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8 result(s) for "Nair Narayanan, Divya"
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Stepping forward: A study protocol for developing and validating a Malaysian diabetic foot self-care practice assessment instrument
Diabetic foot ulcers impose significant financial burdens and diminished quality of life. Effective management relies on patients' self-care, yet often overlooked by patients as neuropathic feet are painless. In Malaysia, primary care facilities focus on prevention by promoting proper foot self-care. However, the lack of a standardised assessment tool hampers nationwide evaluation. This paper outlines the methodology for developing and validating an instrument tailored to the Malaysian context to assess diabetic foot self-care practices. A structured methodological process will be employed to guide the instrument's development and subsequent validation. The instrument aims to encompass comprehensible questions with a simple scoring and interpretation mechanism to foster its daily use. The study will consist of two phases. Phase 1 focuses on the development of the Malaysian instrument. This phase encompasses a literature review, item development tailored to the Malaysian context, content validity through expert panel evaluations, translations, pre-tests and a follow-up stakeholder engagement to ensure the instrument meets their requirements. Incorporating perspectives from experts and comprehensibility by local patients ensures the instrument's relevance to the local context. Phase 2 involves instrument validation through a cross-sectional study. This phase entails a pilot test and field test of the instrument among diabetic patients for validation. Cut-off ranges and their interpretations will also be established in this phase. The study sites encompass a mix of urban and rural public health clinics across Peninsular as well as East Malaysia. By developing a standard validated instrument to assess diabetic foot self-care practices, services provision gaps can be identified, and targeted interventions to improve these gaps in practices can be implemented. Individually tailored diabetes foot care education is crucial in preventing foot ulcers. This instrument can also facilitate the monitoring of improvements in patients' foot self-care practices longitudinally.
Development of the National Policy for Quality in Healthcare for Malaysia
Background Quality in healthcare is a fundamental pillar of health systems performance, leading to improved health outcomes and reduced waste. The World Health Organization recommends that countries establish a national quality policy and strategy (NQPS) to steer the provision of safe and high-performing healthcare services and foster a quality culture. This paper describes the development process and key content of Malaysia’s new 5-year National Policy for Quality in Healthcare. Methods The development process was managed by a technical working group led by the Institute for Health Systems Research in the Ministry of Health. Situational analysis was conducted through a multi-pronged approach, underpinned by a review of the past and present healthcare sectoral and quality plans and guided by the WHO NQPS framework. This approach involved: (i) review of quality-related policy documents, (ii) online surveys of healthcare providers and the public, (iii) key-informant facilitated discussions and (iv) mapping of existing quality improvement initiatives (QIIs). Data gathered from these approaches informed the content of the new policy. Following thematic analysis, the findings were grouped into specific domains, which were then organized into a strengths, weaknesses, opportunities, and threats (SWOT) framework. Results Ten key areas of concern identified were (i) a people-centred holistic approach, (ii) governance for quality, (iii) resources, (iv) quality culture, (v) stakeholder engagement, (vi) health management information system, (vii) workforce competency, (viii) knowledge exchange, (ix) quality indicators and (x) monitoring and evaluation of quality activities. These led to the formulation of seven strategic priorities  for the planning of improvements aimed at addressing the key areas of concern. The national definition of quality was affirmed. A total of 40 QIIs were mapped and grouped into three broad categories, namely (i) regulatory, (ii) domain-specific QIIs and (iii) Quality Improvement (QI) method. Conclusions The National Policy for Quality in Healthcare for Malaysia was developed through a comprehensive situational analysis using a multi-method approach that identified priorities across national, state, institutional and community levels. This evidence-informed approach led to meaningful contextual adaptation of the NQPS framework to shape the strategic direction to advance quality and achieve effective and safe outcomes for all Malaysians.
In vitro efficacy of amitraz, coumaphos, deltamethrin and lindane against engorged female Rhipicephalus (Boophilus) annulatus and Haemaphysalis bispinosa ticks
The present study compares the in vitro efficacy of four chemical acaricides, viz. amitraz, coumaphos, deltamethrin and lindane, against Rhipicephalus (Boophilus) annulatus and Haemaphysalis bispinosa ticks based on adult immersion tests. Amitraz, at 350 ppm, elicited 29.2 ± 4.17% mortality against R. (B.) annulatus, 100% inhibition of fecundity and absence of hatching of eggs laid by treated ticks. The same compound at 300 ppm caused 62.5 ± 12.5% mortality against H. bispinosa, 96.7% inhibition of fecundity and complete blocking of eclosion. The LC50 value of amitraz against susceptible H. bispinosa was 181 ppm. Deltamethrin at 400 ppm, elicited 25.0 ± 4.81% adult R. (B.) annulatus mortality, 97.5% inhibition of fecundity and absence of egg hatching. Complete blocking of egg hatching was observed even at 30 ppm. However, deltamethrin (at 50 ppm) elicited 75.0 ± 10.76% mortality against H. bispinosa, 65.8% inhibition of fecundity and very low egg hatching (10%). The LC50 for deltamethrin against susceptible H. bispinosa was 33.8 ppm. Coumaphos at 50 ppm, caused mortality of 70.8 ± 4.17% with R. (B.) annulatus whereas 100% mortality was observed against H. bispinosa. The LC50 values of coumaphos against R. (B.) annulatus and H. bispinosa were 9 and 8.75 ppm, respectively. Complete inhibition (100%) of fecundity was observed even at 30 ppm against both parasites. Complete blocking of egg hatching was also observed even at 10 ppm of coumaphos. Lindane at 1000 ppm caused mortality of 87.5 ± 7.98% against R. (B.) annulatus and 83.3% mortality against H. bispinosa at 100 ppm. The LC50 values of lindane against R. (B.) annulatus and H. bispinosa were 157 and 8.61 ppm, respectively. Complete inhibition of fecundity was observed with R. (B.) annulatus treated with lindane above 200 ppm and with H. bispinosa at a concentration above 50 ppm. Complete blocking of egg hatching was observed in R. (B.) annulatus, even at 100 ppm. Lindane caused 100% blocking of egg hatching at 1 ppm in the case of H. bispinosa.
Influence of Pyrexia on Pharmacokinetics of Azithromycin and Its Interaction With Tolfenamic Acid in Goats
Azithromycin is a macrolide antimicrobial agent of the azalide group with a broad spectrum of activity against gram-negative and gram-positive bacterial organisms. Tolfenamic acid is a non-steroidal anti-inflammatory drug of the fenamate group, which is used extensively in humans and animals due to its anti-inflammatory, analgesic, and antipyretic properties. There is dearth of literature on any type of drug interaction between azithromycin and tolfenamic acid in any species, including human beings and alteration of its pharmacokinetics by fever. Therefore, the objective of this study was to investigate the alteration of disposition kinetics of azithromycin alone and in the presence of tolfenamic acid in Malabari goats by fever, following an intravenous administration at a dose rate of 20 mg/kg body weight. Blood samples collected from both afebrile and febrile goats at predetermined time intervals after the administration of azithromycin alone and then in combination with tolfenamic acid (2 mg/kg, intravenously), respectively, were analyzed using high-performance liquid chromatography. Non-compartmental analysis was used to determine the peak blood concentration ( C max ), time-to-peak plasma concentration ( T max ), half-life ( t 1/2λ z ), area under the curve (AUC 0−t , AUC 0−inf ), area under the first moment curve (AUMC 0−inf ), mean residence time (MRT 0−inf ), apparent volume of distribution at steady state ( V ss ), and the total body clearance of drug from the blood (Cl). In febrile animals, significant differences were noted in the values of C max , Cl, and V ss . Thus, azithromycin disappears into an additional compartment in febrile goats, which may be due to its extended cellular penetration into the inflammatory cells, resulting in anti-inflammatory activity. Tolfenamic acid significantly altered the pharmacokinetics of azithromycin in both normal and febrile animals. Tolfenamic acid, being a better anti-inflammatory agent, suppresses the inflammatory mediators, reducing the possibility of increased utilization of azithromycin in febrile condition.
Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain
Fatal neurodegenerative disorders termed transmissible spongiform encephalopathies (TSEs) are associated with the accumulation of fibrils of misfolded prion protein PrP. The noble gas xenon accommodates into four transiently enlarged hydrophobic cavities located in the well-folded core of human PrP(23–230) as detected by [ 1 H, 15 N]-HSQC spectroscopy. In thermal equilibrium a fifth xenon binding site is formed transiently by amino acids A120 to L125 of the presumably disordered N-terminal domain and by amino acids K185 to T193 of the well-folded domain. Xenon bound PrP was modelled by restraint molecular dynamics. The individual microscopic and macroscopic dissociation constants could be derived by fitting the data to a model including a dynamic opening and closing of the cavities. As observed earlier by high pressure NMR spectroscopy xenon binding influences also other amino acids all over the N-terminal domain including residues of the AGAAAAGA motif indicating a structural coupling between the N-terminal domain and the core domain. This is in agreement with spin labelling experiments at positions 93 or 107 that show a transient interaction between the N-terminus and the start of helix 2 and the end of helix 3 of the core domain similar to that observed earlier by Zn 2+ -binding to the octarepeat motif.
In silico characterization of a novel β-1,3-glucanase gene from Bacillus amyloliquefaciens—a bacterial endophyte of Hevea brasiliensis antagonistic to Phytophthora meadii
We report the molecular characterization of β-1,3-glucanase-producing Bacillus amyloliquefaciens —an endophyte of Hevea brasiliensis antagonistic to Phytophthora meadii . After cloning and sequencing, the β-1,3-glucanase gene was found to be 747 bp in length. A homology model of the β-1,3-glucanase protein was built from the amino acid sequence obtained upon translation of the gene. The target β-1,3-glucanase protein and the template protein, endo β-1,3-1,4-glucanase protein (PDB ID: 3o5s), were found to share 94 % sequence identity and to have similar secondary and tertiary structures. In the modeled structure, three residues in the active site region of the template—Asn52, Ile157 and Val158—were substituted with Asp, Leu and Ala, respectively. Computer-aided docking studies of the substrate disaccharide (β-1, 3-glucan) with the target as well as with the template proteins showed that the two protein-substrate complexes were stabilized by three hydrogen bonds and by many van der Waals interactions. Although the binding energies and the number of hydrogen bonds were the same in both complexes, the orientations of the substrate in the active sites of the two proteins were different. These variations might be due to the change in the three amino acids in the active site region of the two proteins. The difference in substrate orientation in the active site could also affect the catalytic potential of the β-1,3 glucanase enzyme.