Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registry
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what money
Authors and funding
25 authors.
László ImreDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.ORCID 0000-0001-9562-6943
Péter NánásiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
Ibtissem BenhamzaDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.ORCID 0009-0000-3219-5744
Kata Nóra EnyediDepartment of Organic Chemistry, Institute of Chemistry, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0003-3724-5936
Gábor MocsárDamjanovich Cell Analysis Core Facility, Department of Biophysics and Cell Biology, University of Debrecen, Faculty of Medicine, Debrecen, Hungary.ORCID 0000-0003-0570-3269
Rosevalentine BosireDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.ORCID 0000-0002-6475-2610
Éva HegedüsDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
Erfaneh Firouzi NiakiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
Ágota CsótiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
Zsuzsanna DarulaSingle Cell Omics Advanced Core Facility, Hungarian Centre of Excellence for Molecular Medicine, Szeged, Hungary.ORCID 0000-0003-1692-7591
Éva CsőszDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.ORCID 0000-0003-4373-2175
Szilárd PóliskaDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.ORCID 0000-0002-9722-251X
Beáta ScholtzDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.ORCID 0000-0002-2737-5027
Gábor MezőDepartment of Organic Chemistry, Institute of Chemistry, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0002-7618-7954
Zsolt BacsóDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.ORCID 0000-0001-6885-3796
H T Marc TimmersGerman Cancer Consortium (DKTK), partner site Freiburg, a partnership between the DKFZ and Medical Center-University of Freiburg and Department of Urology, Medical Center-University of Freiburg, Breisacher Str. 66, Freiburg, Germany.ORCID 0000-0001-7062-1417
Masayuki KusakabeBiosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, 657-8501, Japan.
Margit BalázsHUN-REN-UD Public Health Research Group, Department of Public Health and Epidemiology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
György VámosiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.ORCID 0000-0002-7940-2787
Juan AusioDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.ORCID 0000-0002-9674-6717
Peter CheungYork University, Toronto, Canada.
Katalin TóthDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.ORCID 0000-0002-0081-4720
David TremethickThe John Curtin School of Medical Research, The Australian National University, Canberra, ACT, 2601, Australia.ORCID 0000-0001-5274-8078
Masahiko HarataLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Gábor SzabóDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary. szabog@med.unideb.hu.ORCID 0000-0002-9163-3465
Funding
EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) no. 739593European Cooperation in Science and Technology (COST) CA15214, CA18127Nemzeti Kutatási, Fejlesztési és Innovációs Hivatal (NKFI Office) K138524, K128770
6 · The paper itself
Abstract
H2A.Z-nucleosomes are present in both euchromatin and heterochromatin and it has proven difficult to interpret their disparate roles in the context of their stability features. Using an in situ assay of nucleosome stability and DT40 cells expressing engineered forms of the histone variant we show that native H2A.Z, but not C-terminally truncated H2A.Z (H2A.Z∆C), is released from nucleosomes of peripheral heterochromatin at unusually high salt concentrations. H2A.Z and H3K9me3 landscapes are reorganized in H2A.Z∆C-nuclei and overall sensitivity of chromatin to nucleases is increased. These tail-dependent differences are recapitulated upon treatment of HeLa nuclei with the H2A.Z-tail-peptide (C9), with MNase sensitivity being increased genome-wide. Fluorescence correlation spectroscopy revealed C9 binding to reconstituted nucleosomes. When introduced into live cells, C9 elicited chromatin reorganization, overall nucleosome destabilization and changes in gene expression. Thus, H2A.Z-nucleosomes influence global chromatin architecture in a tail-dependent manner, what can be modulated by introducing the tail-peptide into live cells.
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.
Epigenetic modulation via the C-terminal tail of H2A.Z. · full record | OpenQuestion