Academic literature on the topic 'Histone post-translational modifications (hPTMs)'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Histone post-translational modifications (hPTMs).'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Histone post-translational modifications (hPTMs)"
Hu, Qiwen, Casey S. Greene, and Elizabeth A. Heller. "Specific histone modifications associate with alternative exon selection during mammalian development." Nucleic Acids Research 48, no. 9 (April 22, 2020): 4709–24. http://dx.doi.org/10.1093/nar/gkaa248.
Full textAndonegui-Elguera, Marco A., Rodrigo E. Cáceres-Gutiérrez, Alejandro López-Saavedra, Fernanda Cisneros-Soberanis, Montserrat Justo-Garrido, José Díaz-Chávez, and Luis A. Herrera. "The Roles of Histone Post-Translational Modifications in the Formation and Function of a Mitotic Chromosome." International Journal of Molecular Sciences 23, no. 15 (August 5, 2022): 8704. http://dx.doi.org/10.3390/ijms23158704.
Full textGhiani, Lavinia, and Susanna Chiocca. "High Risk-Human Papillomavirus in HNSCC: Present and Future Challenges for Epigenetic Therapies." International Journal of Molecular Sciences 23, no. 7 (March 23, 2022): 3483. http://dx.doi.org/10.3390/ijms23073483.
Full textTibana, Ramires, Octávio Franco, Rinaldo Pereira, James Navalta, and Jonato Prestes. "Exercise as an Effective Transgenerational Strategy to Overcome Metabolic Syndrome in the Future Generation: Are We There?" Experimental and Clinical Endocrinology & Diabetes 125, no. 06 (May 11, 2017): 347–52. http://dx.doi.org/10.1055/s-0042-120538.
Full textTaylor, Bethany C., and Nicolas L. Young. "Combinations of histone post-translational modifications." Biochemical Journal 478, no. 3 (February 10, 2021): 511–32. http://dx.doi.org/10.1042/bcj20200170.
Full textHattori, Takamitsu, Joseph M. Taft, Kalina M. Swist, Hao Luo, Heather Witt, Matthew Slattery, Akiko Koide, et al. "Recombinant antibodies to histone post-translational modifications." Nature Methods 10, no. 10 (August 18, 2013): 992–95. http://dx.doi.org/10.1038/nmeth.2605.
Full textFan, Jing, Kimberly A. Krautkramer, Jessica L. Feldman, and John M. Denu. "Metabolic Regulation of Histone Post-Translational Modifications." ACS Chemical Biology 10, no. 1 (January 6, 2015): 95–108. http://dx.doi.org/10.1021/cb500846u.
Full textTolsma, Thomas O., and Jeffrey C. Hansen. "Post-translational modifications and chromatin dynamics." Essays in Biochemistry 63, no. 1 (March 22, 2019): 89–96. http://dx.doi.org/10.1042/ebc20180067.
Full textMéndez-Acuña, L., M. V. Di Tomaso, F. Palitti, and W. Martínez-López. "Histone Post-Translational Modifications in DNA Damage Response." Cytogenetic and Genome Research 128, no. 1-3 (2010): 28–36. http://dx.doi.org/10.1159/000296275.
Full textda Cunha, Julia Pinheiro Chagas, Ernesto Satoshi Nakayasu, Igor Correia de Almeida, and Sergio Schenkman. "Post-translational modifications of Trypanosoma cruzi histone H4." Molecular and Biochemical Parasitology 150, no. 2 (December 2006): 268–77. http://dx.doi.org/10.1016/j.molbiopara.2006.08.012.
Full textDissertations / Theses on the topic "Histone post-translational modifications (hPTMs)"
GHIANI, LAVINIA. "THE HISTONE POST-TRANSLATIONAL MODIFICATION LANDSCAPE IN HPV+ AND HPV- HEAD AND NECK SQUAMOUS CELL CARCINOMA: CHARACTERIZING THE ONCOGENIC ROLE OF THE H3K36ME2 METHYLTRANSFERASE NSD2." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/820678.
Full textParameswaran, Kalaivani Nithyha. "Understanding the mechanisms of histone modifications in vivo." Thesis, Strasbourg, 2016. http://www.theses.fr/2016STRAJ097/document.
Full textPost-translational modifications (PTMs) of histones have emerged as key players in the regulation of gene expression. However, little is known to what extent PTMs can directly impact chromatin. It has been suggested that PTMs of core histones (H2A, H2B, H3 and H4) have the potential to govern chromatin function according to the so called ‘‘histone code’’ hypothesis by recruiting specific binding proteins. The goal of my project is to gain insight in the function acetylation within the globular domain of H3 and to compare these modifications with histone tail modifications, in vivo by using the CRISPR in mouse embryonic stem cells (ES). To study the impact of PTMs in vivo, all endogenous wild type (WT) H3 gene copies have to be replaced with mutant copies. Hence, the primary focus of my project is to establish cell lines that exclusively express mutated H3 (e.g. mimicking acetylation) in order to study effects of H3 globular domain modifications on (a) gene expression (b) chromatin architecture as well as to study (c) cross talks and synergisms between globular domain modifications and (d) compare the effects with tail modifications in an vivo system
Bodey, Elijah D. "Evaluation of Cell Permeability of Intact Histone Complexes in Mammalian Cells." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1525705861000928.
Full textKurtz, Katryn Lucille. "Structure of chromatin, protein transitions, and post-translational histone modifications in several sperm models." Doctoral thesis, Universitat de Barcelona, 2008. http://hdl.handle.net/10803/1158.
Full textFor three different models using four marine species, protein transitions, chromatin condensation, and acetylation patterns were described during spermiogeneis. Specifically, changes in chromatin architecture and its protein complement was extensively studied using mainly transmission electron microscopy, inmunocytochemistry using anti-histone, anti-precursor protamine, and anti-acetyl group antibodies, as well as high resolution polyacrylamide gel electrophoresis (PAGE) and western blotting.
A model of specialized sperm chromatin (crustacean type) has been included in this study, since for decades this type of chromatin has remained poorly understood. Crustacean type sperm, once believed to have nuclei void of basic DNA-associated proteins, was found to contain histones, and is considered a derivation of the "H" model. Three species of brachyuran crabs from two different families were used to compositionally and ultrastructurally study this unusually decondensed mature sperm chromatin. Characterization of the histones from these sperm using HPLC and amino acid analysis confirm that the basic proteins extracted from sperm of these crabs are indeed typical and canonical histones, though some appear modified by post-translational modifications such as acetylation, which has never before been described in mature sperm. Additionally, in Maja brachydactyla, histones H3 and H2B appear in stoichiometric amounts different to what would be found in somatic chromatin. By performing micrococcal nuclease digestions, the presence of nucleosomes (or nucleosome-like particles) in the sperm of these species was confirmed, and demonstrated that histones are found interacting with the sperm DNA. Further, the histone/DNA ratio was evaluated in two Cancer species, and it was determined that these sperm only contain slightly over half the amount of basic protein per DNA unit compared to other sperm types. These results concerning the composition of the crustacean-type sperm chromatin help to explain its decondensed nature.
Minshull, Tom. "Studying the effects of severe sepsis on histone post translational modifications using mass spectrometry." Thesis, University of Sheffield, 2016. http://etheses.whiterose.ac.uk/13244/.
Full textBock, Ina [Verfasser]. "Recognition of post-translational histone modifications by antibodies and epigenetic reading domains / Ina Bock." Bremen : IRC-Library, Information Resource Center der Jacobs University Bremen, 2013. http://d-nb.info/1037013751/34.
Full textLópez, Ramos Rita. "Linker histone post-translational modifications and effects of phosphorylation on secondary structure and chromatin aggregation." Doctoral thesis, Universitat Autònoma de Barcelona, 2013. http://hdl.handle.net/10803/131313.
Full textLinker histones play an important role in establishing and maintaining chromatin higher-order structure and in transcriptional regulation. Histone H1 in vertebrates has a characteristic three-domain structure consisting of a short flexible N-terminal domain, a central globular domain and a long C-terminal domain. The amino- and carboxyl-terminal (CTD) domains are highly basic and mainly unstructured in aqueous solution. The charge distribution is quite uniform along the CTD. Because of that, chromatin condensation is mediated through charge-neutralization of the negatively charged linker DNA, facilitating chromatin condensation into the 30nm fibre and also intermolecular aggregation. Interaction with DNA induces the complete folding of the CTD under physiological conditions in a very stable manner, which allows to classify this domain as an intrinsically disordered protein, with coupled binding and folding. Post-translational phosphorylation of the CTD of H1 has effects on secondary structure and DNA condensation. Secondary structure of the entire H10 was analysed by infrared spectroscopy. H10, as the isolated CTD, also folded upon DNA interaction and the secondary structure was modulated by phosphorylation. The structural change following phosphorylation was characterized by an increase in the amount of β‐structure that was more significant when bound to DNA and was dependant on the protein/DNA ratio. The proportion of β‐structure reached 54 % suggesting that the CTD was in an all‐β conformation in the entire protein. Concomitant with the increase in β‐structure, there was a remarkable decrease of α‐helix that suggested the loss of some of the α‐helix in the globular domain; probably associated to the propagation of the β‐structure from the CTD towards the rest of the protein. In the presence of SDS, H10 folded with percentages of secondary structure motifs similar to those found when bound to DNA. At a molar ratio 14:1 (SDS/protein) the triphosphorylated protein had 55% of β‐structure indicating that the CTD within histone H10 was also in an all‐β conformation and formed amyloid fibres. Mature chicken erythrocyte nuclei contain highly condensed and inert chromatin, mainly consisting of DNA and histone proteins. Chicken erythrocyte chromatin was used to analyse linker histones post-translational modifications and the effect of phosphorylation by CDK2 on chromatin aggregation. The nuclei were digested with micrococcal nuclease and fractionated by centrifugation in low-salt buffer into soluble and insoluble fractions. Post-translational modifications (PTMs) of the purified linker histones of both fractions were analyzed by Tandem MS. All six histone H1 subtypes (H1.01, H1.02, H1.03, H1.10, H1.1L and H1.1R) and histone H5 were identified. In our study, we identified eight novel post-translational modifications: two were identified in histone H5 and six in histone H1 subtypes. Some of the identified modifications were specific of one chromatin fraction suggesting the differential distribution of some PTMs within chromatin. Comparison of the PTMs found with other previously reported for other species showed that most of them are conserved through evolution. Since histone H1 develops its function within chromatin; chicken erythrocyte chromatin was phosphorylated ex vivo with CDK2 in the S/T-P-X-Z motifs present in linker histones in order to study the effects of ex vivo phosphorylation of linker histones on chromatin aggregation. Proteomic analyses by HPCE and MALDITOF-MS showed that the the number of phosphate groups increased with the time of phosphorylation, reaching, in the case of H5, 54% of phosphorylated species (mono and diphosphorylated) after overnight phosphorylation. Tandem MS after proteolytic digestion revealed that in all linker histones the S/T-PX-Z motifs were unphosphorylated in native chromatin indicating that the phosphorylated peptides found at other times of reaction were modified ex vivo. In H5, only S148 was identified in all samples and was phosphorylated after 1 hour. In the Tandem MS analysis of histone H1 subtypes, all the CDK2 consensus sequences, except S171(H1.1R numbering) were identified for H1.03, H1.1L and H1.1R. H1.03T16 was found phosphorylated after 15 minutes; H1.1LS192 and H1.1RS186 after 1 hour; H1.03S155, H1.1LS155 and H1.1RS153 after3 hours. Once ex vivo phosphorylation of linker histones within chromatin was confirmed, the effect of linker histones ex vivo phosphorylation on chromatin aggregation induced by MgCl2 (1.6 mM) was analysed by Dynamic Light Scattering (DLS). The most remarkable result associated to ex vivo phosphorylation of linker histones within chromatin was a decrease in the hydrodynamic diameter of the aggregated molecules. The differences became greater with the increase of phosphorylation time and with the size of the chromatin fragments. These results indicated that linker histones phosphorylation impaired chromatin aggregation.
Shahidian, Lara [Verfasser], and Robert [Akademischer Betreuer] Schneider. "The role of novel histone post-translational modifications in transcription / Lara Shahidian ; Betreuer: Robert Schneider." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2020. http://d-nb.info/1236502051/34.
Full textKarim, Muhammed. "Study of the post-translational modifications of histone H4 by Fourier transform ion cyclotron resonance mass spectrometry." Thesis, University of Edinburgh, 2014. http://hdl.handle.net/1842/9780.
Full textGoudarzi, Afsaneh. "Male genome programming guided by histone acylations." Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAV059/document.
Full textThe main focus of the investigations reported in this manuscript is the understanding of the regulatory events that are based on histone lysine modifications in post-meiotic male germ cells, where specific and chromosome-wide regulations of gene expression occur. In the first part of my work we designed a strategy to specifically investigate the role of the histone acetyl-transferases (HATs), Cbp and p300, in post-meiotic male germ cells.Accordingly, we generated double Cbp and p300 conditional knock-out mice resulting in a partial depletion of Cbp and p300 in post-meiotic cells. Although the mice were fertile and spermatogenesis seemed to take place normally, a transcriptomic analysis of early and late post-meiotic germ cells led to the identification of a specific subset of genes with an increased expression in late spermatogenic cells that is highly sensitive to the decreased amounts of Cbp and p300. In conclusion, these results have revealed an interesting new gene expression program specific to post-meiotic male germ cells that are specifically regulated by the considered HATs.Taking into account the occurrence of a variety of histone lysine acylations, we extended these investigations to a four-carbon histone lysine modification, butyrylation. Accordingly, we have undertaken a comprehensive comparative analysis of histone H4 acetylation and butyrylation on its K5 and K8 positions in differentiating male germ cells. Genome-wide mapping of H4K5ac, H4K5bu, H4K8ac and H4K8bu at two critical developmental stages, meiotic and post-meiotic haploid cells, shows an interchangeable use of acetylation and butyrylation in the Transcriptional Start Sites (TSSs) of the most highly expressed genes in both meiotic and haploid round spermatids. Interestingly, many of these promoters are also bound by the essential regulator of spermatogenic gene expression, the BET bromodomain-containing factor, Brdt. A detailed analysis of Brdt binding capacity of H4 tails bearing various combinations of K5 and K8 acetylation and butyrylation showed that H4K5 butyrylation severely interferes with Brdt-binding. Our results therefore indicate that not only Brdt is required for the activation of a meiotic and post-meiotic gene expression program, but also its turnover induced by H4K5 butyrylation is equally important. This work hence highlights how an interplay between two different acylations occurring on the same lysines can play an essential regulatory role by increasing the chromatin binding dynamics of a critical lysine acetyl-reader, Brdt.Finally, in a collaborative work with structural biologists we showed that while p300 is a robust acetylase, its activity gets weaker with increasing acyl chain length. These results suggest that in vivo, p300 would use a specific co-factor to ensure non-acetyl histone acylations.Overall, these investigations shed an important light on how the male genome programming is guided by histone acylations and revealed for the first time a molecular network that regulates histone acylations and mediates its functional impact
Books on the topic "Histone post-translational modifications (hPTMs)"
Chess, Andrew, and Schahram Akbarian. The Human Brain and its Epigenomes. Edited by Dennis S. Charney, Eric J. Nestler, Pamela Sklar, and Joseph D. Buxbaum. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190681425.003.0003.
Full textBook chapters on the topic "Histone post-translational modifications (hPTMs)"
Senda, Toshiya, and Naruhiko Adachi. "Post-Translational Modifications, Histone." In Encyclopedia of Systems Biology, 1730. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_1490.
Full textRatnakumar, Kajan, Avnish Kapoor, and Emily Bernstein. "Regulation of Chromatin Structure and Transcription Via Histone Modifications." In Post-Translational Modifications in Health and Disease, 365–85. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6382-6_15.
Full textVidali, Giorgio, Nicoletta Ferrari, and Ulrich Pfeffer. "Histone Acetylation: A Step in Gene Activation." In Advances in Post-Translational Modifications of Proteins and Aging, 583–96. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-9042-8_49.
Full textZhou, Mowei, Si Wu, David L. Stenoien, Zhaorui Zhang, Lanelle Connolly, Michael Freitag, and Ljiljana Paša-Tolić. "Profiling Changes in Histone Post-translational Modifications by Top-Down Mass Spectrometry." In Methods in Molecular Biology, 153–68. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6518-2_12.
Full textTanguay, Robert M., and Richard Desrosiers. "Histone Methylation and Modulation of Gene Expression in Response to Heat Shock and Chemical Stress in Drosophila." In Advances in Post-Translational Modifications of Proteins and Aging, 353–62. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-9042-8_28.
Full textCastillo, Josefa, Gerardo López-Rodas, and Luis Franco. "Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions." In Advances in Experimental Medicine and Biology, 65–92. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/5584_2017_58.
Full textZhang, Yu, Wei Shen, Jin Zou, and Shibo Ying. "p300/CBP Methylation is Involved in the Potential Carcinogenic Mechanism of Lung Cancer." In Post-Translational Modifications in Cellular Functions and Diseases. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97241.
Full textMitchell, Amanda C., Yan Jiang, Cyril J. Peter, Ki A. Goosens, and Schahram Akbarian. "The Brain and Its Epigenome." In Neurobiology of Mental Illness, edited by Karl Deisseroth, 172–82. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199934959.003.0013.
Full textUmamaheswari, A., A. Puratchikody, and Sakthivel Balasubramaniyan. "Target Identification of HDAC8 Isoform for the Treatment of Cancer." In Advances in Medical Technologies and Clinical Practice, 140–72. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-7326-5.ch007.
Full textFarooq, Zeenat, Ambreen Shah, Mohammad Tauseef, Riyaz A. Rather, and Mumtaz Anwar. "Evolution of Epigenome as the Blueprint for Carcinogenesis." In Epigenetics - “A Parallel Universe” in the Study of Cancer Biology [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97379.
Full textConference papers on the topic "Histone post-translational modifications (hPTMs)"
Beaudet, Lucille, Jean-Philippe Lévesque Sergerie, Marie Boulé, Anne Labonté, Jean-François Michaud, Nathalie Rouleau, and Mathieu Arcand. "Abstract 3879: High-throughput, homogeneousin cytoassays to monitor histone H3 post-translational modifications." 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.am2012-3879.
Full textXu, Songhui, Lingling Fan, Xiaolu Cui, Fengbo Zhang, Arif Hussain, Ladan Fazli, Martin Gleave, and Jianfei Qi. "Abstract 4389: Post-translational modifications of histone demethylase JMJD1A in prostate cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4389.
Full textXu, Songhui, Lingling Fan, Xiaolu Cui, Fengbo Zhang, Arif Hussain, Ladan Fazli, Martin Gleave, and Jianfei Qi. "Abstract 4389: Post-translational modifications of histone demethylase JMJD1A in prostate cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4389.
Full textCarrero, Gustavo, Nikhil Raghuram, John Th’ng, Michael Hendzel, Theodore E. Simos, George Psihoyios, and Ch Tsitouras. "A Method for Assessing Kinetic Changes of Histone H1 after Post-Translational Modifications." In NUMERICAL ANALYSIS AND APPLIED MATHEMATICS: International Conference on Numerical Analysis and Applied Mathematics 2009: Volume 1 and Volume 2. AIP, 2009. http://dx.doi.org/10.1063/1.3241319.
Full textDavies, GF, AR Ross, BH Juurlink, and HA Troy. "The thiazolidinedione peroxisome proliferator-activated receptor gamma (PPARγ) agonist troglitazone alters histone post-translational modifications in MCF7 breast cancer cells." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-2140.
Full text