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    HPF1 histone PARylation factor 1 [ Homo sapiens (human) ]

    Gene ID: 54969, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Dispensability of HPF1 for cellular removal of DNA single-strand breaks.

    Dispensability of HPF1 for cellular removal of DNA single-strand breaks.
    Hrychova K, Burdova K, Polackova Z, Giamaki D, Valtorta B, Brazina J, Krejcikova K, Kuttichova B, Caldecott KW, Hanzlikova H., Free PMC Article

    11/5/2024
    Germline HPF1 retrogene insertion in RB1 gene involved in cancer predisposition.

    Germline HPF1 retrogene insertion in RB1 gene involved in cancer predisposition.
    Le Gall J, Dehainault C, Boutte M, Petitalot A, Caputo SM, Courtois L, Vacher S, Bieche I, Radvanyi F, Pacquement H, Doz F, Lumbroso-Le Rouic L, Gauthier Villars M, Stoppa-Lyonnet D, Lallemand F, Houdayer C, Golmard L.

    01/11/2024
    HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.

    HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.
    Rudolph J, Roberts G, Muthurajan UM, Luger K., Free PMC Article

    02/12/2022
    HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.

    HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.
    Langelier MF, Billur R, Sverzhinsky A, Black BE, Pascal JM., Free PMC Article

    01/1/2022
    Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.

    Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.
    Kurgina TA, Moor NA, Kutuzov MM, Naumenko KN, Ukraintsev AA, Lavrik OI., Free PMC Article

    12/18/2021
    The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.

    The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
    Hendriks IA, Buch-Larsen SC, Prokhorova E, Elsborg JD, Rebak AKLFS, Zhu K, Ahel D, Lukas C, Ahel I, Nielsen ML., Free PMC Article

    11/6/2021
    Serine-linked PARP1 auto-modification controls PARP inhibitor response.

    Serine-linked PARP1 auto-modification controls PARP inhibitor response.
    Prokhorova E, Zobel F, Smith R, Zentout S, Gibbs-Seymour I, Schützenhofer K, Peters A, Groslambert J, Zorzini V, Agnew T, Brognard J, Nielsen ML, Ahel D, Huet S, Suskiewicz MJ, Ahel I., Free PMC Article

    08/7/2021
    HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.

    HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.
    Sun FH, Zhao P, Zhang N, Kong LL, Wong CCL, Yun CH., Free PMC Article

    02/27/2021
    Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1.

    Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1.
    Gaullier G, Roberts G, Muthurajan UM, Bowerman S, Rudolph J, Mahadevan J, Jha A, Rae PS, Luger K., Free PMC Article

    12/26/2020
    Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.

    Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.
    Bilokapic S, Suskiewicz MJ, Ahel I, Halic M., Free PMC Article

    10/24/2020
    HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation; as HPF1 forms a joint active site with PARP1 or PARP2, our data implicate HPF1 as an important determinant of the response to clinical PARP inhibitors

    HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.
    Suskiewicz MJ, Zobel F, Ogden TEH, Fontana P, Ariza A, Yang JC, Zhu K, Bracken L, Hawthorne WJ, Ahel D, Neuhaus D, Ahel I., Free PMC Article

    06/6/2020
    Here, the authors show that serine ADP-ribosylation represents the major fraction of ADP-ribosylation synthesized after DNA damage in mammalian cells and that globally serine ADP-ribosylation is dependent on HPF1, PARP1 and ARH3. In the absence of HPF1, glutamate/aspartate becomes the main target residues for ADP-ribosylation.

    Serine is the major residue for ADP-ribosylation upon DNA damage.
    Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I., Free PMC Article

    07/20/2019
    Serine residues can be ADP-ribosylated by PARP-1 and PARP-2. This serine specificity is conferred by HPF1, a protein that interacts with PARP-1/2.

    Serine ADP-Ribosylation Depends on HPF1.
    Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I., Free PMC Article

    09/9/2017
    HPF1/C4orf27 Is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity in the DNA damage response.

    HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity.
    Gibbs-Seymour I, Fontana P, Rack JGM, Ahel I., Free PMC Article

    08/5/2017
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
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