Results 161 to 170 of about 2,358 (202)
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Analytical Biochemistry, 1995
Glycosylphosphatidylinositol (GPI) membrane anchors are synthesized in the endoplasmic reticulum of eukaryotic cells. Synthesis of the core GPI structure is achieved by the sequential transfer of monosaccharides and phosphoethanolamine to phosphatidylinositol. The assembly process can be reproduced in vitro using membrane preparations supplemented with
Bütikofer P, Boschung M, Menon AK
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Glycosylphosphatidylinositol (GPI) membrane anchors are synthesized in the endoplasmic reticulum of eukaryotic cells. Synthesis of the core GPI structure is achieved by the sequential transfer of monosaccharides and phosphoethanolamine to phosphatidylinositol. The assembly process can be reproduced in vitro using membrane preparations supplemented with
Bütikofer P, Boschung M, Menon AK
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Structure, biosynthesis, and function of glycosylphosphatidylinositols
Biochemistry, 1990The last few years have witnessed an explosion in our knowledge of GPI membrane anchors and related glycolipids and molecules where structure details are available, as illustrated in Figure 2. There is now sufficient information on a handful of these molecules to allow a detailed comparison of their chemical structures.
J R, Thomas, R A, Dwek, T W, Rademacher
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Semisynthesis of a Glycosylphosphatidylinositol‐Anchored Prion Protein
Angewandte Chemie International Edition, 2008Pinning down the role of the anchor: The chemical synthesis of a cysteine-modified glycosylphosphatidylinositol (GPI) anchor provides access to homogeneous GPI-anchored prion protein through expressed protein ligation (see scheme). By this method, it should be possible to investigate the influence of the complex posttranslational GPI modification on ...
Becker Christian. F. W. +5 more
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Synthetic Glycosylphosphatidylinositol as Tools for Glycoparasitology Research
OMICS: A Journal of Integrative Biology, 2010Abstract Carbohydrate–protein interactions are involved in various intracellular functions and play an essential role in biological system, particularly at the level of cell–cell recognition, cell adhesion, and cell signaling processes.
Azzouz, N., Kamena, F., Seeberger, P.
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Anchoring of Glycosylphosphatidylinositol–Proteins to Liposomes
2003Publisher Summary This chapter presents the anchoring of glycosylphosphatidylinositol (GPI) proteins to liposomes. In vivo , GPI-anchored proteins concentrate exclusively into the exoleaflet of eukaryotic cell plasma membranes, together with cholesterol and most of the glycolipids.
Olivier, Nosjean, Bernard, Roux
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Methods in enzymology, 1995
Cleavage by the GPI-PLD provides definitive evidence of a minimal GPI structure: glucosamine-phosphatidylinositol. Unlike the case for PI-PLC, cleavage by the GPI-PLD is unaffected by acylation of the inositol ring. Thus the GPI-PLD provides an excellent simple enzymatic tool for analyzing the basic core structure of GPI anchors.
M A, Deeg, M A, Davitz
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Cleavage by the GPI-PLD provides definitive evidence of a minimal GPI structure: glucosamine-phosphatidylinositol. Unlike the case for PI-PLC, cleavage by the GPI-PLD is unaffected by acylation of the inositol ring. Thus the GPI-PLD provides an excellent simple enzymatic tool for analyzing the basic core structure of GPI anchors.
M A, Deeg, M A, Davitz
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1995
Publisher Summary This chapter discusses the use of the enzyme glycosylphosphatidylinositol–phospholipase D (GPI-PLD) as a tool for structural analysis of GPI-anchored proteins. The GPI–PLD is a phospholipase D present in all mammalian plasma.
Mark A. Deeg, Michael A. Davitz
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Publisher Summary This chapter discusses the use of the enzyme glycosylphosphatidylinositol–phospholipase D (GPI-PLD) as a tool for structural analysis of GPI-anchored proteins. The GPI–PLD is a phospholipase D present in all mammalian plasma.
Mark A. Deeg, Michael A. Davitz
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Insertion of a Glycosylphosphatidylinositol-Anchored Enzyme into Liposomes
Journal of Membrane Biology, 2004Incorporation of alkaline phosphatase (AP), a glycosylphosphatidylinositol (GPI)-anchored protein, into liposomes containing detergent, followed by detergent removal with hydrophobic resin was performed. Incorporation media were collected during different steps of detergent removal and were analyzed by flotation in sucrose gradient.
F, Ronzon +3 more
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Identification of a subgroup of glycosylphosphatidylinositol-anchored tryptases
Biochemical and Biophysical Research Communications, 2005The tryptase locus on mouse chromosome 17A3.3 contains 13 genes that encode enzymatically active serine proteases with different tissue expression profiles and substrate specificities. Mouse mast cell protease (mMCP) 6, mMCP-7, mMCP-11/protease serine member S (Prss) 34, tryptase 6/Prss33, tryptase epsilon/Prss22, implantation serine protease (Isp) 1 ...
G William, Wong, Richard L, Stevens
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