Publications by authors named "M Jodeane Pringle"

Background: Bovine respiratory disease (BRD) is common in intensively raised cattle and is often treated with antibiotics. For practitioners, knowledge of the bacteria involved in an outbreak and their antibiotic susceptibility is warranted. To this end, samples from the upper or lower respiratory tract of calves can be submitted for bacteriological culture and susceptibility testing of relevant isolates.

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Proteins entering the secretory pathway need to attain native disulfide pairings to fold correctly. For proteins with complex disulfides, this process requires the reduction and isomerisation of non-native disulfides. Two key members of the protein disulfide isomerase (PDI) family, ERp57 and ERdj5 (also known as PDIA3 and DNAJC10, respectively), are thought to be required for correct disulfide formation but it is unknown whether they act as a reductase, an isomerase or both.

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SignificanceMembrane and secretory proteins are synthesized in the endoplasmic reticulum (ER). Perturbations to ER function disrupts protein folding, causing misfolded proteins to accumulate, a condition known as ER stress. Cells adapt to stress by activating the unfolded protein response (UPR), which ultimately restores proteostasis.

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Background: Land clearing generates coarse woody debris (CWD), much of which ultimately becomes atmospheric CO. Schemes for greenhouse gas accounting must consider the contribution from land clearing, but the timing of the contribution will have large uncertainty, due to a paucity of knowledge about the rate of CWD disappearance. To better understand above-ground CWD disappearance following a land clearing event-through the actions of microorganisms, invertebrates, wildfire, or deliberate burning-we combined statistical modelling with an archive of semi-quantitative observations (units of CWD %), made within Queensland, Australia.

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N-linked glycosylation of proteins entering the secretory pathway is an essential modification required for protein stability and function. Previously, it has been shown that there is a temporal relationship between protein folding and glycosylation, which influences the occupancy of specific glycosylation sites. Here, we used an in vitro translation system that reproduces the initial stages of secretory protein translocation, folding and glycosylation under defined redox conditions.

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