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020			_a9781493929788
024	7		_a10.1007/978-1-4939-2978-8 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aRC632 .A5
245	0	0	_aProtein Amyloid Aggregation : _bMethods and Protocols _cedited by David Eliezer
250			_a1st edition 2016
264		1	_aNew York, NY _bSpringer International Publishing _c2016
300			_a1 recurso en línea (XIV, 314 páginas) _b73 ilustraciones, 49 ilustraciones a color
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_aarchivo de texto _bPDF
490	0		_aMethods in Molecular Biology _x1940-6029 _v1345
505	0		_aSemisynthesis and Enzymatic Preparation of Post-Translationally Modified α-Synuclein -- Isotope-Labeled Amyloids Via Synthesis, Expression and Chemical Ligation for Use in FTIR, 2D IR and NMR Studies -- Inter-Molecular Paramagnetic Relaxation Enhancement (PRE) Studies of Transient Complexes in Intrinsically Disordered Proteins -- Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins -- Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo -- Deep UV Resonance Raman Spectroscopy for Characterizing Amyloid Aggregation -- Analyzing Tau Aggregation with Electron Microscopy -- Characterization of Amyloid Oligomers by Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry (ESI-IMS-MS) -- Formation and Characterization of α-Synuclein Oligomers -- Fluorescence Methods for Unraveling Oligomeric Amyloid Intermediates -- Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy -- Spin Labeling and Characterization of Tau Fibrils Using Electron Paramagnetic Resonance (EPR) -- Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers -- Quenched Hydrogen Exchange NMR of Amyloid Fibrils -- Studying the Early Stages of Protein Aggregation Using Replica Exchange Molecular Dynamics Simulations -- Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels -- Analyzing Ensembles of Amyloid Proteins Using Bayesian Statistics -- In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles -- Cell Models to Study Cell-to-Cell Transmission of α-Synuclein -- Preparation of Amyloid Fibrils Seeded from Brain and Meninges.
520			_aThis detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils, and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.   Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists, and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.
988			_aSpringer_Protocols_2016
650		7	_2embne _9145189 _aAmiloidosis _vManuales de laboratorio
776	0	8	_iPrinted edition: _z9781493929771
776	0	8	_iPrinted edition: _z9781493929795
776	0	8	_iPrinted edition: _z9781493950058
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-4939-2978-8 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b11/2023 _dz _eu _zSI