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Relevant bibliographies by topics / Histone acetylation

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Academic literature on the topic 'Histone acetylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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Journal articles on the topic "Histone acetylation"

1

Chicoine, L. G., R. Richman, R. G. Cook, M. A. Gorovsky, and C. D. Allis. "A single histone acetyltransferase from Tetrahymena macronuclei catalyzes deposition-related acetylation of free histones and transcription-related acetylation of nucleosomal histones." Journal of Cell Biology 105, no. 1 (1987): 127–35. http://dx.doi.org/10.1083/jcb.105.1.127.

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A salt-extracted histone acetyltransferase activity from Tetrahymena macronuclei acetylates mostly histone H3 and H4 when free histones are used as substrate. Free histone H4 is acetylated first at position 11 (monoacetylated) or positions 11 and 4 (diacetylated). This activity strongly resembles in vivo, deposition-related acetylation of newly synthesized histones. When acetylase-free mononucleosomes are used as substrate, all four core histones are acetylated by the same extract, and H4 is acetylated first at position 7 (monoacetylated) or positions 7 and 4 (diacetylated). In this respect, t

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2

Cuevas-Bennett, Christian, and Thomas Shenk. "Dynamic Histone H3 Acetylation and Methylation at Human Cytomegalovirus Promoters during Replication in Fibroblasts." Journal of Virology 82, no. 19 (2008): 9525–36. http://dx.doi.org/10.1128/jvi.00946-08.

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ABSTRACT Human cytomegalovirus DNA is packaged in virions without histones but associates with histones upon reaching the nucleus of an infected cell. Since transcription is modulated by the interplay of histone modifications, we used chromatin immunoprecipitation to detect acetylation and methylation of histone H3 at viral promoters at different times during the viral replication cycle. Histone H3 at immediate-early promoters is acetylated at the start of infection, while it is initially methylated at early and late promoters. Acetylation at immediate-early promoters is dynamic, with a high l

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Legartová, Soňa, Stanislav Kozubek, Michal Franek, et al. "Cell differentiation along multiple pathways accompanied by changes in histone acetylation status." Biochemistry and Cell Biology 92, no. 2 (2014): 85–93. http://dx.doi.org/10.1139/bcb-2013-0082.

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Post-translational modification of histones is fundamental to the regulation of basic nuclear processes and subsequent cellular events, including differentiation. In this study, we analyzed acetylated forms of histones H2A, H2B, and H4 during induced differentiation in mouse (mESCs) and human (hESCs) embryonic stem cells and during induced enterocytic differentiation of colon cancer cells in vitro. Endoderm-like differentiation of mESCs induced by retinoic acid and enterocytic differentiation induced by histone deacetylase inhibitor sodium butyrate were accompanied by increased mono-, di-, and

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Kring, Friedhelm, and Peter Böger. "Histone Acetylation is not Affected by Chloroacetamides in vitro." Zeitschrift für Naturforschung C 49, no. 5-6 (1994): 309–11. http://dx.doi.org/10.1515/znc-1994-5-605.

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Abstract The effects of chloroacetamides on the acetylation of histone protein in maize (Zea mays) were studied in an in vitro assay. Neither alachlor nor metazachlor showed any influence on both of the investigated acetylating enzymes, the nuclear histone acetyltransferase A and the cytoplasmic histone acetyltransferase B. Furthermore, an effect of these herbicides on deacetylation of histones could be excluded.

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Waterborg, Jakob H., and Tamás Kapros. "Kinetic analysis of histone acetylation turnover and Trichostatin A induced hyper- and hypoacetylation in alfalfa." Biochemistry and Cell Biology 80, no. 3 (2002): 279–93. http://dx.doi.org/10.1139/o02-021.

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Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially

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Demyanenko, Svetlana, and Svetlana Sharifulina. "The Role of Post-Translational Acetylation and Deacetylation of Signaling Proteins and Transcription Factors after Cerebral Ischemia: Facts and Hypotheses." International Journal of Molecular Sciences 22, no. 15 (2021): 7947. http://dx.doi.org/10.3390/ijms22157947.

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Histone deacetylase (HDAC) and histone acetyltransferase (HAT) regulate transcription and the most important functions of cells by acetylating/deacetylating histones and non-histone proteins. These proteins are involved in cell survival and death, replication, DNA repair, the cell cycle, and cell responses to stress and aging. HDAC/HAT balance in cells affects gene expression and cell signaling. There are very few studies on the effects of stroke on non-histone protein acetylation/deacetylation in brain cells. HDAC inhibitors have been shown to be effective in protecting the brain from ischemi

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Deckert, Jutta, and Kevin Struhl. "Histone Acetylation at Promoters Is Differentially Affected by Specific Activators and Repressors." Molecular and Cellular Biology 21, no. 8 (2001): 2726–35. http://dx.doi.org/10.1128/mcb.21.8.2726-2735.2001.

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ABSTRACT We analyzed the relationship between histone acetylation and transcriptional regulation at 40 Saccharomyces cerevisiaepromoters that respond to specific activators and repressors. In accord with the general correlation between histone acetylation and transcriptional activity, Gcn4 and the general stress activators (Msn2 and Msn4) cause increased acetylation of histones H3 and H4. Surprisingly, Gal4-dependent activation is associated with a dramatic decrease in histone H4 acetylation, whereas acetylation of histone H3 is unaffected. A specific decrease in H4 acetylation is also observe

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Ito, Takashi, Tsuyoshi Ikehara, Takeya Nakagawa, W. Lee Kraus, and Masami Muramatsu. "p300-Mediated acetylation facilitates the transfer of histone H2A–H2B dimers from nucleosomes to a histone chaperone." Genes & Development 14, no. 15 (2000): 1899–907. http://dx.doi.org/10.1101/gad.14.15.1899.

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We have used a purified recombinant chromatin assembly system, including ACF (Acf-1 + ISWI) and NAP-1, to examine the role of histone acetylation in ATP-dependent chromatin remodeling. The binding of a transcriptional activator (Gal4–VP16) to chromatin assembled using this recombinant assembly system dramatically enhances the acetylation of nucleosomal core histones by the histone acetyltransferase p300. This effect requires both the presence of Gal4-binding sites in the template and the VP16-activation domain. Order-of-addition experiments indicate that prior activator-meditated, ATP-dependen

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Abaturov, O. E., and A. O. Nikulina. "Histones post-translational modifications associated with the development of metabolic dysfunction-associated fatty liver disease. Part 3. Histon acetylation." GASTROENTEROLOGY 59, no. 1 (2025): 56–67. https://doi.org/10.22141/2308-2097.59.1.2025.664.

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Based on the analysis of literature sources from the Pubmed, MEDLINE, The Cochrane Library, Embase databases, the authors of the article highlight general provisions regarding histone acetylation. They emphasize that it is acetylation of the lysine residue that is the key post-translational modification of histones by epigenetic mechanisms of gene expression regulation. To date, at least 2000 human proteins have been identified that can be modified at lysine residues by acetylation. About 1000 proteins in human liver tissue undergo modification by lysine acetylation. Acetylation is mediated by

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CraneRobinson, Colyn. "Playing tag: Histone acetylation." Biochemist 29, no. 4 (2007): 9–13. http://dx.doi.org/10.1042/bio02904009.

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Acetylation of the e-amino group of specific lysine residues of core histones – principally but not exclusively in their unstructured N-terminal tails – is a key biochemical modification for establishing the transcriptional competence of genes bound by such histones. High resolution mapping of acetylated core histones by chromatin IPs (ChIPs) has shown them to be preferentially located at the promoters and enhancers of active genes rather than throughout the transcribed regions. Particular distributions of acetylated lysines are part of the nucleosomal ‘histone code’ that defines and to a cons

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Dissertations / Theses on the topic "Histone acetylation"

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Choi, Jennifer Kristel. ""Open" chromatin : histone acetylation, linker histones & histone variants." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/45271.

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Man, Pui-sum Ellen. "Histone acetylation in gynaecological malignancies." Click to view the E-thesis via HKUTO, 2004. http://sunzi.lib.hku.hk/hkuto/record/B31972068.

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Cervoni, Nadia. "DNA demethylation and histone acetylation." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=38166.

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Unlike in somatic cells, cancer cells adopt an aberrant pattern of methylation as well as histone acetylation, and therefore distort the chromatin structure. Chapters 2--4 of this thesis look at mechanisms carried out by the recently cloned DNA demethylase, how its demethylation activity is closely linked with the semblance of acetylation of chromatin, and how this relationship can be skewed in cancer. The three intriguing mechanisms described provide attractive models by which to explain general genome wide demethylation, site specific demethylation of genes upon their activation, and the rel

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Man, Pui-sum Ellen, and 萬佩心. "Histone acetylation in gynaecological malignancies." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2004. http://hub.hku.hk/bib/B31972068.

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Venkataraman, Shanmugasundaram. "Histone acetylation and nucleosome dynamics." Thesis, University of Edinburgh, 2001. http://hdl.handle.net/1842/23234.

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In this report, I will describe purification of core histone octamers from chicken blood, HeLa nuclei and yeast cells, along with preparation of DNA fragments containing the 208 bp 5S rDNA gene and the adult beta (b<sup>A</sup>)-globin gene promoter. <i>In vitro</i> experiments studying the effect of histone acetylation on the positioning and mobility of nucleosomes on the sea urchin 5S rDNA gene and the chicken b<sup>A</sup>-globin gene promoter will be described. The former provides a well studied nucleosome positioning and mobility model system, while the latter is a developmentally regulat

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Hebbes, T. R. "Histone acetylation and transcriptionally active chromatin." Thesis, University of Portsmouth, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.382541.

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Clayton, Alison Louise. "Core histone acetylation of active genes." Thesis, University of Portsmouth, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240358.

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Choudhury, Mahua Shukla Shivendra D. "Alcohol induced histone acetylation mediated by histone acetyl transferase GCN5 in liver." Diss., Columbia, Mo. : University of Missouri-Columbia, 2008. http://hdl.handle.net/10355/6866.

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The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from PDF of title page (University of Missouri--Columbia, viewed on April 6, 2010). Vita. Thesis advisor: Shivendra D. Shukla. "August 2008" Includes bibliographical references

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Ou, Jing Ni. "Epigenetic crosstalk between DNA demethylation and histone acetylation." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=32413.

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Abnormal methylation patterns such as regional hypermethylation and genomic hypomethylation often result in transcriptional changes of critical genes that are central to the progression of human cancers. It is therefore important to identify the mechanisms that are responsible for the alterations in order to identify proper pharmacological targets. This thesis examines whether specific cellular factors are involved in establishing the state of DNA hypomethylation in cancer cells and whether changes in chr

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Smith, Anna Elizabeth. "The role of histone acetylation in recognition memory." Thesis, University of Bristol, 2016. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.715770.

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Books on the topic "Histone acetylation"

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Gregory, Bock, Goode Jamie, Novartis Foundation, and Symposium on Reversible Protein Acetylation (2003 London, England), eds. Reversible protein acetylation. Wiley, 2004.

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2

O'Neill, Laura Patricia. Histone acetylation and transcription in Eukaryotic cells. University of Birmingham, 1994.

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Halasa, Marta, and Anna Wawruszak, eds. Histone and Non-Histone Reversible Acetylation in Development, Aging and Disease. Springer Nature Switzerland, 2025. https://doi.org/10.1007/978-3-031-91459-1.

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4

Johnson, Helen Louise. Site-specific acetylation of histone H4 and its functional significance. University of Birmingham, 1997.

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5

Evans, Dain R. Targeted and widespread acetylation of histones H3 and H4 at the chicken [beta]-globin locus. Institute of Biomedical and Biomolecular Sciences, 2001.

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6

Berlin, Freie Universität, ed. A new approach to the function of histone acetylation. 1987.

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7

Johnston, Michael V. Coffin-Lowry Syndrome. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0057.

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Coffin-Lowry syndrome (CLS) is a relatively rare (1:50,000-100,000 incidence) sex-linked neurodevelopmental disorder that includes severe intellectual disability, dysmorphic features including facial and digital abnormalities, growth retardation, and skeletal changes. Most cases are sporadic with only 20% to 30% of cases having an additional family member. CLS is caused by variable loss of function mutations in the RPS6KA3 gene that maps to Xp22.2 and codes for the hRSK2 S6 kinase that phosphorylates the transcription factor CREB (cAMP response element binding protein) as well as other nuclear

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Book chapters on the topic "Histone acetylation"

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Turner, Bryan M. "Histone Acetylation." In Genome Structure and Function. Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5550-2_8.

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Wang, Shaowen, Yan Yan-Neale, Marija Zeremski, and Dalia Cohen. "Transcription Regulation by Histone Deacetylases." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch18.

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Marks, Paul A., Victoria M. Richon, Wm Kevin Kelly, Judy H. Chiao, and Thomas Miller. "Histone Deacetylase Inhibitors: Development as Cancer Therapy." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch20.

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Schotta, Gunnar, Monika Lachner, Antoine H. F. M. Peters, and Thomas Jenuwein. "The Indexing Potential of Histone Lysine Methylation." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch3.

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Marmorstein, Ronen. "Structural and Chemical Basis of Histone Acetylation." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch6.

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Kiss, Anna K. "Polyphenols and Histone Acetylation." In Handbook of Nutrition, Diet, and Epigenetics. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-55530-0_105.

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Kiss, Anna K. "Polyphenols and Histone Acetylation." In Handbook of Nutrition, Diet, and Epigenetics. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-31143-2_105-1.

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Wang, Yanming, Wolfgang Fischle, Wang Cheung, Steven Jacobs, Sepideh Khorasanizadeh, and C. David Allis. "Beyond the Double Helix: Writing and Reading the Histone Code." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch2.

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McKinsey, Timothy A., and Eric N. Olson. "Dual Roles of Histone Deacetylases in the Control of Cardiac Growth." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch9.

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Mahadevan, Louis C., Alison L. Clayton, Catherine A. Hazzalin, and Stuart Thomson. "Phosphorylation and Acetylation of Histone H3 at Inducible Genes: Two Controversies Revisited." In Reversible Protein Acetylation. John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch7.

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Conference papers on the topic "Histone acetylation"

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Price, Bo J. "Histone binding factor ENAP1 retrains seed germination through ABI5 dependent histone acetylation regulation." In ASPB PLANT BIOLOGY 2020. ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1048264.

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Deng, Yangyang, and Xianhua Dai. "Similar Histone Acetylation Pattern of Neighboring Genes in Yeast." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.91.

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Stefanowicz, Dorota, Tillie-Louise Hackett, Peter D. Paré, and Darryl A. Knight. "Alterations In Histone Acetylation In Asthmatic Airway Epithelial Cells." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1448.

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Zakarya, R., H. Chen, C. A. A. Brandsma, I. M. Adcock, and B. G. G. Oliver. "Small Airway Fibrosis in COPD Is Mediated by Histone Acetylation." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5776.

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Purushothaman, Anurag, and Ralph D. Sanderson. "Abstract A17: Glycosaminoglycans regulates histone acetylation status in multiple myeloma." In Abstracts: AACR Special Conference on Chromatin and Epigenetics in Cancer - June 19-22, 2013; Atlanta, GA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.cec13-a17.

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Carrer, Alessandro, Joyce V. Lee, Supriya Shah, et al. "Abstract PR03: Exploring the link between Kras and histone acetylation." In Abstracts: AACR Special Conference: Chromatin and Epigenetics in Cancer; September 24-27, 2015; Atlanta, GA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.chromepi15-pr03.

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Roccaro, Aldo M., Antonio Sacco, Abdel Kareem Azab, et al. "Abstract 2060: microRNA-dependent modulation of histone acetylation in Waldenstrom's Macroglobulinemia." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2060.

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Zakarya, R., Y. L. Chan, H. Chen, C. A. A. Brandsma, I. M. Adcock, and B. G. G. Oliver. "BET Protein Propagated Histone Acetylation Mediates ECM Changes in COPD Airways." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6431.

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Shah, Supriya, Joyce V. Lee, Alessandro Carrer, Nathaniel W. Snyder, and Kathryn E. Wellen. "Abstract A31: Akt-dependent metabolic reprogramming regulates tumor cell histone acetylation." In Abstracts: AACR Special Conference: Targeting the PI3K-mTOR Network in Cancer; September 14-17, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.pi3k14-a31.

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Carrer, Alessandro, Joyce V. Lee, Supriya Shah, et al. "Abstract B40: Oncogenic Kras induces histone acetylation in pancreatic ductal adenocarcinoma." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-b40.

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Reports on the topic "Histone acetylation"

1

Kovacs, Jeffrey J. Regulation of EGF Receptor Signaling by Histone Deacetylase 6 (HDAC6)-Mediated Reversible Acetylation. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada435267.

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Meiri, Noam, Michael D. Denbow, and Cynthia J. Denbow. Epigenetic Adaptation: The Regulatory Mechanisms of Hypothalamic Plasticity that Determine Stress-Response Set Point. United States Department of Agriculture, 2013. http://dx.doi.org/10.32747/2013.7593396.bard.

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Our hypothesis was that postnatal stress exposure or sensory input alters brain activity, which induces acetylation and/or methylation on lysine residues of histone 3 and alters methylation levels in the promoter regions of stress-related genes, ultimately resulting in long-lasting changes in the stress-response set point. Therefore, the objectives of the proposal were: 1. To identify the levels of total histone 3 acetylation and different levels of methylation on lysine 9 and/or 14 during both heat and feed stress and challenge. 2. To evaluate the methylation and acetylation levels of histone

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