Prior to UO

1. Ruetz, M., Mascarenhas, R., Widner, F., Kieninger, C., Koutmos, M., Kräutler,B., Banerjee, R., A Noble Metal Substitution Leads to B12 Cofactor Mimicry by a Rhodibalamin (2024) Biochemistry,63 (15), 1955-1962.

2. Roman, J., Mascarenhas, R., Ceric,K., Ballou,D.P., Banerjee, R.(2023) Disease-causing cystathionine β-synthase linker mutations impair allosteric regulation. J.Biol.Chem. 299(12):105449

3. Mascarenhas, R., Guha, A., Li, Z., An, S., Ruetz, M., Servalli, J., Banerjee, R. (2023) Cobalt-sulfur coordination chemistry drives B12 loading onto methionine synthase. J Am Chem Soc 145 (45), 24678-24689

4. Gouda, H., Mascarenhas, R., Ruetz, M., Yaw, M., Banerjee, R. (2023) Bivalent molecular mimicry by ADP protects metal redox state and promotes coenzyme B12 repair. Proc Natl Acad Sci U.S.A. 120 (11), e2220677120

5. Mascarenhas, R#., Ruetz, M#., Gouda, H., Yaw, M., Heitman, N., Banerjee, R. (2023) Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B12 delivery and repair. Nat Commun 14, 4332 (2023)

6. Mascarenhas, R#., Gouda#, H., Ruetz, M., Banerjee, R. (2022) Human B12-dependent enzymes: Methionine synthase and Methylmalonyl-CoA mutase. Methods in enzymology 668, 309-32

7. Gouda, H#., Mascarenhas, R#., Pillay, S., Ruetz, M., Koutmos, M., Banerjee, R. (2021) Patient mutations in human ATP:cobalamin adenosyl transferase differentially affect its catalytic versus chaperone functions J.Biol.Chem. 297(6):101373

8. Mascarenhas, R., Li, Z., Gherasim, C., Ruetz, M., Banerjee, R. (2020) The human B12 trafficking protein CblC processes nitrocobalamin J.Biol.Chem. 295(28), 9030-9640

9. Mascarenhas, R#., Ruetz, M#., McDevitt, L., Koutmos, M., Banerjee, R. (2020) Mobile loops in adenosyltransferase control ergonomic binding and reactivity of coenzyme B12 Proc Natl Acad Sci U.S.A. 117(48), 30412-30422

10. Li, Z., Mascarenhas, R., Twahir, U.T., Kallon, A., Deb, A., Yaw, M., Penner-Hahn, J., Koutmos, M., Warncke, K., Banerjee, R., An interprotein Co-S coordination complex in the B12-trafficking pathway (2020) J Am Chem Soc 142(38), 16334-16345

11. Reidl, C.,#  Mascarenhas, R.,#  Mohammad, T.,  Lutz Jr., M., Thomas,P.,  Fast,W.,  Liu,D., and Becker, D (2021) Cyclobutanone Inhibitor of Cobalt-Functionalized Metallo-γ-Lactonase AiiA with Cyclobutanone Ring Opening in the Active Site ACS Omega 6, 21, 13567–13578

12. Asencion Diez, MD., Figueroa,C.M., Esper,M.C., Mascarenhas, R., Aleanzi, M.C., Liu, D., Ballicora, M.A, Iglesias, A.A., (2020) On the simultaneous activation of Agrobacterium tumefaciens ADP-glucose pyrophosphorylase by pyruvate and fructose-6-phosphate. Biochimie, 171-172, 23-30

13. Juncosa, J. I., K. Takaya, H. V. Le, M. J. Moschitto, P. M. Weerawarna, R. Mascarenhas, D. Liu, S. L. Dewey & R. B. Silverman (2018) Design and Mechanism of (S)-3-Amino-4(difluoromethylenyl)cyclopent-1-ene-1-carboxylic Acid, a Highly Potent gamma-Aminobutyric Acid Aminotransferase Inactivator for the Treatment of Addiction. J Am Chem Soc, 140, 2151-2164.

Highlighted: Service, R. F. “Chemists seek antiaddiction drugs to battle hijacked brain.” Science 2018, 360, 139-140.

14. Hill, B.,# Mascarenhas, R.,# Patel, H., Diez, M. A., Wu, R., Iglesias, A. A., Liu, D., & Ballicora, M.A., (2018) The pyruvate regulatory site of the Agrobacterium tumefaciens ADP-glucose pyrophosphorylase. J.Biol.Chem. 294(4), 1338-1348

15. Mascarenhas, R., H. V. Le, K. D. Clevenger, H. J. Lehrer, D. Ringe, N. L. Kelleher, R. B. Silverman & D. Liu (2017) Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover. Biochemistry, 56, 4951-4961.

16. Clevenger, K. D., R. Mascarenhas, D. Catlin, R. Wu, N. L. Kelleher, E. J. Drake, A. M. Gulick, D. Liu & W. Fast (2017) Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ. ACS Chem Biol, 12, 643-647.

17. Mascarenhas, R., P. W. Thomas, C. X. Wu, B. P. Nocek, Q. Q. Hoang, D. Liu & W. Fast (2015) Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity. Biochemistry, 54, 4342-53.

# Indicates equal contribution