U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    H1-1 H1.1 linker histone, cluster member [ Homo sapiens (human) ]

    Gene ID: 3024, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Brain age estimation at tract group level and its association with daily life measures, cardiac risk factors and genetic variants.

    Brain age estimation at tract group level and its association with daily life measures, cardiac risk factors and genetic variants.
    Salih A, Boscolo Galazzo I, Raisi-Estabragh Z, Rauseo E, Gkontra P, Petersen SE, Lekadir K, Altmann A, Radeva P, Menegaz G., Free PMC Article

    02/5/2022
    Data indicate that IgGs possessing an affinity to histone H1 were isolated by affinity chromatography and size exclusion chromatography.

    Anti-histone H1 IgGs possess proliferative activity towards human T-leukaemia CEM cells.
    Kit Y, Magorivska I, Bilyi R, Myronovskij S, Stoika R.

    07/1/2017
    Proper binding of histone H1.1 to chromatin is determined by the simultaneous and synergistic binding of its folded wing helix domain -C-terminal domains to the nucleosome.

    Interaction of chromatin with a histone H1 containing swapped N- and C-terminal domains.
    Hutchinson JB, Cheema MS, Wang J, Missiaen K, Finn R, Gonzalez Romero R, Th'ng JP, Hendzel M, Ausió J., Free PMC Article

    12/17/2016
    HIST1 cluster PcG methylation has a role in epigenesis in acute myeloid leukemia

    PcG methylation of the HIST1 cluster defines an epigenetic marker of acute myeloid leukemia.
    Tiberi G, Pekowska A, Oudin C, Ivey A, Autret A, Prebet T, Koubi M, Lembo F, Mozziconacci MJ, Bidaut G, Chabannon C, Grimwade D, Vey N, Spicuglia S, Calmels B, Duprez E.

    08/8/2015
    Results suggest the potential for histone H1 phosphorylation at threonine 146 as a clinical biomarker in breast cancer.

    Histone H1 phosphorylation in breast cancer.
    Harshman SW, Hoover ME, Huang C, Branson OE, Chaney SB, Cheney CM, Rosol TJ, Shapiro CL, Wysocki VH, Huebner K, Freitas MA., Free PMC Article

    04/25/2015
    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
    fluorescence recovery after photobleaching analyses suggested that TAF-I beta enhances the dissociation of H1.1 from chromatin in the living cell

    Role of Template Activating Factor-I as a chaperone in linker histone dynamics.
    Kato K, Okuwaki M, Nagata K.

    01/14/2012
    Data show that the multifunctional histone chaperone NPM1 interacts with linker histone H1 through its first acidic stretch (residues 120-132).

    The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone.
    Gadad SS, Senapati P, Syed SH, Rajan RE, Shandilya J, Swaminathan V, Chatterjee S, Colombo E, Dimitrov S, Pelicci PG, Ranga U, Kundu TK.

    08/6/2011
    Observational study of gene-disease association. (HuGE Navigator)

    Investigation 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.

    12/5/2010
    histone H2A.X phosphorylation by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding

    Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.
    Li A, Yu Y, Lee SC, Ishibashi T, Lees-Miller SP, Ausió J., Free PMC Article

    06/28/2010
    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 C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo

    The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo.
    Hendzel MJ, Lever MA, Crawford E, Th'ng JP.

    01/21/2010
    firstprevious page of 1 nextlast