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107 results for “protein localization”
Image data of co-localization of IgG and HEV ORF2 protein in a case of hepatitis E-associated kidney disease
<p><span>Image data for a co-localization study of IgG with HEV ORF2 protein in a </span><span>de novo immune complex-mediated glomerulonephritis (GN) case in</span><span> a kidney transplant recipient </span><span>with chronic hepatitis E (Leblond and Helmchen, et al. 2024).<span> </span>Immunofluorescence images are provided for 25 glomeruli at low magnification (20x, 0.227 micron/pixel) and for 16 glomeruli at high magnification (100x, 0.0454 micron/pixel). For each example glomeruli the green channel represents IgG antibody staining with FITC, and the magenta channel represent anti-HEV ORF2 staining using Alexa Fluor 546.</span></p> <p><span>Methods: </span></p> <p><span>Mouse monoclonal antibody clone 1E6 against the HEV ORF2 protein was incubated for 1h at a dilution of 1:125 followed by a mix of Alexa Fluor 546-conjugated goat anti-mouse antibody (Invitrogen BV, A11018) and FITC-conjugated Rabbit anti-Human IgG (Gamma chain, Diagnostic Biosystem, F008) for 1hat a dilution of 1:50. Following automated staining, the slides were hand -washed in distilled H<sub>2</sub>O. Tissue was covered with Vectashield® Antifade Mounting Medium with DAPI (VectorLaboratories, H-1200), covered with a coverslip and stored at 4°C until evaluation.</span></p> <p><span>Immunofluorescence images were acquired with an upright fluorescence microscope (AxioImager.Z2 controlled by ZEN Blue software; 89 North Photofluor LM-75 light source, and Axiocam 503 mono camera; Zeiss, Jena, Germany), equipped with the following objectives: 20x (NA 0.5, Plan-NEOFLUAR), 40x (NA 1.4 oil, Plan-APOCHROMAT), and 100x (NA 1.45 oil, Plan-APOCHROMAT) objectives. This setup provides an excellent spatial resolution (nominally about 200 nm lateral resolution in our study; pixel size was 45.4 nm for 100x objective). High resolution images were taken with the 100x objective using the ApoTome.2 module with deconvolution (grid 5 lp/mm; section thickness 0.7 µm). We used Vysis Abbott Chroma filter sets (Blue: excitation (ex) 335-383 nm, emission (em) 420-470; green: ex 481-507 nm; em 521-551 nm; red: ex 534-556 nm, em 574- 606 nm). Co-localization of IgG and HEV ORF2 staining was quantified using Fiji software (Schindelin et al., 2012) and the JACoP ImageJ plug-in. </span></p>
Evaluating Changes in the Local Protein Physicochemical En-vironment induced by Molecular Dynamics Simulation
<p><span>Mutation of a single amino acid residue may significantly affect the structure and function of an entire protein. The effect of single amino acid substitutions can be assessed by examining the physicochemical environment surrounding the amino acid of interest, an emerging form of quantification of which is multidimensional tensors. However, the effect with respect to a protein variant’s inherent dynamics in tensor space is rarely assessed despite the potential importance of this form of analysis in revealing local physicochemical properties of the protein and response to mutation. Using the wild-type and 936 mutant structures of the protein domain 1pga, the present research evaluated the effects of local protein context and single amino acid substitutions on molecular dynamics simulation-derived structural distributions via the use of tensors capturing a range of biochemical properties. It was observed that the extent of simulated </span><span>physicochemical</span><span> variation local to a substituted amino acid is positively associated with local mechanical stiffness, loss of protein thermostability and decreased local hydrophobicity. In addition, it was observed that the largest tensor variation occurs in densely-packed, hydrophobic core-associated regions of protein structures. In summary, the pattern of tensor change aligns with prior knowledge about protein stability and physicochemical properties.</span></p>
Genetic modification of the bee parasite Crithidia bombi for improved visualization and protein localization
<p><em>Crithidia bombi </em>is a trypanosomatid parasite that infects several species of bumble bees (<em>Bombus</em> spp.), by adhering to their intestinal tract. <em>Crithidia bombi </em>infection impairs learning and reduces survival of workers and overwintering queens. Although there is extensive research on the ecology of this host-pathogen system, we understand far less about the mechanisms that mediate internal infection dynamics. <em>Crithidia bombi</em> infects hosts by attaching to the hindgut via the flagellum, and one previous study found that a nectar secondary compound removed the flagellum, preventing attachment. However, approaches that allow more detailed observation of parasite attachment and growth would allow us to better understand factors mediating this host-pathogen relationship. We established techniques for genetic manipulation and visualization of cultured <em>C. bombi.</em> Using constructs established for <em>Crithidia fasciculata, </em>we successfully generated <em>C. bombi </em>cells expressing ectopic fluorescent transgenes using two different selectable markers. To our knowledge, this is the first genetic modification of this species. We also introduced constructs that label the mitochondrion and nucleus of the parasite, showing that subcellular targeting signals can function across parasite species to highlight specific organelles. Finally, we visualized fluorescently tagged parasites <em>in vitro</em> in both their swimming and attached forms, and <em>in vivo </em>in bumble bee (<em>Bombus impatiens</em>) hosts. Expanding our cell and molecular toolkit for <em>C. bombi </em>will help us better understand how factors such as host diet, immune system, and physiology mediate outcomes of infection by these common parasites.</p>
SLC35A2 deficiency reduces protein levels of core 1 β-1,3-galactosyltransferase 1 (C1GalT1) and its chaperone Cosmc and affects their subcellular localization - yet unpublished supplementary data
<p>The upload contains raw data files used for the article "SLC35A2 deficiency reduces protein levels of core 1 β-1,3-galactosyltransferase 1 (C1GalT1) and its chaperone Cosmc and affects their subcellular localization".</p> <p><strong>Article abstract</strong></p> <p>Nucleotide sugar transporters (NSTs) are multitransmembrane proteins, localized in the Golgi apparatus and/or endoplasmic reticulum, which provide glycosylation enzymes with their substrates. It has been demonstrated that NSTs may form complexes with functionally related glycosyltransferases, especially in the N-glycosylation pathway. However, potential interactions of NSTs with enzymes mediating the biosynthesis of mucin-type O-glycans have not been addressed to date. Here we report that UDP-galactose transporter (UGT; SLC35A2) associates with core 1 β-1,3-galactosyltransferase 1 (C1GalT1; T-synthase). This provides the first example of an interaction between an enzyme that acts exclusively in the O-glycosylation pathway and an NST. We also found that SLC35A2 associated with the C1GalT1-specific chaperone Cosmc, and that the endogenous Cosmc was localized in both the endoplasmic reticulum and Golgi apparatus of wild-type HEK293T cells. Furthermore, in SLC35A2-deficient cells protein levels of C1GalT1 and Cosmc were decreased and their Golgi localization was less pronounced. Finally, we identified SLC35A2 as a novel molecular target for the antifungal agent itraconazole. Based on our findings we propose that NSTs may contribute to the stabilization of their interaction partners and help them to achieve target localization in the cell, most likely by facilitating their assembly into larger functional units. </p> <p>The Word document (Data description.docx) contains a description of each file.</p>
Text-fig. 9. Lusitanispermum choffatii gen. et sp. nov. seeds from the Early Cretaceous Famalicão locality (sample 025), Portugal; Synchrotron radiation X-ray tomographic microscopy (SRXTM, orthoslices). a) Longitudinal orthoslice (yz0769) through the median plane of the seed (S174345) showing expanded exotestal cells (ex, arrow head) in the hilar region and well-preserved cellular nutritive tissue with an embedded tiny embryo (asterisk markes the margin of the embryo); note well-developed mesotesta (me) on the raphal side of seed. b) Longitudinal orthoslice (yz0750) in the median plane showing detail of micropylar part of seed with well-preserved exotesta (ex) and mesotesta (me) and tiny embryo with two rudimentary cotyledons (asterisks mark the margin of the cotyledons); note numerous granular bodies in the cellular nutritive tissue that are probably the remains of protein and lipid bodies. c) Transverse orthoslice (xy0311) through seed below hilum showing the bulging exotesta (arrow heads) (S174472); note that the exotestal cells in this region have thinner walls (arrows). d) Transverse orthoslice (xy0900) through the middle of a seed showing the uneven thickening of the anticlinal walls of the exotestal cells (ex), which are thicker towards the outside and very thin towards the inside; note also mesotesta (me) and the well-preserved cellular nutritive tissue (S174472). Scale bars = 500 µm (a, d); 250 µm (b, c). in Extinct Taxa Of Exotestal Seeds Close To Austrobaileyales And Nymphaeales From The Early Cretaceous Of Portugal
Text-fig. 9. Lusitanispermum choffatii gen. et sp. nov. seeds from the Early Cretaceous Famalicão locality (sample 025), Portugal; Synchrotron radiation X-ray tomographic microscopy (SRXTM, orthoslices). a) Longitudinal orthoslice (yz0769) through the median plane of the seed (S174345) showing expanded exotestal cells (ex, arrow head) in the hilar region and well-preserved cellular nutritive tissue with an embedded tiny embryo (asterisk markes the margin of the embryo); note well-developed mesotesta (me) on the raphal side of seed. b) Longitudinal orthoslice (yz0750) in the median plane showing detail of micropylar part of seed with well-preserved exotesta (ex) and mesotesta (me) and tiny embryo with two rudimentary cotyledons (asterisks mark the margin of the cotyledons); note numerous granular bodies in the cellular nutritive tissue that are probably the remains of protein and lipid bodies. c) Transverse orthoslice (xy0311) through seed below hilum showing the bulging exotesta (arrow heads) (S174472); note that the exotestal cells in this region have thinner walls (arrows). d) Transverse orthoslice (xy0900) through the middle of a seed showing the uneven thickening of the anticlinal walls of the exotestal cells (ex), which are thicker towards the outside and very thin towards the inside; note also mesotesta (me) and the well-preserved cellular nutritive tissue (S174472). Scale bars = 500 µm (a, d); 250 µm (b, c).
Genetic modification of the bee parasite Crithidia bombi for improved visualization and protein localization
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Characterization and cellular localization of a SFT-2/Got-1- like transporter protein of Leishmania infantum
<p><strong>Abstract</strong>: Background: Visceral leishmaniasis affects approximately 12 million people worldwide. Current existing drugs cause several side effects and resistance, the identification of new therapeutic targets for the development of new drugs is necessary. The vesicular trafficking in the parasite flagellar pocket is essential for parasite survival and proliferation, but little is known about the proteins involved in the endocytic/secretory pathways. In this work, we are describing the characterization of a transporter cargo protein SFT-2/Got-1 like in <em>Leishmania infantum</em>. <strong>Material and Methods:</strong> Using bioinformatics tools, the putative Got-1 protein A4HSK3 was characterized structurally and phylogenetically. Molecular biology was used to clone and express the protein and confocal fluorescence to determine its subcellular localization. <strong>Results:</strong> The Got-1 like protein presents four alpha helix TM conserved domains (aa38-aa147) characteristics of the Got-1/SFT-2 family proteins and an important PEN-2 conserved motif LGDYXXF located in the extracellular loop. Confocal microscopy suggests that Got-1/SFT-2 like is localized in the flagellar pocket, and is partially co-localized with the <em>L. infantum</em> presenilin-like protein. Phylogenetically, the <em>Leishmania sp</em> Got-1 like is contained in a subgroup of proteins clearly detached from the other Trypanosomatidae, such as <em>T. cruzi</em> and <em>T. brucei</em>. <strong>Conclusions:</strong> Our data show the presence of an important transported proteins, and its colocalizatoin with the presenilin aspartyl protease in the flagelar pocket of the <em>L. infantum</em> open new perspectives to identify novel targets, which can be an alternative therapeutic strategy against leishmaniasis</p>
Molecular dynamics-generated ensemble dataset of ubiquitin; for "PROTHON: A Local Order Parameter-Based Method for Efficient Comparison of Protein Ensembles"
<p>The molecular dynamics-generated ensemble dataset (229Mb zip file) for ubiquitin, used in the manuscript "PROTHON: A Local Order Parameter-Based Method for Efficient Comparison of Protein Ensembles", submitted to the Journal of Chemical Information and Modeling (JCIM). The dataset consists of 6 .dcd files, and one .pdb file. </p>
Data from: Expression, subcellular localization, and mechanistic analysis of intellectual disability syndrome protein ABBA
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Protein Subcellular localization prediction data used in the article entitled "MSclassifier: Median-Supplement model-based Classification tool for automated knowledge discovery"
<p>This repository contains data used to obtain results from a 5-fold cross-validation testing of how MSclassifier and other packages accurately predict protein subcellular localization in the software article entitled "MSclassifier: median-supplement model-based classification tool for automated knowledge discovery." The data used in the software article is derived from data generated in "G. K. Acquaah-Mensah, S. M. Leach, and C. Guda, Predicting the subcellular localization of human proteins using machine learning and exploratory data analysis, Genomics Proteomics Bioinformatics, 4(2):120-133, 2006, <a href="https://doi.org/10.1016/S1672-0229(06)60023-5">https://doi.org/10.1016/S1672-0229(06)60023-5</a>"</p>
Datasets generated for the manuscript: The basement membrane regulates the cellular localization and the cytoplasmic interactome of Yes-Associated Protein (YAP) in mammary epithelial cells
<p><strong>File proteinGroups-CoIP-Yap1:</strong> Dataset of co-Immunoprecipitation followed of Yes-associated protein (YAP) followed by proteomics to identify YAP interactants.</p> <p><strong>File Gene_set_file_YAP: </strong>Gene sets used for gene set enrichment analysis.</p> <p><strong>Files enrichr_x: </strong>output of the EnrichR tool</p>
Global analysis of cell behavior and protein localization dynamics reveals region-specific functions for Shroom3 and N-cadherin during neural tube closure
<p>Failures of neural tube closure are common and serious birth defects, yet we have a poor understanding of the interaction of genetics and cell biology during neural tube closure. Additionally, mutations that cause neural tube defects (NTDs) tend to affect anterior or posterior regions of the neural tube but rarely both, indicating a regional specificity to NTD genetics. To better understand the regional specificity of cell behaviors during neural tube closure, we analyzed the dynamic localization of actin and N-cadherin via high-resolution tissue-level time-lapse microscopy during Xenopus neural tube closure. To investigate the regionality of gene function, we generated mosaic mutations in shroom3, a key regulator or neural tube closure This approach elucidates new differences between cell behaviors during cranial/anterior and spinal/posterior neural tube closure, provides mechanistic insight into the function of shroom3 and demonstrates the ability of tissue-level imaging and analysis to generate cell-biological mechanistic insights into neural tube closure.</p>
Arabidopsis SAUR63 seedling phenotypes and fluorescent fusion protein localization
<p>In plants, regulated cell expansion determines organ size and shape. Several members of the family of redundantly acting Small Auxin Up RNA (SAUR) proteins can stimulate plasma membrane (PM) H+-ATPase proton pumping activity by inhibiting PM-associated PP2C.D phosphatases, thereby increasing the PM electrochemical potential, acidifying the apoplast, and stimulating cell expansion. Similarly, Arabidopsis thaliana SAUR63 was able to increase growth of various organs, antagonize PP2C.D5 phosphatase, and increase H+-ATPase activity. This dataset includes i) measurements of seedling growth in plants with altered activity of SAUR63 and PP2C.D5; ii) data from fluorescent images to measure extracellular pH; iii) analyses of subcellular localization of SAUR63:YFP fusion protein variants in roots; and iv) SAUR63:YFP localization after transient expression in Nicotiana benthamiana leaves with perturbed plasma membrane lipid composition. These data underlie figures presented in the linked manuscript. Using a gain-of-function approach to bypass genetic redundancy, we dissected structural requirements for SAUR63 growth-promoting activity. The divergent N-terminal domain of SAUR63 has a predicted basic amphipathic α-helix, and was able to drive partial PM association. Deletion of the N-terminal domain decreased PM association of a SAUR63 fusion protein, as well as decreasing protein level and eliminating growth-promoting activity. Conversely, forced PM association restored ability to promote H+-ATPase activity and cell expansion, indicating that SAUR63 is active when PM-associated. Lipid binding assays and perturbations of PM lipid composition indicate that the N-terminal domain can interact with PM anionic lipids. Mutations in the conserved SAUR domain also reduced PM association in root cells. Thus, both the N-terminal domain and the SAUR domain may cooperatively mediate the SAUR63 PM association required to promote growth. Data is licensed by the authors for use and distribution subject to citation of the original source in accordance with the Creative Commons Attribution (CC BY) license.</p>
Determination of protein stoichiometries via dual-color colocalization with single molecule localization microscopy
<p>This entry contains the datasets for the manuscript titled as listed.</p>
Fig. 7 in Analysis of major sperm proteins in two nematode species from two classes, Enoplus brevis (Enoplea, Enoplida) and Panagrellus redivivus (Chromadorea, Rhabditida), reveals similar localization, but less homology of protein sequences than expected for Nematoda phylum
Fig. 7 Immunolocalization of MSP in E. brevis sperm. a Immature spermatozoon from male. MSP is diffusely distributed in cytoplasm and concentrated in large granules (scale bar 10 µm). b Spermatozoon recovered from male and partially activated by 10-min incubation in sea water. MSP undergoes transformation resulting in appearance of
Fig. 5 in Analysis of major sperm proteins in two nematode species from two classes, Enoplus brevis (Enoplea, Enoplida) and Panagrellus redivivus (Chromadorea, Rhabditida), reveals similar localization, but less homology of protein sequences than expected for Nematoda phylum
Fig. 5 Western blot analysis of MSP in E. brevis. a MSP has unusual mobility in gel and is found as protein with weight 36–38 kDa. Both male and female samples reveal MSP signal, because the latter include inseminated females. α-Tubulin was used as a loading control (approximate weight 55 kDa). b Peptide competition assay confirms reactivity of anti-MSP antibodies with protein band of 36–38 kDa
Fig. 2 in Analysis of major sperm proteins in two nematode species from two classes, Enoplus brevis (Enoplea, Enoplida) and Panagrellus redivivus (Chromadorea, Rhabditida), reveals similar localization, but less homology of protein sequences than expected for Nematoda phylum
Fig. 2 Western blot analysis of MSP in P. redivivus. In adult animals, MSP is detected as double band with approximate weight 15 and 16 kDa. a Both male and female samples reveal MSP signal, because the latter include mated females. α-Tubulin was used as a loading control (approximate weight 55 kDa). b Analysis of young males and females. MSP is not detected in females, because most of them are unmated. Abbreviations: m, males; f, females
Fig. 3 in Analysis of major sperm proteins in two nematode species from two classes, Enoplus brevis (Enoplea, Enoplida) and Panagrellus redivivus (Chromadorea, Rhabditida), reveals similar localization, but less homology of protein sequences than expected for Nematoda phylum
Fig. 3 Schematic representation of P. redivivus spermatozoa based on transmission electron microscopy. a Morphology of immature and mature spermatozoa. Immature spermatozoon is an unpolarized cell with nucleus devoid of nuclear envelope, mitochondria, and membranous organelles. Mature spermatozoon in female reproductive system is a bipolar cell with anterior pseudopodium and posterior main cell body containing chromatin, mitochondria, and membranous organelles that attached to cell membrane and open to the exterior via pores. Reproduced from Zograf (2014) with the permission from copyright holder (Russian Journal of Nematology). b Chain of conjugated mature spermatozoa in female reproductive system. Abbreviations: N, nucleus; mt, mitochondria; mo, membranous organelles; ch, nuclear chromatin; ps, pseudopodium; mcb, mail cell body
Fig. 1 in Analysis of major sperm proteins in two nematode species from two classes, Enoplus brevis (Enoplea, Enoplida) and Panagrellus redivivus (Chromadorea, Rhabditida), reveals similar localization, but less homology of protein sequences than expected for Nematoda phylum
Fig. 1 Phylogeny of nematodes and MSP-based sperm motility. Phylogenetic relationships within phylum Nematoda derived primarily from SSU rDNA sequence data are given according to De Ley and Blaxter (2002). Suborders of the order Rhabditida, in which representatives highly homologous MSPs are found at DNA, RNA, or protein levels, are marked by underlining. Taxa whose species used in this study are marked with asterisks. Orders Trefusi- ida, Isolaimida, Dioctophyma- tida, Muspiceida, Marimermith- ida, and Desmoscolecida are not shown in this tree
Fig. 8 in Analysis of major sperm proteins in two nematode species from two classes, Enoplus brevis (Enoplea, Enoplida) and Panagrellus redivivus (Chromadorea, Rhabditida), reveals similar localization, but less homology of protein sequences than expected for Nematoda phylum
Fig. 8 Putative MSPs those are most similar to peptide antigen. a P. redivivus MSPs aligned with peptide antigen. Protein sequences (Pan_g61.t1, Pan_g6018.t1, Pan_g6424.t1, Pan_g9068.t1, Pan_ g19433.t1, and Pan_g21178.t1) were found by Blast using peptide
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Allen Brain Atlas
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Annotated Behaviour and Observability Dataset (ABODe)
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