RNA by proteins and small molecules. RNA is important in all steps of gene expression and usually acts in concert with proteins. Thus, an understanding of the recognition of RNA by proteins and small molecules is necessary for a complete description of biological processes involving RNA and the development of small molecules capable of modulating these processes. One goal of our research is to determine how proteins achieve high affinity and specificity for RNA. To quantify and rationally modulate energetic contributions, we systematically modify protein sequences and RNA nucleotides. We use computational and fluorescence methods to understand and predict the contributions of energetic coupling and dynamic processes to the recognition of RNA by proteins. We have principally studied RNA recognition by proteins containing the RNA recognition motif (RRM), which is one of the most common RNA-binding domains and is found in proteins that function in nearly every step of post-transcriptional gene expression. A second goal of our research is to develop a fundamental understanding of the recognition of non-helical nucleic acid structures by small molecules. Specific, high affinity ligands for RNA would be valuable tools for probing biological processes involving RNA and could be effective drugs. We use a combination of rational design, computational docking, and high throughput screening of small molecule libraries to identify compounds that bind to RNA. Our RNA targets include RNA tetraloops that are essential for ribosome structure and function, Stem Loop 3 of Y RNA of HIV, and bulged CUG and CCUG repeat RNAs that are the cause of myotonic dystrophy. Chemical Education, Curricular Development, and Assessment. The chemistry department at the University of California, Berkeley serves a large population of undergraduate and graduate students and is a national and international leader in research. Therefore, the chemistry department is positioned to be a leader in the development of innovative programs in chemistry education that impact a large number of students. An overall goal our work is to increase the numbers of students in science, technology, engineering, and mathematics (STEM) fields and improve the scientific knowledge of both STEM students and students who do not ultimately choose to major in a STEM area. To achieve this, we are pursuing three broad topics: 1) curricular development, 2) improving the participation of underrepresented groups in our programs, and 3) developing rigorous and on-going evaluation of the program and assessment of student learning to allow an approach for educational reform based on hard data.

近期论文

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Purcell, S. C.; Pande, P.; Lin,Y.; Rivera,E.J.; LatishaPawU, L.; Smallwood, L.M.; Kerstiens, G.A.; Armstrong, L.B.; Robak, M.T.; Baranger, A.M.; Douskey, M.C. “Extraction and Antibacterial Properties of Thyme Leaf Extracts: Authentic Practice of Green Chemistry” J. Chem. Ed. ASAP. Linn, M.L., Palmer, E., Baranger, A., Gerard, E., Stone, E."Undergraduate research experiences: Impacts and opportunities" Science, 2015, 347, 627 Ramisetty, R.R.; Baranger, A.M. “Cooperative Binding of a Quinoline Derivative to an RNA Stem Loop Containing a Dangling End”, Bioorg. Med. Chem. Lett. 2010 3134. Benitex, Y.; Baranger, A.M. “Control of the Stability of a Protein-RNA Complex by the Position of Fluorine in a Base Analog”, J. Am. Chem. Soc. 2011, 133, 3687. Kormos, B.L.; Pieniazek, S.N.; Beveridge, D.L.; Baranger, A.M. “U1A Protein – Stem Loop 2 RNA Recognition: Prediction of Structural Differences from Protein Mutations ”, Biopolymers, 2011, 95, 591. Anunciado, D.; Dhar, A.; Gruebele, M; Baranger, A.M. "Multistep Kinetics of the U1A-SL2 RNA Complex Dissociation", J. Mol. Biol. 2011, 408, 896. Wong, C.-H.; Fu, Y.; Ramisetty, S.R.; Baranger, A.M.; Zimmerman, S.C. “Selective inhibition of MBNL1–CCUG interaction by small molecules toward potential therapeutic agents for myotonic dystrophy type 2 (DM2)”, Nucleic Acids Res. 2011, 39, 8881. Warui, D.M.; Baranger, A.M. “Identification of Small Molecule Inhibitors of the HIV-1 Nucleocapsid-SL3 RNA Complex”, J. Med. Chem. 2012, 55, 4132. Fu, Y.; Ramisetty, S.R.; Hussain, N.; Baranger, A.M. “MBNL1–RNA Recognition: Contributions of MBNL1 Sequence and RNA Conformation”, ChemBioChem 2012, 13, 112. Wong, C.-H.; Richardson, S.L.; Ho, Y.-J.; Lucas, A.M.H.; Tuccinardi, T.; Baranger, A.M.; Zimmerman, S.C. “Investigating the Binding Mode of an Inhibitor of the MBNL1-RNA Complex in Myotonic Dystrophy Type 1 (DM1) Leads to the Unexpected Discovery of a DNA-Selective Binder”, ChemBioChem, 2012, 13, 2505. Jahromi, A.H.; Nguyen, L.; Fu, Y.; Miller, K.A., Anne M. Baranger, A.M.; Zimmerman, S.C. “A Novel CUGexp·MBNL1 Inhibitor with Therapeutic Potential for Myotonic Dystrophy Type 1”, ACS Chem. Biol., 2013, 8, 1037 Jahromi, A.H.; Fu, Y.; Nguyen, L.; Miller, K.; Baranger, A.M.; Zimmerman, S.C. “Developing Bivalent Ligands to Target CUG Triplet Repeats, the Causative Agent of Myotonic Dystrophy Type 1" J. Med. Chem. 2013, 56, 9471. Wong, C.-H.; Nguyen, L.; Peh, J.; Luu, L.M.; Sanchez, J.S.; Richardson, S.L.; Tuccinardi, T.; Tsoi, H.; Chan, W.Y.; Chan, H.Y.E.; Baranger, A.M.; Hergenrother, P.J.; Zimmerman, S.C. “Targeting Toxic RNAs that Cause Myotonic Dystrophy Type 1 (DM1) with a Bisamidinium Inhibitor”, J. Am. Chem. Soc. 2014, 136, 6355. Guzman, I.; Ghaemi, Z.; Baranger, A.; Luthey-Schulten, Z.; Gruebele, M. “Native Conformational Dynamics of the Spliceosomal U1A Protein” J. Phys. Chem. B 2015, 119, 3651. Linn, M.C.; Palmer, E.; Baranger, A.; Gerard, E.; Stone, E. “Undergraduate Research Experiences: Impacts and Opportunities” Science 2015, 347, 627. Luchansky, S.; Nolan, S.J.; Baranger, A.M. “Contribution of RNA Conformation to the Stability of a High-Affinity RNA-Protein Complex”, J. Am. Chem. Soc. 2000, 122, 7130. Blakaj, D.M.; McConnell, K.J.; Beveridge, D.L.; Baranger, A.M. "Molecular Dynamics and Thermodynamics of a Protein-RNA Complex: Mutation of a Conserved Aromatic Residue Modifies Stacking Interactions and Structural Adaptation in the U1A-stem Loop 2 RNA Complex", J. Am. Chem. Soc. 2001, 123, 2548. Shiels, J.C.; Jerkovic, B.; Baranger, A.M.; Bolton, P.H. “RNA-DNA Hybrids Containing Damaged DNA are Substrates for RNase H”, Bioorg. Med. Chem. Lett. 2001, 11, 2623. Shiels, J.C.; Tuite, J.B.; Nolan, S.J.; Baranger, A.M. "Investigation of a Conserved Stacking Interaction in Target Site Recognition by the U1A Protein", Nucleic Acids Res. 2002, 30, 550. Pitici, F.; Baranger, A.M., Beveridge, D.L. “Molecular Dynamics Simulation Studies of Induced Fit and Conformational Capture in U1A-RNA Binding: Do Molecular Substates Code for Specificity?”, Biopolymers 2002, 65, 424. Gayle, A.Y.; Baranger, A.M. “Inhibition of the U1A-RNA Complex by an Aminoacridine Derivative”, Bioorg. Med. Chem. Lett. 2002, 12, 2839. Tuite, J.B.; Shiels, J.C.; Baranger, A.M. “Substitution of an Essential Adenine in the U1A-RNA Complex with a Non-polar Isostere”, Nucleic Acids Res. 2002, 30, 5269, cover article. Zhao, Y.; Baranger, A.M. “Design of an Adenosine Analog that Selectively Improves the Affinity of a Mutant U1A Protein for RNA”, J. Am. Chem. Soc. 2003, 125, 2480. Yan, Z.; Baranger, A.M. “Binding of an Aminoacridine Derivative to a Tetraloop RNA”, Bioorg. Med. Chem. Lett. 2004, 14, 5889. Zhao, Y.; Kormos, B.L.; Beveridge, D.L.; Baranger, A.M. “Molecular Dynamics Simulation Studies of a Protein-RNA Complex with a Selectively Modified Binding Interface”, Biopolymers 2006, 81, 256.