Artigos de revistas sobre o tema "Histone acylation"
Crie uma referência precisa em APA, MLA, Chicago, Harvard, e outros estilos
Veja os 50 melhores artigos de revistas para estudos sobre o assunto "Histone acylation".
Ao lado de cada fonte na lista de referências, há um botão "Adicionar à bibliografia". Clique e geraremos automaticamente a citação bibliográfica do trabalho escolhido no estilo de citação de que você precisa: APA, MLA, Harvard, Chicago, Vancouver, etc.
Você também pode baixar o texto completo da publicação científica em formato .pdf e ler o resumo do trabalho online se estiver presente nos metadados.
Veja os artigos de revistas das mais diversas áreas científicas e compile uma bibliografia correta.
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, n.º 14 (14 de julho de 2021): 8037–59. http://dx.doi.org/10.1093/nar/gkab607.
Texto completo da fonteYan, 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, n.º 4 (janeiro de 2020): eaax0021. http://dx.doi.org/10.1126/sciadv.aax0021.
Texto completo da fonteNeja, Sultan, Wan Mohaiza Dashwood, Roderick H. Dashwood e Praveen Rajendran. "Histone Acyl Code in Precision Oncology: Mechanistic Insights from Dietary and Metabolic Factors". Nutrients 16, n.º 3 (30 de janeiro de 2024): 396. http://dx.doi.org/10.3390/nu16030396.
Texto completo da fonteSoffers, Jelly H. M., Xuanying Li, Susan M. Abmayr e Jerry L. Workman. "Reading and Interpreting the Histone Acylation Code". Genomics, Proteomics & Bioinformatics 14, n.º 6 (dezembro de 2016): 329–32. http://dx.doi.org/10.1016/j.gpb.2016.12.001.
Texto completo da fonteKlein, Brianna J., Johayra Simithy, Xiaolu Wang, JaeWoo Ahn, Forest H. Andrews, Yi Zhang, Jacques Côté, Xiaobing Shi, Benjamin A. Garcia e Tatiana G. Kutateladze. "Recognition of Histone H3K14 Acylation by MORF". Structure 25, n.º 4 (abril de 2017): 650–54. http://dx.doi.org/10.1016/j.str.2017.02.003.
Texto completo da fonteKhan, Abid, Joseph B. Bridgers e Brian D. Strahl. "Expanding the Reader Landscape of Histone Acylation". Structure 25, n.º 4 (abril de 2017): 571–73. http://dx.doi.org/10.1016/j.str.2017.03.010.
Texto completo da fonteJo, Chanhee, Seokjae Park, Sungjoon Oh, Jinmi Choi, Eun-Kyoung Kim, Hong-Duk Youn e Eun-Jung Cho. "Histone acylation marks respond to metabolic perturbations and enable cellular adaptation". Experimental & Molecular Medicine 52, n.º 12 (dezembro de 2020): 2005–19. http://dx.doi.org/10.1038/s12276-020-00539-x.
Texto completo da fonteZheng, 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, n.º 13 (24 de junho de 2021): 7347–60. http://dx.doi.org/10.1093/nar/gkab536.
Texto completo da fonteZhao, Dan, Yuanyuan Li, Xiaozhe Xiong, Zhonglei Chen e Haitao Li. "YEATS Domain—A Histone Acylation Reader in Health and Disease". Journal of Molecular Biology 429, n.º 13 (junho de 2017): 1994–2002. http://dx.doi.org/10.1016/j.jmb.2017.03.010.
Texto completo da fonteSharma, Deepika, Swati Sharma e Preeti Chauhan. "Acetylation of Histone and Modification of Gene Expression via HDAC Inhibitors Affects the Obesity". Biomedical and Pharmacology Journal 14, n.º 1 (28 de março de 2021): 153–61. http://dx.doi.org/10.13005/bpj/2110.
Texto completo da fonteYuan, Zhao-Di, Wei-Ning Zhu, Ke-Zhi Liu, Zhan-Peng Huang e Yan-Chuang Han. "Small Molecule Epigenetic Modulators in Pure Chemical Cell Fate Conversion". Stem Cells International 2020 (20 de outubro de 2020): 1–12. http://dx.doi.org/10.1155/2020/8890917.
Texto completo da fonteCao, Ji, Lei Sun, Pornpun Aramsangtienchai, Nicole A. Spiegelman, Xiaoyu Zhang, Weishan Huang, Edward Seto e Hening Lin. "HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2". Proceedings of the National Academy of Sciences 116, n.º 12 (28 de fevereiro de 2019): 5487–92. http://dx.doi.org/10.1073/pnas.1815365116.
Texto completo da fonteGao, 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, n.º 4 (julho de 2021): 109460. http://dx.doi.org/10.1016/j.celrep.2021.109460.
Texto completo da fonteZubrytski, Dzmitry M., Gábor Zoltán Elek, Margus Lopp e Dzmitry G. Kananovich. "Generation of Mixed Anhydrides via Oxidative Fragmentation of Tertiary Cyclopropanols with Phenyliodine(III) Dicarboxylates". Molecules 26, n.º 1 (30 de dezembro de 2020): 140. http://dx.doi.org/10.3390/molecules26010140.
Texto completo da fonteChristott, 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, n.º 2 (25 de outubro de 2018): 133–41. http://dx.doi.org/10.1177/2472555218809904.
Texto completo da fonteEtier, Aurelie, Fabien Dumetz, Sylvain Chéreau e Nadia Ponts. "Post-Translational Modifications of Histones Are Versatile Regulators of Fungal Development and Secondary Metabolism". Toxins 14, n.º 5 (29 de abril de 2022): 317. http://dx.doi.org/10.3390/toxins14050317.
Texto completo da fontePonnan, 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.
Texto completo da fonteJoshi, Joha, Micah J. McCauley, Allison Cross, Michael Morse, Mattew C. Amato, Nicole A. Becker, Ioulia F. Rouzina, Louis J. Maher e Mark C. Williams. "Acylation of key sites in the histone octamer core destabilizes nucleosome arrays". Biophysical Journal 121, n.º 3 (fevereiro de 2022): 210a. http://dx.doi.org/10.1016/j.bpj.2021.11.1675.
Texto completo da fonteAmamoto, 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, n.º 22 (23 de maio de 2017): 7568–76. http://dx.doi.org/10.1021/jacs.7b02138.
Texto completo da fonteZhao, Yuqin, Shuailin Hao, Wenchi Wu, Youhang Li, Kaiping Hou, Yu Liu, Wei Cui, Xingzhi Xu e Hailong Wang. "Lysine Crotonylation: An Emerging Player in DNA Damage Response". Biomolecules 12, n.º 10 (5 de outubro de 2022): 1428. http://dx.doi.org/10.3390/biom12101428.
Texto completo da fonteXu, Huiwen, Maoyan Wu, Xiumei Ma, Wei Huang e Yong Xu. "Function and Mechanism of Novel Histone Posttranslational Modifications in Health and Disease". BioMed Research International 2021 (3 de março de 2021): 1–13. http://dx.doi.org/10.1155/2021/6635225.
Texto completo da fonteOurailidou, Maria E., Paul Dockerty, Martin Witte, Gerrit J. Poelarends e Frank J. Dekker. "Metabolic alkene labeling and in vitro detection of histone acylation via the aqueous oxidative Heck reaction". Organic & Biomolecular Chemistry 13, n.º 12 (2015): 3648–53. http://dx.doi.org/10.1039/c4ob02502d.
Texto completo da fonteVarner, 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, n.º 9 (setembro de 2020): 200187. http://dx.doi.org/10.1098/rsob.200187.
Texto completo da fonteLiu, Yuexia, Yizhou Li, Juntong Liang, Zhuwen Sun e Chao Sun. "Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning". International Journal of Molecular Sciences 23, n.º 21 (22 de outubro de 2022): 12733. http://dx.doi.org/10.3390/ijms232112733.
Texto completo da fonteWilson, John P., Anuradha S. Raghavan, Yu-Ying Yang, Guillaume Charron e 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, n.º 3 (14 de novembro de 2010): M110.001198. http://dx.doi.org/10.1074/mcp.m110.001198.
Texto completo da fonteBarnes, Claire E., David M. English e Shaun M. Cowley. "Acetylation & Co: an expanding repertoire of histone acylations regulates chromatin and transcription". Essays in Biochemistry 63, n.º 1 (abril de 2019): 97–107. http://dx.doi.org/10.1042/ebc20180061.
Texto completo da fonteDeng, 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, n.º 10 (28 de setembro de 2016): 1812–20. http://dx.doi.org/10.1021/acs.oprd.6b00280.
Texto completo da fonteBrewster, Richard C., e Alison N. Hulme. "Halomethyl-Triazoles for Rapid, Site-Selective Protein Modification". Molecules 26, n.º 18 (8 de setembro de 2021): 5461. http://dx.doi.org/10.3390/molecules26185461.
Texto completo da fonteGan, 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 de junho de 2021): 1–12. http://dx.doi.org/10.1155/2021/6652297.
Texto completo da fonteAleshin, V. A., D. A. Sibiryakina, A. V. Kazantsev, A. V. Graf e V. I. Bunik. "Acylation of the rat brain proteins is affected by the inhibition of pyruvate dehydrogenase <i>in vivo</i>". Биохимия 88, n.º 1 (15 de janeiro de 2023): 147–63. http://dx.doi.org/10.31857/s0320972523010116.
Texto completo da fonteRonan, Jade L., Nadia Kadi, Stephen A. McMahon, James H. Naismith, Lona M. Alkhalaf e Gregory L. Challis. "Desferrioxamine biosynthesis: diverse hydroxamate assembly by substrate-tolerant acyl transferase DesC". Philosophical Transactions of the Royal Society B: Biological Sciences 373, n.º 1748 (23 de abril de 2018): 20170068. http://dx.doi.org/10.1098/rstb.2017.0068.
Texto completo da fonteCrespo, 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, n.º 8 (17 de março de 2020): 4115–38. http://dx.doi.org/10.1093/nar/gkaa163.
Texto completo da fonteZhao, Shuai, Xingrun Zhang e Haitao Li. "Beyond histone acetylation—writing and erasing histone acylations". Current Opinion in Structural Biology 53 (dezembro de 2018): 169–77. http://dx.doi.org/10.1016/j.sbi.2018.10.001.
Texto completo da fonteSabari, Benjamin R., Di Zhang, C. David Allis e Yingming Zhao. "Metabolic regulation of gene expression through histone acylations". Nature Reviews Molecular Cell Biology 18, n.º 2 (7 de dezembro de 2016): 90–101. http://dx.doi.org/10.1038/nrm.2016.140.
Texto completo da fonteDutta, Arnob, Susan M. Abmayr e Jerry L. Workman. "Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function". Molecular Cell 63, n.º 4 (agosto de 2016): 547–52. http://dx.doi.org/10.1016/j.molcel.2016.06.038.
Texto completo da fonteFernandes, Mariane Font, e Marco Aurélio Ramirez Vinolo. "Histone acylations as a mechanism for regulation of intestinal epithelial cells". Digestive Medicine Research 7 (março de 2024): 4. http://dx.doi.org/10.21037/dmr-23-3.
Texto completo da fonteShi, Jiale, Xuemei Jia, Yujia He, Xinyue Ma, Xiaoyu Qi, Wan Li, Shou-Jiang Gao, Qin Yan e Chun Lu. "Immune evasion strategy involving propionylation by the KSHV interferon regulatory factor 1 (vIRF1)". PLOS Pathogens 19, n.º 4 (6 de abril de 2023): e1011324. http://dx.doi.org/10.1371/journal.ppat.1011324.
Texto completo da fontePeterson, Francis C., Dawei Chen, Betsy L. Lytle, Marianna N. Rossi, Ivan Ahel, John M. Denu e Brian F. Volkman. "Orphan Macrodomain Protein (Human C6orf130) Is an O-Acyl-ADP-ribose Deacylase". Journal of Biological Chemistry 286, n.º 41 (17 de agosto de 2011): 35955–65. http://dx.doi.org/10.1074/jbc.m111.276238.
Texto completo da fonteOlp, Michael D., Nan Zhu e Brian C. Smith. "Metabolically Derived Lysine Acylations and Neighboring Modifications Tune the Binding of the BET Bromodomains to Histone H4". Biochemistry 56, n.º 41 (5 de outubro de 2017): 5485–95. http://dx.doi.org/10.1021/acs.biochem.7b00595.
Texto completo da fonteWang, Bo, Po-Hsien Huang, Ching-Shih Chen e 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, n.º 4 (18 de fevereiro de 2011): 1140–50. http://dx.doi.org/10.1021/jo102478x.
Texto completo da fonteNelson, John, Neil V. McFerran, Géraldine Pivato, Emma Chambers, Caroline Doherty, David Steele e David J. Timson. "The 67 kDa laminin receptor: structure, function and role in disease". Bioscience Reports 28, n.º 1 (1 de fevereiro de 2008): 33–48. http://dx.doi.org/10.1042/bsr20070004.
Texto completo da fonteLIAU, Y. H., J. ZIELENSKI, S. R. CARTER, A. SLOMIANY e B. L. SLOMIANY. "Enzymatic Acylation of Mucus Glycoprotein in Rat Salivary Glands". Annals of the New York Academy of Sciences 494, n.º 1 Third Colloqu (maio de 1987): 345–47. http://dx.doi.org/10.1111/j.1749-6632.1987.tb29568.x.
Texto completo da fonteRICH, JOSEPH O., e JONATHAN S. DORDICK. "Controlling Regioselectivity in Enzyme-catalyzed Acylation of Polyhydroxyl Compounds". Annals of the New York Academy of Sciences 799, n.º 1 Enzyme Engine (outubro de 1996): 226–30. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33205.x.
Texto completo da fonteIto, Minami, Yuya Nishida, Tatsuya Iwamoto, Akiko Kanai, Shuhei Aoyama, Kyosei Ueki, Hirotsugu Uzawa, Hitoshi Iida e 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 (junho de 2024): 149960. http://dx.doi.org/10.1016/j.bbrc.2024.149960.
Texto completo da fonteHu, Bin, Han Gong, Chaoying Yang, Ling Nie, Ji Zhang, Long Liang, Mohandas Narla, Yue Sheng e Jing Liu. "Dynamic Changes in Lysine Succinylation As Important Regulators of Erythropoiesis". Blood 142, Supplement 1 (28 de novembro de 2023): 2448. http://dx.doi.org/10.1182/blood-2023-182646.
Texto completo da fonteDACQUET, CATHERINE, CHRISTELLE MACIA e MICHAEL SPEDDING. "Acylation Differentiates Two Forms of Agonist Binding to Rat 5-HT1AReceptors." Annals of the New York Academy of Sciences 812, n.º 1 Receptor Clas (maio de 1997): 178. http://dx.doi.org/10.1111/j.1749-6632.1997.tb48165.x.
Texto completo da fonteDUUREN, BENJAMIN L. "Direct-Acting Alkylating and Acylating Agents." Annals of the New York Academy of Sciences 534, n.º 1 Living in a C (junho de 1988): 620–34. http://dx.doi.org/10.1111/j.1749-6632.1988.tb30153.x.
Texto completo da fonteKODELIA, G., e 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, n.º 1 Enzyme Engine (novembro de 1992): 451–57. http://dx.doi.org/10.1111/j.1749-6632.1992.tb32712.x.
Texto completo da fonteZHUANG, YING-PING, JIAN-HE XU e 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, n.º 1 ENZYME ENGINE (dezembro de 1998): 656–59. http://dx.doi.org/10.1111/j.1749-6632.1998.tb10399.x.
Texto completo da fonteBhattacharya, Saikat, e Benjamin P. Tu. "Histone acylation at a glance". Journal of Cell Science 137, n.º 11 (1 de junho de 2024). http://dx.doi.org/10.1242/jcs.261250.
Texto completo da fonte