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289 results for “phosphatases”
North Temperate Lakes LTER: Alkaline Phosphatase Activity in Lake Mendota 2000 - 2001
Parameters characterizing the alkaline phosphatase activity of Lake Mendota. Samples were collected at one station in the deepest part of each lake from an integrated sample of the epilimnion. Sampling Frequency: fortnightly during ice-free season - every 6 weeks during ice-covered season Number of sites: 1
SH2-containing-inositol-5-phosphatases (INPP5D); A Target Enabling Package
<p>SH2-containing-inositol-5-phosphatases (SHIP1 and SHIP2, coded for by genes <em>INPP5D</em> and <em>INPPL1</em>, respectively) dephosphorylate phosphatidylinositol-3,4,5-trisphosphate (PI(3,4,5)P<sub>3</sub>) to produce phosphatidylinositol-3,4-bisphosphate (PI(3,4)P<sub>2</sub>). This is an important part of the PI3K/AKT/mTOR signalling pathway. The SHIPs have been linked to a range of conditions, including cancer, diabetes, hypertension, and graft versus host disease. A link has also been demonstrated by GWAS between a non-coding mutation in the <em>INPP5D</em> (SHIP1) gene and increased risk of late-onset Alzheimer’s disease. The role of SHIP1 in Alzheimer’s disease is believed to be mediated through inflammatory processes such as the regulation of microglia and cytokine release. The distinction between the effects of SHIP1 and SHIP2 on these processes is not fully understood. In this TEP we present an apo structure of the phosphatase and C2 domains of SHIP1 and a structure with a magnesium ion and a phosphate ion bound to the active site. We also present 91 fragment bound structures that may act as starting points for the modulation of SHIP1. We are also able to crystallise an equivalent construct of SHIP2 and purify a range of other inositol-5-phosphatases to serve as a selectivity panel for the development of specific compounds. An assay has also been developed.</p>
Western blots supporting "Phosphatases modified by LH signaling in ovarian follicles: testing their role in regulating the NPR2 guanylyl cyclase"
<p>Western blots used to generate figures 2-6 and S4 of the publication, Egbert JR, Silbern I, Uliasz TF, Lowther KM, Yee S-P, Urlaub H, and Jaffe LA. 2023. Phosphatases modified by LH signaling in ovarian follicles: testing their role in regulating the NPR2 guanylyl cyclase. <i>Biology of Reproduction</i>, ioad130. <a href="https://doi.org/10.1093/biolre/ioad130">https://doi.org/10.1093/biolre/ioad130</a></p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) mutant G258A (PDB entry 7AAL)
<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289), mutant G258A.</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.9999 Å wavelength and a PILATUS3 6M detector. The dataset consists of 2400 images (0.15 degree oscillation per image). Crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.19 Å, b=73.02 Å, c=205.25 Å. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 2.92 Å in the direction b* and the highest limits were 1.97 Å and 2.09 in the directions a* and c*, respectively.</p> <p> </p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code 7AAL:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aal">https://www.ebi.ac.uk/pdbe/entry/pdb/7aal</a></p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) bound to the C-terminal homology (CTH) segment of the phosphatase LYP (PTPN22) (PDB entry 7AAM)
<p>Diffraction images of a crystal of the F-BAR domain of human PSTPIP1 (residues 1-289, Uniprot reference O43586-1) in complex with the CTH of LYP (residues 787-807, Uniprot Q9Y2R2-1).</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 Å wavelength and a PILATUS3 6M detector. The dataset consists of 3 groups, each containing of 1800 images (0.1 degree oscillation per image), collected at three different positions of the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.0 Å, b=72.0 Å, c=205.0 Å. The asymmetric unit contains an homodimer of the F-BAR domain bound to a LYP-CTH (~53% solvent content), which is the biological complex.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 4.05 Å in the direction b* and the highest limits were 2.11 Å and 2.10 in the directions a* and c*, respectively.</p> <p> </p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code <strong>7AAM</strong>:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aam">https://www.ebi.ac.uk/pdbe/entry/pdb/7aam</a></p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) (PDB entry 7AAN)
<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289).</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 Å wavelength and a PILATUS3 6M detector. The dataset consists of 3600 images (0.15 degree oscillation per image) that were collected: 2400 at one position and the other 1200 at a second site in the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.3 Å, b=71.9 Å, c=204.6 Å. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 4.32 Å in the direction b* and the highest limits were 2.12 Å and 2.17 in the directions a* and c*, respectively.</p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code <strong>7AAN</strong>:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aan">https://www.ebi.ac.uk/pdbe/entry/pdb/7aan</a></p>
Data files for manuscript "Prenatal phenotype of PNKP-related primary microcephaly associated with variants in the FHA and Phosphatase domain"
<p>#2021-08-26<br> #Summary<br> This ZIP-file contains the Excel files used for the clinical and variant analyses of the PNKP protein/gene for the manuscript "Prenatal phenotype of PNKP-related primary microcephaly associated with variants in the FHA and Phosphatase domain".</p> <p>#Folder structure<br> ./ (parent directory containing this README file and all subfolders)<br> ./Clinical/ (contains an Excel sheet with complete clinical data of 4 affected individuals)<br> ./Variants/ (contains an Excel sheet with all variant annotation and domain information used in 6 sheets)</p> <p>#Files and checksums<br> 4B5BE914E77EB6511DF3DB94C6918E45 ./Clinical/FileS2_PNKP_Clinical.xlsx<br> 0228C6EF543D597C1C800B8D78E3097D ./Variants/FileS3_PNKP_Variants.xlsx</p>
AlphaFold-Multimer (v3) model of a complex of Protein Phosphatase 2A catalytic subunit (PP2A/C), PP2A scaffold subunit (PP2A/A), the B55alpha substrate binding subunit, and FAM122A, a PP2A inhibitor protein.
<p>AlphaFold-Multimer (v3) model structure of a complex of Protein Phosphatase 2A catalytic subunit (PP2A/C), PP2A scaffold subunit (PP2A/A), the B55alpha substrate binding subunit, and FAM122A, a PP2A inhibitor protein. The protein sequences were obtained from UniProt:</p> <p>P67775 · PP2AA_HUMAN</p> <p>P30153 · 2AAA_HUMAN</p> <p>P63151 · 2ABA_HUMAN</p> <p>Q96E09 · PBIR1_HUMAN</p> <p>Coordinates are in mmCIF format. A PyMOL session file is included.</p> <p>Modeling was performed with AlphaFold-Multimer v3, downloaded from DeepMind's github. Structure prediction was performed without templates. The model was relaxed with Amber.</p> <p>FAM122A binds using a short linear motif (SLIM) (residues 84-89) first identified in RBL1 (p107) (Fowle et al., eLife, <a href="https://doi.org/10.7554/eLife.63181">https://doi.org/10.7554/eLife.63181</a> in the form of a short alpha helix (residues 84-92). This is followed by a long alpha helix (residues 96-122) which blocks access to the active site of the catalytic subunit. There are further contacts of FAM122A (residues 150-170) with one of the beta sheets of the B55alpha beta propeller domain. FAM122A regulates PP2A activity during the cell cycle.</p> <p> </p>
Supporting Data for "Allostery in Protein Tyrosine Phosphatases is Enabled by Divergent Dynamics"
<p>Molecular dynamics topologies (.prmtop), initial coordinates (.inpcrd), and trajectories (.nc) associated with the preprint: https://doi.org/10.1101/2023.07.23.550226. Tarballs are included for each of the six systems, named by the PDB ID for the starting structure and state (ligand/apo). The four replicates of 155ns are included in each tarball in AMBER's netcdf format (.nc). All trajectories have been stripped of solvent and ions and are autoimaged. Input files and an example script for running simulations in AMBER20 are provided (infiles.tar.gz) as well as the topologies and coordinates for the solvated systems (solvated_topologies.tar.gz).</p>
Data from: The pathogenic E139D mutation stabilizes a non-canonical active state of the multi-domain phosphatase SHP2
Open the record for dataset details and reuse information.
Data from: Deep mutational scanning of the multi-domain phosphatase SHP2 reveals mechanisms of regulation and pathogenicity
Open the record for dataset details and reuse information.
SIRAH-CoV2 initiative: Apo ADP ribose phosphatase of NSP3 from SARS CoV-2 (PDB id: 6W02)
<p>This dataset contains the trajectory of a 10 microseconds-long coarse-grained molecular dynamics simulation of SARS-CoV2 ADP ribose phosphatase of NSP3 from SARS CoV-2 in its APO form (PDB id: 6W02, Bioassembly 1). Simulations have been performed using the SIRAH force field running with the Amber18 package at the Uruguayan National Center for Supercomputing (ClusterUY) under the conditions reported in <a href="https://pubs.acs.org/doi/10.1021/acs.jctc.9b00006">Machado et al. JCTC 2019</a>, adding 150 mM NaCl according to <a href="https://pubs.acs.org/doi/10.1021/acs.jctc.9b00953">Machado & Pantano JCTC 2020</a>. </p> <p>The file 6W02_SIRAHcg_rawdata.tar contains all the raw information required to visualize (on VMD), analyze, backmap, and eventually continue the simulations using Amber18 or higher. Step-By-Step tutorials for running, visualizing, and analyzing CG trajectories using <a href="https://academic.oup.com/bioinformatics/article/32/10/1568/1743152">SirahTools</a> can be found at www.sirahff.com.</p> <p>Additionally, the file 6W02_SIRAHcg_10us_prot.tar contains only the protein coordinates, while 6W02_SIRAHcg_10us_prot_skip10ns.tar contains one frame every 10ns.</p> <p>To take a quick look at the trajectory:</p> <p>1- Untar the file 6W02_SIRAHcg_10us_prot_skip10ns.tar</p> <p>2- Open the trajectory on VMD using the command line:</p> <p>vmd 6W02_SIRAHcg_prot.prmtop 6W02_SIRAHcg_prot.ncrst 6W02_SIRAHcg_prot_10us_skip10ns.nc -e sirah_vmdtk.tcl</p> <p>Note that you can use normal VMD drawing methods as vdw, licorice, etc., and coloring by restype, element, name, etc. </p> <p>This dataset is part of the SIRAH-CoV2 initiative.</p> <p>For further details, please contact Exequiel Barrera (ebarrera@pasteur.edu.uy) or Sergio Pantano (spantano@pasteur.edu.uy).</p>
Tomato Protein Phosphatase 2C (SlPP2C3) influences fruit ripening onset and fruit glossiness
<p><span>Abscisic acid (ABA) plays a vital role in coordinating physiological processes during fresh fruit ripening. ABA can bind to ABA receptors which interacts and inhibits their co-receptors type 2C phosphatases (PP2Cs). However, the dissected mechanism of PP2C during fruit ripening is unclear. In this study, we identify the role of SlPP2C3, a tomato type 2C phosphatase, as a negative regulator of ABA signaling and fruit ripening. SlPP2C3 selectively interacted with monomeric ABA receptors and SlSnRK2.8 kinase in both yeast and tobacco epidermal cells. Expressions of <i>SlPP2C3 </i>were observed in all tissues, and it negatively correlated with the fruit ripening which was induced by exogenous ABA. Tomato plants with suppressed <i>SlPP2C3</i> expression exhibited enhanced sensitivity to ABA, while <i>SlPP2C3</i> over-expressed plants were less sensitive to ABA. Meaningfully, lack of <i>SlPP2C3</i> expression causes the acceleration of fruit ripening onset via the alternation of ABA signaling activity, and the fruit gloss is affected by the changes of outer epidermis structure. RNA-seq analysis found significant different expression of cuticle-related genes in pericarp between wild-type and <i>SlPP2C3</i> suppressed lines. Taken together, our finding demonstrate that SlPP2C3 plays an important role in the regulation of fruit ripening and fruit appearance quality in tomato. </span></p>
Improving the understanding of phosphate fertilization in soil P content, acid phosphatase and production of sugarcane
<p>The sugarcane crop is grown in large areas and has a productive chain of billions of dollars. In its chain, they are involved from sugar production to second generation hydrated alcohol. Phosphate nutrition is of great importance for culture, therefore requiring further studies. We sought to evaluate sources and doses of P in the absence/presence of filter cake. The first three models refer to P<sub>2</sub>O<sub>5</sub> sources and doses in the absence of the filter cake and the last three models refer to P<sub>2</sub>O<sub>5</sub> sources and doses in the presence of the filter cake (7.5 Mg ha<sup>-1</sup>, in dry weight). As a statistical basis, we used average, median, maximum, minimum and standard deviation data for the variables evaluated.</p>
Autoimmunity-associated allele of tyrosine phosphatase gene PTPN22 enhances anti-viral immunity
<p>The 1858C>T allele of the tyrosine phosphatase <em>PTPN22</em> is present in 5-10% of the North American population and is strongly associated with numerous autoimmune diseases. Although research has been done to define how this allele potentiates autoimmunity, the influence <em>PTPN22</em> and its pro-autoimmune allele have in anti-viral immunity remains poorly defined. Here, we use single-cell RNA-sequencing and functional studies to interrogate the impact of this pro-autoimmune allele on anti-viral immunity during Lymphocytic Choriomeningitis Virus clone 13 (LCMV-cl13) infection. Mice homozygous for this allele (PEP-619WW) clear the LCMV-cl13 virus whereas wildtype (PEP-WT) mice cannot. This is associated with enhanced anti-viral CD4 T cell responses and a more immunostimulatory CD8a<sup>-</sup> cDC phenotype. Adoptive transfer studies demonstrated that PEP-619WW enhanced anti-viral CD4 T cell function through virus-specific CD4 T cell-intrinsic and extrinsic mechanisms. Taken together, our data show that the pro-autoimmune allele of <em>Ptpn22</em> drives a beneficial anti-viral immune response thereby preventing what is normally a chronic virus infection.</p>
The Effect of Bone Graft Substitute in Healing Fractures with Bone Defects Through Examination of Alkaline Phosphatase and Radiology in the Murine Model (Rattus norvegicus) Wistar strain
<p>Raw data for manuscript with the title <strong>The Effect of Bone Graft Substitute in Healing Fractures with Bone Defects Through Examination of Alkaline Phosphatase and Radiology in the Murine Model (<em>Rattus norvegicus</em>) Wistar strain </strong></p>
Sensitization of FOLFOX-resistant colorectal cancer cells via the modulation of a novel pathway involving protein phosphatase 2A
<p>The treatment of colorectal cancer (CRC) with FOLFOX shows some efficacy, but these tumors quickly develop resistance to this treatment. We have observed an increased phosphorylation of AKT1/mTOR/4EBP1 and levels of p21 in FOLFOX-resistant CRC cells. We have identified a small molecule, NSC49L, that stimulates protein phosphatase 2A (PP2A) activity, downregulates the AKT1/mTOR/4EBP1-axis, and inhibits p21 translation. We have provided evidence that NSC49L- and TRAIL-mediated sensitization is synergistically induced in p21-knockdown CRC cells, which is reversed in p21-overexpressing cells. p21 binds with procaspase 3 and prevents activation of caspase 3. We have shown that TRAIL induces apoptosis through the activation of caspase 3 by NSC49L-mediated downregulation of p21 translation, and thereby cleavage of procaspase 3 into caspase 3. NSC49L does not affect global protein synthesis. These studies provide a mechanistic understanding of NSC49L as a PP2A agonist, and how its combination with TRAIL sensitizes FOLFOX-resistant CRC cells.</p>
Alpha-synuclein aggregates are phosphatase resistant
<p>Data and uncut images from manuscript.</p>
Conduction in the Right and Left Ventricle is Differentially Regulated by Protein Kinases and Phosphatases: Implications for Arrhythmogenesis
<p>Movies of paced activation and of arrhythmia acquired during perfusion of isolated rabbit hearts with CaMKII inhibitor KN93 or PKA inhibitor H89</p>
Figure 4 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'
<p><strong>Raw data for Figure 4 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan</strong></p> <p><strong>Figure 4A - sequences of the chimaeras.txt:</strong></p> <p>Aminoacid sequences of the chimaeric proteins used in the assays</p> <p> </p> <p><strong>Figure 4B.tif:</strong><br> Coomassie stained gel of recombinant PPM phosphatases shown in Fig.4B. Last lane containing phosphatase PPM1A not shown in figure.</p> <p> </p> <p><strong>Figure 4CD Malachite.xlsx:</strong></p> <p>Numerical data for the charts shown in Fig.4C and Fig.4D.</p> <p> </p> <p><strong>Figure 4E 700.tif:</strong><br> Top to bottom:</p> <ol> <li>Total LRRK2 blot shown in Fig.4E</li> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.4E</li> <li>GAPDH loading controls for blots in Fig.4E</li> <li>HA blot for Rab8A shown in Fig.4E</li> </ol> <p> </p> <p><strong>Figure 4E 800.tif:</strong></p> <ol> <li>Phospho-Rab8A Thr72 blot shown in Fig.4E</li> </ol> <p> </p> <p><strong>Figure 4F 700.tif:</strong><br> Top to bottom:</p> <ol> <li>Total LRRK2 blot shown in Fig.4E</li> <li>HA blot for PPM phosphatases (PPM constructs). HA blot was not used for Fig.4F. Membrane was reblotted, shown in <strong>tif file Figure 4F 700-2</strong></li> <li>GAPDH loading controls for blots in Fig.4F</li> <li>HA blot for Rab10. HA blot was not used for Fig.4F. Membrane was reblotted, shown in <strong>tif file Figure 4F 700-2</strong></li> </ol> <p> </p> <p><strong>Figure 4F 700-2.tif:</strong><br> Top to bottom:</p> <ol> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.4E</li> <li>GAPDH loading controls for blots in Fig.4F</li> <li>HA blot for Rab8A shown in Fig.4E</li> </ol> <p> </p> <p><strong>Figure 4F 800.tif:</strong></p> <ol> <li>Phospho-Rab10 Thr73 blot shown in Fig.4F</li> </ol>
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
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DANDI Archive for NWB datasets
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International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.