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Items: 1 to 20 of 171

1.
Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2
Philip Saumer, Martin Scheffner, Andreas Marx, Florian Stengel
Nucleic Acids Res. 2024 Jan 11; 52(1): 101–113. Published online 2023 Nov 22. doi: 10.1093/nar/gkad1113
PMCID:
PMC10783519
AbstractArticlePDF–1.3M
2.
Site-specific ubiquitylation acts as a regulator of linker histone H1
Eva Höllmüller, Simon Geigges, Marie L. Niedermeier, Kai-Michael Kammer, Simon M. Kienle, Daniel Rösner, Martin Scheffner, Andreas Marx, Florian Stengel
Nat Commun. 2021; 12: 3497. Published online 2021 Jun 9. doi: 10.1038/s41467-021-23636-5
PMCID:
PMC8190259
AbstractArticlePDF–4.1M
3.
The linker histone H1.2 is a novel component of the nucleolar organizer regions
Junjie Chen, Boon Heng Dennis Teo, Yitian Cai, Seng Yin Kelly Wee, Jinhua Lu
J Biol Chem. 2018 Feb 16; 293(7): 2358–2369. Published online 2018 Jan 4. doi: 10.1074/jbc.M117.810184
PMCID:
PMC5818188
AbstractArticlePDF–3.2M
4.
Histone HIST1H1C/H1.2 regulates autophagy in the development of diabetic retinopathy
Wenjun Wang, Qing Wang, Danyang Wan, Yue Sun, Lin Wang, Hong Chen, Chengyu Liu, Robert B. Petersen, Jianshuang Li, Weili Xue, Ling Zheng, Kun Huang
Autophagy. 2017; 13(5): 941–954. Published online 2017 Mar 2. doi: 10.1080/15548627.2017.1293768
PMCID:
PMC5446066
AbstractArticlePDF–1.5M
5.
Mapping of six somatic linker histone H1 variants in human breast cancer cells uncovers specific features of H1.2
Lluís Millán-Ariño, Abul B. M. M. K. Islam, Andrea Izquierdo-Bouldstridge, Regina Mayor, Jean-Michel Terme, Neus Luque, Mónica Sancho, Núria López-Bigas, Albert Jordan
Nucleic Acids Res. 2014 Apr; 42(7): 4474–4493. Published online 2014 Jan 28. doi: 10.1093/nar/gku079
PMCID:
PMC3985652
AbstractArticlePDF–13M
6.
Histone H1.2 Inhibited EMCV Replication through Enhancing MDA5-Mediated IFN-β Signaling Pathway
Yangran Song, Huixia Li, Ruiya Lian, Xueer Dou, Shasha Li, Jingying Xie, Xiangrong Li, Ruofei Feng, Zhiqiang Li
Viruses. 2024 Feb; 16(2): 174. Published online 2024 Jan 24. doi: 10.3390/v16020174
PMCID:
PMC10892618
AbstractArticlePDF–4.2M
7.
The RNA interactome of human telomerase RNA reveals a coding-independent role for a histone mRNA in telomere homeostasis
Roland Ivanyi-Nagy, Syed Moiz Ahmed, Sabrina Peter, Priya Dharshana Ramani, Peh Fern Ong, Oliver Dreesen, Peter Dröge
eLife. 2018; 7: e40037. Published online 2018 Oct 25. doi: 10.7554/eLife.40037
PMCID:
PMC6249008
AbstractArticlePDF–5.1M
8.
Linker Histone H1.2 Directs Genome-wide Chromatin Association of the Retinoblastoma Tumor Suppressor Protein and Facilitates Its Function
Shonagh Munro, Edward S. Hookway, Melanie Floderer, Simon M. Carr, Rebecca Konietzny, Benedikt M. Kessler, Udo Oppermann, Nicholas B. La Thangue
Cell Rep. 2017 Jun 13; 19(11): 2193–2201. Published online 2017 Jun 13. doi: 10.1016/j.celrep.2017.05.053
PMCID:
PMC5478878
AbstractArticlePDF–1.9M
9.
Hormone‐induced repression of genes requires BRG1‐mediated H1.2 deposition at target promoters
Ana Silvina Nacht, Andy Pohl, Roser Zaurin, Daniel Soronellas, Javier Quilez, Priyanka Sharma, Roni H Wright, Miguel Beato, Guillermo P Vicent
EMBO J. 2016 Aug 15; 35(16): 1822–1843. Published online 2016 Jul 7. doi: 10.15252/embj.201593260
PMCID:
PMC5010049
AbstractArticlePDF–2.2M
10.
Functional interplay between p53 acetylation and H1.2 phosphorylation in p53-regulated transcription
Kyunghwan Kim, Kwang Won Jeong, Hyunjung Kim, Jongkyu Choi, Wange Lu, Michael R. Stallcup, Woojin An
Oncogene. Author manuscript; available in PMC 2013 Mar 27.
Published in final edited form as: Oncogene. 2012 Sep 27; 31(39): 4290–4301. Published online 2012 Jan 16. doi: 10.1038/onc.2011.605
PMCID:
PMC3330162
AbstractArticlePDF–1.2M
11.
Identification of Binding Proteins for TSC22D1 Family Proteins Using Mass Spectrometry
Ryouta Kamimura, Daisuke Uchida, Shin-ichiro Kanno, Ryo Shiraishi, Toshiki Hyodo, Yuta Sawatani, Michiko Shimura, Tomonori Hasegawa, Maki Tsubura-Okubo, Erika Yaguchi, Yuske Komiyama, Chonji Fukumoto, Sayaka Izumi, Atsushi Fujita, Takahiro Wakui, Hitoshi Kawamata
Int J Mol Sci. 2021 Oct; 22(20): 10913. Published online 2021 Oct 9. doi: 10.3390/ijms222010913
PMCID:
PMC8536140
AbstractArticlePDF–2.7M
12.
Quantitative Mass Spectrometry Reveals that Intact Histone H1 Phosphorylations are Variant Specific and Exhibit Single Molecule Hierarchical Dependence
Yu Chen, Michael E. Hoover, Xibei Dang, Alan A. Shomo, Xiaoyan Guan, Alan G. Marshall, Michael A. Freitas, Nicolas L. Young
Mol Cell Proteomics. 2016 Mar; 15(3): 818–833. Published online 2015 Jul 24. doi: 10.1074/mcp.M114.046441
PMCID:
PMC4813703
AbstractArticlePDF–4.3M
13.
The C-terminal domain (CTD) in linker histones antagonizes anti-apoptotic proteins to modulate apoptotic outcomes at the mitochondrion
M Garg, N Ramdas, M Vijayalakshmi, G V Shivashankar, A Sarin
Cell Death Dis. 2014 Feb; 5(2): e1058. Published online 2014 Feb 13. doi: 10.1038/cddis.2014.20
PMCID:
PMC3944238
AbstractArticlePDF–2.3M
14.
Destabilization of linker histone H1.2 is essential for ATM activation and DNA damage repair
Zhiming Li, Yinglu Li, Ming Tang, Bin Peng, Xiaopeng Lu, Qiaoyan Yang, Qian Zhu, Tianyun Hou, Meiting Li, Chaohua Liu, Lina Wang, Xingzhi Xu, Ying Zhao, Haiying Wang, Yang Yang, Wei-Guo Zhu
Cell Res. 2018 Jul; 28(7): 756–770. Published online 2018 May 29. doi: 10.1038/s41422-018-0048-0
PMCID:
PMC6028381
AbstractArticlePDF–3.8M
15.
A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences.
M. H. Parseghian, A. H. Henschen, K. G. Krieglstein, B. A. Hamkalo
Protein Sci. 1994 Apr; 3(4): 575–587. doi: 10.1002/pro.5560030406
PMCID:
PMC2142865
SummaryPDF–5.0M
16.
Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma
Hongxiu Li, Mark S. Kaminski, Yifeng Li, Mehmet Yildiz, Peter Ouillette, Siân Jones, Heather Fox, Kathryn Jacobi, Kamlai Saiya-Cork, Dale Bixby, Daniel Lebovic, Diane Roulston, Kerby Shedden, Michael Sabel, Lawrence Marentette, Vincent Cimmino, Alfred E. Chang, Sami N. Malek
Blood. 2014 Mar 6; 123(10): 1487–1498. Prepublished online 2014 Jan 16. doi: 10.1182/blood-2013-05-500264
PMCID:
PMC4729540
AbstractArticle
17.
High-throughput kinase assays with protein substrates using fluorescent polymer superquenching
Frauke Rininsland, Casey Stankewicz, Wendy Weatherford, Duncan McBranch
BMC Biotechnol. 2005; 5: 16. Published online 2005 May 31. doi: 10.1186/1472-6750-5-16
PMCID:
PMC1166542
AbstractArticlePDF–569K
18.
N6-Methyladenosine modification of the TRIM7 positively regulates tumorigenesis and chemoresistance in osteosarcoma through ubiquitination of BRMS1
Chenliang Zhou, Zhichang Zhang, Xiaoshi Zhu, Guowei Qian, Yan Zhou, Yong Sun, Wenxi Yu, Jiahui Wang, Haiyang Lu, Feng Lin, Zan Shen, Shuier Zheng
EBioMedicine. 2020 Sep; 59: 102955. Published online 2020 Aug 24. doi: 10.1016/j.ebiom.2020.102955
PMCID:
PMC7452680
AbstractArticlePDF–5.1M
19.
The Proteomic Investigation of Chromatin Functional Domains Reveals Novel Synergisms among Distinct Heterochromatin Components
Monica Soldi, Tiziana Bonaldi
Mol Cell Proteomics. 2013 Mar; 12(3): 764–780. Published online 2013 Jan 14. doi: 10.1074/mcp.M112.024307
PMCID:
PMC3591667
AbstractArticlePDF–2.8M
20.
A unified phylogeny-based nomenclature for histone variants
Paul B Talbert, Kami Ahmad, Geneviève Almouzni, Juan Ausió, Frederic Berger, Prem L Bhalla, William M Bonner, W Zacheus Cande, Brian P Chadwick, Simon W L Chan, George A M Cross, Liwang Cui, Stefan I Dimitrov, Detlef Doenecke, José M Eirin-López, Martin A Gorovsky, Sandra B Hake, Barbara A Hamkalo, Sarah Holec, Steven E Jacobsen, Kinga Kamieniarz, Saadi Khochbin, Andreas G Ladurner, David Landsman, John A Latham, Benjamin Loppin, Harmit S Malik, William F Marzluff, John R Pehrson, Jan Postberg, Robert Schneider, Mohan B Singh, M Mitchell Smith, Eric Thompson, Maria-Elena Torres-Padilla, David John Tremethick, Bryan M Turner, Jakob Harm Waterborg, Heike Wollmann, Ramesh Yelagandula, Bing Zhu, Steven Henikoff
Epigenetics Chromatin. 2012; 5: 7. Published online 2012 Jun 21. doi: 10.1186/1756-8935-5-7
PMCID:
PMC3380720
AbstractArticlePDF–747K

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