| Histone H1.2 Inhibited EMCV Replication through Enhancing MDA5-Mediated IFN-beta Signaling Pathway. | Histone H1.2 Inhibited EMCV Replication through Enhancing MDA5-Mediated IFN-β Signaling Pathway.
Song Y, Li H, Lian R, Dou X, Li S, Xie J, Li X, Feng R, Li Z., Free PMC Article | 02/28/2024 |
| Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2. | Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2.
Saumer P, Scheffner M, Marx A, Stengel F., Free PMC Article | 01/26/2024 |
| Site-specific ubiquitylation acts as a regulator of linker histone H1. | Site-specific ubiquitylation acts as a regulator of linker histone H1.
Höllmüller E, Geigges S, Niedermeier ML, Kammer KM, Kienle SM, Rösner D, Scheffner M, Marx A, Stengel F., Free PMC Article | 06/26/2021 |
| these findings suggest that linker histone H1.2 functions as a physiological barrier for ATM to target the chromatin, and PARylation-mediated active H1.2 turnover is required for robust ATM activation and DNA damage repair. | Destabilization of linker histone H1.2 is essential for ATM activation and DNA damage repair.
Li Z, Li Y, Tang M, Peng B, Lu X, Yang Q, Zhu Q, Hou T, Li M, Liu C, Wang L, Xu X, Zhao Y, Wang H, Yang Y, Zhu WG., Free PMC Article | 10/12/2019 |
| Taken together, these data provide important insights into a surprisingly complex hTR-RNA interaction network and define an unexpected non-coding RNA role for HIST1H1C in regulating telomere length homeostasis. | The RNA interactome of human telomerase RNA reveals a coding-independent role for a histone mRNA in telomere homeostasis.
Ivanyi-Nagy R, Ahmed SM, Peter S, Ramani PD, Ong PF, Dreesen O, Dröge P., Free PMC Article | 03/16/2019 |
| The linker histone H1.2 is a novel component of nucleolar organizer regions. | The linker histone H1.2 is a novel component of the nucleolar organizer regions.
Chen J, Teo BHD, Cai Y, Wee SYK, Lu J., Free PMC Article | 02/9/2019 |
| results define a network of E2F target genes as susceptible to the regulatory influence of H1.2, where H1.2 augments global association of pRb with chromatin, enhances transcriptional repression by pRb, and facilitates pRb-dependent cell-cycle arrest | Linker Histone H1.2 Directs Genome-wide Chromatin Association of the Retinoblastoma Tumor Suppressor Protein and Facilitates Its Function.
Munro S, Hookway ES, Floderer M, Carr SM, Konietzny R, Kessler BM, Oppermann U, La Thangue NB., Free PMC Article | 06/2/2018 |
| BRG1 participates in gene repression by interacting with H1.2, facilitating its deposition and stabilizing nucleosome positioning around the transcription start site. | Hormone-induced repression of genes requires BRG1-mediated H1.2 deposition at target promoters.
Nacht AS, Pohl A, Zaurin R, Soronellas D, Quilez J, Sharma P, Wright RH, Beato M, Vicent GP., Free PMC Article | 07/1/2017 |
| Results show that histones H1.2 and H1.4 were observed in MDA-MB-231 metastatic breast cancer cells. The phosphorylation at S173 of histone H1.2 and S172, S187, T18, T146, and T154 of H1.4 significantly increases during M phase suggesting that these events are cell cycle-dependent. Also, the study reports the observation of the H1.2 SNP variant A18V in MCF-10A cells. | Quantitative Mass Spectrometry Reveals that Intact Histone H1 Phosphorylations are Variant Specific and Exhibit Single Molecule Hierarchical Dependence.
Chen Y, Hoover ME, Dang X, Shomo AA, Guan X, Marshall AG, Freitas MA, Young NL., Free PMC Article | 12/17/2016 |
| Integration with apoptotic intermediates (via C-terminal tail interactions) may constitute a more generalized function of linker histone isoforms in apoptotic cascades. | The C-terminal domain (CTD) in linker histones antagonizes anti-apoptotic proteins to modulate apoptotic outcomes at the mitochondrion.
Garg M, Ramdas N, Vijayalakshmi M, Shivashankar GV, Sarin A., Free PMC Article | 10/25/2014 |
| Histone H1.2-T165 post translational modifications are dispensable for chromatin binding and cell proliferation while the H1.4-K26 modifications are essential for proper cell cycle progression. | Dynamics and dispensability of variant-specific histone H1 Lys-26/Ser-27 and Thr-165 post-translational modifications.
Terme JM, Millán-Ariño L, Mayor R, Luque N, Izquierdo-Bouldstridge A, Bustillos A, Sampaio C, Canes J, Font I, Sima N, Sancho M, Torrente L, Forcales S, Roque A, Suau P, Jordan A. | 08/16/2014 |
| H1.2 interacts with Cul4A and PAF1 to activate developmental regulatory genes. | Linker Histone H1.2 cooperates with Cul4A and PAF1 to drive H4K31 ubiquitylation-mediated transactivation.
Kim K, Lee B, Kim J, Choi J, Kim JM, Xiong Y, Roeder RG, An W., Free PMC Article | 08/16/2014 |
| H1.2 is less abundant than other histone H1 variants at the transcription start sites of inactive genes, and promoters enriched in H1.2 are different from those enriched in other histone H1 variants and tend to be repressed. | Mapping of six somatic linker histone H1 variants in human breast cancer cells uncovers specific features of H1.2.
Millán-Ariño L, Islam AB, Izquierdo-Bouldstridge A, Mayor R, Terme JM, Luque N, Sancho M, López-Bigas N, Jordan A., Free PMC Article | 07/12/2014 |
| Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma. | Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma.
Li H, Kaminski MS, Li Y, Yildiz M, Ouillette P, Jones S, Fox H, Jacobi K, Saiya-Cork K, Bixby D, Lebovic D, Roulston D, Shedden K, Sabel M, Marentette L, Cimmino V, Chang AE, Malek SN., Free PMC Article | 05/10/2014 |
| These data suggest that p53 acetylation-H1.2 phosphorylation cascade serves as a unique mechanism for triggering p53-dependent DNA damage response pathways. | Functional interplay between p53 acetylation and H1.2 phosphorylation in p53-regulated transcription.
Kim K, Jeong KW, Kim H, Choi J, Lu W, Stallcup MR, An W., Free PMC Article | 01/5/2013 |
| Observational study of gene-disease association. (HuGE Navigator) | See all PubMed (2) articlesInvestigation of genetic susceptibility factors for human longevity - a targeted nonsynonymous SNP study.
Flachsbart F, Franke A, Kleindorp R, Caliebe A, Blanché H, Schreiber S, Nebel A. Examination of genetic polymorphisms in newborns for signatures of sex-specific prenatal selection.
Ucisik-Akkaya E, Davis CF, Do TN, Morrison BA, Stemmer SM, Amadio WJ, Dorak MT. | 09/15/2010 |
| Histone H1.2 was translocated from the nucleus to the mitochondria after treatment with bleomycin and co-localized with Bak in mitochondria. | Histone H1.2 is translocated to mitochondria and associates with Bak in bleomycin-induced apoptotic cells.
Okamura H, Yoshida K, Amorim BR, Haneji T. | 01/21/2010 |
| Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator) | Calbindin 1, fibroblast growth factor 20, and alpha-synuclein in sporadic Parkinson's disease.
Mizuta I, Tsunoda T, Satake W, Nakabayashi Y, Watanabe M, Takeda A, Hasegawa K, Nakashima K, Yamamoto M, Hattori N, Murata M, Toda T. | 07/2/2008 |
| that the recruitment of YB1, PURalpha, and H1.2 to the p53 target gene Bax is required for repression of p53-induced transcription. | Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription.
Kim K, Choi J, Heo K, Kim H, Levens D, Kohno K, Johnson EM, Brock HW, An W., Free PMC Article | 01/21/2010 |
| confirmed N-terminal acetylation on all isoforms plus a single internal acetylation site; phosphorylation sites were located on peptides containing the cyclin dependent kinase (CDK) consensus motif | Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry.
Garcia BA, Busby SA, Barber CM, Shabanowitz J, Allis CD, Hunt DF. | 01/21/2010 |
| The binding of histone H1 to a general amyloid-like motif indicates that histone H1 may play an important common role in diseases associated with amyloid-like fibrils. | Linker histone H1 binds to disease associated amyloid-like fibrils.
Duce JA, Smith DP, Blake RE, Crouch PJ, Li QX, Masters CL, Trounce IA. | 01/21/2010 |