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2,216 results for “membrane”

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zenodo40/100

Figure 1 in Morphology of the arthrodial membrane gland in a Neotropical harvester (Arachnida: Opiliones)

Figure 1. External morphology of a male harvester Mischonyx squalidus: (A) dorsal view. The anterior region is on the right, legs I, II and III were removed. The square shows the arthrodial membrane in the leg IV and the pore plate (pp); (B) regions with folds (Fo) and without folds; (B–D) show increasing zoom of the pore plate, a region without folds. Arrows show pores.

opencc-by-4.0Jul 2023View details →
zenodo40/100

Figure 2 in Morphology of the arthrodial membrane gland in a Neotropical harvester (Arachnida: Opiliones)

Figure 2. Sections through an arthrodial membrane of the coxa (CX) - trochanter (TR) articulation of a leg IV in a male harvester Mischonyx squalidus: (A) frontal longitudinal section; (B) transversal section between the coxa and the trochanter of leg IV. (AM) Arthrodial membrane, (c) cuticle (sclerite cuticle), (m) muscle.

opencc-by-4.0Jul 2023View details →
zenodo40/100

Figure 4 in Morphology of the arthrodial membrane gland in a Neotropical harvester (Arachnida: Opiliones)

Figure 4. Sagital sections through an arthrodial membrane of the coxa-trochanter articulation of a leg IV in a male harvester Mischonyx squalidus: (A) staining with bromophenol blue; (B) staining with PAS. (AM) Arthrodial membrane, (SC) secretory cells, (cc) cuticular canals.

opencc-by-4.0Jul 2023View details →
zenodo40/100

Lithium recovery from brines by lithium membrane flow capacitive deionization (Li-MFCDI) – A proof of concept

<p>Dataset to&nbsp;H.M. Saif et al.,&nbsp;<a href="https://www.sciencedirect.com/journal/journal-of-membrane-science-letters">Journal of Membrane Science Letters</a>,&nbsp;<a href="https://www.sciencedirect.com/journal/journal-of-membrane-science-letters/vol/3/issue/2">Volume 3, Issue 2</a>,&nbsp;November 2023, 100059</p> <p>The demand of lithium for electric vehicles and energy storage devices is increasing rapidly, thus new sources of<br> lithium (such as seawater and natural or industrial brines), as well as sustainable methods for its recovery, will<br> need to be explored/developed soon. This work presents a novel electromembrane process, called Lithium<br> Membrane Flow Capacitive Deionization (Li-MFCDI), which was tested to recover lithium from a synthetic<br> geothermal brine containing a much higher mass concentration of sodium than lithium (more than 650 times).<br> Specifically, a ceramic lithium-selective membrane was integrated into a flow capacitive deionization (FCDI)<br> cell, which was specifically designed, and 3D printed, to allow simultaneous charging and regeneration of the<br> employed flow electrodes. Despite the extremely high Na+/Li+ mass ratio in the feed stream, 99.98% of the<br> sodium was rejected and the process selectivity for lithium over other monovalent cations was 141 &plusmn; 5.85 for<br> Li+/Na+ and 46 &plusmn; 1.46 for Li+/K+. The Li-MFCDI process exhibited a stable behaviour over a 7-day test period,<br> and the estimated energy consumption was 16.70 &plusmn; 1.63 kWh/kg of Li+ recovered in the draw solution. These<br> results demonstrate promising potential of the Li-MFCDI for the sustainable lithium recovery from saline streams.</p>

opencc-by-4.0Aug 2023View details →
zenodo40/100

An ancestral dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes

<p>Trajectories, run input files, and custom analysis script&nbsp;for simulations described in the&nbsp;article:<strong>&nbsp;An ancestral dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes</strong> (Silale <em>et al,&nbsp;</em>2023).&nbsp;</p> <p>Preprint:&nbsp;https://doi.org/10.1101/2023.08.14.552755&nbsp;</p>

opencc-by-4.0Sep 2023View details →
zenodo40/100

Dataset from "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (wtChR2-mEos3.2)

<p>This dataset contains raw microscopy data from the article "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (doi.org/10.1002/anie.202307555)</p> <p>Zip file contains PALM measurements of HEK293 cells expressing ChR2<sub>WT</sub> fused with mEos3.2.<br>Each folder in .zip file contains one PALM measurement (TIFF format) and recording settings (.xml) automatically created by acquiring software. For technical reasons, single measurements are divided into TIFF files of =&lt;4088 frames.</p> <p>Detailed protocols for sample preparation and data acquisition are described in the article.<br>Some details are listed below.</p> <p><strong>SAMPLE PREPARATION</strong></p> <p>cell line: Flp-In&trade; T-REx&trade; 293<br>transfection method: modified calcium-phosphate transient transfection [1]<br>fixation method: 4% paraformaldehyde solution in PBS for 30 min at room temperature<br>imaging buffer: PBS</p> <p><strong>PALM ACQUISITION</strong></p> <p>A custom-built setup for single-molecule localization microscopy is described in [2].<br>mEos3.2 was simultaneously photoconverted, imaged and photobleached by gradually increasing UV illumination (405 nm; up to 1 mW at the sample) and continuous excitation at 561 nm (approximately 50 mW at the sample).<br>PALM movies of cell plasma membrane were recorded in total internal reflection fluorescence (TIRF) mode using an EMCCD camera:<br>exposure time = 100 ms<br>frame size = 512x512 pixels<br>pixel size = 80 nm</p> <p>&nbsp;</p> <p>[1] Chen C, Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Molecular and cellular biology. 1987 Aug 1;7(8):2745-52.<br>[2] Tang Y, Dai L, Zhang X, Li J, Hendriks J, Fan X, Gruteser N, Meisenberg A, Baumann A, Katranidis A, Gensch T. SNSMIL, a real-time single molecule identification and localization algorithm for super-resolution fluorescence microscopy. Scientific reports. 2015 Jun 22;5(1):11073</p>

opencc-by-4.0Sep 2023View details →
zenodo40/100

Dataset from "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (ChR2(C34A/C36A)-mEos3.2)

<p>This dataset contains raw microscopy data from the article "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (doi.org/10.1002/anie.202307555)</p> <p>Zip file contains PALM measurements of HEK293 cells expressing ChR2<sub>C34A/C36A</sub> fused with mEos3.2.<br>Each folder in .zip file contains one PALM measurement (TIFF format) and recording settings (.xml) automatically created by acquiring software. For technical reasons, single measurements are divided into TIFF files of =&lt;4088 frames.</p> <p>Detailed protocols for sample preparation and data acquisition are described in the article.<br>Some details are listed below.</p> <p><strong>SAMPLE PREPARATION</strong></p> <p>cell line: Flp-In&trade; T-REx&trade; 293<br>transfection method: modified calcium-phosphate transient transfection [1]<br>fixation method: 4% paraformaldehyde solution in PBS for 30 min at room temperature<br>imaging buffer: PBS</p> <p><strong>PALM ACQUISITION</strong></p> <p>A custom-built setup for single-molecule localization microscopy is described in [2].<br>mEos3.2 was simultaneously photoconverted, imaged and photobleached by gradually increasing UV illumination (405 nm; up to 1 mW at the sample) and continuous excitation at 561 nm (approximately 50 mW at the sample).<br>PALM movies of cell plasma membrane were recorded in total internal reflection fluorescence (TIRF) mode using an EMCCD camera:<br>exposure time = 100 ms<br>frame size = 512x512 pixels<br>pixel size = 80 nm</p> <p>&nbsp;</p> <p>[1] Chen C, Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Molecular and cellular biology. 1987 Aug 1;7(8):2745-52.<br>[2] Tang Y, Dai L, Zhang X, Li J, Hendriks J, Fan X, Gruteser N, Meisenberg A, Baumann A, Katranidis A, Gensch T. SNSMIL, a real-time single molecule identification and localization algorithm for super-resolution fluorescence microscopy. Scientific reports. 2015 Jun 22;5(1):11073</p>

opencc-by-4.0Sep 2023View details →
zenodo40/100

Dataset from "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (b1AR-mEos3.2)

<p>This dataset contains raw microscopy data from the article "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (doi.org/10.1002/anie.202307555)</p> <p>Zip file contains PALM measurements of HEK293 cells expressing &szlig;<sub>1</sub>AR fused with mEos3.2.<br>Each folder in .zip file contains one PALM measurement (TIFF format) and recording settings (.xml) automatically created by acquiring software. For technical reasons, single measurements are divided into TIFF files of =&lt;4088 frames.</p> <p>Detailed protocols for sample preparation and data acquisition are described in the article.<br>Some details are listed below.</p> <p><strong>SAMPLE PREPARATION</strong></p> <p>cell line: Flp-In&trade; T-REx&trade; 293<br>transfection method: modified calcium-phosphate transient transfection [1]<br>fixation method: 4% paraformaldehyde solution in PBS for 30 min at room temperature<br>imaging buffer: PBS</p> <p><strong>PALM ACQUISITION</strong></p> <p>A custom-built setup for single-molecule localization microscopy is described in [2].<br>mEos3.2 was simultaneously photoconverted, imaged and photobleached by gradually increasing UV illumination (405 nm; up to 1 mW at the sample) and continuous excitation at 561 nm (approximately 50 mW at the sample).<br>PALM movies of cell plasma membrane were recorded in total internal reflection fluorescence (TIRF) mode using an EMCCD camera:<br>exposure time = 100 ms<br>frame size = 512x512 pixels<br>pixel size = 80 nm</p> <p>&nbsp;</p> <ol> <li>Chen C, Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Molecular and cellular biology. 1987 Aug 1;7(8):2745-52.</li> <li>Tang Y, Dai L, Zhang X, Li J, Hendriks J, Fan X, Gruteser N, Meisenberg A, Baumann A, Katranidis A, Gensch T. SNSMIL, a real-time single molecule identification and localization algorithm for super-resolution fluorescence microscopy. Scientific reports. 2015 Jun 22;5(1):11073</li> </ol>

opencc-by-4.0Sep 2023View details →
zenodo40/100

Dataset from "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (CD28-mEos3.2)

<p>This dataset contains raw microscopy data from the article "Channelrhodopsin-2 Oligomerization in Cell Membrane Revealed by Photo-Activated Localization Microscopy" (doi.org/10.1002/anie.202307555)</p> <p>Zip file contains PALM measurements of HEK293 cells expressing CD28 fused with mEos3.2.<br>Each folder in .zip file contains one PALM measurement (TIFF format) and recording settings (.xml) automatically created by acquiring software. For technical reasons, single measurements are divided into TIFF files of =&lt;4088 frames.</p> <p>Detailed protocols for sample preparation and data acquisition are described in the article.<br>Some details are listed below.</p> <p><strong>SAMPLE PREPARATION</strong></p> <p>cell line: Flp-In&trade; T-REx&trade; 293<br>transfection method: modified calcium-phosphate transient transfection [1]<br>fixation method: 4% paraformaldehyde solution in PBS for 30 min at room temperature<br>imaging buffer: PBS</p> <p><strong>PALM ACQUISITION</strong></p> <p>A custom-built setup for single-molecule localization microscopy is described in [2].<br>mEos3.2 was simultaneously photoconverted, imaged and photobleached by gradually increasing UV illumination (405 nm; up to 1 mW at the sample) and continuous excitation at 561 nm (approximately 50 mW at the sample).<br>PALM movies of cell plasma membrane were recorded in total internal reflection fluorescence (TIRF) mode using an EMCCD camera:<br>exposure time = 100 ms<br>frame size = 512x512 pixels<br>pixel size = 80 nm</p> <p>&nbsp;</p> <ol> <li>Chen C, Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Molecular and cellular biology. 1987 Aug 1;7(8):2745-52.</li> <li>Tang Y, Dai L, Zhang X, Li J, Hendriks J, Fan X, Gruteser N, Meisenberg A, Baumann A, Katranidis A, Gensch T. SNSMIL, a real-time single molecule identification and localization algorithm for super-resolution fluorescence microscopy. Scientific reports. 2015 Jun 22;5(1):11073</li> </ol>

opencc-by-4.0Sep 2023View details →
zenodo40/100

Cell membrane buckling governs early-stage ridge formation in butterfly wing scales: data

<p>This repository contains the raw data for:<br> JF Totz, AD McDougal, L Wagner, S Kang, PTC So, J Dunkel, BD Wilts, and M Kolle, Cell membrane buckling governs early-stage ridge formation in butterfly wing scales, (forthcoming).</p> <p>The raw data is of a volumetric time series of scales growing on the wing of an individual <em>Vanessa cardui</em> pupa, collected with quantitative phase imaging.</p> <p>Additional details may be found in the Materials and Methods, as well as the SI, of the above publication.</p> <p>&nbsp;</p> <p>The companion code repository may be found on Zenodo:</p> <p>JF Totz, AD McDougal, L Wagner, S Kang, PTC So, J Dunkel, BD Wilts, and M Kolle. (Forthcoming). &quot;Cell membrane buckling governs early-stage ridge formation in butterfly wing scales:code&quot; (v1.0) [Data set]. Zenodo. <a href="https://doi.org/10.5281/zenodo.8369163">https://doi.org/10.5281/zenodo.8369163</a></p> <p>&nbsp;</p> <p>Note that file A-40-01_11_04_34_set_115.mat was previously released in: AD McDougal, S Kang, Z Yaqoob, PTC So, and M Kolle, Data and analysis codes for &ldquo;In vivo visualization of butterfly scale cell morphogenesis in Vanessa cardui.&rdquo; Zenodo. https://doi.org/10.5281/zenodo.5532941. We include it here for completeness of this time series.</p>

opencc-by-4.0Sep 2023View details →
zenodo40/100

The GET insertase exhibits conformational plasticity and induces membrane thinning - The Molecular Dynamics Dataset

<p>The molecular dynamics&nbsp;simulation systems.</p> <p>List of files:&nbsp;</p> <ol> <li><strong>SimulationSystems.pdf</strong>: List of&nbsp;all simulation systems reported and their compositions</li> <li><strong>ProteinComplex.pdb</strong>:&nbsp;The initial model for the hsGet2&Delta;N-Get1/Get3 complex used in simulations was constructed based on the cryo-EM structure (PDB accession 6SO5). Missing residues (except the terminal ones) were modeled using Modeller.</li> <li><strong>prod.mdp</strong>: The GROMACS molecular dynamics parameters (mdp) file used for&nbsp;all simulations</li> <li><strong>toppar.zip</strong>: The Charmm36(m) force field parameter and topology set&nbsp;used for all simulations generated by CHARMM-GUI.</li> <li>Compressed&nbsp;&nbsp;(zip) files containing&nbsp;simulations inputs and trajectories</li> </ol> <p><strong>1-PC.zip<br> 2-1:4_PI:PC.zip<br> 3-1:4_PE:PC.zip<br> 4-1:4_PS:PC.zip<br> 5-1:4_CL:PC.zip<br> 6-1:4_chol:PC.zip<br> 7-1:1:1:1_PC:PI:PS:PE.zip<br> 8-1:1:1:1:1:1_PC:PDPC:PS:PI:PE:chol.zip</strong></p> <p>Each zip file contains the following files:</p> <ol> <li><strong>System_0ns.pdb</strong>: The initial configuration used for the simulations generated using&nbsp;CHARMM-GUI&nbsp;and&nbsp;equilibrated following the CHARMM-GUI equilibration protocol</li> <li><strong>index.ndx</strong>: GROMACS index file</li> <li><strong>topol.top</strong>: GROMACS&nbsp;topology file</li> <li><strong>prod0.tpr,&nbsp;prod1.tpr,&nbsp;prod2.tpr</strong>:&nbsp; GROMACS run topology files (tpr) for each repeat</li> <li><strong>prod0.gro, prod1.gro,&nbsp;prod2.gro</strong>: The final configuration after 3 &mu;s production runs for each repeat</li> <li><strong>noW_0ns.pdb</strong>: The initial configuration without the water molecules.</li> <li><strong>noW_0.xtc,&nbsp;noW_1.xtc,&nbsp;noW_2.xtc</strong>:&nbsp;The&nbsp;3 &mu;s processed production trajectories. The water molecules were removed, and the trajectories were subsampled at 1 ns intervals.</li> </ol> <p>&nbsp;</p> <p>&nbsp;</p>

openOct 2023View details →
zenodo40/100

Membrane screening parameters and Permeation data

<p><span>CO2SMOS&rsquo; task 2.4.3 aims at developing Thin Film Composite Membranes for selective water extraction. This dataset shows the screened parameters and the results of the permeation assays</span></p>

opencc-by-4.0Aug 2024View details →
dryad40/100

A role for myosin II cluster and membrane energy in cortex rupture for Dictyostelium discoideum cells

Open the record for dataset details and reuse information.

publicMar 2022View details →
dryad40/100

Data for: Exocytosis of the silicified cell wall of diatoms involves extensive membrane disintegration

Open the record for dataset details and reuse information.

publicDec 2022View details →
dryad40/100

Data from: Free energy analysis of peptide-induced pore formation in lipid membranes by bridging atomistic and coarse-grained simulations

Open the record for dataset details and reuse information.

publicOct 2024View details →
dryad40/100

Data from: Sorting states of environmental DNA: Effects of isolation method and water matrix on recovery of membrane-bound, dissolved, and adsorbed states of eDNA

Open the record for dataset details and reuse information.

publicApr 2024View details →
dryad40/100

Data for: Human atlastin-3 is a constitutive ER membrane fusion catalyst (phylogenetic and sequence analysis)

Open the record for dataset details and reuse information.

publicMay 2023View details →
dryad40/100

Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat

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publicMay 2023View details →
zenodo36/100

Raw data for the manuscript under the title "Mitochondrial RNA granules are fluid condensates, positioned by membrane dynamics".

<p><strong>This is the data-repository</strong> to contain all relevant raw-data used and referred to in the manuscript entitled:<br> &quot;Mitochondrial RNA granules are fluid condensates, positioned by membrane dynamics&quot;<br> [manuscript under revision, and thus not citable as published article]</p> <p>The repository is structured analogous to the manuscript. Find a more detailed description in the README.</p>

opencc-by-4.0Apr 2020View details →
dryad36/100

Data from: A multiscale biophysical model for the recruitment of actin nucleating proteins at the membrane interface

<p>The dynamics and organization of the actin cytoskeleton are crucial to many cellular events such as motility, polarization, cell shaping, and cell division. The intracellular and extracellular signaling associated with this cytoskeletal network is communicated through cell membranes. Hence the organization of membrane macromolecules and actin filament assembly are highly interdependent. Although the actin-membrane linkage is known to happen through many routes, the major class of interactions is through the direct interaction of actin-binding proteins with the lipid class containing poly-phosphatidylinositols (PPIs). Among the PPIs, phosphatidylinositol bisphosphate (PI(4,5)P<sub>2</sub>) acts as a significant factor controlling actin polymerization in the proximity of the membrane by binding to actin-associated proteins. The molecular interactions between these actin-binding proteins and the membrane lipids remain elusive. Here, using molecular modeling, analytical theory, and experimental methods, we investigate the binding of three different actin-binding proteins, mDia2, NWASP, and gelsolin, to membranes containing PI(4,5)P<sub>2</sub> lipids. We perform molecular dynamics simulations on the protein-bilayer system and analyze the membrane binding in the form of hydrogen bonds and salt bridges at various PI(4,5)P<sub>2</sub> and cholesterol concentrations. Our experimental study with PI(4,5)P<sub>2</sub>-containing large unilamellar vesicles mimics the computational experiments. Using the multivalencies of the proteins obtained in molecular simulations and the cooperative binding mechanisms of the proteins, we also propose a multivalent binding model that predicts the actin filament distributions at various PI(4,5)P<sub>2 </sub>and protein concentrations.</p>

opencc-zeroMay 2020View details →

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dandi-nwb
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Last verified 2026-04-29Open record