Practice development in nursing / / edited by Brendan McCormack, Kim Manley, and Robert Garbett

• Record Nr.: UNINA9910144671803321
• Pubbl/distr/stampa: Oxford ; ; Malden, Mass., : Blackwell Pub., 2004
• ISBN: 1-282-25217-8; 9786612252174; 0-470-69888-8; 0-470-69834-9
• Edizione: [1st ed.]
• Descrizione fisica: 1 online resource (xvi, 336 pages) : illustrations
• Altri autori (Persone): McCormackBrendan; ManleyKim, MN.; GarbettRobert
• Disciplina: 610.73
• Soggetti: Nursing; Nurse practitioners
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: A concept analysis of practice development -- Practice development: purpose, methodology, facilitation, & evaluation -- Transformational culture: a culture of effectiveness -- Evaluating practice developments -- Research implementation: evidence, context and facilitation - the PARIHS framework -- Helping relationships for practice development: critical companionship -- Including the older person with a dementia in practice development -- Practice development in child health nursing: a personal perspective --; Acute mental healthcare: transforming cultures, a practice development approach -- Developing a corporate strategy to develop effective and patient-centred care -- From conception to delivery: a journey to a trust-wide strategy to develop a culture of patient-centeredness -- Developing and implementing a family health assessment: from project worker to practice developer -- A clearer vision of practice development?
• Sommario/riassunto: Practice development depends on understanding current research and practice in order to improve healthcare for patients and users. Practice ; Development in Nursing explores the basis of practice development, its aims, implementation and impact on health care, and goes on to propose a conceptual basis for developing practice. It is aimed at practitioners, managers, and educators as well as those with a primary practice development role, in order to enable them to effectively develop practice.

Microbiological identification using MALDI-TOF and tandem mass spectrometry : industrial and environmental applications / / edited by Saheer E. Gharbia [and four others]

• Record Nr.: UNINA9910830392803321
• Pubbl/distr/stampa: Chichester, England : , : John Wiley & Sons Ltd, , [2023]; ©2023
• ISBN: 1-119-81408-1; 1-119-81406-5
• Descrizione fisica: 1 recurso en liña (560 páxinas)
• Disciplina: 572.36
• Soggetti: Biomolecules - Analysis; Matrix-assisted laser desorption-ionization; Time-of-flight mass spectrometry
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Cover -- Title Page -- Copyright Page -- Contents -- List of Contributors -- Preface -- Chapter 1 Progress in the Microbiological Applications of Mass Spectrometry: from Electron Impact to Soft Ionization Techniques, MALDI-TOF MS and Beyond -- 1.1 Introduction -- 1.1.1 Algorithms Based upon Traditional Carbohydrate Fermentation Tests -- 1.1.2 Dynamic Changes in the Chemotaxonomic Era (c. 1970-1985) through the Lens of the Genus Bacteroides -- 1.1.3 Microbial Lipids as Diagnostic Biomarkers -- Resurgence of Interest in MALDI-TOF MS with Advances in Lipidomics -- 1.2 The Dawn of MALDI-TOF MS: Establishing Proof of Concept for Diagnostic Microbiology -- 1.2.1 ; Development of a MALDI-TOF MS Database for Human Infectious Diseases -- 1.2.2 The Dilemma with Clostridium difficile: from Intact Cells to Intracellular Proteins, MALDI-TOF MS Enters a New Phase -- 1.3 Linear/Reflectron MALDI-TOF MS to Tandem Mass Spectrometry -- 1.3.1 Tandem MALDI-TOF Mass Spectrometry -- 1.3.2 Electrospray-based Mass Analysers -- 1.3.3 Tandem Mass Spectrometry -- 1.3.4 Mass Spectrometry-based Proteomics -- 1.3.5 Case Study: LC-MS/MS of Biothreat Agents, Proteomes of Pathogens and Strain-level Tying Using Bottom-up and Top-down Proteomics -- 1.3.6 Discovery Proteomics -- 1.3.7 Targeted Proteomics -- 1.3.8 Top-down Proteomics -- 1.3.9 Targeted Protein Quantitation -- 1.4 The Application of MALDI-MS Profiling and Imaging in Microbial Forensics: Perspectives -- 1.4.1 MALDI-MSP of Microorganisms and their Products -- 1.5 Hydrogen/Deuterium Exchange Mass Spectrometry in Microbiology -- 1.6 The Omnitrap, a Novel MS Instrument that Combines Many Applications of Mass Spectrometry -- References -- Chapter 2 Machine Learning in Analysis of Complex FloraUsing Mass Spectrometry -- 2.1 Introduction.; 2.2 An Improved MALDI-TOF MS Data Analysis Pipeline for the Identification of Carbapenemase-producing Klebsiella pneumoniae -- 2.2.1 Motivation -- 2.2.2 Materials and Methods -- 2.2.3 Spectra Acquisition -- 2.2.4 Results -- 2.2.5 Discussion -- 2.3 Detection of Vancomycin-Resistant Enterococcus faecium -- 2.3.1 Motivation -- 2.3.2 Materials and Methods -- 2.3.3 Results and Discussion -- 2.4 Detection of Azole Resistance in Aspergillus fumigatus Complex Isolates -- 2.4.1 Introduction -- 2.4.2 Material and Methods -- 2.4.3 Results -- 2.4.4 Discussion -- 2.5 Peak Analysis for Discrimination of Cryptococcus neoformans Species Complex and their Interspecies Hybrids -- 2.5.1 Motivation -- 2.5.2 Material and Methods -- 2.5.3 Results and Discussion -- 2.6 Conclusions -- References -- Chapter 3 Top-down Identification of Shiga Toxin (and Other Virulence Factors and Biomarkers) from Pathogenic E. coli using MALDI-TOF/TOF Tandem Mass Spectrometry -- 3.1 Introduction -- 3.2 Decay of Metastable Peptide and Protein Ions by the Aspartic Acid Effect -- 3.3 Energy Deposition during Desorption/Ionization by MALDI -- 3.4 Protein Denaturation and Fragmentation Efficiency of PSD -- 3.5 Arginine and its Effect on Fragment Ion Detection and MS/MS Spectral Complexity -- 3.6 Inducing Gene Expression in Wild-type Bacteria for Identification by Top-Down Proteomic Analysis -- 3.7 Top-down Proteomic Identification of B-Subunit of Shiga Toxin from STEC Strains -- 3.8 Furin-digested Shiga Toxin and Middle-down Proteomics -- 3.9 Top-down Identification of an Immunity Cognate of a Bactericidal Protein Produced from a STEC Strain -- 3.10 LC-MALDI-TOF/TOF -- 3.11 Conclusions -- References -- Chapter 4 Liquid Atmospheric Pressure (LAP) - MALDI MS(/MS) Biomolecular Profiling for Large-scale Detection of Animal Disease and Food Adulteration and Bacterial Identification -- 4.1 Introduction.; 4.2 Background to LAP-MALDI MS -- 4.3 Bacterial Identification by LAP-MALDI MS -- 4.4 Food Adulteration and Milk Quality Analysis by LAP-MALDI MS -- 4.5 Animal Disease Detection by LAP-MALDI MS -- 4.6 Antibiotic Resistance Detection of Microbial Consortia by LAP-MALDI MS -- 4.7 Future Directions for LAP-MALDI MS Applications -- References -- Chapter 5 Development of a MALDI-TOF Mass Spectrometry Test for Viruses -- 5.1 Introduction -- 5.2 Understanding the Systems Biology of the Virus and Viral Infections -- 5.3 Understanding the Nature of Viral Proteins and Molecular Biology -- 5.4 Virion Protein Solubilization and Extraction -- 5.5 Sampling and Virion Enrichment -- 5.6 Peak Identification: Quantification and Bioinformatics ; -- 5.7 Promise and Pitfalls of Machine Learning Bioinformatics -- 5.8 Accelerating MALDI-TOF Assay Protocol Development Using Pseudotypes/pseudoviruses -- 5.9 Understanding the Operational Parameters of your MALDI-TOF MS -- 5.10 Understanding the Operational Requirements of the Clinical Testing Laboratory: Validation and International Accreditation -- 5.10.1 Limitation and Advantages of CLIA LDTs -- 5.11 MALDI-TOF MS Screening Test for SARS-CoV-2s -- 5.11.1 Prepare Positive Control -- 5.11.2 Prepare Gargle-saliva Samples -- 5.11.3 Viral Particle Enrichment -- 5.11.4 Dissolution of Virions and Solubilization of Viral Proteins -- 5.11.5 MALDI-TOF MS -- 5.12 CLIA LDT Validation of a MALDI-TOF MS Test for SARS-CoV-2 -- 5.12.1 Limit of Detection -- 5.12.2 Interfering Substances and Specificity -- 5.12.3 Clinical Performance Evaluation -- 5.12.4 Reproducibility -- 5.12.5 Stability -- 5.12.6 Validation Disposition -- References -- Chapter 6 A MALDI-TOF MS Proteotyping Approach for Environmental, Agricultural and Food Microbiology -- 6.1 Introduction -- 6.2 Serotyping of Salmonella enterica Subspecies enterica.; 6.3 Discrimination of the Lineages of Listeria monocytogenes and Species of Listeria -- 6.4 Discrimination of the Bacillus cereus Group and Identification of Cereulide -- 6.5 Identification of Alkylphenol Polyethoxylate-degrading Bacteria in the Environment -- 6.6 Conclusions and Future Perspectives -- References -- Chapter 7 Diversity, Transmission and Selective Pressure on the Proteome of Pseudomonas aeruginosa -- 7.1 Introduction: Diversity -- 7.1.1 P. aeruginosa: from 'Atypical' to Diverse -- 7.1.2 Phenotypical Diversity in Isolates from Different Environments -- 7.1.3 The Relationship Between Phenotypical and Proteomic Diversity -- 7.1.4 Techniques and Practical Considerations for Studying Proteomic Diversity -- 7.1.5 Proteomic Diversity and MS Applications -- 7.2 Transmission -- 7.2.1 The History of P. aeruginosa Transmission -- 7.2.2 Proteomics and P. aeruginosa Transmission -- 7.2.3 The Impact of Proteomic Diversity on Transmission -- 7.3 Selective Pressures on the Proteome -- 7.3.1 Tandem MS Systems for Studying Selected Proteomes -- 7.3.2 Microenvironment Selection -- 7.3.3 Antimicrobial Selection -- 7.4 Conclusions on Studies of the Proteome -- 7.5 Genomic Studies on Pseudomonas aeruginosa Strains Revealing the Presence of Two Distinct Clades -- 7.5.1 Phylogenomic Analysis Reveals the Presence of Two Distinct Clades Within P. aeruginosa -- 7.5.2 Identification of Molecular Markers Distinguishing the Two P. aeruginosa Clades -- 7.6 Final Conclusions -- References -- Chapter 8 Characterization of Biodegradable Polymers by MALDI-TOF MS -- 8.1 Introduction -- 8.2 Structural Characterization of Poly(-caprolactone) Using MALDI-TOF MS -- 8.3 Biodegradation Profiles of a Terminal-modified PCL Observed by MALDI-TOF MS -- 8.4 Bacterial Biodegradation Mechanisms of Non-ionic Surfactants.; 8.5 Advanced Molecular Characterization by High-resolution MALDI-TOF MS Combined with KMD Analysis -- 8.6 Structural Characterization of High-molecular-weight Biocopolyesters by High-resolution MALDI-TOF MS Combined with KMD Analysis -- References -- Chapter 9 Phytoconstituents and Antimicrobiological Activity -- 9.1 Introduction to Phytochemicals -- 9.2 An Application to Bacteriology -- 9.2.1 Allicin Leads to a Breakdown of the Cell Wall of Staphylococcus aureus -- 9.3 Applications to Parasitology -- 9.3.1 Drug Discovery -- 9.3.2 Parasite Characterization -- 9.4 A Proteomic Approach: Leishmania Invasion of Macrophages -- 9.5 Intracellular Leishmania Amastigote Spreading between Macrophages -- 9.6 Potential Virus Applications -- Acknowledgements -- References -- Chapter 10 Application of MALDI-; TOF MS in Bioremediation and Environmental Research -- 10.1 Introduction -- 10.2 Microbial Identification: Molecular Methods and MALDI-TOF MS -- 10.2.1 PCR-based Methods -- 10.2.2 MALDI-TOF MS -- 10.3 Combination of MALDI-TOF MS with Other Methods for the Identification of Microorganisms -- 10.4 Application of MALDI-TOF MS in Environmental and Bioremediation Studies -- 10.4.1 The Atmospheric Environment -- 10.4.2 The Aquatic Environment -- 10.4.3 The Terrestrial Environment -- 10.4.4 Bioremediation Research Applications -- 10.5 Microbial Products and Metabolite Activity -- 10.6 Challenges of Environmental Applications -- 10.7 Opportunities and Future Outlook -- 10.8 Conclusions -- References -- Chapter 11 From Genomics to MALDI-TOF MS: Diagnostic Identification and Typing of Bacteria in Veterinary Clinical Laboratories -- 11.1 Introduction -- 11.2 Genomics -- 11.3 Defining Bacterial Species Through Genomics -- 11.4 MALDI-TOF MS -- 11.5 Combining Genomics with MALDI-TOF MS to Classify Bacteria at the Subspecies Level -- 11.6 Data Exploration with MALDI-TOF MS.; 11.7 Validation of Typing Strategies.