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Philip Hanoian, Ph.D. - Publications

Affiliations: 
2014 Pennsylvania State University, State College, PA, United States 
Area:
Molecular Chemistry
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2015 Hanoian P, Liu CT, Hammes-Schiffer S, Benkovic S. Perspectives on electrostatics and conformational motions in enzyme catalysis. Accounts of Chemical Research. 48: 482-9. PMID 25565178 DOI: 10.1021/Ar500390E  0.464
2014 Liu CT, Layfield JP, Stewart RJ, French JB, Hanoian P, Asbury JB, Hammes-Schiffer S, Benkovic SJ. Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase. Journal of the American Chemical Society. 136: 10349-60. PMID 24977791 DOI: 10.1021/Ja5038947  0.458
2014 Schwans JP, Hanoian P, Lengerich BJ, Sunden F, Gonzalez A, Tsai Y, Hammes-Schiffer S, Herschlag D. Experimental and computational mutagenesis to investigate the positioning of a general base within an enzyme active site. Biochemistry. 53: 2541-55. PMID 24597914 DOI: 10.1021/Bi401671T  0.377
2013 Liu CT, Hanoian P, French JB, Pringle TH, Hammes-Schiffer S, Benkovic SJ. Functional significance of evolving protein sequence in dihydrofolate reductase from bacteria to humans. Proceedings of the National Academy of Sciences of the United States of America. 110: 10159-64. PMID 23733948 DOI: 10.1073/Pnas.1307130110  0.392
2011 Hanoian P, Hammes-Schiffer S. Water in the active site of ketosteroid isomerase. Biochemistry. 50: 6689-700. PMID 21710970 DOI: 10.1021/Bi200703Y  0.393
2010 Hanoian P, Sigala PA, Herschlag D, Hammes-Schiffer S. Hydrogen bonding in the active site of ketosteroid isomerase: electronic inductive effects and hydrogen bond coupling. Biochemistry. 49: 10339-48. PMID 21049962 DOI: 10.1021/Bi101428E  0.321
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