H2AFB1 Polyclonal Antibody (Catalog # A62726)

Total Page：16

File Type：pdf, Size：1020Kb

H2AFB1 Polyclonal Antibody (Catalog # A62726)

EPIGENTEK USA Tel: 1-877-374-4368 Int. Tel: 1-718-484-3990 Complete Solutions for Epigenetics [email protected] www.epigentek.com H2AFB1 Polyclonal Antibody (Catalog # A62726) Background Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis. Description H2AFB1 Polyclonal Antibody. Unconjugated. Raised in: Rabbit. Formulation Liquid. 0.03% Proclin 300, 50% Glycerol, 0.01M PBS, PH 7.4. Specificity Human Isotype IgG Uniprot ID P0C5Y9 Purification >95%, Protein G purified Immunogen Recombinant Human Histone H2A-Bbd type 1 protein (1-115AA) Storage Shipped at 4°C. Upon delivery aliquot and store at -20°C (short-term) or -80°C (long-term). Avoid repeated freeze. Alternative Names Histone H2A-Bbd type 1, H2A Barr body-deficient, H2A.Bbd, H2AFB1 Application ELISA, IHC, IF; Recommended dilution: IHC:1:20-1:200, IF:1:50-1:200 This product is for research purposes only. Not intended for use in diagnostic procedures. 2020-11-19-A62726 Immunohistochemistry of paraffin-embedded human liver tissue using H2AFB1 Polyclonal Antibody at dilution of 1:100 Immunofluorescent analysis of MCF-7 cells using H2AFB1 Polyclonal Antibody at a dilution of 1:100 and Alexa Fluor 488- congugated AffiniPure Goat Anti-Rabbit IgG (H+L) This product is for research purposes only. Not intended for use in diagnostic procedures. 2020-11-19-A62726 .

Copy Link

Recommended publications

A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
[Show full text]
Histone H2A Bbd (H2AFB1) (NM 001017990) Human Recombinant Protein Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TP316020 Histone H2A Bbd (H2AFB1) (NM_001017990) Human Recombinant Protein Product data: Product Type: Recombinant Proteins Description: Recombinant protein of human H2A histone family, member B1 (H2AFB1) Species: Human Expression Host: HEK293T Tag: C-Myc/DDK Predicted MW: 12.5 kDa Concentration: >50 ug/mL as determined by microplate BCA method Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol Preparation: Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps. Storage: Store at -80°C. Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. RefSeq: NP_001017990 Locus ID: 474382 UniProt ID: P0C5Y9 RefSeq Size: 517 Cytogenetics: Xq28 RefSeq ORF: 345 Synonyms: H2A.B; H2A.Bbd; H2AFB1 This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 Histone H2A Bbd (H2AFB1) (NM_001017990) Human Recombinant Protein – TP316020 Summary: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4).
[Show full text]
Charakterisierung Der Interaktion Der Merkelzell-Polyomavirus Kodierten T-Antigene Mit Dem Wirtsfaktor Kap1 Svenja Siebels
Charakterisierung der Interaktion der Merkelzell-Polyomavirus kodierten T-Antigene mit dem Wirtsfaktor Kap1 DISSERTATION zur Erlangung des Doktorgrades (Dr. rer. nat.) an der Fakultät für Mathematik, Informatik und Naturwissenschaften Fachbereich Biologie der Universität Hamburg vorgelegt von Svenja Siebels Hamburg, Juli 2018 Gutachter: Prof. Dr. Nicole Fischer Prof. Dr. Thomas Dobner Disputation: 19. Oktober 2018 Für meine Familie. Zusammenfassung Das Merkelzell-Polyomavirus (MCPyV) ist nachweislich für ca. 80 % aller Merkelzellkarzinome (Merkel cell carcinoma (MCC)) verantwortlich. Das virale Genom ist dabei monoklonal in die DNA der Wirtszelle integriert und trägt zusätzlich charakteristische Mutationen im T-Lokus. Das MCPyV kodiert wie alle Polyomaviren (PyV) die Tumor-Antigene (T-Ag) Large T-Ag und small T-Ag, die transformierende Eigenschaften besitzen. Dennoch sind viele Fragen zur MCC-Entstehung weiterhin ungeklärt. Insbesondere die Ursprungszelle, aus der das MCC hervorgeht, ist ungewiss. Das unvollständige Wissen um den viralen Lebenszyklus sowie die kontroversen Modelle hinsichtlich des Reservoirs des Virus erschweren zusätzlich das Verständnis zur Tumorentstehung. Um das transformierende Potential des MCPyV LT-Ags zu beleuchten, wurden vor Beginn dieser Arbeit neue zelluläre Interaktionspartner des LT-Ags mithilfe von Tandem-Affinitäts-Aufreinigung und anschließender multidimensionaler Protein-Interaktions-Technologie (MudPIT) identifiziert (M. Czech-Sioli, Manuskript in Arbeit). Unter den Kandidaten befand sich das Chromatin-modifizierende Protein, Zellzyklusregulator und Korepressor Kap1 (KRAB-associated protein 1) als putativer Interaktionspartner des LT-Ags. Die Interaktion des LT-Ags, sT-Ags und des verkürzten tLT-Ags (tLT-Ags) mit dem Wirtsfaktor Kap1 wurde in dieser Arbeit mithilfe von Koimmunpräzipitationen in unterschiedlichen Tumorzelllinien bestätigt. Weiterhin wurde die Bindung des LT-Ags an Kap1 auf den N-Terminus des LT-Ags und die RBCC-Domäne von Kap1 eingegrenzt.
[Show full text]
Chew Et Al-2021-Nature Communi
Short H2A histone variants are expressed in cancer Guo-Liang Chew, Marie Bleakley, Robert Bradley, Harmit Malik, Steven Henikoff, Antoine Molaro, Jay Sarthy To cite this version: Guo-Liang Chew, Marie Bleakley, Robert Bradley, Harmit Malik, Steven Henikoff, et al.. Short H2A histone variants are expressed in cancer. Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.490. 10.1038/s41467-020-20707-x. hal-03118929 HAL Id: hal-03118929 https://hal.archives-ouvertes.fr/hal-03118929 Submitted on 22 Jan 2021 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ARTICLE https://doi.org/10.1038/s41467-020-20707-x OPEN Short H2A histone variants are expressed in cancer Guo-Liang Chew 1, Marie Bleakley2, Robert K. Bradley 3,4,5, Harmit S. Malik4,6, Steven Henikoff 4,6, ✉ ✉ Antoine Molaro 4,7 & Jay Sarthy 4 Short H2A (sH2A) histone variants are primarily expressed in the testes of placental mammals. Their incorporation into chromatin is associated with nucleosome destabilization and modulation of alternate splicing. Here, we show that sH2As innately possess features similar to recurrent oncohistone mutations associated with nucleosome instability. Through 1234567890():,; analyses of existing cancer genomics datasets, we ﬁnd aberrant sH2A upregulation in a broad array of cancers, which manifest splicing patterns consistent with global nucleosome destabilization.
[Show full text]
Characterizing Genomic Duplication in Autism Spectrum Disorder by Edward James Higginbotham a Thesis Submitted in Conformity
Characterizing Genomic Duplication in Autism Spectrum Disorder by Edward James Higginbotham A thesis submitted in conformity with the requirements for the degree of Master of Science Graduate Department of Molecular Genetics University of Toronto © Copyright by Edward James Higginbotham 2020 i Abstract Characterizing Genomic Duplication in Autism Spectrum Disorder Edward James Higginbotham Master of Science Graduate Department of Molecular Genetics University of Toronto 2020 Duplication, the gain of additional copies of genomic material relative to its ancestral diploid state is yet to achieve full appreciation for its role in human traits and disease. Challenges include accurately genotyping, annotating, and characterizing the properties of duplications, and resolving duplication mechanisms. Whole genome sequencing, in principle, should enable accurate detection of duplications in a single experiment. This thesis makes use of the technology to catalogue disease relevant duplications in the genomes of 2,739 individuals with Autism Spectrum Disorder (ASD) who enrolled in the Autism Speaks MSSNG Project. Fine-mapping the breakpoint junctions of 259 ASD-relevant duplications identified 34 (13.1%) variants with complex genomic structures as well as tandem (193/259, 74.5%) and NAHR- mediated (6/259, 2.3%) duplications. As whole genome sequencing-based studies expand in scale and reach, a continued focus on generating high-quality, standardized duplication data will be prerequisite to addressing their associated biological mechanisms. ii Acknowledgements I thank Dr. Stephen Scherer for his leadership par excellence, his generosity, and for giving me a chance. I am grateful for his investment and the opportunities afforded me, from which I have learned and benefited. I would next thank Drs.
[Show full text]
The Changing Chromatome As a Driver of Disease: a Panoramic View from Different Methodologies
The changing chromatome as a driver of disease: A panoramic view from different methodologies Isabel Espejo1, Luciano Di Croce,1,2,3 and Sergi Aranda1 1. Centre for Genomic Regulation (CRG), Barcelona Institute of Science and Technology, Dr. Aiguader 88, Barcelona 08003, Spain 2. Universitat Pompeu Fabra (UPF), Barcelona, Spain 3. ICREA, Pg. Lluis Companys 23, Barcelona 08010, Spain *Corresponding authors: Luciano Di Croce ([email protected]) Sergi Aranda ([email protected]) 1 GRAPHICAL ABSTRACT Chromatin-bound proteins regulate gene expression, replicate and repair DNA, and transmit epigenetic information. Several human diseases are highly influenced by alterations in the chromatin- bound proteome. Thus, biochemical approaches for the systematic characterization of the chromatome could contribute to identifying new regulators of cellular functionality, including those that are relevant to human disorders. 2 SUMMARY Chromatin-bound proteins underlie several fundamental cellular functions, such as control of gene expression and the faithful transmission of genetic and epigenetic information. Components of the chromatin proteome (the “chromatome”) are essential in human life, and mutations in chromatin-bound proteins are frequently drivers of human diseases, such as cancer. Proteomic characterization of chromatin and de novo identification of chromatin interactors could thus reveal important and perhaps unexpected players implicated in human physiology and disease. Recently, intensive research efforts have focused on developing strategies to characterize the chromatome composition. In this review, we provide an overview of the dynamic composition of the chromatome, highlight the importance of its alterations as a driving force in human disease (and particularly in cancer), and discuss the different approaches to systematically characterize the chromatin-bound proteome in a global manner.
[Show full text]
A Meta-Learning Approach for Genomic Survival Analysis
bioRxiv preprint doi: https://doi.org/10.1101/2020.04.21.053918; this version posted April 23, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. A meta-learning approach for genomic survival analysis Yeping Lina Qiu1;2, Hong Zheng2, Arnout Devos3, Olivier Gevaert2;4;∗ 1Department of Electrical Engineering, Stanford University 2Stanford Center for Biomedical Informatics Research, Department of Medicine, Stanford University 3School of Computer and Communication Sciences, Swiss Federal Institute of Technology Lausanne (EPFL) 4Department of Biomedical Data Science, Stanford University ∗To whom correspondence should be addressed: [email protected] Abstract RNA sequencing has emerged as a promising approach in cancer prognosis as sequencing data becomes more easily and affordably accessible. However, it remains challenging to build good predictive models especially when the sample size is limited and the number of features is high, which is a common situation in biomedical settings. To address these limitations, we propose a meta-learning framework based on neural networks for survival analysis and evaluate it in a genomic cancer research setting. We demonstrate that, compared to regular transfer- learning, meta-learning is a significantly more effective paradigm to leverage high-dimensional data that is relevant but not directly related to the problem of interest. Specifically, meta-learning explicitly constructs a model, from abundant data of relevant tasks, to learn a new task with few samples effectively. For the application of predicting cancer survival outcome, we also show that the meta- learning framework with a few samples is able to achieve competitive performance with learning from scratch with a significantly larger number of samples.
[Show full text]
Short Histone H2A Variants: Small in Stature but Not in Function
cells Review Short Histone H2A Variants: Small in Stature but not in Function Xuanzhao Jiang, Tatiana A. Soboleva * and David J. Tremethick * The John Curtin School of Medical Research, The Australian National University, P.O. Box 334, 2601 Canberra, Australia; [email protected] * Correspondence: [email protected] (T.A.S.); [email protected] (D.J.T.); Tel.: +61-2-53491 (T.A.S.); +61-2-52326 (D.J.T.) Received: 9 March 2020; Accepted: 31 March 2020; Published: 2 April 2020 Abstract: The dynamic packaging of DNA into chromatin regulates all aspects of genome function by altering the accessibility of DNA and by providing docking pads to proteins that copy, repair and express the genome. Diﬀerent epigenetic-based mechanisms have been described that alter the way DNA is organised into chromatin, but one fundamental mechanism alters the biochemical composition of a nucleosome by substituting one or more of the core histones with their variant forms. Of the core histones, the largest number of histone variants belong to the H2A class. The most divergent class is the designated “short H2A variants” (H2A.B, H2A.L, H2A.P and H2A.Q), so termed because they lack a H2A C-terminal tail. These histone variants appeared late in evolution in eutherian mammals and are lineage-speciﬁc, being expressed in the testis (and, in the case of H2A.B, also in the brain). To date, most information about the function of these peculiar histone variants has come from studies on the H2A.B and H2A.L family in mice.
[Show full text]
Introduction to Gene Set Analysis Lecture (Pdf)
Extracting Biological Information from Gene Lists Simon Andrews, Laura Biggins, Boo Virk [email protected] [email protected] v2020-10 Analysis of processed Biological Sample for sample: Data acquisition – material analysis sequencing, microarray analysis, mass spectrometry Isolation of Sample DNA, RNA or processing proteins What does this mean??? Raw data Results Table file(s) Containing hits – genes, transcripts or proteins Public databases Data analysis: identification of genes, transcripts or proteins Biological themes are not always obvious from gene lists Relate the hits to existing knowledge Descriptions aren’t always informative Gene Description Gpr55 G protein-coupled receptor 55 [Source:MGI Symbol;Acc:MGI:2685064] Ncl nucleolin [Source:MGI Symbol;Acc:MGI:97286] Aspm asp (abnormal spindle)-like, microcephaly associated (Drosophila) [Source:MGI Symbol;Acc:MGI:1334448] Tnfsf4 tumor necrosis factor (ligand) superfamily, member 4 [Source:MGI Symbol;Acc:MGI:104511] Ephx1 epoxide hydrolase 1, microsomal [Source:MGI Symbol;Acc:MGI:95405] Setx senataxin [Source:MGI Symbol;Acc:MGI:2443480] Angptl2 angiopoietin-like 2 [Source:MGI Symbol;Acc:MGI:1347002] Ggta1 glycoprotein galactosyltransferase alpha 1, 3 [Source:MGI Symbol;Acc:MGI:95704] Dab2ip disabled homolog 2 (Drosophila) interacting protein [Source:MGI Symbol;Acc:MGI:1916851] Neb nebulin [Source:MGI Symbol;Acc:MGI:97292] Ermn ermin, ERM-like protein [Source:MGI Symbol;Acc:MGI:1925017] Ckap5 cytoskeleton associated protein 5 [Source:MGI Symbol;Acc:MGI:1923036] Prr5l proline rich 5 like [Source:MGI Symbol;Acc:MGI:1919696] Arhgap11a Rho GTPase activating protein 11A [Source:MGI Symbol;Acc:MGI:2444300] Bub1b budding uninhibited by benzimidazoles 1 homolog, beta (S.
[Show full text]
Nucleosome Adaptability Conferred by Sequence and Structural Variations
Available online at www.sciencedirect.com ScienceDirect Nucleosome adaptability conferred by sequence and structural variations in histone H2A–H2B dimers Alexey K Shaytan, David Landsman and Anna R Panchenko Nucleosome variability is essential for their functions in located at certain distances from each other along the DNA compacting the chromatin structure and regulation of molecule and nucleosome spacing is shown to be species transcription, replication and cell reprogramming. The DNA and tissue dependent [3,4]. Once thought to play merely molecule in nucleosomes is wrapped around an octamer structural role, nucleosomes now unravel their dual nature composed of four types of core histones (H3, H4, H2A, H2B). as key players in epigenetic regulation of transcription, Nucleosomes represent dynamic entities and may change their replication and reprogramming. It is becoming more rec- conformation, stability and binding properties by employing ognized that nucleosomes represent dynamic entities [5,6], different sets of histone variants or by becoming post- namely, they may change their conformation, histone translationally modified. There are many variants of histones content, employ a set of different histone variants (see H2A and H2B. Specific H2A and H2B variants may definition below), and become post-translationally modi- preferentially associate with each other resulting in different fied upon certain conditions. Nucleosome variability is combinations of variants and leading to the increased essential to adapt chromatin structure and function in order combinatorial complexity of nucleosomes. In addition, the to respond to environmental stimuli and fulfill cellular H2A–H2B dimer can be recognized and substituted by function [7]. Some of the recent striking examples of chaperones/remodelers as a distinct unit, can assemble nucleosome adaptability include: role of H2A.Z histone independently and is stable during nucleosome unwinding.
[Show full text]
SLY Regulates Genes Involved in Chromatin Remodeling and Interacts with TBL1XR1 During Sperm Differentiation
Cell Death and Differentiation (2017) 24, 1029–1044 OPEN Ofﬁcial journal of the Cell Death Differentiation Association www.nature.com/cdd SLY regulates genes involved in chromatin remodeling and interacts with TBL1XR1 during sperm differentiation Charlotte Moretti1,2,3,8, Maria-Elisabetta Serrentino1,2,3,8, Côme Ialy-Radio1,2,3, Marion Delessard1,2,3, Tatiana A Soboleva4, Frederic Tores5, Marjorie Leduc6, Patrick Nitschké5, Joel R Drevet7, David J Tremethick4, Daniel Vaiman1,2,3, Ayhan Kocer7 and Julie Cocquet*,1,2,3 Sperm differentiation requires unique transcriptional regulation and chromatin remodeling after meiosis to ensure proper compaction and protection of the paternal genome. Abnormal sperm chromatin remodeling can induce sperm DNA damage, embryo lethality and male infertility, yet, little is known about the factors which regulate this process. Deficiency in Sly, a mouse Y chromosome-encoded gene expressed only in postmeiotic male germ cells, has been shown to result in the deregulation of hundreds of sex chromosome-encoded genes associated with multiple sperm differentiation defects and subsequent male infertility. The underlying mechanism remained, to date, unknown. Here, we show that SLY binds to the promoter of sex chromosome-encoded and autosomal genes highly expressed postmeiotically and involved in chromatin regulation. Specifically, we demonstrate that Sly knockdown directly induces the deregulation of sex chromosome-encoded H2A variants and of the H3K79 methyltransferase DOT1L. The modifications prompted by loss of Sly alter the postmeiotic chromatin structure and ultimately result in abnormal sperm chromatin remodeling with negative consequences on the sperm genome integrity. Altogether our results show that SLY is a regulator of sperm chromatin remodeling.
[Show full text]
Short H2A Histone Variants Are Expressed in Cancer
ARTICLE https://doi.org/10.1038/s41467-020-20707-x OPEN Short H2A histone variants are expressed in cancer Guo-Liang Chew 1, Marie Bleakley2, Robert K. Bradley 3,4,5, Harmit S. Malik4,6, Steven Henikoff 4,6, ✉ ✉ Antoine Molaro 4,7 & Jay Sarthy 4 Short H2A (sH2A) histone variants are primarily expressed in the testes of placental mammals. Their incorporation into chromatin is associated with nucleosome destabilization and modulation of alternate splicing. Here, we show that sH2As innately possess features similar to recurrent oncohistone mutations associated with nucleosome instability. Through 1234567890():,; analyses of existing cancer genomics datasets, we ﬁnd aberrant sH2A upregulation in a broad array of cancers, which manifest splicing patterns consistent with global nucleosome destabilization. We posit that short H2As are a class of “ready-made” oncohistones, whose inappropriate expression contributes to chromatin dysfunction in cancer. 1 The Cancer Science Institute of Singapore, National University of Singapore, Singapore, Singapore. 2 Clinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA. 3 Computational Biology Program, Public Health Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA. 4 Basic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA. 5 Department of Genome Sciences, University of Washington, Seattle, WA, USA. 6 Howard Hughes Medical Institute, Fred Hutchinson Cancer Research Center, Seattle, WA, USA. 7Present address: ✉ Genetics, Reproduction and Development (GReD) Institute, Université Clermont Auvergne, Clermont-Ferrand, France. email: [email protected]; [email protected] NATURE COMMUNICATIONS | (2021) 12:490 | https://doi.org/10.1038/s41467-020-20707-x | www.nature.com/naturecommunications 1 ARTICLE NATURE COMMUNICATIONS | https://doi.org/10.1038/s41467-020-20707-x ucleosomes, the fundamental subunit of chromatin, con- contribute to cancer.
[Show full text]