Zeitschriftenartikel zum Thema „Histone acylation“
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Xiao, Yanhui, Wenjing Li, Hui Yang, Lulu Pan, Liwei Zhang, Lu Lu, Jiwei Chen et al. „HBO1 is a versatile histone acyltransferase critical for promoter histone acylations“. Nucleic Acids Research 49, Nr. 14 (14.07.2021): 8037–59. http://dx.doi.org/10.1093/nar/gkab607.
Der volle Inhalt der QuelleYan, Kezhi, Justine Rousseau, Keren Machol, Laura A. Cross, Katherine E. Agre, Cynthia Forster Gibson, Anne Goverde et al. „Deficient histone H3 propionylation by BRPF1-KAT6 complexes in neurodevelopmental disorders and cancer“. Science Advances 6, Nr. 4 (Januar 2020): eaax0021. http://dx.doi.org/10.1126/sciadv.aax0021.
Der volle Inhalt der QuelleNeja, Sultan, Wan Mohaiza Dashwood, Roderick H. Dashwood und Praveen Rajendran. „Histone Acyl Code in Precision Oncology: Mechanistic Insights from Dietary and Metabolic Factors“. Nutrients 16, Nr. 3 (30.01.2024): 396. http://dx.doi.org/10.3390/nu16030396.
Der volle Inhalt der QuelleSoffers, Jelly H. M., Xuanying Li, Susan M. Abmayr und Jerry L. Workman. „Reading and Interpreting the Histone Acylation Code“. Genomics, Proteomics & Bioinformatics 14, Nr. 6 (Dezember 2016): 329–32. http://dx.doi.org/10.1016/j.gpb.2016.12.001.
Der volle Inhalt der QuelleKlein, Brianna J., Johayra Simithy, Xiaolu Wang, JaeWoo Ahn, Forest H. Andrews, Yi Zhang, Jacques Côté, Xiaobing Shi, Benjamin A. Garcia und Tatiana G. Kutateladze. „Recognition of Histone H3K14 Acylation by MORF“. Structure 25, Nr. 4 (April 2017): 650–54. http://dx.doi.org/10.1016/j.str.2017.02.003.
Der volle Inhalt der QuelleKhan, Abid, Joseph B. Bridgers und Brian D. Strahl. „Expanding the Reader Landscape of Histone Acylation“. Structure 25, Nr. 4 (April 2017): 571–73. http://dx.doi.org/10.1016/j.str.2017.03.010.
Der volle Inhalt der QuelleJo, Chanhee, Seokjae Park, Sungjoon Oh, Jinmi Choi, Eun-Kyoung Kim, Hong-Duk Youn und Eun-Jung Cho. „Histone acylation marks respond to metabolic perturbations and enable cellular adaptation“. Experimental & Molecular Medicine 52, Nr. 12 (Dezember 2020): 2005–19. http://dx.doi.org/10.1038/s12276-020-00539-x.
Der volle Inhalt der QuelleZheng, Lanlan, Chen Li, Xueping Ma, Hanlin Zhou, Yuan Liu, Ping Wang, Huilan Yang et al. „Functional interplay of histone lysine 2-hydroxyisobutyrylation and acetylation in Arabidopsis under dark-induced starvation“. Nucleic Acids Research 49, Nr. 13 (24.06.2021): 7347–60. http://dx.doi.org/10.1093/nar/gkab536.
Der volle Inhalt der QuelleZhao, Dan, Yuanyuan Li, Xiaozhe Xiong, Zhonglei Chen und Haitao Li. „YEATS Domain—A Histone Acylation Reader in Health and Disease“. Journal of Molecular Biology 429, Nr. 13 (Juni 2017): 1994–2002. http://dx.doi.org/10.1016/j.jmb.2017.03.010.
Der volle Inhalt der QuelleSharma, Deepika, Swati Sharma und Preeti Chauhan. „Acetylation of Histone and Modification of Gene Expression via HDAC Inhibitors Affects the Obesity“. Biomedical and Pharmacology Journal 14, Nr. 1 (28.03.2021): 153–61. http://dx.doi.org/10.13005/bpj/2110.
Der volle Inhalt der QuelleYuan, Zhao-Di, Wei-Ning Zhu, Ke-Zhi Liu, Zhan-Peng Huang und Yan-Chuang Han. „Small Molecule Epigenetic Modulators in Pure Chemical Cell Fate Conversion“. Stem Cells International 2020 (20.10.2020): 1–12. http://dx.doi.org/10.1155/2020/8890917.
Der volle Inhalt der QuelleCao, Ji, Lei Sun, Pornpun Aramsangtienchai, Nicole A. Spiegelman, Xiaoyu Zhang, Weishan Huang, Edward Seto und Hening Lin. „HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2“. Proceedings of the National Academy of Sciences 116, Nr. 12 (28.02.2019): 5487–92. http://dx.doi.org/10.1073/pnas.1815365116.
Der volle Inhalt der QuelleGao, Mengqing, Jin Wang, Sophie Rousseaux, Minjia Tan, Lulu Pan, Lijun Peng, Sisi Wang et al. „Metabolically controlled histone H4K5 acylation/acetylation ratio drives BRD4 genomic distribution“. Cell Reports 36, Nr. 4 (Juli 2021): 109460. http://dx.doi.org/10.1016/j.celrep.2021.109460.
Der volle Inhalt der QuelleZubrytski, Dzmitry M., Gábor Zoltán Elek, Margus Lopp und Dzmitry G. Kananovich. „Generation of Mixed Anhydrides via Oxidative Fragmentation of Tertiary Cyclopropanols with Phenyliodine(III) Dicarboxylates“. Molecules 26, Nr. 1 (30.12.2020): 140. http://dx.doi.org/10.3390/molecules26010140.
Der volle Inhalt der QuelleChristott, Thomas, James Bennett, Carmen Coxon, Octovia Monteiro, Charline Giroud, Viktor Beke, Suet Ling Felce et al. „Discovery of a Selective Inhibitor for the YEATS Domains of ENL/AF9“. SLAS DISCOVERY: Advancing the Science of Drug Discovery 24, Nr. 2 (25.10.2018): 133–41. http://dx.doi.org/10.1177/2472555218809904.
Der volle Inhalt der QuelleEtier, Aurelie, Fabien Dumetz, Sylvain Chéreau und Nadia Ponts. „Post-Translational Modifications of Histones Are Versatile Regulators of Fungal Development and Secondary Metabolism“. Toxins 14, Nr. 5 (29.04.2022): 317. http://dx.doi.org/10.3390/toxins14050317.
Der volle Inhalt der QuellePonnan, Prija, Ajit Kumar, Prabhjot Singh, Prachi Gupta, Rini Joshi, Marco Gaspari, Luciano Saso et al. „Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT“. Scientific World Journal 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/578956.
Der volle Inhalt der QuelleJoshi, Joha, Micah J. McCauley, Allison Cross, Michael Morse, Mattew C. Amato, Nicole A. Becker, Ioulia F. Rouzina, Louis J. Maher und Mark C. Williams. „Acylation of key sites in the histone octamer core destabilizes nucleosome arrays“. Biophysical Journal 121, Nr. 3 (Februar 2022): 210a. http://dx.doi.org/10.1016/j.bpj.2021.11.1675.
Der volle Inhalt der QuelleAmamoto, Yoshifumi, Yuki Aoi, Nozomu Nagashima, Hiroki Suto, Daisuke Yoshidome, Yasuhiro Arimura, Akihisa Osakabe et al. „Synthetic Posttranslational Modifications: Chemical Catalyst-Driven Regioselective Histone Acylation of Native Chromatin“. Journal of the American Chemical Society 139, Nr. 22 (23.05.2017): 7568–76. http://dx.doi.org/10.1021/jacs.7b02138.
Der volle Inhalt der QuelleZhao, Yuqin, Shuailin Hao, Wenchi Wu, Youhang Li, Kaiping Hou, Yu Liu, Wei Cui, Xingzhi Xu und Hailong Wang. „Lysine Crotonylation: An Emerging Player in DNA Damage Response“. Biomolecules 12, Nr. 10 (05.10.2022): 1428. http://dx.doi.org/10.3390/biom12101428.
Der volle Inhalt der QuelleXu, Huiwen, Maoyan Wu, Xiumei Ma, Wei Huang und Yong Xu. „Function and Mechanism of Novel Histone Posttranslational Modifications in Health and Disease“. BioMed Research International 2021 (03.03.2021): 1–13. http://dx.doi.org/10.1155/2021/6635225.
Der volle Inhalt der QuelleOurailidou, Maria E., Paul Dockerty, Martin Witte, Gerrit J. Poelarends und Frank J. Dekker. „Metabolic alkene labeling and in vitro detection of histone acylation via the aqueous oxidative Heck reaction“. Organic & Biomolecular Chemistry 13, Nr. 12 (2015): 3648–53. http://dx.doi.org/10.1039/c4ob02502d.
Der volle Inhalt der QuelleVarner, Erika L., Sophie Trefely, David Bartee, Eliana von Krusenstiern, Luke Izzo, Carmen Bekeova, Roddy S. O'Connor et al. „Quantification of lactoyl-CoA (lactyl-CoA) by liquid chromatography mass spectrometry in mammalian cells and tissues“. Open Biology 10, Nr. 9 (September 2020): 200187. http://dx.doi.org/10.1098/rsob.200187.
Der volle Inhalt der QuelleLiu, Yuexia, Yizhou Li, Juntong Liang, Zhuwen Sun und Chao Sun. „Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning“. International Journal of Molecular Sciences 23, Nr. 21 (22.10.2022): 12733. http://dx.doi.org/10.3390/ijms232112733.
Der volle Inhalt der QuelleWilson, John P., Anuradha S. Raghavan, Yu-Ying Yang, Guillaume Charron und Howard C. Hang. „Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters RevealsS-Acylation of Histone H3 Variants“. Molecular & Cellular Proteomics 10, Nr. 3 (14.11.2010): M110.001198. http://dx.doi.org/10.1074/mcp.m110.001198.
Der volle Inhalt der QuelleBarnes, Claire E., David M. English und Shaun M. Cowley. „Acetylation & Co: an expanding repertoire of histone acylations regulates chromatin and transcription“. Essays in Biochemistry 63, Nr. 1 (April 2019): 97–107. http://dx.doi.org/10.1042/ebc20180061.
Der volle Inhalt der QuelleDeng, Yijun, Christina Ng DiMarco, Tanya Vakhilt, Marco Jonas, Jaclyn White, Dennis Arefyev, Ramachandar Tokala et al. „Process Development of the Soft Histone Deacetylate Enzyme Inhibitor SHP-141: Acylation of Methyl Paraben and Suberyl Hydroxamic Acid Formation“. Organic Process Research & Development 20, Nr. 10 (28.09.2016): 1812–20. http://dx.doi.org/10.1021/acs.oprd.6b00280.
Der volle Inhalt der QuelleBrewster, Richard C., und Alison N. Hulme. „Halomethyl-Triazoles for Rapid, Site-Selective Protein Modification“. Molecules 26, Nr. 18 (08.09.2021): 5461. http://dx.doi.org/10.3390/molecules26185461.
Der volle Inhalt der QuelleGan, Qing, Donge Tang, Qiang Yan, Jiejing Chen, Yong Xu, Wen Xue, Lu Xiao et al. „Differential Expression Study of Lysine Crotonylation and Proteome for Chronic Obstructive Pulmonary Disease Combined with Type II Respiratory Failure“. Canadian Respiratory Journal 2021 (15.06.2021): 1–12. http://dx.doi.org/10.1155/2021/6652297.
Der volle Inhalt der QuelleAleshin, V. A., D. A. Sibiryakina, A. V. Kazantsev, A. V. Graf und V. I. Bunik. „Acylation of the rat brain proteins is affected by the inhibition of pyruvate dehydrogenase <i>in vivo</i>“. Биохимия 88, Nr. 1 (15.01.2023): 147–63. http://dx.doi.org/10.31857/s0320972523010116.
Der volle Inhalt der QuelleRonan, Jade L., Nadia Kadi, Stephen A. McMahon, James H. Naismith, Lona M. Alkhalaf und Gregory L. Challis. „Desferrioxamine biosynthesis: diverse hydroxamate assembly by substrate-tolerant acyl transferase DesC“. Philosophical Transactions of the Royal Society B: Biological Sciences 373, Nr. 1748 (23.04.2018): 20170068. http://dx.doi.org/10.1098/rstb.2017.0068.
Der volle Inhalt der QuelleCrespo, Marion, Annelaure Damont, Melina Blanco, Emmanuelle Lastrucci, Sara El Kennani, Côme Ialy-Radio, Laila El Khattabi et al. „Multi-omic analysis of gametogenesis reveals a novel signature at the promoters and distal enhancers of active genes“. Nucleic Acids Research 48, Nr. 8 (17.03.2020): 4115–38. http://dx.doi.org/10.1093/nar/gkaa163.
Der volle Inhalt der QuelleZhao, Shuai, Xingrun Zhang und Haitao Li. „Beyond histone acetylation—writing and erasing histone acylations“. Current Opinion in Structural Biology 53 (Dezember 2018): 169–77. http://dx.doi.org/10.1016/j.sbi.2018.10.001.
Der volle Inhalt der QuelleSabari, Benjamin R., Di Zhang, C. David Allis und Yingming Zhao. „Metabolic regulation of gene expression through histone acylations“. Nature Reviews Molecular Cell Biology 18, Nr. 2 (07.12.2016): 90–101. http://dx.doi.org/10.1038/nrm.2016.140.
Der volle Inhalt der QuelleDutta, Arnob, Susan M. Abmayr und Jerry L. Workman. „Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function“. Molecular Cell 63, Nr. 4 (August 2016): 547–52. http://dx.doi.org/10.1016/j.molcel.2016.06.038.
Der volle Inhalt der QuelleFernandes, Mariane Font, und Marco Aurélio Ramirez Vinolo. „Histone acylations as a mechanism for regulation of intestinal epithelial cells“. Digestive Medicine Research 7 (März 2024): 4. http://dx.doi.org/10.21037/dmr-23-3.
Der volle Inhalt der QuelleShi, Jiale, Xuemei Jia, Yujia He, Xinyue Ma, Xiaoyu Qi, Wan Li, Shou-Jiang Gao, Qin Yan und Chun Lu. „Immune evasion strategy involving propionylation by the KSHV interferon regulatory factor 1 (vIRF1)“. PLOS Pathogens 19, Nr. 4 (06.04.2023): e1011324. http://dx.doi.org/10.1371/journal.ppat.1011324.
Der volle Inhalt der QuellePeterson, Francis C., Dawei Chen, Betsy L. Lytle, Marianna N. Rossi, Ivan Ahel, John M. Denu und Brian F. Volkman. „Orphan Macrodomain Protein (Human C6orf130) Is an O-Acyl-ADP-ribose Deacylase“. Journal of Biological Chemistry 286, Nr. 41 (17.08.2011): 35955–65. http://dx.doi.org/10.1074/jbc.m111.276238.
Der volle Inhalt der QuelleOlp, Michael D., Nan Zhu und Brian C. Smith. „Metabolically Derived Lysine Acylations and Neighboring Modifications Tune the Binding of the BET Bromodomains to Histone H4“. Biochemistry 56, Nr. 41 (05.10.2017): 5485–95. http://dx.doi.org/10.1021/acs.biochem.7b00595.
Der volle Inhalt der QuelleWang, Bo, Po-Hsien Huang, Ching-Shih Chen und Craig J. Forsyth. „Total Syntheses of the Histone Deacetylase Inhibitors Largazole and 2-epi-Largazole: Application ofN-Heterocyclic Carbene Mediated Acylations in Complex Molecule Synthesis“. Journal of Organic Chemistry 76, Nr. 4 (18.02.2011): 1140–50. http://dx.doi.org/10.1021/jo102478x.
Der volle Inhalt der QuelleNelson, John, Neil V. McFerran, Géraldine Pivato, Emma Chambers, Caroline Doherty, David Steele und David J. Timson. „The 67 kDa laminin receptor: structure, function and role in disease“. Bioscience Reports 28, Nr. 1 (01.02.2008): 33–48. http://dx.doi.org/10.1042/bsr20070004.
Der volle Inhalt der QuelleLIAU, Y. H., J. ZIELENSKI, S. R. CARTER, A. SLOMIANY und B. L. SLOMIANY. „Enzymatic Acylation of Mucus Glycoprotein in Rat Salivary Glands“. Annals of the New York Academy of Sciences 494, Nr. 1 Third Colloqu (Mai 1987): 345–47. http://dx.doi.org/10.1111/j.1749-6632.1987.tb29568.x.
Der volle Inhalt der QuelleRICH, JOSEPH O., und JONATHAN S. DORDICK. „Controlling Regioselectivity in Enzyme-catalyzed Acylation of Polyhydroxyl Compounds“. Annals of the New York Academy of Sciences 799, Nr. 1 Enzyme Engine (Oktober 1996): 226–30. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33205.x.
Der volle Inhalt der QuelleIto, Minami, Yuya Nishida, Tatsuya Iwamoto, Akiko Kanai, Shuhei Aoyama, Kyosei Ueki, Hirotsugu Uzawa, Hitoshi Iida und Hirotaka Watada. „Protein acylations induced by a ketogenic diet demonstrate diverse patterns depending on organs and differ between histones and global proteins“. Biochemical and Biophysical Research Communications 712-713 (Juni 2024): 149960. http://dx.doi.org/10.1016/j.bbrc.2024.149960.
Der volle Inhalt der QuelleHu, Bin, Han Gong, Chaoying Yang, Ling Nie, Ji Zhang, Long Liang, Mohandas Narla, Yue Sheng und Jing Liu. „Dynamic Changes in Lysine Succinylation As Important Regulators of Erythropoiesis“. Blood 142, Supplement 1 (28.11.2023): 2448. http://dx.doi.org/10.1182/blood-2023-182646.
Der volle Inhalt der QuelleDACQUET, CATHERINE, CHRISTELLE MACIA und MICHAEL SPEDDING. „Acylation Differentiates Two Forms of Agonist Binding to Rat 5-HT1AReceptors.“ Annals of the New York Academy of Sciences 812, Nr. 1 Receptor Clas (Mai 1997): 178. http://dx.doi.org/10.1111/j.1749-6632.1997.tb48165.x.
Der volle Inhalt der QuelleDUUREN, BENJAMIN L. „Direct-Acting Alkylating and Acylating Agents.“ Annals of the New York Academy of Sciences 534, Nr. 1 Living in a C (Juni 1988): 620–34. http://dx.doi.org/10.1111/j.1749-6632.1988.tb30153.x.
Der volle Inhalt der QuelleKODELIA, G., und F. N. KOLISIS. „Studies on the Reaction Catalyzed by Protease for the Acylation of Flavonoids in Organic Solvents“. Annals of the New York Academy of Sciences 672, Nr. 1 Enzyme Engine (November 1992): 451–57. http://dx.doi.org/10.1111/j.1749-6632.1992.tb32712.x.
Der volle Inhalt der QuelleZHUANG, YING-PING, JIAN-HE XU und SI-LIANG ZHANG. „Effects of Organic Solvent and Acylating Agent on Lipase-Catalyzed Esterification of a Chiral Chlorohydrin in Nonaqueous Mediaa“. Annals of the New York Academy of Sciences 864, Nr. 1 ENZYME ENGINE (Dezember 1998): 656–59. http://dx.doi.org/10.1111/j.1749-6632.1998.tb10399.x.
Der volle Inhalt der QuelleBhattacharya, Saikat, und Benjamin P. Tu. „Histone acylation at a glance“. Journal of Cell Science 137, Nr. 11 (01.06.2024). http://dx.doi.org/10.1242/jcs.261250.
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