ArticleBiomolecular NMR assignments2026
NMR study of human macroPARPs domains:
Article in Biomolecular NMR assignments, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-ribosylation is a reversible post-translational modification that regulates diverse cellular processes, including DNA damage repair, transcription, cell proliferation and innate immune responses, and is primarily catalyzed by members of the PARP family. While all 17 human PARPs contain a conserved C-terminal ADP-ribosyltransferase (ART) domain, only catalytically active members transfer ADP-ribose (ADPr) from nicotinamide adenine dinucleotide (NAD⁺) onto proteins or nucleic acids, and their N-terminal accessory domains, such as macro domains (MDs), WWE domains or RNA-binding motifs, mediate interactions that diversify PARP functions. Human PARP9 (hPARP9), known also as BAL1, is catalytically inactive due to sequence variations in catalytically important residues in the ART domain, but plays crucial roles in antiviral and antibacterial defense, stress responses and tumor progression through its heterodimeric interaction with the E3 ubiquitin ligase DTX3L. hPARP9 contains two tandem MDs (MD1 and MD2), with MD1 acting as a MacroD-type hydrolase "eraser" of mono-ADP-ribosylation (MARylation), while MD2 functions as an ADPr "reader". Their different role in the ADP-ribosylation pathway highlights the importance of structural and functional characterization for understanding ADPr-mediated cellular signaling. In this study, we report the NMR backbone and side-chain resonance assignments of hPARP9 MD1 in both apo and ADPr bound states. In addition, the secondary structure predictions using TALOS+ server and the Chemical Shift Perturbation (CSP) analysis upon ADPr binding are presented. The latter illustrates the MD substrate's accommodation mode and identifies the residues involved in ADPr binding, thus related to MDs' hydrolytic activity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.