Relevant bibliographies by topics / Phosphatidylinositol phosphate analogues

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Academic literature on the topic 'Phosphatidylinositol phosphate analogues'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Phosphatidylinositol phosphate analogues"

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Gregory, Mark, Meng-Xin Yin, Malcolm J. McConville, Eleanor Williams, Alex N. Bullock, Stuart J. Conway, Antony W. Burgess, Bruno Catimel, and Andrew B. Holmes. "Synthesis of Highly Water-Soluble Adamantyl Phosphoinositide Derivatives." Australian Journal of Chemistry 68, no. 4 (2015): 543. http://dx.doi.org/10.1071/ch14543.

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Phosphatidylinositol phosphates are key regulators of cell signalling pathways and membrane trafficking in eukaryotic cells, and there is a need for new chemical probes to further understand how they interact with lipid-binding proteins. Here, the synthesis of phosphatidylinositol phosphate analogues containing adamantyl carboxylic ester groups, in place of the natural lipid side chains, is described. These derivatives are considerably more soluble in water than analogues containing other lipid side chains and do not form large aggregates such as liposomes or micelles. These adamantyl analogues bind to known phosphoinositide-binding proteins with similar affinities to native ligands and will facilitate future studies on the substrate specificities of these proteins involving cocrystallisation studies with proteins.
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Ibrahim, Muktar Musa, Adamu Uzairu, Muhammad Tukur Ibrahim, and Abdullahi Bello Umar. "Modelling PIP4K2A inhibitory activity of 1,7-naphthyridine analogues using machine learning and molecular docking studies." RSC Advances 13, no. 6 (2023): 3402–15. http://dx.doi.org/10.1039/d2ra07382j.

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Smith, C. D., and K. J. Chang. "Regulation of Brain Phosphatidylinositol-4-phosphate Kinase by GTP Analogues." Journal of Biological Chemistry 264, no. 6 (February 1989): 3206–10. http://dx.doi.org/10.1016/s0021-9258(18)94052-4.

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Boronenkov, Igor V., Joost C. Loijens, Masato Umeda, and Richard A. Anderson. "Phosphoinositide Signaling Pathways in Nuclei Are Associated with Nuclear Speckles Containing Pre-mRNA Processing Factors." Molecular Biology of the Cell 9, no. 12 (December 1998): 3547–60. http://dx.doi.org/10.1091/mbc.9.12.3547.

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Phosphoinositide signal transduction pathways in nuclei use enzymes that are indistinguishable from their cytosolic analogues. We demonstrate that distinct phosphatidylinositol phosphate kinases (PIPKs), the type I and type II isoforms, are concentrated in nuclei of mammalian cells. The cytosolic and nuclear PIPKs display comparable activities toward the substrates phosphatidylinositol 4-phosphate and phosphatidylinositol 3-phosphate. Indirect immunofluorescence revealed that these kinases were associated with distinct subnuclear domains, identified as “nuclear speckles,” which also contained pre-mRNA processing factors. A pool of nuclear phosphatidylinositol bisphosphate (PIP2), the product of these kinases, was also detected at these same sites by monoclonal antibody staining. The localization of PIPKs and PIP2 to speckles is dynamic in that both PIPKs and PIP2 reorganize along with other speckle components upon inhibition of mRNA transcription. Because PIPKs have roles in the production of most phosphatidylinositol second messengers, these findings demonstrate that phosphatidylinositol signaling pathways are localized at nuclear speckles. Surprisingly, the PIPKs and PIP2 are not associated with invaginations of the nuclear envelope or any nuclear membrane structure. The putative absence of membranes at these sites suggests novel mechanisms for the generation of phosphoinositides within these structures.
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Morii, Hiroyuki, Tatsuo Okauchi, Hiroki Nomiya, Midori Ogawa, Kazumasa Fukuda, and Hatsumi Taniguchi. "Studies of inositol 1-phosphate analogues as inhibitors of the phosphatidylinositol phosphate synthase in mycobacteria." Journal of Biochemistry 153, no. 3 (December 5, 2012): 257–66. http://dx.doi.org/10.1093/jb/mvs141.

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Pratt, Clifford, Yue-Jin Liu, Ting-Yi Chu, Karin Melkonian, Burton E. Tropp, and Robert Engel. "Phosphonolipids. 3. Phosphonic acid analogues of phosphatidylinositol and related materials." Canadian Journal of Chemistry 70, no. 8 (August 1, 1992): 2135–41. http://dx.doi.org/10.1139/v92-268.

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A convergent synthesis of an isosteric phosphonic acid analogue of phosphatidylinositol has been accomplished in which a non-hydrolyzable P—C—C linkage is present in place of the normal P—O—C esteric linkage joining the phosphate and diacylglycerol portions of the molecule. The synthetic route used provides the configuration at each stereogenic center to correspond to that present in the biologically generated phospholipid. In addition, the approach provides asymmetric introduction of acyl functions, placing saturated and unsaturated acyl groups in the terminal and internal positions respectively of the backbone portion of the analogue, corresponding to that present in the biologically generated phospholipid.
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Xu, Yong, Stephanie A. Lee, Tatiana G. Kutateladze, Diego Sbrissa, Assia Shisheva, and Glenn D. Prestwich. "Chemical Synthesis and Molecular Recognition of Phosphatase-Resistant Analogues of Phosphatidylinositol-3-phosphate." Journal of the American Chemical Society 128, no. 3 (January 2006): 885–97. http://dx.doi.org/10.1021/ja0554716.

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Graves, J. D., S. C. Lucas, D. R. Alexander, and D. A. Cantrell. "Guanine nucleotide regulation of inositol phospholipid hydrolysis and CD3-antigen phosphorylation in permeabilized T lymphocytes." Biochemical Journal 265, no. 2 (January 15, 1990): 407–13. http://dx.doi.org/10.1042/bj2650407.

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A method of membrane permeabilization of T lymphocytes with the bacterial cytotoxin streptolysin O has allowed the effect of guanine nucleotide analogues on phosphatidylinositol metabolism and protein kinase C (PKC) activation to be investigated. The data demonstrate that, in permeabilized cells, phosphorylation of the gamma subunit of the CD3 antigen can be induced in response to the PKC activator phorbol 12,13-dibutyrate, the polyclonal mitogen phytohaemagglutinin (PHA) and the stimulatory guanine nucleotide analogue guanosine 5′-[gamma-thio]triphosphate (GTP[S]). Application of a pseudo-substrate inhibitor of PKC indicated that CD3gamma-chain phosphorylation induced in response to all three agonists was mediated by PKC. PHA and GTP[S] also stimulated inositol phospholipid turnover and inositol phosphate accumulation. The kinetics and concentration-dependence of PHA-induced inositol phospholipid hydrolysis correlated with PHA-induced CD3gamma phosphorylation, suggesting that PHA may regulate CD3gamma phosphorylation via diacylglycerol produced as a consequence of inositol phospholipid hydrolysis. However, there was an inconsistency in that PHA induced greater (greater than 200%) levels of inositol phospholipid turnover than did GTP[S], but much weaker (less than 50%) levels of CD3-antigen phosphorylation. There was also a discrepancy between GTP[S] effects on phosphatidylinositol turnover and PKC activation, in that the half-maximal GTP[S] concentration for inositol phosphate production and CD3gamma-chain phosphorylation was 0.75 microM and 75 microM respectively. Moreover, 10 microM-GTP[S] induced maximal inositol phosphate production, but only 10% of maximal CD3gamma-chain phosphorylation. The data are consistent with the idea that other signal-transduction pathways, in addition to those involving inositol phosphate production, exist for the regulation of PKC in T lymphocytes.
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Taylor, S. J., and J. H. Exton. "Guanine-nucleotide and hormone regulation of polyphosphoinositide phospholipase C activity of rat liver plasma membranes. Bivalent-cation and phospholipid requirements." Biochemical Journal 248, no. 3 (December 15, 1987): 791–99. http://dx.doi.org/10.1042/bj2480791.

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The effect of the GTP analogue guanosine 5′-[gamma-thio]triphosphate (GTP[S]) on the polyphosphoinositide phospholipase C (PLC) of rat liver was examined by using exogenous [3H]phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]. GTP[S] stimulated the membrane-bound PLC up to 20-fold, with a half-maximal effect at approx. 100 nM. Stimulation was also observed with guanosine 5′-[beta gamma-imido]triphosphate, but not with adenosine 5′-[gamma-thio]triphosphate, and was inhibited by guanosine 5′-[beta-thio]diphosphate. Membrane-bound PLC was entirely Ca2+-dependent, and GTP[S] produced both a decrease in the Ca2+ requirement and an increase in activity at saturating [Ca2+]. The stimulatory action of GTP[S] required millimolar Mg2+. [8-arginine]Vasopressin (100 nM) stimulated the PLC activity approx. 2-fold in the presence of 10 nM-GTP[S], but had no effect in the absence of GTP[S] or at 1 microM-GTP[S]. The hydrolysis of PtdIns(4,5)P2 by membrane-bound PLC was increased when the substrate was mixed with phosphatidylethanolamine, phosphatidylcholine or various combinations of these with phosphatidylserine. With PtdIns(4,5)P2, alone or mixed with phosphatidylcholine, GTP[S] evoked little or no stimulation of the PLC activity. However, maximal stimulation by GTP[S] was observed in the presence of a 2-fold molar excess of phosphatidylserine or various combinations of phosphatidylethanolamine and phosphatidylserine. Hydrolysis of [3H]phosphatidylinositol 4-phosphate by membrane-bound PLC was also increased by GTP[S]. However, [3H]phosphatidylinositol was a poor substrate, and its hydrolysis was barely affected by GTP[S]. Cytosolic PtdIns(4,5)P2-PLC exhibited a Ca2+-dependence similar to that of the membrane-bound activity, but was unaffected by GTP[S]. It is concluded that rat liver plasma membranes possess a Ca2+-dependent polyphosphoinositide PLC that is activated by hormones and GTP analogues, depending on the Mg2+ concentration and phospholipid environment. It is proposed that GTP analogues and hormones, acting through a guanine nucleotide-binding protein, activate the enzyme mainly by lowering its Ca2+ requirement.
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Lobasso, Simona, Patrizia Lopalco, Roberto Angelini, Rita Vitale, Harald Huber, Volker Müller, and Angela Corcelli. "Coupled TLC and MALDI-TOF/MS Analyses of the Lipid Extract of the Hyperthermophilic ArchaeonPyrococcus furiosus." Archaea 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/957852.

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The lipidome of the marine hyperthermophilic archaeonPyrococcus furiosuswas studied by means of combined thin-layer chromatography and MALDI-TOF/MS analyses of the total lipid extract. 80–90% of the major polar lipids were represented by archaeol lipids (diethers) and the remaining part by caldarchaeol lipids (tetraethers). The direct analysis of lipids on chromatography plate showed the presence of the diphytanylglycerol analogues of phosphatidylinositol and phosphatidylglycerol, theN-acetylglucosamine-diphytanylglycerol phosphate plus some caldarchaeol lipids different from those previously described. In addition, evidence for the presence of the dimeric ether lipid cardiolipin is reported, suggesting that cardiolipins are ubiquitous in archaea.
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Dissertations / Theses on the topic "Phosphatidylinositol phosphate analogues"

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ORSATO, ALEXANDRE. "Studies on tumor drug targeting." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2011. http://hdl.handle.net/10281/19200.

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Tumor drug targeting is one of the most promising therapeutic strategies in oncology. The aim of this PhD work was the study of the essential features required for the assembly of tumor targeting conjugates.This work was focused on the deveploment of ligands for the GRP receptor that should function as carrier molecules for the targeting of tumor cells overexpressing this receptor. For this purpose, non-peptide GRP mimetics were designed, using a computer-based drug design technique, synthesized and tested. Two analogue compounds based on a bicyclic scaffold exerted an antagonist behaviour on the GRP receptor. Synthetic studies have been performed to optimize their production as well as biological tests to determine their potential as carrier molecules. Apart from the targeting moiety, we also studied the antineoplastic part of tumor targeting conjugates. Akt is a proto-oncogenic kinase that has been associated to cancer development. Therefore, the Akt inhibitory activity of phosphatidylinositol phosphate analogues was exploited. A small library of iminosugar-based phosphatidylinositol phosphate analogues was designed and synthesized. During the biological evaluation, target compounds displayed low to moderate inhibitory activity for Akt, which suggests their feasibility for the development of new and more potent Akt inhibitors.
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Book chapters on the topic "Phosphatidylinositol phosphate analogues"

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Bruzik, Karol S., Gialih Lin, and Ming-Daw Tsai. "Phosphorothioate Analogues of Phosphatidylinositol and Inositol 1,2-Cyclic Phosphate." In ACS Symposium Series, 172–85. Washington, DC: American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0463.ch013.

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Schmidt, M., G. Vereb, M. Varsányi, D. Klix, C. E. Dreefs, and L. M. G. Heilmeyer. "Renaturation of Phosphatidylinositol 4- and Phosphatidylinositol 4-Phosphate 5′-Kinases Following Polyacrylamide Gelelectrophoresis in Presence of SDS. Studies on their Substrate Binding Requirements Using Synthetic Substrate Analogues." In Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling, 197–200. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78247-3_24.

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Conference papers on the topic "Phosphatidylinositol phosphate analogues"

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de Chaffov de Courcelles, D., F. De Clerck, and P. Roevens. "EVALUATION OF THE PROPOSED FUNCTIONS OF PROTEIN KINASE C IN PLATELET SIGNAL TRANSDUCTION BY THE USE OF A DIACYLGLYCEROL KINASE INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644632.

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Protein kinase C is suggested to play a major role in propagation as well as in termination of excitatory signal transduction in the platelet. Most of its properties were discovered by the use of synthetic diacylglycerol analogs or phorbol esters that directly stimulate protein kinase C. It is, however, unknown to what extent activation of the protein kinase C by these exogenously added compounds can be compared to that after receptor activation. To evaluate the role of protein kinase C in excitatory signal transduction, we transiently elevated the endogenous diacylglycerol level after receptor activation by the use of a diacylglycerol kinase inhibitor (R 59 949). On addition of the agonist vasopressin to platelets prelabeled with [32P] orthophosphate, 32P-phosphatidic acid (PA) formation was inhibited by R 59 949 in a dose-dependent manner (IC50 α 10−6 M). Vasopressin induced formation of 32P-phosphatidylinositol-4’-phosphate (PIP) and the phosphorylation of the 40 k Da protein (major substrate of the protein kinase C) were increased in the presence of the compound. In platelets prelabeled with [3H]-inositol, the agonist-induced formation of all the water-soluble inositol phosphates was inhibited in the presence of the diacylglycerol kinase inhibitor and Li+. Vasopressin induced increase in intracellular Ca2+ was lower in the presence of R 59 949. The platelet shape change induced by a threshold concentration of vasopressin was reduced by the compound. By contrast, the rate and the maximum of the first-wave aggregation was enhanced in the presence of R 59 949.These data evidence that protein kinase C, stimulated by endogenously generated diacylglycerol after receptor activation, plays a major inhibitory role on the primary steps of signal transduction since its activation reduces i) phospholipase C activity and ii) the increase in intracellular Ca2+ and the concomitant shape change reaction. The inhibitory role of protein kinase C on signal transduction is largely independent of its stimulatory role on platelet aggregation. Our data further confirm that stimulation of protein kinase C induces the formation of PIP but questions the role of the kinase in the breakdown process of inositoltrisphosphate.
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