Monash University

About: Monash University is a education organization based out in Melbourne, Victoria, Australia. It is known for research contribution in the topics: Population & Poison control. The organization has 35920 authors who have published 100681 publications receiving 3027002 citations.

A simple method for quantifying functional selectivity and agonist bias.

Abstract: Activation of seven-transmembrane (7TM) receptors by agonists does not always lead to uniform activation of all signaling pathways mediated by a given receptor. Relative to other ligands, many agonists are “biased” toward producing subsets of receptor behaviors. A hallmark of such “functional selectivity” is cell type dependence; this poses a particular problem for the profiling of agonists in whole cell test systems removed from the therapeutic one(s). Such response-specific cell-based variability makes it difficult to guide medicinal chemistry efforts aimed at identifying and optimizing therapeutically meaningful agonist bias. For this reason, we present a scale, based on the Black and Leff operational model, that contains the key elements required to describe 7TM agonism, namely, affinity (KA–1) for the receptor and efficacy (τ) in activating a particular signaling pathway. Utilizing a “transduction coefficient” term, log(τ/KA), this scale can statistically evaluate selective agonist effects in a manne...

Malaria parasite proteins that remodel the host erythrocyte

Abstract: Exported proteins of the malaria parasite Plasmodium falciparum interact with proteins of the erythrocyte membrane and induce substantial changes in the morphology, physiology and function of the host cell. These changes underlie the pathology that is responsible for the deaths of 1-2 million children every year due to malaria infections. The advent of molecular transfection technology, including the ability to generate deletion mutants and to introduce fluorescent reporter proteins that track the locations and dynamics of parasite proteins, has increased our understanding of the processes and machinery for export of proteins in P. falciparum-infected erythrocytes and has provided us with insights into the functions of the parasite protein exportome. We review these developments, focusing on parasite proteins that interact with the erythrocyte membrane skeleton or that promote delivery of the major virulence protein, PfEMP1, to the erythrocyte membrane.

A novel quadruple-cation absorber for universal hysteresis elimination for high efficiency and stable perovskite solar cells

Abstract: Organic–inorganic metal halide perovskite solar cells (PSCs) have made a striking breakthrough with a power conversion efficiency (PCE) over 22%. However, before moving to commercialization, the hysteresis of PSCs, characterized as an inconsistent photovoltaic conversion property at varied electric fields, should be eliminated for stable performance. Herein, we present a novel quadruple-cation perovskite absorber, KxCs0.05(FA0.85MA0.15)0.95Pb(I0.85Br0.15)3 (labeled as KCsFAMA), with which the hysteresis in PSCs can be fully eliminated irrespective of the electron transportation layers. The incorporation of potassium intensively promotes the crystallization of the perovskite film with a grain size up to ∼1 μm, doubled compared to the K free counterparts. Further characterization revealed that a lower interface defect density, longer carrier lifetime and fast charge transportation have all made contributions to the hysteresis-free, stable and high PCE (20.56%) of the KCsFAMA devices. Moreover, we present a 6 × 6 cm2 sub-module with the KCsFAMA composition achieving a high efficiency of 15.76% without hysteresis. This result suggests that the quadruple-cation perovskite is a highly attractive candidate for future developments of efficient and stable PSC modules.