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High mobility group nucleosomal binding domain 2

member of a family of non-histone chromosomal proteins [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: HMG-14, Histone, CAN, ACID, H1
Papers on HMG-17
HMGNs: The enhancer charmers.
Ausió et al., Victoria, Canada. In Bioessays, Jan 2016
For over 35 years, the high-mobility group nucleosome-binding chromosomal proteins HMGN1 and HMGN2 have been shown to play a role in the establishment of these chromatin-accessible domains at transcriptional regulatory elements, namely promoters and enhancers.
Functional compensation among HMGN variants modulates the DNase I hypersensitive sites at enhancers.
Bustin et al., Bethesda, United States. In Genome Res, Sep 2015
We now show that HMGN1 and HMGN2, nucleosome-binding proteins that are ubiquitously expressed in vertebrate cells, maintain the DHS landscape of mouse embryonic fibroblasts (MEFs) synergistically.
[High Mobility Group Chromosal Protein N2 Is Expected to be as A Target of Cellular Immunetherapy in Leukemia and Tumors].
Wang et al., Beijing, China. In Zhongguo Shi Yan Xue Ye Xue Za Zhi, Aug 2015
Recent studies have found that high mobility group protein N2 (high mobility group chromosal protein N2, HMGN2) is the excellent target of tumor-associated antigen in lymphocytes, is the antitumor effector molecule of CD8(+) T cells, which has the ability of trends and specific identify/binding in myeloid leukemia, breast cancer, cervical cancer and other tumor cells.
Discovery of novel vitamin D-regulated proteins in INS-1 cells: a proteomic approach.
Thorsby et al., Oslo, Norway. In Diabetes Metab Res Rev, Jul 2015
Proteins whose expression levels markedly increased in the presence of 1,25-(OH)2 D3 included Crat, Hmgn2, Protein Tmsbl1 and Gdap1.
High-mobility group nucleosome-binding domain 2 protein inhibits the invasion of Klebsiella pneumoniae into mouse lungs in vivo.
Huang et al., Chengdu, China. In Mol Med Report, Jul 2015
In previous studies by our group, high-mobility group nucleosome-binding domain 2 (HMGN2) protein was shown to exhibit anti-bacterial activity in vitro.
Surface localization of high-mobility group nucleosome-binding protein 2 on leukemic B cells from patients with chronic lymphocytic leukemia is related to secondary autoimmune hemolytic anemia.
Giordano et al., Buenos Aires, Argentina. In Leuk Lymphoma, Apr 2015
Here we show that the major binding site of Band 3 on leukemic cells is an extrinsic protein identified as high-mobility group nucleosome binding protein 2 (HMGN2), a nucleosome-interacting factor which has not been previously reported at the cell surface.
Nucleosome-binding protein HMGN2 exhibits antitumor activity in human SaO2 and U2-OS osteosarcoma cell lines.
Zhou et al., China. In Oncol Rep, Mar 2015
However, the effects and molecular mechanisms of HMGN2 on osteosarcoma progression remain to be determined.
HMGN2 protein inhibits the growth of infected T24 cells in vitro.
Chen et al., Chengdu, China. In J Cancer Res Ther, 2014
High mobility group nucleosomal-binding domain 2 (HMGN2) may be one of the effector molecules of CTL and NK cells.
HMGN2, a new anti-tumor effector molecule of CD8⁺ T cells.
Feng et al., Chengdu, China. In Mol Cancer, 2013
Our previous research has shown that high mobility group nucleosomal-binding domain 2 (HMGN2) could be released by IL-2 and PHA stimulated peripheral blood mononuclear cells (PBMCs) and also induced tumor cells apoptosis at low doses.
A multi-resource data integration approach: identification of candidate genes regulating cell proliferation during neocortical development.
Nowakowski et al., Tallahassee, United States. In Front Neurosci, 2013
We used a mouse in situ hybridization dataset (The Allen Institute for Brain Science) to identify 13 genes (Cdon, Celsr1, Dbi, E2f5, Eomes, Hmgn2, Neurog2, Notch1, Pcnt, Sox3, Ssrp1, Tead2, Tgif2) with high correlation of expression in the proliferating cells of the VZ of the neocortex at early stages of development (E15.5).
The role of the nucleosome acidic patch in modulating higher order chromatin structure.
Hansen et al., Fort Collins, United States. In J R Soc Interface, 2013
The co-structures of five different proteins with the nucleosome (LANA, IL-33, RCC1, Sir3 and HMGN2) recently have been examined by experimental and computational studies.
Development of a chemical genetic approach for human aurora B kinase identifies novel substrates of the chromosomal passenger complex.
Lens et al., Utrecht, Netherlands. In Mol Cell Proteomics, 2012
HMGN2 is a bona fide Aurora B substrate in vivo and show that its dynamic association to chromatin is controlled by Aurora B.
The chromosomal protein HMGN2 mediates the LPS-induced expression of β-defensins in mice.
Huang et al., Chengdu, China. In Inflammation, 2012
study demonstrates a role of HMGN2 in modulating specific gene expression and identifies beta-defensin-1, beta-defensin-3, and beta-defensin-4 as HMGN2 targets during the development of ICR mice treated with LPS
Ectopic expression of Hmgn2 antagonizes mouse erythroid differentiation in vitro.
Sugiyama et al., Fukuoka, Japan. In Cell Biol Int, 2012
The ectopic expression of Hmgn2 antagonizes mouse erythroid differentiation in vitro, which may be due to enhancement of DNA replication and/or blocking entry of mitosis at S-phase.
HMGN2 inducibly binds a novel transactivation domain in nuclear PRLr to coordinate Stat5a-mediated transcription.
Clevenger et al., Chicago, United States. In Mol Endocrinol, 2011
The association of the PRLr with HMGN2 enables Stat5a-responsive promoter binding, thus facilitating transcriptional activation and promoting anchorage-independent growth.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Bai et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2011
HMGN2 binds to both the acidic patch in the histone H2A-H2B dimer and to nucleosomal DNA near the entry/exit point, "stapling" the histone core and the DNA.
HMGNs, DNA repair and cancer.
Gerlitz, Bethesda, United States. In Biochim Biophys Acta, 2010
In addition, emerging roles for HMGN5 in cancer progression and for HMGN2 as a potential tool in cancer therapy will be discussed.
Signalling to chromatin through post-translational modifications of HMGN.
Mahadevan et al., Oxford, United Kingdom. In Biochim Biophys Acta, 2010
We focus particularly on HMGN1, the most extensively studied family member to date, and to a lesser extent on HMGN2.
The HMG-14/-17 chromosomal protein family: architectural elements that enhance transcription from chromatin templates.
Postnikov et al., Bethesda, United States. In Semin Cell Biol, 1995
Chromosomal proteins HMG-14 and HMG-17 enhance the transcriptional potential of chromatin when incorporated into nucleosomes during, but not after, chromatin assembly on replicating DNA.
Autoantibodies to nucleosomal proteins: antibodies to HMG-17 in autoimmune diseases.
Klippel et al., In Science, 1982
The results suggest that, in SLE, antibodies are formed against a subset of nucleosomes which contain protein HMG-17.
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