All Outputs (3)

Ligand selectivity in stabilising tandem parallel folded G-quadruplex motifs in human telomeric DNA sequences (2014)
Journal Article
Cousins, A. R., Searle, M. S., Ritson, D., Sharma, P., Stevens, M. F., & Moses, J. E. (2014). Ligand selectivity in stabilising tandem parallel folded G-quadruplex motifs in human telomeric DNA sequences. Chemical Communications, 50(96), 15202-15205. https://doi.org/10.1039/c4cc07487d

© The Royal Society of Chemistry 2014. Biophysical studies of ligand interactions with three human telomeric repeat sequences (d(AGGG(TTAGGG)n, n = 3, 7 and 11)) show that an oxazole-based 'click' ligand, which induces parallel folded quadruplexes, p... Read More about Ligand selectivity in stabilising tandem parallel folded G-quadruplex motifs in human telomeric DNA sequences.

Formal synthesis of kingianin A based upon a novel electrochemically-induced radical cation Diels–Alder reaction (2014)
Journal Article
Moore, J. C., Davies, E. S., Walsh, D. A., Sharma, P., & Moses, J. E. (2014). Formal synthesis of kingianin A based upon a novel electrochemically-induced radical cation Diels–Alder reaction. Chemical Communications, 50(83), 12523-12525. https://doi.org/10.1039/c4cc05906a

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.