Academic literature on the topic 'Pateamine'

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Journal articles on the topic "Pateamine"

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Matthews, James H., David R. Maass, Peter T. Northcote, Paul H. Atkinson, and Paul H. Teesdale-Spittle. "The Cellular Target Specificity of Pateamine A." Zeitschrift für Naturforschung C 68, no. 9-10 (October 1, 2013): 406–15. http://dx.doi.org/10.1515/znc-2013-9-1008.

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The natural product pateamine A (pateamine) from the sponge Mycale hentscheli is active against a wide range of dividing cells and has been shown to inhibit the functions of the eukaryotic initiation factor 4A (eIF4A). We have identifi ed that pateamine is additionally able to modulate the formation of actin fi laments and microtubules in vitro but at higher concentrations than required for inhibition of eIF4A. Cell cycle analysis confi rmed that actin and tubulin are not major mediators of the cellular activity of pateamine. The range of targets identifi ed demonstrates the value of multiple approaches to determining the mode of action of biologically active compounds
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Dang, Yongjun, Nancy Kedersha, Woon-Kai Low, Daniel Romo, Myriam Gorospe, Randal Kaufman, Paul Anderson, and Jun O. Liu. "Eukaryotic Initiation Factor 2α-independent Pathway of Stress Granule Induction by the Natural Product Pateamine A." Journal of Biological Chemistry 281, no. 43 (September 2, 2006): 32870–78. http://dx.doi.org/10.1074/jbc.m606149200.

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Stress granules are aggregates of small ribosomal subunits, mRNA, and numerous associated RNA-binding proteins that include several translation initiation factors. Stress granule assembly occurs in the cytoplasm of higher eukaryotic cells under a wide variety of stress conditions, including heat shock, UV irradiation, hypoxia, and exposure to arsenite. Thus far, a unifying principle of eukaryotic initiation factor 2α phosphorylation prior to stress granule formation has been observed from the majority of experimental evidence. Pateamine A, a natural product isolated from marine sponge, was recently reported to inhibit eukaryotic translation initiation and induce the formation of stress granules. In this report, the protein composition and fundamental progression of stress granule formation and disassembly induced by pateamine A was found to be similar to that for arsenite. However, pateamine A-induced stress granules were more stable and less prone to disassembly than those formed in the presence of arsenite. Most significantly, pateamine A induced stress granules independent of eukaryotic initiation factor 2α phosphorylation, suggesting an alternative mechanism of formation from that previously described for other cellular stresses. Taking into account the known inhibitory effect of pateamine A on eukaryotic translation initiation, a model is proposed to account for the induction of stress granules by pateamine A as well as other stress conditions through perturbation of any steps prior to the rejoining of the 60S ribosomal subunit during the entire translation initiation process.
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Pattenden, Gerald, Douglas J. Critcher, and Modesto Remuiñán. "Total synthesis of (–)-pateamine A, a novel immunosuppressive agent from Mycale sp." Canadian Journal of Chemistry 82, no. 2 (February 1, 2004): 353–65. http://dx.doi.org/10.1139/v03-199.

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A convergent synthesis of the unique thiazole-containing polyene bis-lactone pateamine A (1) isolated from the marine sponge Mycale sp is described. The synthesis features the ubiquitous Stille sp2–sp2 coupling reaction to elaborate the E,Z-diene macrolide core 23 and the all-E polyenamine side chain in the natural product. It also highlights the scope for enantiopure sulfinimine intermediates in the synthesis of chiral β-amino ester moieties in complex structures.Key words: pateamine A, immunosuppressive agent from marine sponge Mycale sp, total synthesis, novel 19-membered bis-lactone, thiazole metabolite, polyenamine, Stille reaction, sulfinimines, chiral β-amino esters.
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Hemi Cumming, A., Sarah L. Brown, Xu Tao, Claire Cuyamendous, Jessica J. Field, John H. Miller, Joanne E. Harvey, and Paul H. Teesdale-Spittle. "Synthesis of a simplified triazole analogue of pateamine A." Organic & Biomolecular Chemistry 14, no. 22 (2016): 5117–27. http://dx.doi.org/10.1039/c6ob00086j.

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Korneeva, Nadejda L. "Translational Dysregulation by Pateamine A." Chemistry & Biology 14, no. 1 (January 2007): 5–7. http://dx.doi.org/10.1016/j.chembiol.2007.01.003.

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Kommaraju, Sai Shilpa, Julieta Aulicino, Shruthi Gobbooru, Jing Li, Mingzhao Zhu, Daniel Romo, and Woon-Kai Low. "Investigation of the mechanism of action of a potent pateamine A analog, des-methyl, des-amino pateamine A (DMDAPatA)." Biochemistry and Cell Biology 98, no. 4 (August 2020): 502–10. http://dx.doi.org/10.1139/bcb-2019-0307.

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The natural product pateamineA (PatA) is a highly potent antiproliferative agent. PatA and the simplified analog desmethyl, desamino pateamineA (DMDAPatA) have exhibited cytotoxicity selective for rapidly proliferating cells, and have been shown to inhibit cap-dependent translation initiation through binding to eIF4A (eukaryotic initiation factor 4A) of the eIF4F complex. PatA and DMDAPatA are both known to stimulate the RNA-dependent ATPase, and ATP-dependent RNA helicase activities of eIF4A. The impact of other eIF4F components, eIF4E and eIF4G, on DMDAPatA action were investigated in vitro and in cultured mammalian cells. The perturbation of the eIF4A–eIF4G association was found to be eIF4E- and mRNA cap-dependent. An inhibitory effect on helicase activity of eIF4A was observed when it was part of a complex that mimicked the eIF4F complex. We propose a model of action for DMDAPatA (and by supposition PatA) where the cellular activity of the compound is dependent on an “active” eIF4F complex.
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Matthews, James H., David R. Maass, Peter T. Northcote, Paul H. Atkinson, and Paul H. Teesdale-Spittle. "The Cellular Target Specifi city of Pateamine A." Zeitschrift für Naturforschung C 68 (2013): 0406. http://dx.doi.org/10.5560/znc.2013.68c0406.

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Kuznetsov, Galina, Qunli Xu, Lori Rudolph-Owen, Karen TenDyke, Junke Liu, Murray Towle, Nanding Zhao, et al. "Potent in vitro and in vivo anticancer activities of des-methyl, des-amino pateamine A, a synthetic analogue of marine natural product pateamine A." Molecular Cancer Therapeutics 8, no. 5 (May 2009): 1250–60. http://dx.doi.org/10.1158/1535-7163.mct-08-1026.

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Zhuo, Chun-Xiang, and Alois Fürstner. "Catalysis-Based Total Syntheses of Pateamine A and DMDA-Pat A." Journal of the American Chemical Society 140, no. 33 (July 28, 2018): 10514–23. http://dx.doi.org/10.1021/jacs.8b05094.

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Low, Woon-Kai, Yongjun Dang, Tilman Schneider-Poetsch, Zonggao Shi, Nam Song Choi, William C. Merrick, Daniel Romo, and Jun O. Liu. "Inhibition of Eukaryotic Translation Initiation by the Marine Natural Product Pateamine A." Molecular Cell 20, no. 5 (December 2005): 709–22. http://dx.doi.org/10.1016/j.molcel.2005.10.008.

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Dissertations / Theses on the topic "Pateamine"

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Brookfield, Frederick Arthur. "Synthetic studies towards pateamine." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.311760.

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Maddock, John. "Synthetic studies towards halichondramide and pateamine." Thesis, University of Nottingham, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335793.

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Fournier, Jérémy. "PALLADIUM : REACTIVITE DE CARBONATES DE DIENOLS ALLYLIQUES APPROCHE SYNTHETIQUE DE LA (−)-PATEAMINE A." Phd thesis, Université Pierre et Marie Curie - Paris VI, 2013. http://pastel.archives-ouvertes.fr/pastel-00905915.

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La réaction d'alkylation allylique, introduite dans les années 60 par Tsuji et al., a connue un essor considérable ces dernières années. Pour notre part, nous l'avons appliquée à des substrats particuliers ; les carbonates de diénols. Une optimisation des conditions réactionnelles, a permis d'accéder à des buténolides α,α-disubstitués de manière énantiosélective. Ceux-ci ce sont révélés être des synthons particulièrement intéressants, car facilement convertibles en furanones γ substituées via un réarrangement de Cope stéréospécifique. Il a également été possible de les engager dans une séquence réactionnelle comportant une étape de réduction suivie d'une étape d'oxydation, pour obtenir les γ butyrolactones β,β-disubstituées correspondantes. L'utilité synthétique de cette méthode a également été démontrée, en l'appliquant à la synthèse totale des acides (−)-néphrostéranique et (−)-roccélarique. Enfin, cette réaction d'alkylation allylique a été intégrée dans une séquence réactionnelle monotope composée d'un réarrangement de Cope, d'une addition nucléophile et d'une déshydratation, pour accéder de manière efficace à une série de furanes et de pyrroles polysubstitués. Une approche synthétique de la (−)-patéamine A et de son analogue des-méthyle-des-amino patéamine A (DMDA-patéamine A) constitue la seconde partie de ce manuscrit. En effet, nous sommes parvenus à synthétiser et à coupler les trois fragments nécessaires à la formation du macrocycle de la DMDA-patéamine A et à effectuer la réaction clé de cyclisation par métathèse de type diène-ène. Enfin, un intermédiaire avancé de la chaine latérale a également été synthétisé à partir du géraniol.
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Book chapters on the topic "Pateamine"

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Low, Woon‐Kai, Yongjun Dang, Tilman Schneider‐Poetsch, Zonggao Shi, Nam Song Choi, Robert M. Rzasa, Helene A. Shea, et al. "Isolation and Identification of Eukaryotic Initiation Factor 4A as a Molecular Target for the Marine Natural Product Pateamine A." In Methods in Enzymology, 303–24. Elsevier, 2007. http://dx.doi.org/10.1016/s0076-6879(07)31014-8.

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Conference papers on the topic "Pateamine"

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Chen, Rong, Mingzhao Zhu, Yuling Chen, Wesley Skillern, Qun Qin, William G. Wierda, Kenneth G. Hull, Daniel Romo, and William Plunkett. "Abstract B21: Novel pateamine A analogs to target pro-survival proteins in chronic lymphocytic leukemia." In Abstracts: AACR Special Conference on Translational Control of Cancer: A New Frontier in Cancer Biology and Therapy; October 27-30, 2016; San Francisco, CA. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.transcontrol16-b21.

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Chen, Rong, Mingzhao Zhu, Rajan R. Chaudhari, Omar Robles, Yuling Chen, Wesley Skillern, Qun Qin, et al. "Abstract 1854: Novel pateamine analogs to target the translation initiation factor eIF4A in chronic lymphocytic leukemia." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1854.

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Chen, Rong, Mingzhao Zhu, Rajan R. Chaudhari, Omar Robles, Yuling Chen, Wesley Skillern, Qun Qin, et al. "Abstract 1854: Novel pateamine analogs to target the translation initiation factor eIF4A in chronic lymphocytic leukemia." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1854.

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Gómez-Hernández, G., N. Varela, H. Bagavant, G. Barturen, M. Alracón-Riquelme, and M. Morell. "PO.1.4 The eIF4 translational inhibitor pateamine a improves immunological and neurological functions in BXSB.Yaa lupus mice." In 13th European Lupus Meeting, Stockholm (October 5–8, 2022). Lupus Foundation of America, 2022. http://dx.doi.org/10.1136/lupus-2022-elm2022.38.

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Gómez-Hernández, Gonzalo, Nieves Varela, Harini Bagavant, Guillermo Barturen, María Morell, and Marta E. Alarcón-Riquelme. "1403 The EIF4 translational inhibitor pateamine a improves immunological and neurological functions in BXSB.yaa lupus mice." In LUPUS 21ST CENTURY 2021 CONFERENCE, Abstracts of the Fifth Biannual Scientific Meeting of the North and South American and Caribbean Lupus Community, Tucson, Arizona, USA – September 22–25, 2021. Lupus Foundation of America, 2021. http://dx.doi.org/10.1136/lupus-2021-lupus21century.80.

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