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  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Nanotechnology. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (227 pages)
    Edition: 1st ed.
    ISBN: 9783662433676
    Series Statement: Advances in Atom and Single Molecule Machines Series
    DDC: 620.5
    Language: English
    Note: Intro -- Preface -- Contents -- Contributors -- 1 Introduction to Single-Molecule Analysis and Computation: The Focus Project -- References -- 2 Computer-Generated Holographic Beams for the Investigation of the Molecular and Circuit Function -- Abstract -- 1…Introduction -- 2…Background and Computational Aspects in CGH -- 2.1 Computation of the Phase Maps -- 3…Hardware for CGH: LCoS-SLM -- 3.1 LCoS-SLM: Working Principle -- 3.2 LCoS-SLM: Temporal Features and Overdriving Procedures -- 3.3 LCoS-SLM: Design of the Device -- 3.4 LCoS-SLM: Optical Properties -- 4…Optical Configurations for CGH -- 4.1 Basic Configuration for CGH -- 4.2 Integration of CGH into Imaging Systems -- 4.3 Optical Figures of CGH -- 4.4 Peculiar Aspects of CGH Beams for Bidimensional Extended Patterns -- 5…Applications and Perspective for CGH -- References -- 3 Super-Resolution Fluorescence Optical Microscopy: Targeted and Stochastic Read-Out Approaches -- Abstract -- 1…Introduction -- 2…Toward Super-Resolution Imaging of Thick ( greaterthan 50 Mu m) Biological Specimens -- 3…Single-Molecule Localization Techniques (Palm-Like) -- 4…Stimulated Emission Depletion (Sted-Like) -- 5…Perspective Note -- References -- 4 Superhydrophobic Devices Molecular Detection -- Abstract -- 1…Introduction -- 1.1 Single-Molecule Detection -- 1.2 Superhydrophobic Surfaces -- 2…Fabrication -- 2.1 Superhydrophobic Pillared Substrates -- 2.2 Polymeric Superhydrophobic Substrates -- 3…Applications -- 3.1 Molecular Detection of Organic and Inorganic Sample's Structural Information Through In-situ X-ray Diffraction -- 3.2 Superhydrophobic Substrate for Raman Detection -- 3.3 Superhydrophobic Substrates for Background-Free TEM DNA Characterization and for Nucleic Acid Pattern Generation -- References -- 5 Tip-Assisted Optical Nanoscopy for Single-Molecule Activation and Detection -- Abstract. , 1…An Overview -- 1.1 A Brief History of the Tip-Assisted Technique -- 2…Theoretical Background -- 2.1 The Evanescent Field -- 2.2 Localized Surface Plasmon Tip -- 2.3 Plasmonic Antenna Tip -- 3…Experimental Setups and Methods -- 3.1 Tips and Tips Engineering -- 3.2 Microscopes Design -- 4…Applications of TERS -- References -- 6 DNA as Nanostructuring Element for Design of Functional Devices -- Abstract -- 1…Introduction -- 2…DNA-Directed Immobilization: Use of Chemically Synthesized Short DNA -- 2.1 DNA as an Immobilization Tool -- 2.2 DNA--Nanoparticle Conjugates -- 3…DNA Origami: Combination of Natural and Chemically Synthesized DNA -- 4…DNA in Design of Thin Films and Optoelectronic Devices: Use of DNA from Natural Sources -- 5…DNA-Based Materials -- 5.1 DNA-Based Hydrogels -- 5.2 DNA-Polymeric Hybrid Materials -- 5.3 DNA Side-Chain Polymers -- 6…Conclusion -- References -- 7 Fast Force Clamp in Optical Tweezers: A Tool to Study the Kinetics of Molecular Reactions -- Abstract -- 1…Single-Molecule Mechanics with Optical Tweezers -- 2…The Dual-Laser Optical Tweezers -- 2.1 Mounting the Specimen in the Experimental Chamber Between the Force and Length Transducers -- 2.2 Calibration of Force -- 2.3 Mechanical Protocols: Length Versus Force Clamp -- 3…Transition Kinetics of the DNA Elongation Revealed by Force Steps -- 4…The Structure of the DNA Overstretching Transition -- 5…Assessing the Force Clamp Description of DNA Overstretching Kinetics: Comparison Between Non-equilibrium and Equilibrium Results -- A.x(118). Appendix: Influence of Viscosity on the Kinetics of the Elongation--Untwisting of the ds-DNA During the Overstretching Transition -- A.x(118).0 Drag Produced on the Trapped Bead by the Viscosity of the Medium -- A.x(118).0 Rotational Drag of the Molecule While Untwisting -- References. , 8 Investigating Adhesion Proteins by Single Cell Force Spectroscopy -- Abstract -- 1…Introduction -- 2…Force-Spectroscopy Measurements and Experimental Details -- 3…Analysis of Force-Distance Curve -- 4…The Advantages of SCFS in the Study of Single Adhesion Proteins -- 5…Quantifying Cell Adhesion at Single Molecule Scale -- 6…Future Perspectives -- References -- 9 Photoswitchable Ion Channels and Receptors -- Abstract -- 1…Introduction -- 2…Pentameric Ligand-Gated Receptors -- 2.1 Introduction -- 2.2 Nicotinic Acetylcholine Receptors (nAChR) -- 2.3 Ionotropic gamma -Aminobutyric Acid Receptor (GABAA) -- 3…Tetrameric Ligand-Gated Receptors -- 3.1 Introduction -- 3.2 Kainate Receptors -- 3.3 AMPA Receptors -- 3.4 Bacterial iGluRs -- 3.5 Metabotropic Glutamate Receptors -- 3.6 Applications -- 4…Trimeric Ligand-Gated Receptors -- 5…Potassium Channels -- 5.1 Introduction -- 5.2 Kv Family -- 5.2.1 2P-Potassium Channels -- 6…Transient Receptor Potential Channels -- 7…Future Challenges -- References -- 10 The Use of Light-Sensitive Organic Semiconductors to Manipulate Neuronal Activity -- Abstract -- 1…Introduction -- 2…Optical Techniques Modulating Neuronal Activity -- 3…Organic Semiconductive Polymers -- 4…Modulation of Membrane Potential Using Light-Sensitive Polymers -- 5…Application of Organic Photovoltaic Devices in Retinal Degenerative Diseases -- 6…Future Research Direction -- 7…Conclusions -- References -- 11 Probing the Lateral Diffusion of Individual Neurotransmitter Receptors -- Abstract -- 1…Introduction -- 2…Measuring the Lateral Diffusion of Neurotransmitter Receptors -- 2.1 Population Diffusion Measurements -- 2.2 Single-particle Tracking Techniques -- 3…Role of Receptor Diffusion in Long-Term Synaptic Plasticity -- 4…Implications of Receptor Diffusion in Fast Synaptic Signaling -- 5…Future Perspectives -- References.
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  • 2
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Focal adhesion kinase (FAK) and the related proline-rich tyrosine kinase 2 (PYK2) are non-receptor protein tyrosine kinases that transduce extracellular signals through the activation of Src family kinases and are highly enriched in neurones. To further elucidate the regulation of FAK and PYK2 in nervous tissue, we investigated their distribution in brain subcellular fractions and analysed their translocation between membrane and cytosolic compartments. We have found that FAK and PYK2 are present in a small membrane-associated pool and a larger cytosolic pool in various neuronal compartments including nerve terminals. In intact nerve terminals, inhibition of Src kinases inhibited the membrane association of FAK, but not of PYK2, whereas tyrosine phosphatase inhibition sharply increased the membrane association of both FAK and PYK2. Disruption of the actin cytoskeleton was followed by a decrease in the membrane-associated pool of FAK, but not of PYK2. For both kinases, a significant correlation was found between autophosphorylation and membrane association. The data indicate that FAK and PYK2 are present in nerve terminals and that the membrane association of FAK is regulated by both phosphorylation and actin assembly, whereas that of PKY2 is primarily dependent on its phosphorylation state.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Several cytokines have short-term effects on synaptic transmission and plasticity that are thought to be mediated by the activation of intracellular protein kinases. We have studied the effects of interleukin-6 (IL-6) on the expression of paired pulse facilitation (PPF), posttetanic potentiation (PTP), and long-term potentiation (LTP) in the CA1 region of the hippocampus as well as on the activation of the signal transducer and activator of transcription-3 (STAT3), the mitogen-activated protein kinase ERK (MAPK/ERK), and the stress-activated protein kinase/c-Jun NH2-terminal kinase (SAPK/JNK). IL-6 induced a marked and dose-dependent decrease in the expression of PTP and LTP that could be counteracted by the simultaneous treatment with the tyrosine kinase inhibitor lavendustin A (LavA) but did not significantly affect PPF. The IL-6-induced inhibition of PTP and LTP was accompanied by a simulation of STAT3 tyrosine phosphorylation and an inhibition of MAPK/ERK dual phosphorylation, in the absence of changes in the state of activation of SAPK/JNK. Both effects of IL-6 on STAT3 and MAPK/ERK activation were effectively counteracted by LavA treatment. The results indicate the tyrosine kinases and MAPK/ERK are involved in hippocampal synaptic plasticity and may represent preferential intracellular targets for the actions of IL-6 in the adult nervous system.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The Ca2+-sensor protein S100A1 was recently shown to bind in vitro to synapsins, a family of synaptic vesicle phosphoproteins involved in the regulation of neurotransmitter release. In this paper, we analyzed the distribution of S100A1 and synapsin I in the CNS and investigated the effects of the S100A1/synapsin binding on the synapsin functional properties. Subcellular fractionation of rat brain homogenate revealed that S100A1 is present in the soluble fraction of isolated nerve endings. Confocal laser scanning microscopy and immunogold immunocytochemistry demonstrated that S100A1 and synapsin codistribute in a subpopulation (5–20%) of nerve terminals in the mouse cerebral and cerebellar cortices. By forming heterocomplexes with either dephosphorylated or phosphorylated synapsin I, S100A1 caused a dose- and Ca2+-dependent inhibition of synapsin-induced F-actin bundling and abolished synapsin dimerization, without affecting the binding of synapsin to F-actin, G-actin or synaptic vesicles. These data indicate that: (i) synapsins and S100A1 can interact in the nerve terminals where they are coexpresssed; (ii) S100A1 is unable to bind to SV-associated synapsin I and may function as a cytoplasmic store of monomeric synapsin I; and (iii) synapsin dimerization and interaction with S100A1 are mutually exclusive, suggesting an involvement of S100A1 in the Ca2+-dependent regulation of synaptic vesicle trafficking.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Cytokines are extracellular mediators that have been reported to affect neurotransmitter release and synaptic plasticity phenomena when applied in vitro. Most of these effects occur rapidly after the application of the cytokines and are presumably mediated through the activation of protein phosphorylation processes. While many cytokines have an inflammatory action, interleukin-6 (IL-6) has been found to have a neuroprotective effect against ischaemia lesions and glutamate excitotoxicity, and to increase neuronal survival in a variety of experimental conditions. In this paper, the functional effects of IL-6 on the spread of excitation visualized by dark-field/infrared videomicroscopy in rat cortical slices and on glutamate release from cortical synaptosomes were analysed and correlated with the activation of the STAT3, mitogen-activated protein kinase ERK (MAPK/ERK) and stress-activated protein kinase/cJun NH2-terminal kinase (SAPK/JNK) pathways. We have found that IL-6 depresses the spread of excitation and evoked glutamate release in the cerebral cortex, and that these effects are accompanied by a stimulation of STAT3 tyrosine phosphorylation, an inhibition of MAPK/ERK activity, a decreased phosphorylation of the presynaptic MAPK/ERK substrate synapsin I and no detectable effects on SAPK/JNK. The effects of IL-6 were effectively counteracted by treatment of the cortical slices with the tyrosine kinase inhibitor lavendustin A. The inhibitory effects of IL-6 on glutamate release and on the spread of excitation in the rat cerebral cortex indicate that the protective effect of IL-6 on neuronal survival could be mediated by a downregulation of neuronal activity, release of excitatory neurotransmitters and MAPK/ERK activity.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that activates Src family kinases via SH2- and SH3-mediated interactions. Specific FAK isoforms (FAK+), responsive to depolarization and neurotransmitters, are enriched in neurons. We analyzed the interactions of endogenous FAK+ and recombinant FAK+ isoforms containing amino acid insertions (boxes 6,7,28) with an array of SH3 domains and the c-Src SH2/SH3 domain tandem. Endogenous FAK+ bound specifically to the SH3 domains of c-Src (but not n-Src), Fyn, Yes, phosphtidylinositol-3 kinase, amphiphysin II, amphiphysin I, phospholipase Cγ and NH2-terminal Grb2. The inclusion of boxes 6,7 was associated with a significant decrease in the binding of FAK+ to the c-Src and Fyn SH3 domains, and a significant increase in the binding to the Src SH2 domain, as a consequence of the higher phosphorylation of Tyr-397. The novel interaction with the amphiphysin SH3 domain, involving the COOH-terminal proline-rich region of FAK, was confirmed by coimmunoprecipitation of the two proteins and a closely similar response to stimuli affecting the actin cytoskeleton. Moreover, an impairment of endocytosis was observed in synaptosomes after internalization of a proline-rich peptide corresponding to the site of interaction. The data account for the different subcellular distribution of FAK and Src kinases and the specific regulation of the transduction pathways linked to FAK activation in the brain and implicate FAK in the regulation of membrane trafficking in nerve terminals.
    Type of Medium: Electronic Resource
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