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020			_a9781592591954
024	7		_a10.1385/1592591957 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aRC523 _b200 EB
245	0	0	_aAlzheimer's Disease : _bMethods and Protocols _cedited by Nigel M. Hooper
250			_a1st edition 2000
264		1	_aTotowa, NJ _bHumana Press _c2000
300			_a1 recurso en línea (XIV, 408 páginas)
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_aarchivo de texto _bPDF
490	0		_aMethods in Molecular Medicine _x1940-6037 _v32
505	0		_ato Alzheimer's Disease -- The Genetics of Alzheimer's Disease -- Advances in Methodology and Current Prospects for Primary Drug Therapies for Alzheimer's Disease -- Production and Functional Assays of Recombinant Secreted Amyloid Precursor Protein (APP) (sAPP?) -- Quantifying A?1-40 and A?1-42 Using Sandwich-ELISA -- Electrophoretic Separation and Immunoblotting of A?1-40 and A?1-42 -- A?-Induced Proinflammatory Cytokine Release from Differentiated Human THP-1 Monocytes -- Effects of the ?-Amyloid Peptide on Membrane Ion Permeability -- Analysis of ?-Amyloid Peptide Degradation In Vitro -- Posttranslational Modifications of Amyloid Precursor Protein -- Posttranslational Modifications of the Amyloid Precursor Protein -- Using an Amyloid Precursor Protein (APP) Reporter to Characterize ?-Secretase -- Inhibition of ?-Secretase by Zinc Metalloproteinase Inhibitors -- Development of Neoepitope Antibodies Against the ?-Secretase Cleavage Site in the Amyloid Precursor Protein -- ?-Secretase -- Using ?-Secretase Inhibitors to Distiguish the Generation of the A? Peptides Terminating at Val-40 and Ala-42 -- Designing Animal Models of Alzheimer's Disease with Amyloid Precursor Protein (APP) Transgenes -- Phosphorylation of Amyloid Precursor Protein (APP) Family Proteins -- Determining the Transmembrane Topology of the Presenilins -- Normal Proteolytic Processing of the Presenilins -- Apoptotic Proteolytic Cleavage of the Presenilins by Caspases -- The Phosphorylation of Presenilin Proteins -- Interaction of the Presenilins with the Amyloid Precursor Protein (APP) -- Distribution of Presenilins and Amyloid Precursor Protein (APP) in Detergent-Insoluble Membrane Domains -- Characterization and Use of Monoclonal Antibodies to Tau and Paired Helical Filament Tau -- Tau Phosphorylation Both In Vitro and in Cells -- Transglutaminase-Catalyzed Formation of Alzheimer-Like Insoluble Complexes from Recombinant Tau.
520			_aWith the molecular mechanisms underlying the various forms of muscular dystrophy now rapidly clarifying, precise diagnosis has become a reality, and even a requirement in clinical practice. In Muscular Dystrophy: Methods and Protocols, Katherine Bushby and Louise Anderson have assembled an outstanding collection of key techniques for the analysis of DNA and protein from patients suspected to suffer from muscular dystrophy. Each method is highly detailed to ensure success and is presented by a hands-on expert who uses it on a day-to-day basis. The various DNA techniques focus on both the X-linked muscular dystrophies and the autosomal recessive muscular dystrophies. The protein methods include expression analysis, multiplex western blot analysis, immunocytochemical analysis, and reviews of immunological reagants and of amplification systems. Also discussed are the use of animal models to understand human muscular dystrophy and the available options for gene-based therapy. Comprehensive and highly practical, Muscular Dystrophy: Methods and Protocols offers today,s diagnostic laboratories, basic and medical researchers, and active clinicians an authoritative collection of tools that will serve as exacting diagnostic tools as well as greatly empowering research on the novel therapeutics now beginning to emerge.
988			_aSpringer_Protocols_2000
650		7	_2embne _9144620 _aAlzheimer, Enfermedad de _vManuales de laboratorio
776	0	8	_iPrinted edition: _z9781617371615
776	0	8	_iPrinted edition: _z9780896037373
776	0	8	_iPrinted edition: _z9781489941503
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592591957 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b01/2024 _dz _eb _zSI