13 research outputs found

    Design Considerations of Capacitive Power Transfer Systems

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    Capacitive power transfer (CPT) is a near-field wireless power transfer (WPT) technology that has attracted attention in different charging applications. By utilizing electric fields, CPT gives charging systems advantages in terms of cost, weight, flexibility, and mobility. This paper surveys a number of empirical published works in a period between 2015 and 2023. Additionally, it discusses theoretical and practical design considerations of a CPT system to understand and improve the technology and its applications. The paper studies the one- and two-port measuring approaches using vector network analyzers to determine the coupling parameters and compares the measurements to the simulated values using COMSOL Multiphysics ©. The two-port approach gives more accurate results than the one-port approach. The paper designs and tests a 13.56MHz CPT system using the two-port measurement results. The system transfers 100W at 87.4% efficiency and 30mm separation distance. Lastly, the paper discusses the design limitations and challenges of the CPT systems, aiming to emphasize the design obstacles that can drive the advancement of the CPT systems for wireless charging applications

    Change in somatosensory evoked potential in the rat recorded at the hemisphere with iron-induced epileptic focus.

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    In rats, microinjection of FeCl3 solution into the left sensorimotor cortex was performed to induce a chronic epileptic focus. One month or more after the microinjection, electrocutaneous stimuli were applied to part of the wrist joint and 50 consecutive somatosensory evoked potentials (SEPs) were averaged. SEP from the left cortex showed only an initial negative monophasic deflection while SEP from the contralateral cortex showed a normal configuration with initial positive-negative biphasic deflection in the majority of experimental animals.</p

    Identification of an elaborate complex mediating postsynaptic inhibition

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    Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. The composition of the inhibitory postsynapse and the mechanistic basis of its regulation, however, remains poorly understood. We used an in vivo chemico-genetic proximity-labeling approach to discover inhibitory postsynaptic proteins. Quantitative mass spectrometry not only recapitulated known inhibitory postsynaptic proteins, but also revealed a large network of new proteins, many of which are either implicated in neurodevelopmental disorders or are of unknown function. CRISPR-depletion of one of these previously uncharacterized proteins, InSyn1, led to decreased postsynaptic inhibitory sites, reduced frequency of miniature inhibitory currents, and increased excitability in the hippocampus. Our findings uncover a rich and functionally diverse assemblage of previously unknown proteins that regulate postsynaptic inhibition and might contribute to developmental brain disorders

    Spine pruning drives antipsychotic-sensitive locomotion via circuit control of striatal dopamine

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    Psychiatric and neurodevelopmental disorders may arise from anomalies in long-range neuronal connectivity downstream of pathologies in dendritic spines. However, the mechanisms that may link spine pathology to circuit abnormalities relevant to atypical behavior remain unknown. Using a mouse model to conditionally disrupt a critical regulator of the dendritic spine cytoskeleton, Arp2/3, we report here a molecular mechanism that unexpectedly reveals the interrelationship of progressive spine pruning, elevated frontal cortical excitation of pyramidal neurons, and striatal hyperdopaminergia within a cortical-to-midbrain circuit abnormality. The main symptomatic manifestations of this circuit abnormality are psychomotor agitation and stereotypical behaviors, which are relieved by antipsychotics. Moreover, antipsychotic-responsive locomotion can be directly mimicked in wildtype mice by optogenetic activation of this circuit. Collectively these results reveal molecular and neural-circuit mechanisms, illustrating how diverse pathologies may converge to drive behaviors relevant to psychiatric disorders

    Peptide Array X-Linking (PAX): A New Peptide-Protein Identification Approach

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    Many protein interaction domains bind short peptides based on canonical sequence consensus motifs. Here we report the development of a peptide array-based proteomics tool to identify proteins directly interacting with ligand peptides from cell lysates. Array-formatted bait peptides containing an amino acid-derived cross-linker are photo-induced to crosslink with interacting proteins from lysates of interest. Indirect associations are removed by high stringency washes under denaturing conditions. Covalently trapped proteins are subsequently identified by LC-MS/MS and screened by cluster analysis and domain scanning. We apply this methodology to peptides with different proline-containing consensus sequences and show successful identifications from brain lysates of known and novel proteins containing polyproline motif-binding domains such as EH, EVH1, SH3, WW domains. These results suggest the capacity of arrayed peptide ligands to capture and subsequently identify proteins by mass spectrometry is relatively broad and robust. Additionally, the approach is rapid and applicable to cell or tissue fractions from any source, making the approach a flexible tool for initial protein-protein interaction discovery.National Institutes of Health (U.S.) (Grant R21-CA-140030-01

    List of Bait Peptides and the Identified Proteins.

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    ★<p>Proteins in italics were previously known to bind to the bait peptides and reproduced in the study. The interactions between proteins in bold italics and the bait proteins were identified in the bioinformatics study.</p

    Experimental outline of PAX methodology.

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    <p>(<b>A</b>) Arrays of bait peptides are synthesized onto PEG-based membrane supports. The photo-activatable amino acid cross-linker (pBpa) is incorporated into the bait peptides so that each peptide spot has pBpa at a different position in the sequence (see inset schematic). (<b>B</b>, <b>C</b>) The membrane is incubated with cell lysate and subjected to 350–365 nm light to cross-link with interacting proteins. (<b>D</b>) The indirect and non-specific interactors are removed by high stringent, denaturing washes. (<b>E</b>, <b>F</b>) Each strip of the bait peptide spots is cut off the membrane, further chopped into small pieces, and trypsinized. (<b>G</b>, <b>H</b>) The samples are filtered to remove PEG and subjected to LC-MS/MS analysis to identify the photo-trapped proteins.</p
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