Relevant bibliographies by topics / Glycophosphatidylinositol

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Glycophosphatidylinositol'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 February 2022

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Journal articles on the topic "Glycophosphatidylinositol"

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PAQUETTE, CARRIE A., VILLA RAKOCHY, ALISON BUSH, and JUDITH L. VAN HOUTEN. "GLYCOPHOSPHATIDYLINOSITOL-ANCHORED PROTEINS INPARAMECIUM TETRAURELIA." Journal of Experimental Biology 204, no. 16 (2001): 2899–910. http://dx.doi.org/10.1242/jeb.204.16.2899.

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SUMMARYWe have begun to characterize the glycophosphatidylinositol (GPI)-anchored proteins of the Paramecium tetraurelia cell body surface where receptors and binding sites for attractant stimuli are found. We demonstrate here (i) that inositol-specific exogenous phospholipase C (PLC) treatment of the cell body membranes (pellicles) removes proteins with GPI anchors, (ii)that, as in P. primaurelia, there is an endogenous lipase that responds differently to PLC inhibitors compared with its response to an exogenous PLC, (iii) that salt and ethanol treatment of cells removes GPI-anchored proteins
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Coussen, Françoise, Annick Ayon, Anne Le Goff, Jacqueline Leroy, Jean Massoulié, and Suzanne Bon. "Addition of a Glycophosphatidylinositol to Acetylcholinesterase." Journal of Biological Chemistry 276, no. 30 (2001): 27881–92. http://dx.doi.org/10.1074/jbc.m010817200.

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Chen, Rui, Elizabeth I. Walter, Gregory Parker, et al. "Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation." Proceedings of the National Academy of Sciences 95, no. 16 (1998): 9512–17. http://dx.doi.org/10.1073/pnas.95.16.9512.

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The glycophosphatidylinositol (GPI) anchors of proteins expressed on human erythrocytes and nucleated cells differ with respect to acylation of an inositol hydroxyl group, a structural feature that modulates their cleavability by PI-specific phospholipase C (PI-PLC). To determine how this GPI anchor modification is regulated, the precursor and protein-associated GPIs in two K562 cell transfectants (ATCC and .48) exhibiting alternatively PI-PLC-sensitive and resistant surface proteins were analyzed and the temporal relationship between GPI protein transfer and acquisition of PI-PLC sensitivity
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SCHENKMAN, S., N. YOSHIDA, and M. CARDOSODEALMEIDA. "Glycophosphatidylinositol-anchored proteins in metacyclic trypomastigotes of Trypanosoma cruzi." Molecular and Biochemical Parasitology 29, no. 2-3 (1988): 141–51. http://dx.doi.org/10.1016/0166-6851(88)90069-2.

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Nishina, Koren A., and Surachai Supattapone. "Immunodetection of glycophosphatidylinositol-anchored proteins following treatment with phospholipase C." Analytical Biochemistry 363, no. 2 (2007): 318–20. http://dx.doi.org/10.1016/j.ab.2007.01.032.

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Barboni, E., B. P. Rivero, A. J. George, et al. "The glycophosphatidylinositol anchor affects the conformation of Thy-1 protein." Journal of Cell Science 108, no. 2 (1995): 487–97. http://dx.doi.org/10.1242/jcs.108.2.487.

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Thy-1 has the structure of a single variable-type immunoglobulin domain anchored to the external face of the plasma membrane via a glycophosphatidylinositol moiety. When the lipid is removed from this anchor by either phospholipase C or D, the reactivity of the delipidated Thy-1 for a range of antibodies, including those known to be determined by amino acid residues, is impaired. We have investigated in detail the effect of delipidation on the reaction with the OX7 monoclonal antibody, determined by the allelic variant residue Arg 89. Analysis of the kinetics of OX7 binding shows that delipida
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Balsamo, Janne, and Jack Lilien. "The retina cell-surface N-acetylgalactosaminylphosphotransferase is anchored by a glycophosphatidylinositol." Biochemistry 32, no. 32 (1993): 8246–50. http://dx.doi.org/10.1021/bi00083a027.

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Kovač, Valerija, and Vladka Čurin Šerbec. "Prion Proteins Without the Glycophosphatidylinositol Anchor: Potential Biomarkers in Neurodegenerative Diseases." Biomarker Insights 13 (January 1, 2018): 117727191875664. http://dx.doi.org/10.1177/1177271918756648.

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Prion protein (PrP) is a biomolecule that is involved in neuronal signaling, myelinization, and the development of neurodegenerative diseases. In the cell, PrP is shed by the ADAM10 protease. This process generates PrP molecules that lack glycophosphatidylinositol anchor, and these molecules incorporate into toxic aggregates and neutralize toxic oligomers. Due to this dual role, these molecules are important biomarkers for neurodegenerative diseases. In this review, we present shed PrP as a potential biomarker, with a focus on PrP226*, which may be the main biomarker for predicting neurodegene
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Khodagholi, Fariba, Razieh Yazdanparast, and Akram Sadeghirizi. "The Glycophosphatidylinositol Anchor Oppositely Affects Unfolding and Refolding of Alkaline Phosphatase." Journal of Biomolecular Structure and Dynamics 25, no. 2 (2007): 189–94. http://dx.doi.org/10.1080/07391102.2007.10507168.

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Kristoffersen, E. K., K. O. Haram, B. Edvardsen, P. Ernst, and L. Bjørge. "Placental Expression of Glycophosphatidylinositol (GPI)-anchored Proteins in Paroxysmal Nocturnal Haemoglobinuria." Scandinavian Journal of Immunology 64, no. 2 (2006): 140–44. http://dx.doi.org/10.1111/j.1365-3083.2006.01777.x.

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Dissertations / Theses on the topic "Glycophosphatidylinositol"

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Nicholson, Thomas Barrett. "Molecular dissection of the functional specificity of glycophosphatidylinositol anchors." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=18463.

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Carcinoembryonic antigen (CEA) is a cell surface protein attached to the membrane by a glycophosphatidylinositol (GPI) anchor, a common modification of cell surface proteins. CEA is overexpressed in many human cancers, and plays a role in tumor progression through its ability to activate certain integrins, thereby blocking cellular differentiation, inhibiting anoikis, and disrupting normal tissue architecture. Previous work established that the CEA GPI anchor contains important and specific information directing these functions, which served as the basis for an investigation of the underlyin
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Venter, Tarryn Lee. "Characterisation of the pre-invasion glycophosphatidylinositol-anchored surface proteins of Plasmodium falciparum merozoites." Diss., University of Pretoria, 2017. http://hdl.handle.net/2263/63040.

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Plasmodium falciparum is a protozoan parasite responsible for causing the most severe form of malaria in humans. This species is responsible for over 90% of malaria mortalities which occur predominantly in Africa. An increase in drug resistant parasites in recent years is threatening the progress made against malaria and thus new antimalarial drugs and vaccines are needed to combat this disease. During the intraerythrocytic phase, merozoites egress from mature schizonts to invade new uninfected erythrocytes. Glycophosphatidylinositol (GPI) -anchored proteins cover most of the exterior s
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Zhou, Ke. "Functional characterization of GPI-anchored proteins of the SKU5/SKS gene family." Phd thesis, Université Paris Sud - Paris XI, 2013. http://tel.archives-ouvertes.fr/tel-01066888.

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ABP1 (Auxin Binding Protein1), who can bind auxin, is essential for the development of plants. It was proved to have the ability to bind auxin and transduce auxin signal into the cells. It is supposed to be localized and functions at the outer surface of plasma membrane through unknown component. In my thesis, we tried to invesitgate the interaction between ABP1 and the candidate of the unknown component, CBP1 (From maize), which is GPI-acnhored and already identified as the binding ability to synthesized C-terminus peptide of ABP1 in 2006. The orthologous of CBP1 in arabidopsis belongs to a g
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Al-Badri, Riadh Rahma Kazim. "Biological and Transcriptomic Comparison of Two Immunologically Distinct Strains of Eimeria maxima (GS and M6) and Characterization of Their Glycophosphatidylinositol (GPI) Anchored Surface Antigen Expression." Thesis, 2013. http://hdl.handle.net/10214/7432.

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Two immunologically distinct strains of poultry coccidium Eimeria maxima, Guelph (GS) and M6 strains, were investigated. Paired in vivo experiments demonstrated that GS and M6 have prepatent periods of approximately 120 h followed by peak oocyst shedding at 144 150 h post inoculation. Fecundity of E. maxima M6 (12.8×103±1.95 oocysts shed/oocyst inoculated) was approximately twice that of GS (6.9×103±3.33) when inoculated with 1×103 infective oocysts per bird. Numerous sequential observations of synchronized populations of oocysts sporulating at 26°C showed no difference in the sporulation kine
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Book chapters on the topic "Glycophosphatidylinositol"

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Robinson, P. J. "Glycophosphatidylinositol-Anchored Membrane Proteins as Coreceptors in T-Cell Activation." In Modern Trends in Human Leukemia IX. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76829-3_43.

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Caras, Ingrid W. "PROBING THE SIGNAL FOR GLYCOPHOSPHATIDYLINOSITOL ANCHOR ATTACHMENT USING DECAY ACCELERATING FACTOR AS A MODEL SYSTEM." In GPI Membrane Anchors. Elsevier, 1992. http://dx.doi.org/10.1016/b978-0-12-159390-2.50010-6.

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You might also be interested in the extended bibliographies on the topic 'Glycophosphatidylinositol' for particular source types:
Journal articles
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