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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 recognition
Website:
http://cnu.edu/people/toddgruber/
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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
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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