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β-amino acids reduce ternary complex stability and alter the translation elongation mechanism.
bioRxiv [Preprint]. 2024 Feb 27:2024.02.24.581891. doi: 10.1101/2024.02.24.581891.
bioRxiv. 2024.
PMID: 38464221
Free PMC article.
Preprint.
An Enzyme with High Catalytic Proficiency Utilizes Distal Site Substrate Binding Energy to Stabilize the Closed State but at the Expense of Substrate Inhibition.
Robertson AJ, Cruz-Navarrete FA, Wood HP, Vekaria N, Hounslow AM, Bisson C, Cliff MJ, Baxter NJ, Waltho JP.
Robertson AJ, et al. Among authors: cruz navarrete fa.
ACS Catal. 2022 Mar 4;12(5):3149-3164. doi: 10.1021/acscatal.1c05524. Epub 2022 Feb 22.
ACS Catal. 2022.
PMID: 35692864
Free PMC article.
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Allomorphy as a mechanism of post-translational control of enzyme activity.
Wood HP, Cruz-Navarrete FA, Baxter NJ, Trevitt CR, Robertson AJ, Dix SR, Hounslow AM, Cliff MJ, Waltho JP.
Wood HP, et al. Among authors: cruz navarrete fa.
Nat Commun. 2020 Nov 2;11(1):5538. doi: 10.1038/s41467-020-19215-9.
Nat Commun. 2020.
PMID: 33139716
Free PMC article.
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1H, 15N and 13C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form.
Cruz-Navarrete FA, Baxter NJ, Wood HP, Hounslow AM, Waltho JP.
Cruz-Navarrete FA, et al.
Biomol NMR Assign. 2019 Oct;13(2):349-356. doi: 10.1007/s12104-019-09904-y. Epub 2019 Aug 8.
Biomol NMR Assign. 2019.
PMID: 31396843
Free PMC article.
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