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1.
Spat Spatiotemporal Epidemiol ; 42: 100521, 2022 08.
Article in English | MEDLINE | ID: mdl-35934330

ABSTRACT

Severe acute respiratory syndrome - coronavirus 2 (SARS-CoV-2) continues to effect communities across the world. One way to combat these effects is to enhance our collective ability to remotely monitor community spread. Monitoring SARS-CoV-2 in wastewater is one approach that enables researchers to estimate the total number of infected people in a region; however, estimates are often made at the sewershed level which may mask the geographic nuance required for targeted interdiction efforts. In this work, we utilize an apportioning method to compare the spatial and temporal trends of daily case count with the temporal pattern of viral load in the wastewater at smaller units of analysis within Austin, TX. We find different lag-times between wastewater loading and case reports. Daily case reports for some locations follow the temporal trend of viral load more closely than others. These findings are then compared to socio-demographic characteristics across the study area.


Subject(s)
COVID-19 , SARS-CoV-2 , COVID-19/epidemiology , Humans , Spatio-Temporal Analysis , Wastewater
2.
BMC Vet Res ; 15(1): 27, 2019 Jan 15.
Article in English | MEDLINE | ID: mdl-30646904

ABSTRACT

BACKGROUND: Producing graduates for a breadth of sectors is a priority for veterinary science programs. Undergraduate career intentions represent de-facto 'outcome' measures of admissions policy and curricula design, as intentions are strong predictors of eventual behaviour. Informed by Ajzen's Theory of Planned Behaviour, this study aimed to identify if contextually relevant attitudes and self-ratings affect student intentions for veterinary career sectors. RESULTS: Survey responses from 844 students enrolled in five Australian veterinary programs in 2014 were analysed. Intention was measured for biomedical research/academia, industry, laboratory animal medicine, public health/government/diagnostic laboratory services, mixed practice, intensive animal production, companion animal practice, not work in the veterinary profession, and business/entrepreneurship. Hierarchical multiple linear regression analysis enabled comparison of explanation of variance in intent by demographics, animal handling experience, species preference, and attitudes to aspects of veterinary work. Career sector intentions were highest for mixed or companion animal clinical practice, then business/entrepreneurship, then non-clinical sectors. Overall, intent was explained to a greater extent by species preferences than by animal experience, attitudes to aspects of veterinary work and demographics (with the exception of mixed practice intent) with gender having no significant effect. Several variables exerted negative effects on career intent for less popular career sectors. CONCLUSION: Ajzen's Theory of Planned Behaviour (TPB) provides a framework to increase understanding of and predict career sector intentions. Incorporation of attitude and self-efficacy measures in our study revealed preference for species types contributes greatly to career sector intentions for veterinary students, particularly for the more popular practice based sectors. Importantly, specific species preferences and other attitudes can have a negative effect on intent for non-aligned veterinary sectors. Further research is required to identify additional attitudes and/or beliefs to better explain variance in intent for less popular career sectors. Veterinary admissions processes may benefit from utilising the TPB framework. Identified effects revealed by this study may stimulate innovation in marketing, recruitment, admissions and curricular design, such as timing and role modelling, to utilise positive effects and mitigate against negative effects identified for sectors requiring greater representation of career intent in the student body.


Subject(s)
Career Choice , Veterinary Medicine , Attitude , Australia , Cross-Sectional Studies , Demography , Female , Humans , Male , Veterinary Medicine/trends , Workforce
3.
Arch Biochem Biophys ; 277(1): 149-54, 1990 Feb 15.
Article in English | MEDLINE | ID: mdl-2306116

ABSTRACT

Evidence for a specific interaction between oncomodulin and glutathione reductase is presented. Glutathione reductase (EC 1.6.4.2) isolated from either the bovine intestinal mucosa or the rat liver was bound in a Ca2(+)-dependent manner to oncomodulin which was covalently attached to Sepharose. In addition, glutathione reductase was able to catalyze the reduction of the disulfide-linked dimer of oncomodulin. The interaction of these proteins could also be indirectly demonstrated by monitoring glutathione reductase activity since oncomodulin was shown to inhibit the enzyme in a dose-dependent manner with an apparent IC50 of approximately 5 microM. The kinetic analysis of the oncomodulin-dependent effects on glutathione reductase activity indicates that oncomodulin interacts at a site other than the active site as the oncomodulin-induced inhibition was of the noncompetitive type. The in vivo inhibition of glutathione reductase appears to be an oncomodulin-specific effect as closely related members of the troponin C superfamily such as rabbit (pI 5.5) or carp (pI 4.25) parvalbumins, as well as calmodulin, failed to affect the activity of this enzyme. The present in vitro study indicating that oncomodulin can regulate the activity of glutathione reductase could be very significant with respect to the elucidation of a physiological role for oncomodulin.


Subject(s)
Calcium-Binding Proteins/pharmacology , Glutathione Reductase/antagonists & inhibitors , Neoplasm Proteins/pharmacology , Animals , Calcium-Binding Proteins/isolation & purification , Cattle , Cell Line , Chromatography, Affinity , Glutathione/analogs & derivatives , Glutathione/metabolism , Glutathione Disulfide , Glutathione Reductase/isolation & purification , Intestinal Mucosa/enzymology , Kinetics , Liver/enzymology , Liver Neoplasms, Experimental , Rats
4.
Biochemistry ; 27(15): 5615-22, 1988 Jul 26.
Article in English | MEDLINE | ID: mdl-3179268

ABSTRACT

Oncomodulin, an oncofetal Ca2+-binding protein, contains a single Cys residue in position 18 of its primary structure. The reactivity of the Cys-18 thiol has been probed with 5,5'-dithiobis(2-nitrobenzoate) (NbS2). The kinetics of the reaction indicate that the thiol group is approximately 10-fold more reactive in the presence of Ca2+ than in its absence. Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol. The kinetics of dimer formation indicate that the second-order rate constant for this reaction is approximately 6-fold higher than that observed for the reaction of the Cys-18 thiol with NbS2, possibly indicating that intermolecular electrostatic interactions precede disulfide formation. The disulfide-linked dimer of oncomodulin appears to be more similar to calmodulin than oncomodulin since the dimer displayed "calmodulin-like" affinity for the amphiphilic peptide melittin. In addition, oncomodulin dimer was shown to activate two calmodulin-dependent enzymes, cyclic nucleotide phosphodiesterase and calcineurin phosphatase, with the activity constants of 63 and 1 nM, respectively, indicating that these enzymes have different domain contact requirements for activation.


Subject(s)
Calcium-Binding Proteins , Animals , Calmodulin , Cysteine , Disulfides , Liver Neoplasms, Experimental/analysis , Macromolecular Substances , Melitten , Oxidation-Reduction , Protein Binding , Protein Conformation , Rats , Structure-Activity Relationship
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