Results 41 to 50 of about 196,399 (287)

The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation [PDF]

, 2011
Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant ...
Bowman, A., El-Mkami, Hassane, Norman, David George, Owen-Hughes, Tom, Singh, Vijender, Ward, Richard, Wiechens, Nicola   +6 more
core   +4 more sources

Arsenite alters global histone H3 methylation [PDF]

Carcinogenesis, 2008
Arsenic (As) is a well-characterized human carcinogen but is generally not mutagenic. The evidence that As induces both loss of global DNA methylation and gene promoter DNA hypermethylation has suggested that epigenetic mechanisms may play an important role in As-induced carcinogenesis.
Xue, Zhou, Hong, Sun, Thomas P, Ellen, Haobin, Chen, Max, Costa   +4 more
openaire   +2 more sources

Recombinant human soluble thrombomodulin is associated with attenuation of sepsis-induced renal impairment by inhibition of extracellular histone release.

PLoS ONE, 2020
Multiple organ dysfunction induced by sepsis often involves kidney injury. Extracellular histones released in response to damage-associated molecular patterns are known to facilitate sepsis-induced organ dysfunction.
Masayuki Akatsuka, Yoshiki Masuda, Hiroomi Tatsumi, Michiaki Yamakage   +3 more
doaj   +1 more source

Structural Basis of Molecular Recognition of Helical Histone H3 Tail by PHD Finger Domains [PDF]

, 2017
The plant homeodomain (PHD) fingers are amongst the largest family of epigenetic domains, first characterized as readers of methylated H3K4. Readout of histone posttranslational modifications by PHDs has been the subject of intense investigation, however
Alessio Bortoluzzi, Alessio Ciulli, Ali, Anastasia Amato, Andrews, Arita, Bochar, Brooks, Chakravarty, Chen, Chen, Cheng, Dreveny, Eberharter, Emsley, Evans, Farmer, Ferguson, Galdeano, Greenfield, Gu, Guetg, Herold, Hol, Holm, Hu, Humphrey, Iwase, Jasanoff, Jones, Kabsch, Kabsch, Katoh, Klein, Klein, Klein, Lallous, Li, Li, Li, Li, Liu, Luo, Mansfield, Manuel Blank, Marley, Matsubara, Miller, Milosevich, Murshudov, Musselman, Musselman, Musselman, Nelson, Pace, Pascual, Patel, Peña, Phillips, Plotnikov, Provencher, Qiu, Rack, Racki, Rajakumara, Ren, Santoro, Shi, Simhadri, Stuckey, Tallant, Taverna, Torres, Tsai, Vranken, Wagner, Wagner, Wang, Wang, Waterhouse, Whitmore, Williamson, Wysocka, Xavier Lucas, Xie, Xiong, Zeng, Zeng, Zhang, Zhang, Zhou   +90 more
core   +3 more sources

Histone H3 lysine 4 methyltransferase KMT2D [PDF]

Gene, 2017
Histone-lysine N-methyltransferase 2D (KMT2D), also known as MLL4 and MLL2 in humans and Mll4 in mice, belongs to a family of mammalian histone H3 lysine 4 (H3K4) methyltransferases. It is a large protein over 5500 amino acids in size and is partially functionally redundant with KMT2C.
Eugene Froimchuk, Younghoon Jang, Kai Ge
openaire   +2 more sources

Tissue-specific expression of histone H3 variants diversified after species separation [PDF]

, 2015
Additional file 3: Predicted CDS of human histone H3/H4 variants, contains Table S2, which lists the CDS locus information of the predicted human histone H3 and H4 variants in an Excel ...
Akihito Harada, Hiroshi Kimura, Kazumitsu Maehara, Keiichi I. Nakayama, Masaki Matsumoto, Yasuyuki Ohkawa, Yuko Sato   +6 more
core   +4 more sources

Histone H3 phosphorylation and cell division [PDF]

Oncogene, 2001
Histone H3 is specifically phosphorylated during both mitosis and meiosis in patterns that are specifically coordinated in both space and time. Histone H3 phosphorylation may initiate at different phases of the cell division in different organisms, but metaphase chromosomes are always found to be heavily phosphorylated.
F, Hans, S, Dimitrov
openaire   +2 more sources

The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification [PDF]

, 2013
Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine ...
A. Bhattacharya, Adams, Ali, B. Yue, Chakraborty, Champagne, D. M. Heery, Dawson, Deguchi, Dou, Doyon, Emsley, Fiedler, Filippakopoulos, Flanagan, H. M. Collins, Harris, Huntly, I. Dreveny, J. Fulton, Karmodiya, Kindle, Kitabayashi, Lan, Lange, Laue, M. Messmer, McCoy, Moriniere, Pelletier, Qiu, Ruthenburg, S. E. Deeves, Sanchez, Schwartzentruber, Sheppard, Strahl, Sturm, Taverna, Thomas, Voss, Wysocka, Zeng, Zuber   +43 more
core   +2 more sources

Reduced Histone H3 Lysine 9 Methylation Contributes to the Pathogenesis of Latent Autoimmune Diabetes in Adults via Regulation of SUV39H2 and KDM4C

Journal of Diabetes Research, 2017
Aims. Latent autoimmune diabetes in adults (LADA) is an autoimmune disease of which the mechanism is not clear. Emerging evidence suggests that histone methylation contributes to autoimmunity. Methods.
Xi-yu Liu, Hong Li
doaj   +1 more source

Dominant effects of the histone mutant H3-L61R on Spt16-gene interactions in budding yeast

Epigenetics, 2022
Recent studies have unveiled an association between an L61R substitution within the human histone H3.3 protein and the presentation of neurodevelopmental disorders in two patients.
Alex Pablo-Kaiser, McKenzie G. Tucker, Grace A. Turner, Elijah G. Dilday, Avery G. Olmstead, Caroline L. Tackett, Andrea A. Duina   +6 more
doaj   +1 more source