Renuka Kadirvelraj
Affiliations: | University of Georgia, Athens, Athens, GA, United States |
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| Kadirvelraj R, Boruah BM, Wang S, et al. (2023) Structural basis for Lewis antigen synthesis by the α1,3-fucosyltransferase FUT9. Nature Chemical Biology |
| Boruah BM, Kadirvelraj R, Liu L, et al. (2020) Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases. The Journal of Biological Chemistry. 295: 17027-17045 |
| Kadirvelraj R, Yang JY, Kim HW, et al. (2020) Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites. The Journal of Biological Chemistry. 100110 |
| Kadirvelraj R, Yang JY, Kim HW, et al. (2020) Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites. The Journal of Biological Chemistry |
| Boruah BM, Kadirvelraj R, Liu L, et al. (2020) Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases. The Journal of Biological Chemistry |
| Shrestha S, Katiyar S, Sanz-Rodriguez CE, et al. (2020) A redox-active switch in fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily. Science Signaling. 13 |
| Keul ND, Oruganty K, Schaper Bergman ET, et al. (2018) The entropic force generated by intrinsically disordered segments tunes protein function. Nature |
| Kadirvelraj R, Yang JY, Sanders JH, et al. (2018) Human -acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite. Proceedings of the National Academy of Sciences of the United States of America |
| Keul ND, Kadirvelraj R, Oruganty K, et al. (2017) The role of intrinsic disorder in human UDP-glucose dehydrogenase Acta Crystallographica Section a Foundations and Advances. 73: a173-a173 |
| Walsh RM, Polizzi SJ, Kadirvelraj R, et al. (2015) Man o' war mutation in UDP-α-D-xylose synthase favors the abortive catalytic cycle and uncovers a latent potential for hexamer formation Biochemistry. 54: 807-819 |