ArticleProceedings of the National Academy of Sciences of the United States of America2020
TiPARP forms nuclear condensates to degrade HIF-1α and suppress tumorigenesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
70 citing papers in PubMed, 1 synthesis or guideline pooled it, 110 citations in OpenAlex.
- Pooled it
- Biomolecular Condensates Integrate Transcriptional and Epigenetic Responses to Hypoxia.International journal of molecular sciences · 2026Review
- High PARP7 Expression is Associated with Higher Estrogen Response and Immune Suppression but Less Cell Proliferation and Better Survival in Breast Cancer.Annals of surgical oncology · 2026Article
- PARP7 alleviates lipopolysaccharide-induced acute kidney injury by inhibiting TBK1-driven inflammation in renal tubular epithelial cells.Molecular medicine (Cambridge, Mass.) · 2026Article
- Temporal variation in markers of immune signaling and wound repair in primary human airway epithelial cells following acute versus repeated woodsmoke condensate exposure.Toxicological sciences : an official journal of the Society of Toxicology · 2026Article
- PARP7 protects the lung epithelial barrier from diverse environmental threats.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- NADCell reports · 2026Article
- PARG regulates the proteasomal degradation of TARG1.Cell reports · 2026Article
- Roles of ADP-Ribosyltransferases in Cancer.Oncology research · 2026Review
- Ubiquitin pathway blockade reveals endogenous ADP-ribosylation marking PARP7 and AHR for degradation.The EMBO journal · 2026Article
- METTL16 Promotes Cerebral Ischemia-Reperfusion Injury via mInternational journal of general medicine · 2026Article
- RNF114 and RNF166 exemplify reader-writer E3 ligases that extend K11 polyubiquitin onto sites of MARUbylation.The EMBO journal · 2025Article
- PARP7 is a proteotoxic stress sensor that labels proteins for degradation.The EMBO journal · 2025Article
- Review
- PARP7 inhibition stabilizes STAT1/STAT2 and relieves experimental autoimmune encephalomyelitis in mice.Cell reports · 2025Article
- Mono-ADP-ribosylating PARP enzymes in cellular signaling and disease.Journal of cell science · 2025Review
- Second-order threat conditioning in the amygdala-posterior piriform cortex network.Communications biology · 2025Article
- Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damage.DNA repair · 2025Article
- PARP7 inhibits type I interferon signaling to prevent autoimmunity and lung disease.The Journal of experimental medicine · 2025Article
- PARP7 as a new target for activating anti-tumor immunity in cancer.EMBO molecular medicine · 2025Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Precisely controlling the activation of transcription factors is crucial for physiology. After a transcription factor is activated and carries out its transcriptional activity, it also needs to be properly deactivated. Here, we report a deactivation mechanism of HIF-1 and several other oncogenic transcription factors. HIF-1 promotes the transcription of an ADP ribosyltransferase, TiPARP, which serves to deactivate HIF-1. Mechanistically, TiPARP forms distinct nuclear condensates or nuclear bodies in an ADP ribosylation-dependent manner. The TiPARP nuclear bodies recruit both HIF-1α and an E3 ubiquitin ligase HUWE1, which promotes the ubiquitination and degradation of HIF-1α. Similarly, TiPARP promotes the degradation of c-Myc and estrogen receptor. By suppressing HIF-1α and other oncogenic transcription factors, TiPARP exerts strong antitumor effects both in cell culture and in mouse xenograft models. Our work reveals TiPARP as a negative-feedback regulator for multiple oncogenic transcription factors, provides insights into the functions of protein ADP-ribosylation, and suggests activating TiPARP as an anticancer strategy.
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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.