Ana Rita Calixto
Affiliations: | 2018- | Chemistry - BMC | Uppsala University, Uppsala, Uppsala län, Sweden |
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"Ana Calixto"
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| Corbella M, Bravo J, Demkiv AO, et al. (2024) Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases. Jacs Au. 4: 3519-3536 |
| Corbella M, Bravo J, Demkiv AO, et al. (2024) Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases. Biorxiv : the Preprint Server For Biology |
| Crean RM, Corbella M, Calixto AR, et al. (2024) Sequence - dynamics - function relationships in protein tyrosine phosphatases. Qrb Discovery. 5: e4 |
| Shen R, Crean RM, Olsen KJ, et al. (2022) Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases. Chemical Science. 13: 13524-13540 |
| Crean RM, Biler M, Corbella M, et al. (2022) Correction to "Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases". Journal of the American Chemical Society. 144: 10091-10093 |
| Calixto AR, Moreira C, Kamerlin SCL. (2020) Recent Advances in Understanding Biological GTP Hydrolysis through Molecular Simulation. Acs Omega. 5: 4380-4385 |
| Sousa SF, Calixto AR, Ferreira P, et al. (2020) Activation Free Energy, Substrate Binding Free Energy,and Enzyme Efficiency Fall in a Very Narrow Range of Values for MostEnzymes Acs Catalysis. 10: 8444-8453 |
| Moreira C, Calixto AR, Richard JP, et al. (2019) The role of ligand-gated conformational changes in enzyme catalysis. Biochemical Society Transactions |
| Calixto AR, Ramos MJ, Fernandes PA. (2019) Conformational diversity induces nanosecond-timescale chemical disorder in the HIV-1 protease reaction pathway. Chemical Science. 10: 7212-7221 |
| Calixto AR, Moreira C, Pabis A, et al. (2019) GTP Hydrolysis Without an Active Site Base: A Unifying Mechanism for Ras and Related GTPases. Journal of the American Chemical Society |