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  • 1
    New York, NY : Springer
    Keywords: Biochemistry ; Biochemistry, general ; Springer eBooks
    Description / Table of Contents: Molecular Dynamics Simulations of the SNARE Complex -- Mesoscale Computational Modelling of Protein-membrane Interactions based on Continuum Mean-field Theory -- EPR Lineshape Analysis to IOnvestigate the SNARE Folding Intermediates -- Dynamic Light Scattering Analysis to Dissect Intermediates of SNARE-Mediated Membrane Fusion -- Kinetic and Thermodynamic Quantification of Protein Complex Assembly: The Example of SNAREpins -- Single-molecule Optical Tweezers Study of Regulated SNARE Assembly -- Studying Munc18:Syntaxin Interactions using Small-angle Scattering -- Using Force Spectroscopy to Probe Coiled-Coil Assembly and Membrane Fusion -- SNAP25 S-Guanylation and SNARE Complex Formation -- Analysis of the Role of Sec3 in SNARE Assembly and Membrane Fusion -- Use of Microscale Thermophoresis (MST) to Measure Binding Affinities of Components of the Fusion Machinery -- Use of Surface Plasmon Resonance (SPR) to Determine Binding Affinities and Kinetic Parameters Between Components Important in Fusion Machinery -- Determination of Sec18-Lipid Interactions by Liposome Binding Assay -- Using Nanodiscs to Probe Ca2+-dependent Membrane Interaction of Synaptotagmin-1 -- Functional reconstitution of Intracellular Vesicle Fusion using Purified SNAREs and Sec1/Munc18 (SM) Proteins -- Assay of Lipid Mixing and Fusion Pore Formation in the Fusion of Yeast Vacuoles -- A nanodisc-cell Fusion Assay with Single Pore Sensitivity and Sub-millisecond Time Resolution -- An In Vitro Assay of trans-SNARE Complex Formation during Yeast Vacuole Fusion using Epitope Tag-free SNAREs -- A Cell-Free Content Mixing Assay for SNARE-Mediated Multivesicular Body-Vacuole Membrane Fusion -- Reconstituted Proteoliposome Fusion Mediated by yeast SNARE-family Proteins -- Real-Time Fluorescence Detection of Calcium Efflux during Vacuolar Membrane Fusion -- Single Molecule Fluorescence Measurement of SNARE-mediated Vesicle Fusion -- Quantifying Intramolecular Protein Conformational Dynamics under Lipid Interaction using smFRET and FCCS -- Visualization of SNARE-Mediated Organelle Membrane Hemifusion By Electron Microscopy -- Studies of the Secretory Machinery Dynamics by Total Internal Reflection Fluorescence Microscopy in Bovine Adrenal Chromaffin Cells -- Imaging SNAP-29 in Drosophila
    Abstract: This book details multiple ways that soluble N-ethylmaleimide-sensitive factor attachment protein receptors( SNAREs) and their function are examined in the laboratory. The methods described in each chapter are described in detail so that novice as well as experienced researchers can explore the mechanisms of SNARE-mediated membrane fusion. Chapters guide readers through an overview of the basic properties of SNAREs, distribution and interaction with regulators of membrane fusion, activation of SNAREs in the priming stage by NSF/Sec18 and a-SNAP/Sec17, examining the structures and interactions of SNAREs, measuring the interactions of SNAREs, interactions of SNAREs, and post-translational modifications of SNAREs and how they affect function.Written in the highly successful Methods in Molecular Biology series format, 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 cutting-edge, SNAREs: Methods and Protocols aims to be a valuable tool for all investigators interested in the field
    Pages: XIV, 407 p. 74 illus., 66 illus. in color. : online resource.
    ISBN: 9781493987603
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  • 2
    ISSN: 0173-0835
    Keywords: Phagosome ; Lysosome ; GTP-binding protein ; Tuberculosis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: One of the most prominent features of pathogenic mycobacteria, which include the potent human pathogens Mycobacterium tuberculosis and Mycobacterium leprae and their opportunistic relatives Mycobacterium avium and Mycobacterium marinum, is their ability to survive and multiply in phagosomes of mononuclear phagocytic cells. The phagocytosed mycobacteria reside in a vacuolar compartment which is exempted from maturation into the phagolysosome. Recently, the arrest of the maturation of phagosomes containing M. tuberculosis complex organisms (Mycobacterium bovis BCG) has been linked to the accumulation on the phagosomal membrane of the small GTP binding protein rab5, specific for the control of fusion within the early endosomal compartment. Furthermore, M. bovis BCG phagosome is devoid of rab7, a rab protein associated with the late endosome. The selective accumulation of rab5 and exclusion of rab7 defines the check point that has been compromised in mycobacterial phagosome maturation. Here we summarize these observations and relates them to other phenomena in the area of membrane and protein trafficking with the emphasis on phagosomes containing intracellular pathogens.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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