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1.
Aust Health Rev ; 2024 Jun 13.
Artigo em Inglês | MEDLINE | ID: mdl-38866423

RESUMO

ObjectiveThis study aimed to describe and compare the proportion of patients classified as an emergency department (ED) mental health presentation under different definitions, including the Australian Institute of Health and Welfare (AIHW) definition.MethodsThis retrospective cohort study enrolled all patients that presented to the EDs of a multi-centre Victorian health service between 1 January 2020 and 30 June 2023. Varying definitions of a mental health presentation were applied to each ED attendance, applying the current AIHW definition (using selected diagnosis codes), broader diagnosis-based coding, the presenting complaint recorded at triage and whether the patient was seen by or referred to the emergency psychiatric service (EPS). The proportion of all ED presentations meeting each definition and any overlap between definitions were calculated. The agreement between each definition and the AIHW definition was evaluated using Kappa's coefficient.ResultsThere were 813,078 presentations to ED of which 34,248 (4.2%) met the AIHW definition for a mental health presentation. Throughout the study, 45,376 (5.6%) patients were seen and/or referred to EPS, and 36,160 (4.4%) patients were allocated a mental health presenting complaint by triage staff. There was moderate interrater agreement between these definitions, with a kappa statistic (95% confidence interval) between the AIHW definition and a mental health presenting complaint recorded at triage of 0.58 (0.58-0.59) and between the AIHW definition and review by EPS of 0.58 (0.57-0.58).ConclusionsThe AIHW definition is a conservative measure of ED mental health presentations and may underestimate emergency psychiatry workload in Australian EDs.

2.
Aust J Gen Pract ; 52(10): 704-710, 2023 10.
Artigo em Inglês | MEDLINE | ID: mdl-37788692

RESUMO

BACKGROUND AND OBJECTIVES: Virtual reality (VR) may be useful for reducing needle-based pain and distress. Our objective was to compare VR against standard care for children undergoing routine four-year-old immunisations. METHOD: This was a randomised controlled superiority trial conducted in a single suburban general practice, comparing a VR sequence of an interactive marine adventure to standard care (parental comfort, distraction of child). Our primary outcome was self-rated pain scores (Faces Pain Scale - Revised and the poker chip tool). Secondary outcomes included observational ratings (visual analogue scales) of pain and distress from caregivers and an observing healthcare provider, and overall enjoyment of the immunisation experience for the parent and child. RESULTS: In all, 42 children received VR and 45 received standard care. There was no difference in the primary outcome, with median interquartile range self-rated pain scores of 2 (0-8) in the standard care group and 2 (0-6) in the VR group. Observer ratings of pain and distress, as well as ratings of overall enjoyment, favoured VR. There were no significant adverse events. DISCUSSION: VR was not superior to standard care for self-rated pain and distress in children aged four years receiving routine immunisations. However, parent and observer ratings of pain and distress and overall ratings of enjoyment all favoured VR.


Assuntos
Medicina Geral , Dor Processual , Realidade Virtual , Criança , Humanos , Pré-Escolar , Dor/etiologia , Imunização
3.
BMJ Open ; 10(8): e038354, 2020 08 20.
Artigo em Inglês | MEDLINE | ID: mdl-32819997

RESUMO

INTRODUCTION: Pain caused by routine immunisations is distressing to children, their parents and those administering injections. If poorly managed, it can lead to anxiety about future medical procedures, needle phobia and avoidance of future vaccinations and other medical treatment. Several strategies, such as distraction, are used to manage the distress associated with routine immunisations. Virtual reality (VR), a technology which transports users into an immersive 'virtual world', has been used to manage pain and distress in various settings such as burns dressing changes and dental treatments. In this study, we aim to compare the effectiveness of VR to standard care in a general practice setting as a distraction technique to reduce pain and distress in 4-year-old children receiving routine immunisations. METHODS AND ANALYSIS: The study is a randomised controlled clinical trial comparing VR with standard care in 100 children receiving routine 4-year-old vaccination. Children attending a single general practice in metropolitan Melbourne, Australia will be allocated using blocked randomisation to either VR or standard care. Children in the intervention group will receive VR intervention prior to vaccination in addition to standard care; the control group will receive standard care. The primary outcome is the difference in the child's self-rated pain scores between the VR intervention and control groups measured using The Faces Pain Scale-Revised. Secondary outcomes include another measure of self-rated pain (the Poker Chip Tool), parent/guardian and healthcare provider ratings of pain (standard 100 mm visual analogue scales) and adverse effects. ETHICS AND DISSEMINATION: Ethics approval has been obtained in Australia from the Royal Australian College of General Practitioners National Research and Evaluation Ethics Committee (NREEC 18-010). Recruitment commenced in July 2019. We plan to submit study findings for publication in a peer-reviewed journal and presentation at relevant conferences. TRIAL REGISTRATION NUMBER: ACTRN12618001363279.


Assuntos
Realidade Virtual , Austrália , Pré-Escolar , Humanos , Imunização , Dor/etiologia , Dor/prevenção & controle , Ensaios Clínicos Controlados Aleatórios como Assunto , Vacinação
4.
Appl Environ Microbiol ; 85(15)2019 08 01.
Artigo em Inglês | MEDLINE | ID: mdl-31126950

RESUMO

ß-Aminopeptidases have the unique capability to hydrolyze N-terminal ß-amino acids, with varied preferences for the nature of ß-amino acid side chains. This unique capability makes them useful as biocatalysts for synthesis of ß-peptides and to kinetically resolve ß-peptides and amides for the production of enantiopure ß-amino acids. To date, six ß-aminopeptidases have been discovered and functionally characterized, five from Gram-negative bacteria and one from a fungus, Aspergillus Here we report on the purification and characterization of an additional four ß-aminopeptidases, one from a Gram-positive bacterium, Mycolicibacterium smegmatis (BapAMs), one from a yeast, Yarrowia lipolytica (BapAYlip), and two from Gram-negative bacteria isolated from activated sludge identified as Burkholderia spp. (BapABcA5 and BapABcC1). The genes encoding ß-aminopeptidases were cloned, expressed in Escherichia coli, and purified. The ß-aminopeptidases were produced as inactive preproteins that underwent self-cleavage to form active enzymes comprised of two different subunits. The subunits, designated α and ß, appeared to be tightly associated, as the active enzyme was recovered after immobilized-metal affinity chromatography (IMAC) purification, even though only the α-subunit was 6-histidine tagged. The enzymes were shown to hydrolyze chromogenic substrates with the N-terminal l-configurations ß-homo-Gly (ßhGly) and ß3-homo-Leu (ß3hLeu) with high activities. These enzymes displayed higher activity with H-ßhGly-p-nitroanilide (H-ßhGly-pNA) than previously characterized enzymes from other microorganisms. These data indicate that the new ß-aminopeptidases are fully functional, adding to the toolbox of enzymes that could be used to produce ß-peptides. Overexpression studies in Pseudomonas aeruginosa also showed that the ß-aminopeptidases may play a role in some cellular functions.IMPORTANCE ß-Aminopeptidases are unique enzymes found in a diverse range of microorganisms that can utilize synthetic ß-peptides as a sole carbon source. Six ß-aminopeptidases have been previously characterized with preferences for different ß-amino acid substrates and have demonstrated the capability to catalyze not only the degradation of synthetic ß-peptides but also the synthesis of short ß-peptides. Identification of other ß-aminopeptidases adds to this toolbox of enzymes with differing ß-amino acid substrate preferences and kinetics. These enzymes have the potential to be utilized in the sustainable manufacture of ß-amino acid derivatives and ß-peptides for use in biomedical and biomaterial applications. This is important, because ß-amino acids and ß-peptides confer increased proteolytic resistance to bioactive compounds and form novel structures as well as structures similar to α-peptides. The discovery of new enzymes will also provide insight into the biological importance of these enzymes in nature.


Assuntos
Aminopeptidases/genética , Proteínas de Bactérias/genética , Burkholderia/genética , Proteínas Fúngicas/genética , Mycobacteriaceae/genética , Yarrowia/genética , Aminopeptidases/metabolismo , Proteínas de Bactérias/metabolismo , Burkholderia/metabolismo , Proteínas Fúngicas/metabolismo , Cinética , Mycobacteriaceae/metabolismo , Especificidade por Substrato , Yarrowia/metabolismo
5.
Acta Crystallogr F Struct Biol Commun ; 73(Pt 7): 386-392, 2017 07 01.
Artigo em Inglês | MEDLINE | ID: mdl-28695846

RESUMO

ß-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal ß-amino acids from synthetic ß-peptides. ß-Peptides can form secondary structures mimicking α-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of ß-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a ß-aminopeptidase from a Gram-negative Burkholderia sp. that was isolated from activated sludge from a wastewater-treatment plant in Australia, is reported. The crystal structure of BcA5-BapA was determined to a resolution of 2.0 Šand showed a tetrameric assembly typical of the ß-aminopeptidases. Each monomer consists of an α-subunit (residues 1-238) and a ß-subunit (residues 239-367). Comparison of the structure of BcA5-BapA with those of other known ß-aminopeptidases shows a highly conserved structure and suggests a similar proteolytic mechanism of action.


Assuntos
Aminopeptidases/química , Proteínas de Bactérias/química , Burkholderia/química , Peptídeos/química , Peptidomiméticos/química , Motivos de Aminoácidos , Aminopeptidases/genética , Aminopeptidases/metabolismo , Proteínas de Bactérias/genética , Proteínas de Bactérias/metabolismo , Burkholderia/enzimologia , Burkholderia/isolamento & purificação , Domínio Catalítico , Clonagem Molecular , Cristalografia por Raios X , Escherichia coli/genética , Escherichia coli/metabolismo , Expressão Gênica , Vetores Genéticos/química , Vetores Genéticos/metabolismo , Humanos , Interações Hidrofóbicas e Hidrofílicas , Modelos Moleculares , Peptídeos/síntese química , Peptídeos/metabolismo , Peptidomiméticos/síntese química , Peptidomiméticos/metabolismo , Ligação Proteica , Conformação Proteica em alfa-Hélice , Conformação Proteica em Folha beta , Domínios e Motivos de Interação entre Proteínas , Multimerização Proteica , Proteólise , Proteínas Recombinantes de Fusão/química , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Especificidade por Substrato , Águas Residuárias/microbiologia
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