All Outputs (3)

Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase (2014)
Journal Article
Moses, J. E., Harper, S., Dempster, S., Dreveny, I., Harper, S., & Moses, J. (2014). Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase. Acta Crystallographica Section D: Biological Crystallography, 70(5), 1484-1490. https://doi.org/10.1107/s1399004714005422

Lactate dehydrogenase A (LDH-A) is a key enzyme in anaerobic respiration that is predominantly found in skeletal muscle and catalyses the reversible conversion of pyruvate to lactate in the presence of NADH. LDH-A is overexpressed in many tumours and... Read More about Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase.

Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains (2014)
Journal Article
Harper, S., Gratton, H. E., Cornaciu, I., Oberer, M., Scott, D. J., Emsley, J., & Dreveny, I. (2014). Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains. Biochemistry, 53(18), 2966-2978. https://doi.org/10.1021/bi500116x

The ubiquitin specific protease 11 (USP11) is implicated in DNA repair, viral RNA replication, and TGFβ signaling. We report the first characterization of the USP11 domain architecture and its role in regulating the enzymatic activity. USP11 consists... Read More about Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains.

The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification (2014)
Journal Article
Dreveny, I., Deeves, S. E., Fulton, J., Yue, B., Messmer, M., Bhattacharya, A., …Heery, D. M. (2014). The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Research, 42(2), 822-835. https://doi.org/10.1093/nar/gkt931

Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine ac... Read More about The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.