tRNA

Structural and biochemical analysis of the dual-specificity Trm10 enzyme from prompts reconsideration of its catalytic mechanism.

Singh, R. Kumar, Feller A., Roovers M., Van Elder D., Wauters L., Droogmans L., and Versées W., "Structural and biochemical analysis of the dual-specificity Trm10 enzyme from prompts reconsideration of its catalytic mechanism.", RNA, vol. 24, issue 8, pp. 1080-1092, 2018 08.

Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis.

Singh, R. Kumar, Steyaert J., and Versées W., "Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis.", Protein Sci, vol. 26, issue 5, pp. 985-996, 2017 05.

Structural and biochemical analysis of ObgE, a central regulator of bacterial persistence.

Gkekas, S., Singh R. Kumar, Shkumatov A. V., Messens J., Fauvart M., Verstraeten N., Michiels J., and Versées W., "Structural and biochemical analysis of ObgE, a central regulator of bacterial persistence.", J Biol Chem, vol. 292, issue 14, pp. 5871-5883, 2017 04 07.

The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of .

Rosado, L. Astolfi, Wahni K., Degiacomi G., Pedre B., Young D., de la Rubia A. G., Boldrin F., Martens E., Marcos-Pascual L., Sancho-Vaello E., et al., "The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of .", J Biol Chem, vol. 292, issue 32, pp. 13097-13110, 2017 08 11.

The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis.

Deyaert, E., Kortholt A., and Versées W., "The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis.", Acta Crystallogr F Struct Biol Commun, vol. 73, issue Pt 9, pp. 520-524, 2017 Sep 01.

A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.

Deyaert, E., Wauters L., Guaitoli G., Konijnenberg A., Leemans M., Terheyden S., Petrovic A., Gallardo R., Nederveen-Schippers L. M., Athanasopoulos P. S., et al., "A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.", Nat Commun, vol. 8, issue 1, pp. 1008, 2017 10 18.

Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts.

Guaitoli, G., Raimondi F., Gilsbach B. K., Gómez-Llorente Y., Deyaert E., Renzi F., Li X., Schaffner A., Jagtap P. Kumar Anku, Boldt K., et al., "Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts.", Proc Natl Acad Sci U S A, vol. 113, issue 30, pp. E4357-66, 2016 07 26.

Skywalker-TBC1D24 has a lipid-binding pocket mutated in epilepsy and required for synaptic function.

Fischer, B., Lüthy K., Paesmans J., De Koninck C., Maes I., Swerts J., Kuenen S., Uytterhoeven V., Verstreken P., and Versées W., "Skywalker-TBC1D24 has a lipid-binding pocket mutated in epilepsy and required for synaptic function.", Nat Struct Mol Biol, vol. 23, issue 11, pp. 965-973, 2016 Nov.

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