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216 results for “endoplasmic reticulum”
Data_Supplemental_Tab3_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of supplemental Tab3, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original supplemental table 3 as PDF-format (PNTD-D-21-00134R2_S_T3.pdf). Related information (meta-data) are provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_ST3_M_1.txt) and three files in PDF format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_ST3_M_1-3.pdf).</p>
Data_Supplemental_Fig4_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of supplemental Fig4, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original supplemental figure 4 as PNG-format (PNTD-D-21-00134R2_SFig4.png). Corresponding raw data and subsequent data analysis obtained from RT-PCR analysis provided as four files in CSV format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF4_1_3-4_1-4.csv), all further experiment related information provided as one meta-data-file in txt format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF4_1_3-4_M_1.txt) and three meta data files in pdf format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF4_M_1-3.pdf).</p>
Data_Supplemental_Fig2_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of supplemental Fig2, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original supplemental figure 2 as PNG-format (PNTD-D-21-00134R2_SFig2.png), original supp. table S1 (31003A-179400_PNTD-D-21-00134R2_FJ_MW_SS_Echinococcus_F1_M_3.pdf) and the original supplemental file S1 (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F1_M_5.pdf).</p> <p>Corresponding raw data, subsequent data analysis and all further experiment related information (meta-data) from Western Blot analysis provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF2_2_1-26_M_1.txt) and two files in PDF format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF2_M_2-3.pdf).</p>
Data_Supplemental_Fig3_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of supplemental Fig3, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original supplemental figure 3 as PNG-format (PNTD-D-21-00134R2_SFig3.png). Corresponding raw data and subsequent data analysis obtained from RT-PCR analysis provided as two files in CSV format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF3_1_1-2_1-2.csv), all further experiment related information provided as one meta-data-file in txt format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF3_1_1-2_M_1.txt) and seven meta data files in pdf format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF3_1_1-2_M_2-4.pdf and 31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF3_M_1-3.pdf).</p>
Data_Supplemental_Fig1_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of supplemental Fig1, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p> </p> <p>The Dataset contains the original supplemental figure 1 as PNG-format (PNTD-D-21-00134R2_SFig1.png). Related information (meta-data) are provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF1_M_1.txt) and one file in PDF format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_SF1_M_2.pdf).</p>
Data_Figure4_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of Fig4, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original figure 4 as PNG-format (PNTD-D-21-00134R2_Fig4.png). Related information (meta-data) are provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_Fig4_M_1.txt).</p>
Data_Figure3_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of Fig3, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original figure 3 as PNG-format (PNTD-D-21-00134R2_Fig3.png), original supp. table S1 (31003A-179400_PNTD-D-21-00134R2_FJ_MW_SS_Echinococcus_F1_M_3.pdf) and raw blots as the original supplemental file S1 (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F1_M_4.pdf). Corresponding raw data, subsequent data analysis and all further experiment related information (meta-data) from Western Blot analysis provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F3_2_13-14_M_1.txt) and one file in PDF format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F3_M_2.pdf).</p>
Data_Figure2_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of Fig2, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p>The Dataset contains the original figure 2 as PNG-format (PNTD-D-21-00134R2_Fig2.png). Corresponding raw data and subsequent data analysis obtained from Multiplex Luminex Cytokine measurement analysis provided as one files in CSV format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F2_22_1-2_1.csv). All further experiment related information (meta-data) provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F2_22_1-2_M_1.txt) and one file in PDF format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F2_M_2.pdf).</p>
Data_Figure1_Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice
<p>Data of Fig1, “Albendazole reduces endoplasmic reticulum stress induced by Echinococcus multilocularis in mice”</p> <p> </p> <p>The Dataset contains the original figure 1 as PNG-format (PNTD-D-21-00134R2_Fig1.png), original supp. table S1 (31003A-179400_PNTD-D-21-00134R2_FJ_MW_SS_Echinococcus_F1_M_3.pdf), original supp. Figure S1 (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F1_M_4.pdf) and the original supplemental file S1 (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F1_M_5.pdf).</p> <p>Corresponding raw data, subsequent data analysis and all further experiment related information (meta-data) from Western Blot analysis provided as one file in TXT format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F1_2_1-26_M_1.txt) and one file in PDF format (31003A-179400_PNTD-D-21-00134R2 _FJ_MW_SS_Echinococcus_F1_M_2.pdf).</p>
Data_Fig1_Monitoring Changes in the Oxidizing Milieu in the Endoplasmic Reticulum of Mammalian Cells Using HyPerER
<p>Data of JB_10.21769_BioProtoc.4076_Figure 1,</p> <p>The Dataset (Original publication Doi:10.21769/BioProtoc.4076) contains the original figure as PNG-format (JB_10.21769_BioProtoc.4076_Fig1.PNG). Corresponding raw data from confocal microscopy measurements provided as two files (31003A_179400_10.21769_BioProtoc.4076_JB_Hyper_14_1/2.avi). Related information provided as one meta-data-file (31003A_179400_10.21769_BioProtoc.4076_JB_Hyper_14_M1.txt) in txt format and two files in pdf format (31003A_179400_10.21769_BioProtoc.4076_JB_Hyper_14_M2/3. pdf).</p>
Raw microscopy data from: Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers
<p>Protein folding homeostasis in the endoplasmic reticulum (ER) is regulated by a signaling network, termed the unfolded protein response (UPR). Inositol-requiring enzyme 1 (IRE1) is an ER membrane-resident kinase/RNase that mediates signal transmission in the most evolutionarily conserved branch of the UPR. Dimerization and/or higher-order oligomerization of IRE1 are thought to be important for its activation mechanism, yet the actual oligomeric states of inactive, active, and attenuated mammalian IRE1 complexes remained unknown. We developed an automated two-color single-molecule tracking approach to dissect the oligomerization of tagged endogenous human IRE1 in live cells. In contrast to previous models, our data indicate that IRE1 exists as a constitutive homodimer at baseline and assembles into small oligomers upon ER stress. We demonstrate that the formation of inactive dimers and stress-dependent oligomers is fully governed by IRE1's lumenal domain. Phosphorylation of IRE1's kinase domain occurs more slowly than oligomerization and is retained after oligomers disassemble back into dimers. Our findings suggest that assembly of IRE1 dimers into larger oligomers specifically enables trans- autophosphorylation, which in turn drives IRE1's RNase activity.</p> <p> </p>
Raw microscopy data from: Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers
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Supplementary videos for "Active flow network generates molecular transport by packets: case of the endoplasmic reticulum"
<p>Videos showing simulated motion on the active flow network for different switching timescales. In particular, compare <span class="math-tex">\(\tau_{\text{switch}} = 3 \text{ s}\)</span> to <span class="math-tex">\(\tau_{\text{switch}} = 30 \text{ ms}\)</span>. The red bubbles are proportional to the number of particles present in a node. Initially, all particles are placed in a central source node.</p>
Endoplasmic Reticulum Associated Aminopeptidase 2 (ERAP2) Is Released in the Secretome of Activated MDMs and Reduces in vitro HIV-1 Infection
<p><strong>Background:</strong> Haplotype-specific alternative splicing of the endoplasmic reticulum (ER) aminopeptidase type 2 (ERAP2) gene results in either full-length (FL, haplotype A) or alternatively spliced (AS, haplotype B) mRNA. HapA/HapA homozygous (HomoA) subjects show a reduced susceptibility to HIV-1 infection, probably secondary to the modulation of the antigen processing/presenting machinery. ERAP1 was recently shown to be secreted from the plasma membrane in response to activation; we investigated whether ERAP2 can be released as well and if the secreted form of this enzyme retains its antiviral function.</p> <p><strong>Methods:</strong> Human monocyte derived macrophages (MDMs) were differentiated from peripheral blood mononuclear cells (PBMCs) isolated from 6 HomoA healthy controls and stimulated with IFNγ and LPS. ERAP2-FL secretion was evaluated by mass spectrometry. PBMCs (14 HomoA and 16 HomoB) and CD8-depleted PBMCs (CD8<sup>−</sup>PBMCs) (4 HomoA and 4 HomoB) were <em>in vitro</em> HIV-infected in the absence/presence of recombinant human ERAP2-FL (rhERAP2) protein; p24 viral antigen quantification was used to assess viral replication. IFNγ and CD69 mRNA expression, as well as the percentage of perforin-producing CD8+ T Lymphocytes, were analyzed 3 and 7-days post <em>in vitro</em> HIV-1-infection, respectively. The effect of rhERAP2 addition in cell cultures on T cell apoptosis, proliferation, activation, and maturation was evaluated as well on 24 h-stimulated PBMCs.</p> <p><strong>Results:</strong> ERAP2 can be secreted from human MDMs in response to IFNγ/LPS stimulation. Notably, the addition of rhERAP2 to PBMC and CD8<sup>−</sup>PBMC cultures resulted in the reduction of viral replication, though these differences were statistically significant only in PBMCs (<em>p</em> < 0.05 in both HomoA and HomoB). This protective effect was associated with an increase in IFNγ and CD69 mRNA expression and in the percentage of perforin-expressing CD107<sup>+</sup>CD8<sup>+</sup> cells. RhERAP2 addition also resulted in an increase in CD8<sup>+</sup> activated lymphocyte (CD25<sup>+</sup>HLA<sup>−</sup>DRII<sup>+</sup>) and Effector Memory/Terminally differentiated CD8<sup>+</sup> T cells ratio.</p> <p><strong>Conclusions:</strong> This is the first report providing evidence for the release of ERAP2 in the secretome of immunocompetent cells. Data herein also indicate that exogenous ERAP2-FL exerts its protective function against HIV-1 infection, even in HomoB subjects who do not genetically produce it. Presumably, this defensive extracellular feature is only partially dependent on immune system modulation.</p>
Processed and additional data for our publication titled "Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers"
<p>This is an updated version of our original data archive (which can be found under the doi 10.5281/zenodo.5513025) that reflects changes we've made to the manuscript over the course of the review process and incorporates the new data we've collected since the time of the initial bioRxiv submission.</p> <p>This data archive contains all raw data EXCEPT for single-particle microscopy movies (which are deposited separately due to their size) for our paper titled "Endoplasmic reticulum stress activates human IRE1a through reversible assembly of inactive dimers into small oligomers". These raw data are stored in "non_SPT_data_final_v2.zip". Additionally, full plasmid sequences for all plasmids used in this paper are stored in GenBank format in the file "plasmid_sequences_v2.zip". Finally, this repository contains processed single-particle movies in the form of dual-color tracks from the TrackMate ImageJ plugin in XML format (file: "SPT_processed_data_and_settings_final_v2.zip").</p> <p>The processed XML tracks are organized in the same way as the raw data files in the separate repository. They are sorted into subfolders by date of acquisition first, followed by experimental conditions. To recreate the figures from the paper, follow instructions in the README.md file included with the source code repository and use the JSON settings files saved here under "analysis_settings".</p>
The effect of antidepressants on genes of endoplasmic reticulum stress in human astrocyte cell line.
<p>Many central nervous system (CNS) diseases, including major depressive disorder (MDD), are underpinned by the unfolded protein response (UPR) activated under endoplasmic reticulum (ER) stress. New, more efficient, therapeutic options for MDD are needed to avoid adverse effects and drug resistance. Therefore, the aim of the work was to determine whether UPR signalling pathway activation in astrocytes may serve as a novel target for antidepressant drugs. Among the tested antidepressants (escitalopram, amitriptyline, S-ketamine), only S-ketamine induced the expression of most ER stress-responsive genes in astrocytes.</p> <p><a href="https://doi.org/10.3390/pharmaceutics14040846">https://doi.org/10.3390/pharmaceutics14040846</a></p> <p> </p>
Data for: Plasmodesmal endoplasmic reticulum proteins regulate intercellular trafficking of Cucumber mosaic virus in Arabidopsis
<p>Plasmodesmata (PD) are plasma membrane (PM)-lined cytoplasmic nanochannels that mediate in cell-to-cell communication across the cell wall. A range of proteins are embedded in the PD PM and endoplasmic reticulum (ER) and function in regulating PD-mediated symplasmic trafficking. However, knowledge of the nature and function of the ER-embedded proteins, in the intercellular movement of non-cell-autonomous proteins, is limited. Here, we report the functional characterization of two ER luminal proteins, AtBiP1/2, and two ER integral membrane proteins, AtERdj2A/B, which are located within the PD. These PD proteins were identified as interacting proteins with <em>Cucumber mosaic virus </em>(CMV) movement protein (MP) in coimmunoprecipitation studies, using an Arabidopsis-derived plasmodesmal-enriched cell wall protein preparation (PECP). The AtBiP1/2 PD location was confirmed by transmission electron microscopy-based immunolocalization, and their AtBiP1/2 signal peptides (SPs) function in PD targeting. <em>In vitro</em>/<em>in vivo</em> pull-down assays revealed the association between AtBiP1/2 and CMV MP, mediated by AtERdj2A, through the formation of an AtBiP1/2-AtERdj2-CMV MP complex within PD. The role of this complex in CMV infection was established, as systemic infection was retarded in <em>bip1</em>/<em>bip2w</em> and <em>erdj2b</em> mutants. Our findings provide a model for a mechanism by which the CMV MP mediates in cell-to-cell trafficking of its viral ribonucleoprotein complex.</p>
Effect of Endoplasmic Reticulum Stress on Metabolic Function
ClinicalTrials.gov study NCT00771901. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Data for: Plasmodesmal endoplasmic reticulum proteins regulate intercellular trafficking of Cucumber mosaic virus in Arabidopsis
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Data from: A cross-kingdom conserved ER-phagy receptor maintains endoplasmic reticulum homeostasis during stress
<p>Eukaryotes have evolved various quality control mechanisms to promote proteostasis in the ER. Selective removal of certain ER domains via autophagy (termed as ER-phagy) has emerged as a major quality control mechanism. However, the degree to which ER-phagy is employed by other branches of ER-quality control remains largely elusive. Here, we identify a cytosolic protein, C53, that is specifically recruited to autophagosomes during ER-stress, in both plant and mammalian cells. C53 interacts with ATG8 via a distinct binding epitope, featuring a shuffled ATG8 interacting motif (sAIM). C53 senses proteotoxic stress in the ER lumen by forming a tripartite receptor complex with the ER-associated ufmylation ligase UFL1 and its membrane adaptor DDRGK1. The C53/UFL1/DDRGK1 receptor complex is activated by stalled ribosomes and induces the degradation of internal or passenger proteins in the ER. Consistently, the C53 receptor complex and ufmylation mutants are highly susceptible to ER stress. Thus, C53 forms an ancient quality control pathway that bridges selective autophagy with ribosome-associated quality control in the ER.</p>
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