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30 results on '"Murray, Jason"'

3. Assessment of novel disinfection technologies, and bacterial contamination in the healthcare setting

Author

Murray, Jason, Gill, Chris, and Ternan, Nigel

Subjects
362.1969, Microbiology, Healthcare, Associated Infections, Contamination
Abstract

Worldwide, hundreds of thousands of healthcare acquired infections (HAIs) are reported each year. HAIs are infections that occur whilst in hospital or as a result of hospital admittance, contamination of hospitals is a source of, and allows dissemination of HAIs. In healthcare settings one of the major vectors of contamination is healthcare workers' uniforms. As surfaces become contaminated, bacteria can then be contacted by patients (direct transmission) or staff who may then indirectly spread those bacteria to patients. Both direct and indirect spread of bacteria could result in infection of patients ultimately resulting in increased infection rates and associated costs. A further consequence of such a scenario is the increased levels of antibiotic use, the survival of antibiotic resistant bacteria and increased prevalence of antimicrobial resistance. A pilot study was conducted at Antrim Area Hospital, Northern Health and Social Care Trust. 100 pre-shift and 100 post-shift healthcare workers' uniforms were assessed for Staphylococcus aureus and Enterococcus spp. isolates. We found increased levels of antibiotic resistant S. aureus and antibiotic resistant Enterococcus spp. contamination on post-shift uniforms compared to zero to minimal contamination of pre-shift uniforms. A biobank of isolates was created and subsequently characterised for antibiotic sensitivity using European Union Committee on Antimicrobial Susceptibility Testing (EUCAST) guidelines - 51% of S. aureus isolates were classed multi-drug resistant. Genomic diversity was assessed using Random Amplification of Polymorphic DNA (RAPD) - high levels of similarity was found amongst isolates. As one means of reducing uniform bioburden, we conducted analysis of a novel surface active organosilane disinfectant named Goldshield (GS). GS was marketed as a long lasting antimicrobial with residual activity to prevent (re)contamination. GS was tested against model HAI bacteria, spores and biofilms with a view to assessing its potential incorporation into infection control practices. GS technology displayed bactericidal, sporicidal and anti-biofilm properties in laboratory testing providing rationale for an intervention where GS could be incorporated into hospital laundry and assessed for potential use in infection control.

Published
2019

4. Cardiac myosin activation with 2-deoxy-ATP via increased electrostatic interactions with actin

Author

Powers, Joseph D, Yuan, Chen-Ching, McCabe, Kimberly J, Murray, Jason D, Childers, Matthew Carter, Flint, Galina V, Moussavi-Harami, Farid, Mohran, Saffie, Castillo, Romi, Zuzek, Carla, Ma, Weikang, Daggett, Valerie, McCulloch, Andrew D, Irving, Thomas C, and Regnier, Michael

Subjects
Heart Disease, Cardiovascular, Bioengineering, 1.1 Normal biological development and functioning, Underpinning research, 2.1 Biological and endogenous factors, Aetiology, Actin Cytoskeleton, Actins, Adenosine Diphosphate, Adenosine Triphosphate, Animals, Cardiac Myosins, Deoxyadenine Nucleotides, Kinetics, Male, Muscle Contraction, Myocardium, Protein Binding, Rats, Rats, Inbred F344, Sarcomeres, Static Electricity, myosin structure, dATP, X-ray diffraction, sarcomere structure, electrostatics
Abstract

The naturally occurring nucleotide 2-deoxy-adenosine 5'-triphosphate (dATP) can be used by cardiac muscle as an alternative energy substrate for myosin chemomechanical activity. We and others have previously shown that dATP increases contractile force in normal hearts and models of depressed systolic function, but the structural basis of these effects has remained unresolved. In this work, we combine multiple techniques to provide structural and functional information at the angstrom-nanometer and millisecond time scales, demonstrating the ability to make both structural measurements and quantitative kinetic estimates of weak actin-myosin interactions that underpin sarcomere dynamics. Exploiting dATP as a molecular probe, we assess how small changes in myosin structure translate to electrostatic-based changes in sarcomere function to augment contractility in cardiac muscle. Through Brownian dynamics simulation and computational structural analysis, we found that deoxy-hydrolysis products [2-deoxy-adenosine 5'-diphosphate (dADP) and inorganic phosphate (Pi)] bound to prepowerstroke myosin induce an allosteric restructuring of the actin-binding surface on myosin to increase the rate of cross-bridge formation. We then show experimentally that this predicted effect translates into increased electrostatic interactions between actin and cardiac myosin in vitro. Finally, using small-angle X-ray diffraction analysis of sarcomere structure, we demonstrate that the proposed increased electrostatic affinity of myosin for actin causes a disruption of the resting conformation of myosin motors, resulting in their repositioning toward the thin filament before activation. The dATP-mediated structural alterations in myosin reported here may provide insight into an improved criterion for the design or selection of small molecules to be developed as therapeutic agents to treat systolic dysfunction.

Published
2019

8. Engineered red blood cells (activating antigen carriers) drive potent T cell responses and tumor regression in mice

Author

Blagovic, Katarina, primary, Smith, Carolyne K., additional, Ramakrishnan, Amritha, additional, Moore, Lindsay, additional, Soto, David R., additional, Thompson, Zachary, additional, Stockmann, Adam P., additional, Kruszelnicki, Sonia, additional, Thakkar, Akshi, additional, Murray, Jason, additional, Torres, Sebastian, additional, Wondimagegnhu, Bersabel, additional, Yi, Roslyn, additional, Dadgar, Maisam, additional, Paracha, Abdul M., additional, Page, Claire, additional, Clear, Louise, additional, Chaudhry, Omer A., additional, Myint, Melissa, additional, Bridgen, Devin T., additional, Gilbert, Jonathan B., additional, Seidl, Katherine J., additional, Sharei, Armon, additional, Loughhead, Scott, additional, Bernstein, Howard, additional, and Yarar, Defne, additional

Published
2022
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10. Structural basis for stop codon recognition in eukaryotes

Author

Brown, Alan, Shao, Sichen, Murray, Jason, Hegde, Ramanujan S., and Ramakrishnan, V.

Subjects
Cell research, Eukaryotes -- Physiological aspects, Codon -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Termination of protein synthesis occurs when a translating ribosome encounters one of three universally conserved stop codons: UAA, UAG or UGA. Release factors recognize stop codons in the ribosomal A-site to mediate release of the nascent chain and recycling of the ribosome. Bacteria decode stop codons using two separate release factors with differing specificities for the second and third bases (1). By contrast, eukaryotes rely on an evolutionarily unrelated omnipotent release factor (eRF1) to recognize all three stop codons (2). The molecular basis of eRF1 discrimination for stop codons over sense codons is not known. Here we present cryoelectron microscopy (cryo-EM) structures at 3.5-3.8 Å resolution of mammalian ribosomal complexes containing eRF1 interacting with each of the three stop codons in the A-site. Binding of eRF1 flips nucleotide A1825 of 18S ribosomal RNA so that it stacks on the second and third stop codon bases. This configuration pulls the fourth position base into the A-site, where it is stabilized by stacking against G626 of 18S rRNA. Thus, eRF1 exploits two rRNA nucleotides also used during transfer RNA selection to drive messenger RNA compaction. In this compacted mRNA conformation, stop codons are favoured by a hydrogen-bonding network formed between rRNA and essential eRF1 residues that constrains the identity of the bases. These results provide a molecular framework for eukaryotic stop codon recognition and have implications for future studies on the mechanisms of canonical and premature translation termination (3,4)., Termination of translation in eukaryotes is initiated when a ternary complex of eRF1-eRF3-GTP binds to a stop codon in the ribosomal A-site (5,6). GTP hydrolysis by eRF3 induces a conformational [...]

Published
2015

16. Enhanced Crossbridge Binding with 2-Deoxy-ATP Results from Increased Electrostatic Interactions between Myosin and Actin in Cardiac Muscle

Author

Yuan, Chen-Ching, primary, Powers, Joseph D., additional, McCabe, Kimberly J., additional, Murray, Jason D., additional, Saffie, Morhan, additional, Romi, Castillo, additional, Carla, Zuzek, additional, Ma, Weikang, additional, McCulloch, Andrew D., additional, Irving, Thomas C., additional, and Regnier, Michael, additional

Published
2019
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21. Liberals should welcome Gorsuch. Like Kagan, he puts law before politics

Author

Murray, Jason

Subjects
Supreme court justices -- Evaluation, Judicial candidates -- Evaluation, General interest, News, opinion and commentary
Abstract

Byline: Jason Murray Many liberals will be tempted to instinctively oppose Supreme Court nominee Neil Gorsuch's confirmation - because he is a self-proclaimed conservative, or because he was nominated by [...]

Published
2017

26. A TAK1 Signaling Pathway Critically Regulates Myocardial Survival and Remodeling

Author

Li, Lei, Chen, Yi, Doan, Jessica, Murray, Jason, Molkentin, Jeffery D., and Liu, Qinghang

Subjects
Heart Failure, Mice, Knockout, Caspase 8, Ventricular Remodeling, Fas-Associated Death Domain Protein, Apoptosis, MAP Kinase Kinase Kinases, Article, Cell Line, Disease Models, Animal, Mice, Necrosis, Receptor-Interacting Protein Serine-Threonine Kinases, Animals, Homeostasis, Myocytes, Cardiac, Signal Transduction
Abstract

Programmed necrosis (necroptosis) plays an important role in development, tissue homeostasis, and disease pathogenesis. The molecular mechanisms that regulate necroptosis in the heart and its physiological relevance in myocardial remodeling and heart failure remain largely unknown.Here, we identified an obligate function for TAK1 (transforming growth factor β-activated kinase 1, gene name Map3k7) in regulating necroptotic myocyte death, myocardial remodeling, and heart failure propensity. Cardiac-specific ablation of Map3k7 in mice induced spontaneous apoptosis and necroptosis that led to adverse remodeling and heart failure, and these effects were abolished by ablation of tumor necrosis factor receptor-1. Mechanistically, TAK1 functions as a molecular switch in tumor necrosis factor receptor-1 signaling by regulating the formation of 2 cell death complexes, RIP 1 (receptor-interacting protein 1)-FADD (Fas-associated protein with death domain)-caspase 8 and RIP1-RIP3, a process that is dependent on FADD and caspase 8 as scaffolding molecules. Importantly, inhibition of RIP1 or RIP3 largely blocked necroptotic cell death, adverse remodeling, and heart failure in TAK1-deficient mice.These results indicate that TAK1 functions as a key survival factor in the heart by directly antagonizing necroptosis, which is critical for the maintenance of myocardial homeostasis and the prevention of adverse myocardial remodeling.

Published
2014

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