Artykuły w czasopismach na temat „Histone acylation”
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Xiao, Yanhui, Wenjing Li, Hui Yang, Lulu Pan, Liwei Zhang, Lu Lu, Jiwei Chen i in. "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.
Pełny tekst źródłaYan, Kezhi, Justine Rousseau, Keren Machol, Laura A. Cross, Katherine E. Agre, Cynthia Forster Gibson, Anne Goverde i in. "Deficient histone H3 propionylation by BRPF1-KAT6 complexes in neurodevelopmental disorders and cancer". Science Advances 6, nr 4 (styczeń 2020): eaax0021. http://dx.doi.org/10.1126/sciadv.aax0021.
Pełny tekst źródłaNeja, Sultan, Wan Mohaiza Dashwood, Roderick H. Dashwood i 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.
Pełny tekst źródłaSoffers, Jelly H. M., Xuanying Li, Susan M. Abmayr i Jerry L. Workman. "Reading and Interpreting the Histone Acylation Code". Genomics, Proteomics & Bioinformatics 14, nr 6 (grudzień 2016): 329–32. http://dx.doi.org/10.1016/j.gpb.2016.12.001.
Pełny tekst źródłaKlein, Brianna J., Johayra Simithy, Xiaolu Wang, JaeWoo Ahn, Forest H. Andrews, Yi Zhang, Jacques Côté, Xiaobing Shi, Benjamin A. Garcia i Tatiana G. Kutateladze. "Recognition of Histone H3K14 Acylation by MORF". Structure 25, nr 4 (kwiecień 2017): 650–54. http://dx.doi.org/10.1016/j.str.2017.02.003.
Pełny tekst źródłaKhan, Abid, Joseph B. Bridgers i Brian D. Strahl. "Expanding the Reader Landscape of Histone Acylation". Structure 25, nr 4 (kwiecień 2017): 571–73. http://dx.doi.org/10.1016/j.str.2017.03.010.
Pełny tekst źródłaJo, Chanhee, Seokjae Park, Sungjoon Oh, Jinmi Choi, Eun-Kyoung Kim, Hong-Duk Youn i Eun-Jung Cho. "Histone acylation marks respond to metabolic perturbations and enable cellular adaptation". Experimental & Molecular Medicine 52, nr 12 (grudzień 2020): 2005–19. http://dx.doi.org/10.1038/s12276-020-00539-x.
Pełny tekst źródłaZheng, Lanlan, Chen Li, Xueping Ma, Hanlin Zhou, Yuan Liu, Ping Wang, Huilan Yang i in. "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.
Pełny tekst źródłaZhao, Dan, Yuanyuan Li, Xiaozhe Xiong, Zhonglei Chen i Haitao Li. "YEATS Domain—A Histone Acylation Reader in Health and Disease". Journal of Molecular Biology 429, nr 13 (czerwiec 2017): 1994–2002. http://dx.doi.org/10.1016/j.jmb.2017.03.010.
Pełny tekst źródłaSharma, Deepika, Swati Sharma i 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.
Pełny tekst źródłaYuan, Zhao-Di, Wei-Ning Zhu, Ke-Zhi Liu, Zhan-Peng Huang i 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.
Pełny tekst źródłaCao, Ji, Lei Sun, Pornpun Aramsangtienchai, Nicole A. Spiegelman, Xiaoyu Zhang, Weishan Huang, Edward Seto i 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.
Pełny tekst źródłaGao, Mengqing, Jin Wang, Sophie Rousseaux, Minjia Tan, Lulu Pan, Lijun Peng, Sisi Wang i in. "Metabolically controlled histone H4K5 acylation/acetylation ratio drives BRD4 genomic distribution". Cell Reports 36, nr 4 (lipiec 2021): 109460. http://dx.doi.org/10.1016/j.celrep.2021.109460.
Pełny tekst źródłaZubrytski, Dzmitry M., Gábor Zoltán Elek, Margus Lopp i 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.
Pełny tekst źródłaChristott, Thomas, James Bennett, Carmen Coxon, Octovia Monteiro, Charline Giroud, Viktor Beke, Suet Ling Felce i in. "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.
Pełny tekst źródłaEtier, Aurelie, Fabien Dumetz, Sylvain Chéreau i 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.
Pełny tekst źródłaPonnan, Prija, Ajit Kumar, Prabhjot Singh, Prachi Gupta, Rini Joshi, Marco Gaspari, Luciano Saso i in. "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.
Pełny tekst źródłaJoshi, Joha, Micah J. McCauley, Allison Cross, Michael Morse, Mattew C. Amato, Nicole A. Becker, Ioulia F. Rouzina, Louis J. Maher i Mark C. Williams. "Acylation of key sites in the histone octamer core destabilizes nucleosome arrays". Biophysical Journal 121, nr 3 (luty 2022): 210a. http://dx.doi.org/10.1016/j.bpj.2021.11.1675.
Pełny tekst źródłaAmamoto, Yoshifumi, Yuki Aoi, Nozomu Nagashima, Hiroki Suto, Daisuke Yoshidome, Yasuhiro Arimura, Akihisa Osakabe i in. "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.
Pełny tekst źródłaZhao, Yuqin, Shuailin Hao, Wenchi Wu, Youhang Li, Kaiping Hou, Yu Liu, Wei Cui, Xingzhi Xu i Hailong Wang. "Lysine Crotonylation: An Emerging Player in DNA Damage Response". Biomolecules 12, nr 10 (5.10.2022): 1428. http://dx.doi.org/10.3390/biom12101428.
Pełny tekst źródłaXu, Huiwen, Maoyan Wu, Xiumei Ma, Wei Huang i Yong Xu. "Function and Mechanism of Novel Histone Posttranslational Modifications in Health and Disease". BioMed Research International 2021 (3.03.2021): 1–13. http://dx.doi.org/10.1155/2021/6635225.
Pełny tekst źródłaOurailidou, Maria E., Paul Dockerty, Martin Witte, Gerrit J. Poelarends i 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.
Pełny tekst źródłaVarner, Erika L., Sophie Trefely, David Bartee, Eliana von Krusenstiern, Luke Izzo, Carmen Bekeova, Roddy S. O'Connor i in. "Quantification of lactoyl-CoA (lactyl-CoA) by liquid chromatography mass spectrometry in mammalian cells and tissues". Open Biology 10, nr 9 (wrzesień 2020): 200187. http://dx.doi.org/10.1098/rsob.200187.
Pełny tekst źródłaLiu, Yuexia, Yizhou Li, Juntong Liang, Zhuwen Sun i 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.
Pełny tekst źródłaWilson, John P., Anuradha S. Raghavan, Yu-Ying Yang, Guillaume Charron i 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.
Pełny tekst źródłaBarnes, Claire E., David M. English i Shaun M. Cowley. "Acetylation & Co: an expanding repertoire of histone acylations regulates chromatin and transcription". Essays in Biochemistry 63, nr 1 (kwiecień 2019): 97–107. http://dx.doi.org/10.1042/ebc20180061.
Pełny tekst źródłaDeng, Yijun, Christina Ng DiMarco, Tanya Vakhilt, Marco Jonas, Jaclyn White, Dennis Arefyev, Ramachandar Tokala i in. "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.
Pełny tekst źródłaBrewster, Richard C., i Alison N. Hulme. "Halomethyl-Triazoles for Rapid, Site-Selective Protein Modification". Molecules 26, nr 18 (8.09.2021): 5461. http://dx.doi.org/10.3390/molecules26185461.
Pełny tekst źródłaGan, Qing, Donge Tang, Qiang Yan, Jiejing Chen, Yong Xu, Wen Xue, Lu Xiao i in. "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.
Pełny tekst źródłaAleshin, V. A., D. A. Sibiryakina, A. V. Kazantsev, A. V. Graf i 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.
Pełny tekst źródłaRonan, Jade L., Nadia Kadi, Stephen A. McMahon, James H. Naismith, Lona M. Alkhalaf i 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.
Pełny tekst źródłaCrespo, Marion, Annelaure Damont, Melina Blanco, Emmanuelle Lastrucci, Sara El Kennani, Côme Ialy-Radio, Laila El Khattabi i in. "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.
Pełny tekst źródłaZhao, Shuai, Xingrun Zhang i Haitao Li. "Beyond histone acetylation—writing and erasing histone acylations". Current Opinion in Structural Biology 53 (grudzień 2018): 169–77. http://dx.doi.org/10.1016/j.sbi.2018.10.001.
Pełny tekst źródłaSabari, Benjamin R., Di Zhang, C. David Allis i Yingming Zhao. "Metabolic regulation of gene expression through histone acylations". Nature Reviews Molecular Cell Biology 18, nr 2 (7.12.2016): 90–101. http://dx.doi.org/10.1038/nrm.2016.140.
Pełny tekst źródłaDutta, Arnob, Susan M. Abmayr i Jerry L. Workman. "Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function". Molecular Cell 63, nr 4 (sierpień 2016): 547–52. http://dx.doi.org/10.1016/j.molcel.2016.06.038.
Pełny tekst źródłaFernandes, Mariane Font, i Marco Aurélio Ramirez Vinolo. "Histone acylations as a mechanism for regulation of intestinal epithelial cells". Digestive Medicine Research 7 (marzec 2024): 4. http://dx.doi.org/10.21037/dmr-23-3.
Pełny tekst źródłaShi, Jiale, Xuemei Jia, Yujia He, Xinyue Ma, Xiaoyu Qi, Wan Li, Shou-Jiang Gao, Qin Yan i Chun Lu. "Immune evasion strategy involving propionylation by the KSHV interferon regulatory factor 1 (vIRF1)". PLOS Pathogens 19, nr 4 (6.04.2023): e1011324. http://dx.doi.org/10.1371/journal.ppat.1011324.
Pełny tekst źródłaPeterson, Francis C., Dawei Chen, Betsy L. Lytle, Marianna N. Rossi, Ivan Ahel, John M. Denu i 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.
Pełny tekst źródłaOlp, Michael D., Nan Zhu i Brian C. Smith. "Metabolically Derived Lysine Acylations and Neighboring Modifications Tune the Binding of the BET Bromodomains to Histone H4". Biochemistry 56, nr 41 (5.10.2017): 5485–95. http://dx.doi.org/10.1021/acs.biochem.7b00595.
Pełny tekst źródłaWang, Bo, Po-Hsien Huang, Ching-Shih Chen i 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.
Pełny tekst źródłaNelson, John, Neil V. McFerran, Géraldine Pivato, Emma Chambers, Caroline Doherty, David Steele i David J. Timson. "The 67 kDa laminin receptor: structure, function and role in disease". Bioscience Reports 28, nr 1 (1.02.2008): 33–48. http://dx.doi.org/10.1042/bsr20070004.
Pełny tekst źródłaLIAU, Y. H., J. ZIELENSKI, S. R. CARTER, A. SLOMIANY i 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 (maj 1987): 345–47. http://dx.doi.org/10.1111/j.1749-6632.1987.tb29568.x.
Pełny tekst źródłaRICH, JOSEPH O., i 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 (październik 1996): 226–30. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33205.x.
Pełny tekst źródłaIto, Minami, Yuya Nishida, Tatsuya Iwamoto, Akiko Kanai, Shuhei Aoyama, Kyosei Ueki, Hirotsugu Uzawa, Hitoshi Iida i 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 (czerwiec 2024): 149960. http://dx.doi.org/10.1016/j.bbrc.2024.149960.
Pełny tekst źródłaHu, Bin, Han Gong, Chaoying Yang, Ling Nie, Ji Zhang, Long Liang, Mohandas Narla, Yue Sheng i 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.
Pełny tekst źródłaDACQUET, CATHERINE, CHRISTELLE MACIA i 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 (maj 1997): 178. http://dx.doi.org/10.1111/j.1749-6632.1997.tb48165.x.
Pełny tekst źródłaDUUREN, BENJAMIN L. "Direct-Acting Alkylating and Acylating Agents." Annals of the New York Academy of Sciences 534, nr 1 Living in a C (czerwiec 1988): 620–34. http://dx.doi.org/10.1111/j.1749-6632.1988.tb30153.x.
Pełny tekst źródłaKODELIA, G., i 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 (listopad 1992): 451–57. http://dx.doi.org/10.1111/j.1749-6632.1992.tb32712.x.
Pełny tekst źródłaZHUANG, YING-PING, JIAN-HE XU i 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 (grudzień 1998): 656–59. http://dx.doi.org/10.1111/j.1749-6632.1998.tb10399.x.
Pełny tekst źródłaBhattacharya, Saikat, i Benjamin P. Tu. "Histone acylation at a glance". Journal of Cell Science 137, nr 11 (1.06.2024). http://dx.doi.org/10.1242/jcs.261250.
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