M
Megan Cross
Researcher at Griffith University
Publications - 20
Citations - 181
Megan Cross is an academic researcher from Griffith University. The author has contributed to research in topics: Enzyme & Trehalose. The author has an hindex of 7, co-authored 20 publications receiving 140 citations. Previous affiliations of Megan Cross include University of the Witwatersrand.
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Journal ArticleDOI
Trading Health for Wealth: The Effect of COVID-19 Response Stringency.
TL;DR: Investigation of response stringency, quantified by the Oxford COVID-19 Government Response Tracker’s Stringency Index, and examined how restrictive interventions affected infection rates and gross domestic product (GDP) in China and OECD countries found that governments who responded to the pandemic faster saw greater reductions in viral transmission, but worse decreases in GDP.
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Role of individual histidines in the pH-dependent global stability of human chloride intracellular channel 1.
TL;DR: It is concluded that both His74 and His185 are involved in triggering the pH changes to the conformational stability of wild-type CLIC1 via their protonation, which stabilizes the intermediate state.
Journal ArticleDOI
Panel docking of small-molecule libraries — Prospects to improve efficiency of lead compound discovery
Pakornwit Sarnpitak,Prashant Mujumdar,Paul Taylor,Megan Cross,Mark J. Coster,Alain-Dominique Gorse,Mikhail Krasavin,Andreas Hofmann,Andreas Hofmann +8 more
TL;DR: By computationally screening a reasonably sized library of 1235 compounds against a panel of 48 mostly human kinases, this article is able to identify five groups of putative lead compounds with substantial diversity when compared to each other.
Journal ArticleDOI
Enzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatases.
Megan Cross,Siji Rajan,Janine Chekaiban,Jake Saunders,Chloe Hamilton,Jeong-Sun Kim,Mark J. Coster,Robin B. Gasser,Andreas Hofmann,Andreas Hofmann +9 more
TL;DR: Analysis of the kinetics of trehalose-6-phosphate hydrolysis reveals that all five enzymes display a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state, which can be explained by multiple global conformational changes in members of this enzyme family during substrate processing.
Journal ArticleDOI
Chemical probing suggests redox-regulation of the carbonic anhydrase activity of mycobacterial Rv1284
Lisa Mary Nienaber,Elysia Cave-Freeman,Megan Cross,Lyndel Mason,Ulla-Maja Bailey,Parisa Amani,Rohan A. Davis,Paul Taylor,Andreas Hofmann,Andreas Hofmann +9 more
TL;DR: It is reported that the catalytic activity of the mycobacterial enzyme Rv1284 can be reversibly inhibited by oxidation and linked conditions of oxidative stress to pH homeostasis of the pathogen.