Affinage

HPF1

Histone PARylation factor 1 · UniProt Q9NWY4

Length
346 aa
Mass
39.4 kDa
Annotated
2026-06-10
29 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

HPF1 is an accessory factor of the DNA-damage-induced ADP-ribosylation machinery that converts PARP1 and PARP2 into serine-specific ADP-ribosyltransferases (PMID:27067600, PMID:28190768). It is recruited to DNA lesions in a PARP1-dependent, catalytic-activity-independent manner, forms a robust complex with PARP1, and limits PARP1 hyper-automodification while promoting in trans ADP-ribosylation of histones (PMID:27067600). Mechanistically, HPF1 is both necessary and sufficient to redirect PARP1/PARP2 modification from aspartate/glutamate to serine residues, including endogenous serine sites in the PARP1 automodification domain (PMID:28190768). Structural and mutagenesis work establishes that HPF1 contributes its own catalytic glutamate (Glu284), positioned by HPF1 Arg239, into a composite active site shared with the PARP catalytic domain; this interaction is allosterically enhanced by NAD+ occupancy and DNA damage (PMID:32028527, PMID:33589610). Cryo-EM of PARP2–HPF1 on nucleosomes shows that DNA-break recognition and nucleosome bridging induce PARP conformational changes that license HPF1 binding and enzyme activation (PMID:32939087, PMID:41698892). HPF1 acts sub-stoichiometrically through a 'hit-and-run' mechanism, rapidly cycling among PARP molecules to initiate serine modification without persisting to interfere with PAR chain elongation, and it partitions reaction product toward shorter chains and free ADP-ribose, effectively tuning polymerase versus hydrolase output (PMID:34795260, PMID:33683197). Functionally, HPF1-dependent histone ADP-ribosylation drives rapid chromatin relaxation at breaks and promotes assembly of both homologous recombination and non-homologous end joining machineries (PMID:37106138), and is required for LIG3-XRCC1 recruitment supporting backup Okazaki fragment ligation (PMID:33872376). HPF1 also shapes base excision repair, stimulating PARP2-dependent histone modification on gapped nucleosome intermediates and enhancing pol β-catalyzed DNA synthesis (PMID:36356486, PMID:40076422). Through its formation of the PARP1–HPF1 complex, HPF1 is a determinant of clinical PARP inhibitor potency, where inhibitor dissociation kinetics from the complex best correlate with cellular efficacy (PMID:32028527, PMID:37531469).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2016 High

    Established HPF1 as a genuine PARP1-associated factor and placed it functionally in the DNA damage response, answering whether C4orf27 has any role in ADP-ribosylation signaling.

    Evidence Co-IP, laser micro-irradiation recruitment, in vitro ADP-ribosylation, and HPF1 knockout sensitivity assays in human cells

    PMID:27067600

    Open questions at the time
    • Molecular basis of how HPF1 redirects modification was unknown
    • Identity of the chemical linkage on histones not yet defined
  2. 2017 High

    Defined the core biochemical function: HPF1 is necessary and sufficient to switch PARP1/PARP2 amino-acid specificity from Asp/Glu to serine, explaining how histone serine ADP-ribosylation arises.

    Evidence Quantitative MS proteomics of HPF1 knockout cells plus in vitro PARP1/PARP2 reconstitution with site mapping

    PMID:28190768

    Open questions at the time
    • Structural mechanism of specificity switch not resolved
    • How HPF1 contributes catalytically was unknown
  3. 2020 High

    Resolved the catalytic mechanism by showing HPF1 forms a composite active site with PARP1/PARP2, donating Glu284 and being allosterically regulated by NAD+ and DNA damage, and structurally licensed by nucleosome bridging.

    Evidence Crystal structure of HPF1–PARP2 catalytic domain, NMR, cryo-EM of PARP2–HPF1–nucleosome complexes, mutagenesis, and cellular assays

    PMID:32028527 PMID:32939087 PMID:33141820 PMID:33186521

    Open questions at the time
    • Kinetics of HPF1 association/dissociation during catalysis unresolved
    • Effect on PAR chain length and product partitioning not quantified
  4. 2021 High

    Refined the catalytic model and kinetics: confirmed the Arg239–Glu284 salt bridge, established the sub-stoichiometric 'hit-and-run' mechanism, and revealed HPF1 shifts PARP1 toward shorter chains and hydrolase activity.

    Evidence Crystallography, mutagenesis, in vitro kinetic and product analyses (TLC/gel), cryo-EM, and titration assays with nucleosomes

    PMID:33589610 PMID:33683197 PMID:34732825 PMID:34795260

    Open questions at the time
    • Concentration/stoichiometry regimes producing stimulation vs inhibition not mapped in cells
    • Physiological NAD+/HPF1 ratios in vivo uncertain
  5. 2021 High

    Linked HPF1-dependent histone ADP-ribosylation to a specific repair outcome, showing it is required for LIG3-XRCC1 recruitment during backup Okazaki fragment ligation.

    Evidence Xenopus egg extract cell-free system with PARP1/HPF1 immunodepletion, chromatin fractionation, and ligation assays

    PMID:33872376

    Open questions at the time
    • Direct histone serine site driving LIG3 recruitment not pinpointed
    • Relevance to human replication not directly tested
  6. 2023 High

    Connected HPF1 enzymatic output to chromatin dynamics, demonstrating that HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation enabling both HR and NHEJ factor assembly at breaks.

    Evidence Live-cell FRAP, laser micro-irradiation, HPF1 knockout cells, chromatin compaction and repair factor recruitment assays

    PMID:37106138

    Open questions at the time
    • Which repair pathway choice is influenced not resolved
    • Chromatin reader of the serine mark not identified
  7. 2023 Medium

    Identified the PARP1–HPF1 complex, not PARP1 alone, as the pharmacologically relevant target whose inhibitor dissociation kinetics predict cellular potency.

    Evidence Kinetic kon/koff binding measurements for 8 PARP inhibitors with PARP1 and PARP1–HPF1, correlated with cellular potency

    PMID:37531469

    Open questions at the time
    • Effects measured for a limited inhibitor panel
    • Structural basis of HPF1-modulated inhibitor binding not solved
  8. 2023 Medium

    Extended HPF1 function beyond chromatin by showing it promotes PARP1-mediated PARylation of the RNA-binding protein HuR, affecting mRNA stability and cellular senescence.

    Evidence Reciprocal co-IP, RNP-IP, IP-based PARylation assays, mRNA half-life measurements in tendon stem/progenitor cells

    PMID:37713069

    Open questions at the time
    • Single lab, single cell system
    • Whether HuR PARylation is serine-linked not established
  9. 2024 Medium

    Delimited the repair contexts requiring HPF1, finding it largely dispensable for single-strand break repair where non-serine PARP1 automodification suffices for XRCC1 recruitment.

    Evidence HPF1-deficient cell lines, genotoxic sensitivity assays, comet assays, XRCC1 recruitment imaging across two cell lines

    PMID:39162207

    Open questions at the time
    • Reconciliation with earlier sensitivity phenotypes not fully resolved
    • Lesion-type specificity of HPF1 dependence incompletely defined
  10. 2025 Low

    Broadened the substrate landscape, showing HPF1 enhances and switches ADP-ribosylation of specific 60S ribosomal proteins and shapes base excision repair DNA synthesis by pol β.

    Evidence In vitro ADP-ribosylation with ribosomal proteins (preprint) and in vitro BER reconstitution with nucleosomes and pol β

    PMID:40076422 PMID:bio_10.1101_2025.09.15.676193

    Open questions at the time
    • Ribosomal protein finding is a non-peer-reviewed preprint from a single lab
    • Cellular relevance of these substrates untested
  11. 2026 High

    Captured the full-length PARP1–HPF1 complex on a DNA break and extended HPF1 regulation to PARylation-dependent biomolecular condensate assembly.

    Evidence Cryo-EM, SAXS, single-molecule DNA dynamics of full-length PARP1–HPF1; AFM and in vitro condensate assays with FUS

    PMID:41698892 PMID:41773021

    Open questions at the time
    • Condensate regulation demonstrated in vitro only
    • In vivo consequences of HPF1-tuned condensate dynamics unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How HPF1-imposed serine ADP-ribosylation is decoded by downstream readers and how its stoichiometric balance is controlled in vivo to dictate repair-pathway choice remain open.
  • No reader of the histone serine ADPr mark identified
  • In-cell control of HPF1:PARP stoichiometry undefined
  • Mechanistic link between specific serine marks and pathway selection unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 3
Localization
GO:0000228 nuclear chromosome 2 GO:0005634 nucleus 1
Pathway
R-HSA-73894 DNA Repair 4 R-HSA-4839726 Chromatin organization 3
Partners
FUSHURPARP1PARP2
Complex memberships
PARP1–HPF1 complexPARP2–HPF1–nucleosome complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2016 HPF1 (C4orf27) forms a robust protein complex with PARP-1 in cells, is recruited to DNA lesions in a PARP-1-dependent but catalytic-activity-independent manner, promotes PARP-1-dependent in trans ADP-ribosylation of histones, and limits DNA damage-induced hyper-automodification of PARP-1. Loss of HPF1 sensitizes human cells to DNA damaging agents and PARP inhibition. Co-immunoprecipitation, laser micro-irradiation recruitment assays, in vitro ADP-ribosylation assays, HPF1 knockout cell lines with genotoxic sensitivity assays Molecular cell High 27067600
2017 HPF1 is necessary and sufficient to redirect PARP-1 and PARP-2 ADP-ribosylation from aspartate/glutamate to serine residues. Adding HPF1 to in vitro PARP-1/PARP-2 reactions produces serine-linked ADP-ribosylation on histones and PARP-1 itself. Serine ADPr does not occur in cells lacking HPF1, and three endogenous serine ADPr sites were mapped to the PARP-1 automodification domain. Quantitative mass spectrometry-based proteomics of HPF1 knockout cells, in vitro PARP-1/PARP-2 ADP-ribosylation reconstitution with and without HPF1, site mapping by MS Molecular cell High 28190768
2020 HPF1 forms a composite (joint) active site with the catalytic domain of PARP1 or PARP2 by contributing a catalytic glutamate residue (Glu284) that is essential for serine-specific ADP-ribosylation after DNA damage. The HPF1–PARP interaction is allosterically enhanced by occupancy of the NAD+-binding site and by DNA damage signals, providing an additional regulatory layer. This composite active site implicates HPF1 as a determinant of response to clinical PARP inhibitors. Crystal/co-structure of HPF1 bound to PARP2 catalytic domain, NMR, biochemical mutagenesis assays, cellular ADP-ribosylation assays Nature High 32028527
2020 Cryo-EM structure of human PARP2–HPF1 bound to a nucleosome shows that PARP2–HPF1 bridges two nucleosomes with broken DNA aligned for ligation. DNA bridging induces structural changes in PARP2 that signal break recognition to the catalytic domain, licensing HPF1 binding and PARP2 activation. Active PARP2 cycles through different conformational states to exchange NAD+ and substrate. Cryo-electron microscopy, biochemical ADP-ribosylation activity assays with nucleosome substrates Nature High 32939087
2020 HPF1 is required for a phospho-guided chemoenzymatic serine ADP-ribosylation reaction; the HPF1/PARP1 writer complex can be used to install authentic serine-linked ADP-ribose at defined positions on peptides in a scalable, precise manner. Chemoenzymatic in vitro reconstitution using HPF1/PARP1 complex, phage display antibody selection, mono-ADPr proteomics Cell Medium 33186521
2020 Cryo-EM structure of two nucleosomes bridged by PARP2 shows that the PARP2 conformation adopted upon damaged-chromatin binding provides a binding platform for HPF1, and the resulting HPF1•PARP2•nucleosome complex is enzymatically active. Cryo-electron microscopy, in vitro ADP-ribosylation activity assays PloS one Medium 33141820
2021 Crystal structures of human HPF1/PARP1-CAT complex and mutagenesis data confirm that HPF1 Arg239 salt-bridges to Glu284/Asp286 to position Glu284 as the catalytic base for serine ADP-ribosylation, maintains the local HPF1 conformation to limit PARP1 automodification, and facilitates HPF1/PARP1 binding by neutralizing negative charge at Glu284. X-ray crystallography (1.98 Å HPF1/PARP1-CAT; 1.57–1.71 Å HPF1 alone), site-directed mutagenesis, quantitative binding assays Nature communications High 33589610
2021 HPF1 efficiently regulates PARP1/2 at sub-stoichiometric ratios matching their relative cellular abundances via a 'hit-and-run' mechanism: HPF1 rapidly associates/dissociates from multiple PARP1 molecules, initiating serine modification before glutamate/aspartate modification initiates, and accelerating initiation to be more comparable to elongation. This ensures HPF1 contributions during initiation do not persist and interfere with PAR chain elongation. Biochemical kinetic assays (in vitro ADP-ribosylation with sub-stoichiometric HPF1), cryo-EM structural analysis of HPF1/PARP1 on DNA break, DNA retention assays Nature communications High 34795260
2021 HPF1 provides Glu284 as a catalytic base that substantially redirects PARylation by PARP1 such that histones in nucleosomes become primary recipients of PAR chains. Surprisingly, HPF1 partitions most reaction product to free ADP-ribose (ADPR), resulting in much shorter PAR chains — a switch from PARP1 polymerase to hydrolase activity. In vitro PARP1 reconstitution with nucleosomes as activators and substrates, product analysis by TLC and gel electrophoresis, mutagenesis eLife High 33683197
2021 HPF1 exhibits dual function: it can stimulate DNA-dependent and DNA-independent autoPARylation of PARP1 and PARP2 as well as heteroPARylation of histones in a defined range of HPF1 and NAD+ concentrations, while at other concentrations it limits PARylation and stimulates NAD+-hydrolase activity. PARP2 is more efficiently stimulated by HPF1 in autoPARylation and is more active in heteroPARylation of histones than in automodification. In vitro biochemical PARylation assays with purified components at varying stoichiometries, nucleosome substrates Communications biology Medium 34732825
2021 PARP1-HPF1-dependent ADP-ribosylation of histone H3 is required for recruitment of LIG3-XRCC1 onto chromatin for backup Okazaki fragment ligation when LIG1 is absent. Depletion of PARP1 or HPF1 in Xenopus egg extracts prevents LIG3 chromatin recruitment and Okazaki fragment joining in LIG1-depleted extracts. Cell-free system from Xenopus egg extracts, immunodepletion of PARP1 or HPF1, chromatin fractionation, in vitro ligation assays Nucleic acids research High 33872376
2023 HPF1 controls prolonged histone ADP-ribosylation at DNA breaks by regulating both the number and length of ADP-ribose chains. HPF1-dependent histone ADP-ribosylation triggers rapid chromatin unfolding (relaxation) near damage sites, facilitating access to DNA and promoting assembly of both homologous recombination and non-homologous end joining repair machineries. Live-cell FRAP/fluorescence microscopy, laser micro-irradiation, HPF1 knockout cells, chromatin compaction assays, repair factor recruitment assays (HR and NHEJ markers) Nature structural & molecular biology High 37106138
2023 The rate of dissociation (koff) of PARP inhibitors from the PARP1–HPF1 complex, rather than from PARP1 alone, best correlates with inhibitor potency in cells. HPF1 slightly increases the affinity of certain inhibitors (e.g., fluzoparib, olaparib) for PARP1. Kinetic binding assays (kon and koff measurements) for 8 PARP inhibitors with PARP1 and PARP1-HPF1 complex, correlation with cellular potency data Biochemistry Medium 37531469
2022 HPF1-dependent histone PARylation catalyzed by PARP2 is specifically and most significantly stimulated by an incised AP site-containing BER DNA intermediate (1-nucleotide gap with 5'-dRP) in the context of nucleosomes. PARP2 affinity for DNA strongly depends on gap presence, and HPF1-induced stimulation of histone modification is a peculiar feature of PARP2 with gapped nucleosome substrates. In vitro PARylation assays with purified PARP1, PARP2, HPF1, and nucleosome core particles bearing defined DNA damage intermediates; binding affinity measurements DNA repair Medium 36356486
2023 HPF1 interacts with PARP1 (confirmed by reciprocal co-IP) and promotes PARP1-mediated poly-ADP ribosylation of the RNA-binding protein HuR. HPF1-mediated HuR PARylation reduces HuR binding to p16 and p21 mRNAs, decreasing their stability (half-life), thereby modulating tendon stem/progenitor cell senescence. Reciprocal co-immunoprecipitation (HPF1 and PARP1), RNP-IP (HuR-mRNA binding), IP-based PARylation assay for HuR, mRNA half-life measurements, siRNA knockdown and overexpression Genes & genomics Medium 37713069
2024 HPF1 loss does not generally increase cellular sensitivity to SSB-inducing genotoxins and SSBR kinetics are largely unaffected in HPF1-deficient cells. Poly-ADP-ribose chains sufficient to recruit XRCC1 are maintained at SSB sites even without HPF1, likely reflecting PARP1 auto-poly-ADP-ribosylation at non-serine residues. HPF1 and histone serine ADP-ribosylation are largely dispensable for PARP1-dependent SSBR. HPF1-deficient cell lines, genotoxic sensitivity assays, SSBR kinetics assays (comet assay, XRCC1 recruitment imaging), ADP-ribosylation detection Nucleic acids research Medium 39162207
2025 HPF1 modulates efficiency of DNA polymerase β (pol β)-catalyzed DNA synthesis in nucleosomes by regulating total poly(ADP-ribosyl)ation by PARP1 and especially PARP2. HPF1-dependent PARylation results in more efficient short-patch BER DNA synthesis in nucleosomes and also positively regulates long-patch BER. In vitro BER reconstitution with nucleosome substrates, DNA synthesis assays with pol β, comparing reactions with/without HPF1 International journal of molecular sciences Medium 40076422
2026 Cryo-EM of full-length PARP1 on a DNA single-strand break with HPF1 and a Timeless fragment shows that PARP1 remains dynamic even when its multi-domain structure is organized on a DNA break, with the minimal catalytic region displaying high mobility relative to DNA-engaging domains. The organization of PARP1 domains on a DNA break releases a tethered, constitutively active catalytic region to modify molecules in a radius surrounding the break. Single-particle cryo-EM, single-molecule DNA dynamics, small-angle X-ray scattering (SAXS) Nature communications High 41698892
2026 HPF1 regulates the formation of FUS-dependent DNA-rich compartments (condensates) by modulating PARP1 and PARP2 PARylation. Excess HPF1 over PARP1 diminishes PARP1 activity and reduces compartment size, but excess HPF1 over PARP2 does not significantly affect PARP2 activity or compartment size. HPF1 stimulates heteroPARylation of FUS (more strongly via PARP2 than PARP1), and HPF1-dependent intensive PARylation of FUS impairs DNA-rich compartment assembly. Atomic force microscopy, biochemical ADP-ribosylation assays, in vitro condensate formation assays Nucleic acids research Medium 41773021
2025 HPF1 enhances ADP-ribosylation of certain free ribosomal proteins from the 60S subunit (RPL4, RPL6, RPL13A/RPL15) by PARP1 and PARP2, and switches the modification preferentially to serine/tyrosine residues on these proteins. HPF1-dependent enhancement is selective for 60S RPs and does not occur for 40S RPs. In vitro ADP-ribosylation assays with radioactively labeled NAD+, ribosomal subunit proteins, and purified HPF1/PARP1/PARP2; SDS-PAGE analysis bioRxivpreprint Low bio_10.1101_2025.09.15.676193
2025 In the presence of HPF1, PARP2 serine 8 and serine 73 in the N-terminus are the predominant automodification sites. Serine 8 (present in both human PARP2 isoforms) is the major automodification site, and PARylation at these N-terminal serines is required for HPF1-dependent release of PARP2 from DNA damage sites. Site-directed mutagenesis of PARP2 serine residues, gel-based PARylation assays, fluorescence polarization DNA-release assay bioRxivpreprint Medium bio_10.1101_2025.07.01.662498

Source papers

Stage 0 corpus · 29 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 Serine ADP-Ribosylation Depends on HPF1. Molecular cell 301 28190768
2016 HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity. Molecular cell 263 27067600
2020 HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation. Nature 227 32028527
2020 Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin. Nature 114 32939087
2020 An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation. Cell 90 33186521
2021 HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones. Nature communications 71 33589610
2021 HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications. Nature communications 63 34795260
2023 HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage. Nature structural & molecular biology 59 37106138
2021 HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase. eLife 57 33683197
2008 Radical-scavenging abilities and antioxidant properties of theaflavins and their gallate esters in H2O2-mediated oxidative damage system in the HPF-1 cells. Toxicology in vitro : an international journal published in association with BIBRA 52 18502093
2021 HPF1-dependent PARP activation promotes LIG3-XRCC1-mediated backup pathway of Okazaki fragment ligation. Nucleic acids research 48 33872376
2020 Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1. PloS one 38 33141820
2021 Dual function of HPF1 in the modulation of PARP1 and PARP2 activities. Communications biology 29 34732825
2020 Intragenic repeat expansion in the cell wall protein gene HPF1 controls yeast chronological aging. Genome research 26 32277013
2024 Dispensability of HPF1 for cellular removal of DNA single-strand breaks. Nucleic acids research 16 39162207
2023 Slow Dissociation from the PARP1-HPF1 Complex Drives Inhibitor Potency. Biochemistry 13 37531469
2022 The HPF1-dependent histone PARylation catalyzed by PARP2 is specifically stimulated by an incised AP site-containing BER DNA intermediate. DNA repair 11 36356486
2017 SERious Surprises for ADP-Ribosylation Specificity: HPF1 Switches PARP1 Specificity to Ser Residues. Molecular cell 10 28257697
2024 High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair. Scientific reports 7 38365924
2023 HTS discovery of PARP1-HPF1 complex inhibitors in cancer. SLAS discovery : advancing life sciences R & D 6 37844763
2023 HPF1 regulates tendon stem/progenitor cell senescence and tendon repair via PARP1-mediated poly-ADP ribosylation of HuR. Genes & genomics 5 37713069
2018 Analysis of hpf1 expression and function in early embryonic development of zebrafish. Development genes and evolution 4 29549427
2023 [Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1]. Molekuliarnaia biologiia 3 37000654
2023 ANP32B promotes colorectal cancer cell progression and reduces cell sensitivity to PRAP1 inhibitor through up-regulating HPF1. Heliyon 3 38192816
2025 HPF1 Regulates Pol β Efficiency in Nucleosomes via the Modulation of Total Poly(ADP-Ribose) Synthesis. International journal of molecular sciences 2 40076422
2023 Germline HPF1 retrogene insertion in RB1 gene involved in cancer predisposition. Journal of medical genetics 1 37541786
2026 PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation. Nature communications 0 41698892
2026 HPF1 regulates the formation of FUS-dependent compartments by PARP1 and PARP2 activation on damaged DNA. Nucleic acids research 0 41773021
2026 The Structure of the Nucleosomal DNA Repair Intermediate Affects the HPF1-Independent Automodification Activity of PARP2. Biochemistry. Biokhimiia 0 41936561

Missed literature

Know a paper Affinage missed for HPF1? Flag it for the maintainers and the community.

No submissions yet.