V
Vicky T. Skamnaki
Researcher at University of Oxford
Publications - 22
Citations - 1353
Vicky T. Skamnaki is an academic researcher from University of Oxford. The author has contributed to research in topics: Glycogen phosphorylase & Phosphorylase kinase. The author has an hindex of 19, co-authored 22 publications receiving 1268 citations.
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Journal ArticleDOI
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.
Edward D. Lowe,Martin E.M. Noble,Vicky T. Skamnaki,Nikos G. Oikonomakos,David J. Owen,Louise N. Johnson +5 more
TL;DR: The structure of a truncated form of the γ‐subunit of phosphorylase kinase (PHKγt) has been solved in a ternary complex with a non‐hydrolysable ATP analogue and a heptapeptide substrate related to both the natural substrate and to the optimal peptide substrate.
Journal ArticleDOI
The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles.
Reiko Honda,Edward D. Lowe,Elena Dubinina,Vicky T. Skamnaki,Atlanta G. Cook,N.R. Brown,Louise N. Johnson +6 more
TL;DR: The structural and kinetic results indicate no inherent substrate discrimination between pCDK2/cyclin E and pCDk2/ cyclin A with model substrates.
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A new allosteric site in glycogen phosphorylase b as a target for drug interactions.
Nikos G. Oikonomakos,Vicky T. Skamnaki,Katerina E. Tsitsanou,Nikos G Gavalas,Louise N. Johnson +4 more
TL;DR: Although over 30 A from the catalytic site, the inhibitor exerts its effects by stabilising the T state at the expense of the R state and thereby shifting the allosteric equilibrium between the two states.
Journal ArticleDOI
Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site.
Nikos G. Oikonomakos,Joachim B. Schnier,Spyros E. Zographos,Vicky T. Skamnaki,Katerina E. Tsitsanou,Louise N. Johnson +5 more
TL;DR: Both flavopiridol and glucose promote the less active T-state through localization of the closed position of the 280s loop which blocks access to the catalytic site, thereby explaining their synergistic inhibition.
Journal ArticleDOI
The Role of the Phospho-CDK2/Cyclin A Recruitment Site in Substrate Recognition
Kin Yip Cheng,Martin E.M. Noble,Vicky T. Skamnaki,N.R. Brown,Ed D. Lowe,Luke Kontogiannis,Kui Shen,Philip A. Cole,Giuliano Siligardi,Louise N. Johnson +9 more
TL;DR: How localization at the recruitment site leads to increased catalytic efficiency and the design of a potent inhibitor is discussed and the notion of a flexible linker between the sites provides an explanation for recognition and discrimination against different substrates.