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7 results for “membrane transport proteins”

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zenodo48/100

Data in: Aging power spectrum of membrane protein transport and other subordinated random walks

<p>Datasets generated in the report &quot;Aging power spectrum of membrane protein transport and other subordinated random walks&quot;. Included data are:</p> <p><strong>Numerical simulations&nbsp;</strong><br> RWdata1.mat: 10,000 realizations, subordinated random walk with Hurst exponent, <em>H</em>=0.3&nbsp;and <span class="math-tex">\(\alpha\)</span>=0.4.<br> RWdata3.mat:&nbsp;10,000 realizations, subordinated random walk with Hurst exponent, <em>H</em>=0.7&nbsp;and <span class="math-tex">\(\alpha\)</span>=0.4.<br> RWdata8.mat:&nbsp;5,000 realizations, subordinated random walk with Hurst exponent, <em>H</em>=0.75&nbsp;and <span class="math-tex">\(\alpha\)</span>=0.8.<br> RWdataCTRW.mat:&nbsp;10,000 realizations, continuous time random walk (CTRW),&nbsp;<span class="math-tex">\(\alpha\)</span>=0.7.</p> <p><strong>Spectra of&nbsp;simulations</strong><br> PSDdata1.mat: Power spectral density (PSD) of a subordinated random walk with Hurst exponent, <em>H</em>=0.3&nbsp;and <span class="math-tex">\(\alpha\)</span>=0.4. Five different realization times are used to compute the PDS: 2^8,&nbsp;2^10,&nbsp;2^12,&nbsp;2^14, and 2^16.<br> PSDdata3.mat:&nbsp;PSD of a subordinated random walk with Hurst exponent, <em>H</em>=0.7&nbsp;and <span class="math-tex">\(\alpha\)</span>=0.4. Five different realization times are used to compute the PDS: 2^8,&nbsp;2^10,&nbsp;2^12,&nbsp;2^14, and 2^16.<br> PSDdata8.mat: PSD of a&nbsp;subordinated random walk with Hurst exponent, <em>H</em>=0.75&nbsp;and <span class="math-tex">\(\alpha\)</span>=0.8.&nbsp;Four&nbsp;different realization times are used to compute the PDS: 2^15,&nbsp;2^16,&nbsp;2^17, and 2^18.<br> PSDs_CTRW.mat: PSD of a&nbsp;continuous-time random walk (CTRW),&nbsp;<span class="math-tex">\(\alpha\)</span>=0.7. Five different realization times are used to compute the PDS: 2^8,&nbsp;2^10,&nbsp;2^12,&nbsp;2^14, and 2^16.</p> <p><strong>Experimental data of Nav1.6 channels in the soma of hippocampal neurons</strong><br> NavMSDtimes.csv: ensemble-averaged (EA) MSD and time-averaged (TA) MSD. The TA-MSD is measured&nbsp;for three observation times, 64, 128, and 256 frames (3.2, 6.4, and 12.8 s).<br> NavPSD.csv: Power spectral density (PSD) measured for&nbsp;three observation times, 64, 128, and 256 frames.</p>

opencc-by-4.0Sep 2021View details →
zenodo44/100

X-Ray Diffraction data from Membrane transport protein AcrB, V612F mutant with bound minocycline, source of 9FHC structure

<p>Crystals were grown of the membrane transport protein AcrB, V612F mutant, with bound minocycline.&nbsp;</p> <p>X-ray diffraction data of this upload: 400 frames of 0.5&deg; width were collected on 2007-04-30 at the X06SA beamline of Swiss Light Source at Paul-Scherrer-Institute (Switzerland).</p> <p>The data can be processed with XDS; XDS.INP is provided as part of the upload.</p> <p>The data are the basis of the PDB 9FHC structure.</p>

opencc-by-4.0Jun 2024View details →
zenodo36/100

Data for "Ceramide-1-phosphate transfer protein enhances lipid transport by disrupting hydrophobic lipid–membrane contacts"

<p>Data for&nbsp;&quot;Ceramide-1-phosphate transfer protein enhances lipid transport by disrupting hydrophobic lipid&ndash;membrane contacts&quot; by Julia R Rogers and Phillip L Geissler (<a href="https://doi.org/10.1371/journal.pcbi.1010992">Rogers, J. R.; Geissler, P. L.&nbsp;<em>PLoS Comput. Biol.</em>&nbsp;<strong>2023</strong>,&nbsp;<em>19</em>, e1010992</a>;&nbsp;bioRxiv DOI: https://doi.org/10.1101/2022.09.10.507427).&nbsp;All input coordinates, topologies, and parameter files in addition to equilibrium simulation trajectories and analysis results&nbsp;are provided.</p>

opencc-by-4.0Sep 2022View details →
dryad32/100

Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress

<p>The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum (ER) that is gated by the nuclear pore complex. It is unknown whether proteins of the INM and ER are degraded through shared or distinct pathways in mammalian cells. We applied dynamic proteomics to profile protein half-lives and report that INM and ER residents turn over at similar rates, indicating that the INM's unique topology is not a barrier to turnover. Using a microscopy approach, we observed that the proteasome can degrade INM proteins in situ. However, we also uncovered evidence for selective, vesicular transport-mediated turnover of a single INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared from the INM by a mechanism that requires emerin's LEM domain to mediate vesicular trafficking to lysosomes. This work demonstrates that the INM can be dynamically remodeled in response to environmental inputs.</p>

opencc-zeroOct 2020View details →
dryad32/100

Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress

Open the record for dataset details and reuse information.

publicOct 2019View details →
geo24/100

Missense mutations in linker-2 of KLF1 impair expression of membrane transporters and cytoskeletal proteins to cause hemolysis

GEO Series GSE240553. Mus musculus. 18 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenJul 2024View details →
geo24/100

Mutations in linker-2 of KLF1 impair expression of membrane transporters and cytoskeletal proteins causing hemolysis

GEO Series GSE94351. Mus musculus. 13 samples. Type: Expression profiling by high throughput sequencing; Genome binding/occupancy profiling by high throughput sequencing.

openGEO-OpenJul 2024View details →

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