Todd D. Gruber, Ph.D. - Publications
Affiliations: | 2004-2009 | Chemistry | University of Wisconsin, Madison, Madison, WI |
2013- | Chemistry | Christopher Newport University, Newport News, VA, United States |
Area:
Biomolecular recognitionWebsite:
http://cnu.edu/people/toddgruber/Year | Citation | Score | |||
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2018 | Gruber TD, Krishnamurthy C, Grimm JB, Tadross MR, Wysocki LM, Gartner ZJ, Lavis LD. Cell-Specific Chemical Delivery Using a Selective Nitroreductase-Nitroaryl Pair. Acs Chemical Biology. PMID 30111097 DOI: 10.1021/Acschembio.8B00524 | 0.367 | |||
2013 | Chakraborty S, Gruber T, Barry CE, Boshoff HI, Rhee KY. Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis. Science (New York, N.Y.). 339: 88-91. PMID 23118010 DOI: 10.1126/Science.1228980 | 0.305 | |||
2009 | Gruber TD, Westler WM, Kiessling LL, Forest KT. X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin. Biochemistry. 48: 9171-3. PMID 19719175 DOI: 10.1021/Bi901437V | 0.642 | |||
2009 | Gruber TD, Borrok MJ, Westler WM, Forest KT, Kiessling LL. Ligand binding and substrate discrimination by UDP-galactopyranose mutase. Journal of Molecular Biology. 391: 327-40. PMID 19500588 DOI: 10.1016/J.Jmb.2009.05.081 | 0.461 | |||
2007 | Chad JM, Sarathy KP, Gruber TD, Addala E, Kiessling LL, Sanders DA. Site-directed mutagenesis of UDP-galactopyranose mutase reveals a critical role for the active-site, conserved arginine residues. Biochemistry. 46: 6723-32. PMID 17511471 DOI: 10.1021/Bi7002795 | 0.613 | |||
2004 | Soltero-Higgin M, Carlson EE, Gruber TD, Kiessling LL. A unique catalytic mechanism for UDP-galactopyranose mutase. Nature Structural & Molecular Biology. 11: 539-43. PMID 15133501 DOI: 10.1038/Nsmb772 | 0.572 | |||
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