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1.
Am J Hypertens ; 34(12): 1328-1335, 2021 12 01.
Article in English | MEDLINE | ID: mdl-34436555

ABSTRACT

BACKGROUND: Low-cost, automated interventions that increase knowledge and skills around diet and lifestyle modifications are recommended for cardiovascular disease risk reduction. METHODS: We initiated a quality improvement program to assess the impact of a web-based diet and lifestyle intervention utilizing short animated videos in adults with high blood pressure (BP) at a primary care clinic in Saudi Arabia. We enrolled adults with elevated BP, not on BP medications, who were identified using the electronic medical record. We delivered a web-linked diet and lifestyle intervention using animated videos covering diet and lifestyle topics. Videos and reminders were sent weekly for 5 weeks. Outcomes were proportion who engaged in the program, returned for a repeat BP within 3 months, and change in BP. RESULTS: We enrolled 269 adult participants, with a mean (SD) age of 41.6 (12.4) years; 77% were male. At the conclusion of the pilot, we demonstrated a high level of engagement: overall, 69% of materials were viewed and 67% of patients returned for BP. Patients who returned had a mean (SD) baseline systolic BP of 138.0 (7.2) mm Hg and a large mean reduction in systolic BP from baseline, -10.5 mm Hg (12.4; P < 0.001). CONCLUSIONS: Overall, the feasibility of a video-assisted, web-based, diet and lifestyle intervention as a support tool for hypertension management demonstrated a high participation rate and a high return rate for reassessment of BP. These findings suggest that this low-cost, automated intervention may have a great potential as a scalable tool for blood pressure management. However, randomized trials to understanding the effectiveness of the support tools are needed.


Subject(s)
Electronic Health Records , Hypertension , Adult , Blood Pressure , Humans , Hypertension/drug therapy , Hypertension/therapy , Male , Patient Education as Topic , Quality Improvement
2.
Curr Drug Targets ; 7(7): 793-811, 2006 Jul.
Article in English | MEDLINE | ID: mdl-16842212

ABSTRACT

Drug efflux proteins are widespread amongst microorganisms, including pathogens. They can contribute to both natural insensitivity to antibiotics and to emerging antibiotic resistance and so are potential targets for the development of new antibacterial drugs. The design of such drugs would be greatly facilitated by knowledge of the structures of these transport proteins, which are poorly understood, because of the difficulties of obtaining crystals of quality. We describe a structural genomics approach for the amplified expression, purification and characterisation of prokaryotic drug efflux proteins of the 'Major Facilitator Superfamily' (MFS) of transport proteins from Helicobacter pylori, Staphylococcus aureus, Escherichia coli, Enterococcus faecalis, Bacillus subtilis, Brucella melitensis, Campylobacter jejuni, Neisseria meningitides and Streptomyces coelicolor. The H. pylori putative drug resistance protein, HP1092, and the S. aureus QacA proteins are used as detailed examples. This strategy is an important step towards reproducible production of transport proteins for the screening of drug binding and for optimisation of crystallisation conditions to enable subsequent structure determination.


Subject(s)
Bacteria/metabolism , Drug Resistance, Bacterial , Membrane Transport Proteins/metabolism , Amino Acid Sequence , Bacteria/genetics , Gene Expression Regulation, Bacterial , Membrane Transport Proteins/chemistry , Membrane Transport Proteins/genetics , Models, Molecular , Molecular Sequence Data , Protein Folding
3.
FEBS Lett ; 555(1): 170-5, 2003 Nov 27.
Article in English | MEDLINE | ID: mdl-14630338

ABSTRACT

A general strategy for the amplified expression in Escherichia coli of membrane transport and receptor proteins from other bacteria is described. As an illustration we report the cloning of the putative alpha-ketoglutarate membrane transport gene from the genome of Helicobacter pylori, overexpression of the protein tagged with RGS(His)6 at the C-terminus, and its purification in mg quantities. The retention of structural and functional integrity was verified by circular dichroism spectroscopy and reconstitution of transport activity. This strategy for overexpression and purification is extended to additional membrane proteins from H. pylori and from other bacteria.


Subject(s)
Bacterial Proteins/genetics , Bacterial Proteins/isolation & purification , Membrane Proteins/genetics , Membrane Proteins/isolation & purification , Base Sequence , Carrier Proteins/genetics , Carrier Proteins/isolation & purification , Circular Dichroism , Cloning, Molecular , DNA, Bacterial/genetics , DNA, Recombinant/genetics , Escherichia coli/genetics , Genes, Bacterial , Genetic Vectors , Helicobacter pylori/genetics , Plasmids/genetics , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Solubility
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