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Studies indicate that high mobility group nucleosome binding domain 1 (HMGN1) preferentially promotes Th1-type immunity, which makes it relevant for the fields of vaccinology, autoimmunity, and oncoimmunology [Review].
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HMGN1 and HMGN 2 remodel core and linker histone tail domains within chromatin.
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RNA-seq evidence of biallelic expression of HMGN1 and 10 neighboring genes in at least one primary human tissue tested indicates that the expression of HMGN1 is uncoupled from the control of the maternally inherited 5mCpG imprints at the WRB differentially methylated region (DMR) in disomic controls or trisomy (Down syndrome) individuals.
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HMGN1 can serve as a useful clinical parameter for evaluating disease progression and predicting the outcomes for early-stage patients with non-small cell lung cancer .
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nucleosome binding protein HMGN1 as a new PCNA-interacting protein that enhances the binding of PCNA to chromatin
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extracellular HMGN1 acts as a novel alarmin critical for LPS-induced development of innate and adaptive immune responses.
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HMGN1 regulates the expression of methyl CpG-binding protein 2 (MECP2) in mouse and human, and affects the behavior of mice
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HMGN1 is not randomly distributed throughout the genome. Instead, the protein preferentially localizes to DNase I hypersensitive (HS) sites, promoters, functional enhancers, and transcription factor binding sites.
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Results show that four serine residues, i.e., Ser6, Ser85, Ser88, and Ser98, can be phosphorylated in high mobility group N1 (HMGN1).
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HMGN1 optimizes the cellular response to ionizing radiation and to other tumorigenic events; therefore, loss of this protein increases the tumor burden in mice.
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SWI/SNF functions independently of HMGN1
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Five serine residues, i.e., Ser6, Ser7, Ser85, Ser88, and Ser98, in HMGN1 can be phosphorylated by the kinase in vitro, and Ser6, Ser7, and Ser85 were new sites among these five sites.
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These findings indicate that HMGN1 regulates the expression of particular genes via specific protein-protein interactions with transcription factors at target gene regulatory regions.
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These studies demonstrate that the mode of binding of HMGNs to chromatin is cell cycle dependent.
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HMGN1 (HMG14) and HMGN2 (HMG17) potently repress ATP-dependent chromatin remodeling by four different molecular motor proteins.