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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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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.
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Panel docking of small-molecule libraries — Prospects to improve efficiency of lead compound discovery

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.
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Enzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatases.

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.
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Chemical probing suggests redox-regulation of the carbonic anhydrase activity of mycobacterial Rv1284

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.