Relevant bibliographies by topics / Hyperacetylation

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'Hyperacetylation'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "Hyperacetylation"

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Sudo, Haruka, and Akira Kubo. "The Aneugenicity of Ketone Bodies in Colon Epithelial Cells Is Mediated by Microtubule Hyperacetylation and Is Blocked by Resveratrol." International Journal of Molecular Sciences 22, no. 17 (2021): 9397. http://dx.doi.org/10.3390/ijms22179397.

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Diabetes mellitus (DM) is considered to be associated with an increased risk of colorectal cancer. Recent studies have also revealed that tubulin hyperacetylation is caused by a diabetic status and we have reported previously that, under microtubule hyperacetylation, a microtubule severing protein, katanin-like (KL) 1, is upregulated and contributes to tumorigenesis. To further explore this phenomenon, we tested the effects of the ketone bodies, acetoacetate and β-hydroxybutyrate, in colon and fibroblast cells. Both induced microtubule hyperacetylation that responded differently to a histone d
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Rao, Rekha, Warren Fiskus, Yonghua Yang, et al. "HDAC6 inhibition enhances 17-AAG–mediated abrogation of hsp90 chaperone function in human leukemia cells." Blood 112, no. 5 (2008): 1886–93. http://dx.doi.org/10.1182/blood-2008-03-143644.

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Abstract Histone deacetylase 6 (HDAC6) is a heat shock protein 90 (hsp90) deacetylase. Treatment with pan-HDAC inhibitors or depletion of HDAC6 by siRNA induces hyperacetylation and inhibits ATP binding and chaperone function of hsp90. Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins. In this study, we determined the effect of hsp90 hyperacetylation on the anti-hsp90 and antileukemia activity of 17-AAG. Hyperacetylation of hsp90 increased i
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Calestagne-Morelli, Alison, and Juan Ausió. "Long-range histone acetylation: biological significance, structural implications, and mechanismsThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (2006): 518–27. http://dx.doi.org/10.1139/o06-067.

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Genomic characterization of various euchromatic regions in higher eukaryotes has revealed that domain-wide hyperacetylation (over several kb) occurs at a range of loci, including individual genes, gene family clusters, compound clusters, and more general clusters of unrelated genes. Patterns of long-range histone hyperacetylation are strictly conserved within each unique cellular system studied and they reflect biological variability in gene regulation. Domain-wide histone acetylation consists generally of nonuniform peaks of enriched hyperacetylation of specific core histones, histone isoform
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Lutter, L. C., L. Judis, and R. F. Paretti. "Effects of histone acetylation on chromatin topology in vivo." Molecular and Cellular Biology 12, no. 11 (1992): 5004–14. http://dx.doi.org/10.1128/mcb.12.11.5004-5014.1992.

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Recently a model for eukaryotic transcriptional activation has been proposed in which histone hyperacetylation causes release of nucleosomal supercoils, and this unconstrained tension in turn stimulates transcription (V. G. Norton, B. S. Imai, P. Yau, and E. M. Bradbury, Cell 57:449-457, 1989; V. G. Norton, K. W. Marvin, P. Yau, and E. M. Bradbury, J. Biol. Chem. 265:19848-19852, 1990). These studies analyzed the effect of histone hyperacetylation on the change in topological linking number which occurs during nucleosome assembly in vitro. We have tested this model by determining the effect of
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Lutter, L. C., L. Judis, and R. F. Paretti. "Effects of histone acetylation on chromatin topology in vivo." Molecular and Cellular Biology 12, no. 11 (1992): 5004–14. http://dx.doi.org/10.1128/mcb.12.11.5004.

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Recently a model for eukaryotic transcriptional activation has been proposed in which histone hyperacetylation causes release of nucleosomal supercoils, and this unconstrained tension in turn stimulates transcription (V. G. Norton, B. S. Imai, P. Yau, and E. M. Bradbury, Cell 57:449-457, 1989; V. G. Norton, K. W. Marvin, P. Yau, and E. M. Bradbury, J. Biol. Chem. 265:19848-19852, 1990). These studies analyzed the effect of histone hyperacetylation on the change in topological linking number which occurs during nucleosome assembly in vitro. We have tested this model by determining the effect of
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Kajino, Hidetoshi, Tomomi Nagatani, Miku Oi, et al. "Synthetic hyperacetylation of nucleosomal histones." RSC Chemical Biology 1, no. 2 (2020): 56–59. http://dx.doi.org/10.1039/d0cb00029a.

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Na, Ann-Yae, Sanjita Paudel, Soyoung Choi, et al. "Global Lysine Acetylome Analysis of LPS-Stimulated HepG2 Cells Identified Hyperacetylation of PKM2 as a Metabolic Regulator in Sepsis." International Journal of Molecular Sciences 22, no. 16 (2021): 8529. http://dx.doi.org/10.3390/ijms22168529.

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Sepsis-induced liver dysfunction (SILD) is a common event and is strongly associated with mortality. Establishing a causative link between protein post-translational modification and diseases is challenging. We studied the relationship among lysine acetylation (Kac), sirtuin (SIRTs), and the factors involved in SILD, which was induced in LPS-stimulated HepG2 cells. Protein hyperacetylation was observed according to SIRTs reduction after LPS treatment for 24 h. We identified 1449 Kac sites based on comparative acetylome analysis and quantified 1086 Kac sites on 410 proteins for acetylation. Int
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Sudo, Haruka. "Microtubule Hyperacetylation Enhances KL1-Dependent Micronucleation under a Tau Deficiency in Mammary Epithelial Cells." International Journal of Molecular Sciences 19, no. 9 (2018): 2488. http://dx.doi.org/10.3390/ijms19092488.

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Enhanced microtubule acetylation has been identified as a negative prognostic indicator in breast cancer. We reported previously that primary cultured human mammary epithelial cells manifest breast cancer-related aneuploidization via the activation of severing protein katanin-like (KL)1 when tau is deficient. To address in this current study whether microtubule hyperacetylation is involved in breast carcinogenesis through mitosis, the effects of tubacin on human mammary epithelial cells were tested using immunofluorescence techniques. Tau-knockdown cells showed enhancement of KL1-dependent eve
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Wu, James T., Sonia Y. Archer, Brian Hinnebusch, Shufen Meng, and Richard A. Hodin. "Transient vs. prolonged histone hyperacetylation: effects on colon cancer cell growth, differentiation, and apoptosis." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 3 (2001): G482—G490. http://dx.doi.org/10.1152/ajpgi.2001.280.3.g482.

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The role of histone hyperacetylation in regard to growth, differentiation, and apoptosis in colon cancer cells was assessed in an in vitro model system. HT-29 cells were grown in ±10% fetal bovine serum with either 5 mM sodium butyrate or 0.3 μM trichostatin A [single dose (T) or 3 doses 8 h apart (TR)] for 24 h. Serum-starved HT-29 cells were further treated with epidermal growth factor or insulin-like growth factor I for an additional 24 h. Apoptosis was quantified with propidium iodide and characterized by electron microscopy. Northern blot analyses were performed with cDNA probes specific
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Gupta, Ramesh C., Kristina Szekely, Kefei Zhang, David E. Lanfear, and Hani N. Sabbah. "Evidence of Hyperacetylation of Mitochondrial Regulatory Proteins in Left Ventricular Myocardium of Dogs with Chronic Heart Failure." International Journal of Molecular Sciences 26, no. 8 (2025): 3856. https://doi.org/10.3390/ijms26083856.

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Increased acetylation or “hyperacetylation” of mitochondrial (MITO) proteins can lead to abnormalities of the electron transport chain (ETC) and oxidative phosphorylation. In this study we examined the levels of proteins that regulate acetylation. Studies were performed in isolated MITO fractions from left ventricular (LV) myocardium of seven healthy normal (NL) dogs and seven dogs with coronary microembolization-induced heart failure (HF, LV ejection fraction ~35%). Protein levels of drivers of hyperacetylation, namely sirtuin-3 (Sirt-3), a MITO deacetylase, and CD38, a regulator of nicotinam
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Dissertations / Theses on the topic "Hyperacetylation"

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Thompson, John William. "DNA Fragmentation and Histone Hyperacetylation in the Hypoxic-Acidotic Cardiomyocyte." Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_dissertations/169.

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Bnip3 is a BH3-only member of the Bcl-2 family of apoptotic proteins. Our laboratory has previously shown that Bnip3 induces a unique pathway of cardiac myocyte cell death, characterized by mitochondrial dysfunction, cytochrome c release and DNA fragmentation. Bnip3 is induced by hypoxia and the death pathway is activated by concurrent acidosis. We have shown that hypoxia-acidosis creates an environment that is permissive to calpain but not caspase activation and is characterized by enhanced DNase(s) activity as evidenced by genomic DNA fragmentation. This dissertation describes the nuclear c
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Oliveira, Clara Slade. "Efeitos da hiperaceleração de histonas na diferenciação in vitro de células tronco embrionárias murinas /." Jaboticabal : [s.n.], 2009. http://hdl.handle.net/11449/98206.

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Orientador: Joaquim Mansano Garcia<br>Banca: Lígia Veiga Pereira<br>Banca: Irina Kerkis<br>Resumo: O estudo dos processos de diferenciação em células tronco embrionárias (CTE) representa uma importante ferramenta para o entendimento das vias moleculares que os regem, apresentando grande aplicação tanto na ciência básica quanto na engenharia de tecidos e medicina regenerativa. Pouco é conhecido sobre as marcas epigenéticas existentes na cromatina destas células, e de que forma a regulação da expressão gênica ocorre no momento da diferenciação. O presente trabalho teve como objetivo o estudo dos
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Oliveira, Clara Slade [UNESP]. "Efeitos da hiperaceleração de histonas na diferenciação in vitro de células tronco embrionárias murinas." Universidade Estadual Paulista (UNESP), 2009. http://hdl.handle.net/11449/98206.

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Made available in DSpace on 2014-06-11T19:29:16Z (GMT). No. of bitstreams: 0 Previous issue date: 2009-02-19Bitstream added on 2014-06-13T20:59:34Z : No. of bitstreams: 1 oliveira_cs_me_jabo.pdf: 1799127 bytes, checksum: 5a858a3a6eed3c27cf1b8f8968db5a50 (MD5)<br>Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)<br>O estudo dos processos de diferenciação em células tronco embrionárias (CTE) representa uma importante ferramenta para o entendimento das vias moleculares que os regem, apresentando grande aplicação tanto na ciência básica quanto na engenharia de tecidos e medicina rege
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Lin, Kuen-Tyng, and 林坤廷. "The epigenetic effects of trichostatin A-induced chromatin histone hyperacetylation on hepatocellular carcinoma cell migration." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/99561964352796142349.

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博士<br>國防醫學院<br>生命科學研究所<br>93<br>Trichostatin A (TSA), a histone deacetylase (HDAC) inhibitor, has been known to block cellular growth, induce apoptosis and inhibit cell migration in human cancer cell lines. In human hepatocellular carcinoma (HCC) cell lines, the effects of TSA treatment on cell migration are still unknown. In order to investigate the roles of epigenetic modulations, especially histone acetylation, on cancer genes participated in HCC metastasis, HCC cell lines were treated with different concentrations of TSA and in vitro migration activity was measured by using the transwell
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Sarikhani, Mohsen. "Understanding the Role of SIRT2 in Cardiac Hypertrophy, Cell Death and Glucose Homeostasis." Thesis, 2018. https://etd.iisc.ac.in/handle/2005/5424.

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Over the last century the major causes of human deaths and ailments has shifted from acute infectious diseases to chronic aging related disorders like cancer and type-2 diabetes. The aging process is a universal property of most organisms, accompanied by a subtle, progressive, and often irreversible decline of physiological and reproductive functions resulting in an increased vulnerability to environmental challenge and a growing risk of disease and death. In molecular terms, it can be understood as a decline of the homeostatic mechanisms that ensure the function of cells, tissues, organs, and
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Conference papers on the topic "Hyperacetylation"

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Reske, Jake J., Mike R. Wilson, and Ronald L. Chandler. "Abstract PO008: ARID1A prevents H3K27-hyperacetylation at active super-enhancers." In Abstracts: AACR Virtual Special Conference: Endometrial Cancer: New Biology Driving Research and Treatment; November 9-10, 2020. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1557-3265.endomet20-po008.

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Methot, Joey L., Melissa Chenard, Close Joshua, et al. "Abstract 5433: Prolonged histone hyperacetylation with a novel class of HDAC1/2 selective inhibitors." 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.am10-5433.

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Ordentlich, Peter. "Abstract PR-6: Pharmacodynamic analysis of ENCORE 301, a placebo-controlled, randomized phase 2 study of exemestane with and without entinostat in postmenopausal ER+ breast cancer patients demonstrates an association of lysine hyperacetylation with clinical outcome." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-pr-6.

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Ha, Kyungsoo, Warren Fiskus, Ramesh Balusu, Rekha Rao, Sreedhar Venkannagari, and Kapil N. Bhalla. "Abstract 4698: Inhibition of histone deacetylase (HDAC) 3 induces hyperacetylation and inhibition of nuclear heat shock protein (hsp) 90 leading to depletion of ATR and CHK1 with sensitization to DNA damage in breast and cervical cancer cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4698.

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