ArticlePloS one2013
Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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
28 citing papers in PubMed, 42 citations in OpenAlex.
- NUPR1 in breast cancer: mechanisms and potential applications.Frontiers in physiology · 2026Review
- The intrinsically disordered protein NUPR1 binds to phospholipids.Protein science : a publication of the Protein Society · 2025Article
- EZH2 inhibition sensitizes MYC-high medulloblastoma cancers to PARP inhibition by regulating NUPR1-mediated DNA repair.Oncogene · 2025Article
- Article
- Development of an efficient NUPR1 inhibitor with anticancer activity.Scientific reports · 2024Article
- Two distinct males absent on the first (MOF)-containing histone acetyltransferases are involved in the epithelial-mesenchymal transition in different ways in human cells.Cellular and molecular life sciences : CMLS · 2022Article
- Design of Inhibitors of the Intrinsically Disordered Protein NUPR1: Balance between Drug Affinity and Target Function.Biomolecules · 2021Article
- NUPR1: A Critical Regulator of the Antioxidant System.Cancers · 2021Review
- Article
- Intrinsically Disordered Proteins as Regulators of Transient Biological Processes and as Untapped Drug Targets.Molecules (Basel, Switzerland) · 2021Review
- Induction of NUPR1 and AP‑1 contributes to the carcinogenic potential of nickel.Oncology reports · 2021Article
- NUPR1 is a critical repressor of ferroptosis.Nature communications · 2021Article
- Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.Frontiers in molecular biosciences · 2021Article
- Nuclear protein 1 imparts oncogenic potential and chemotherapeutic resistance in cancer.Cancer letters · 2020Review
- The Paralogue of the Intrinsically Disordered Nuclear Protein 1 Has a Nuclear Localization Sequence that Binds to Human Importin α3.International journal of molecular sciences · 2020Article
- ZZW-115-dependent inhibition of NUPR1 nuclear translocation sensitizes cancer cells to genotoxic agents.JCI insight · 2020Article
- A Phosphorylation-Induced Switch in the Nuclear Localization Sequence of the Intrinsically Disordered NUPR1 Hampers Binding to Importin.Biomolecules · 2020Article
- Targeting intrinsically disordered proteins involved in cancer.Cellular and molecular life sciences : CMLS · 2020Review
- Review
- Ligand-based design identifies a potent NUPR1 inhibitor exerting anticancer activity via necroptosis.The Journal of clinical investigation · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The stress protein Nupr1 is a highly basic, multifunctional, intrinsically disordered protein (IDP). MSL1 is a histone acetyl transferase-associated protein, known to intervene in the dosage compensation complex (DCC). In this work, we show that both Nupr1 and MSL1 proteins were recruited and formed a complex into the nucleus in response to DNA-damage, which was essential for cell survival in reply to cisplatin damage. We studied the interaction of Nupr1 and MSL1, and their binding affinities to DNA by spectroscopic and biophysical methods. The MSL1 bound to Nupr1, with a moderate affinity (2.8 µM) in an entropically-driven process. MSL1 did not bind to non-damaged DNA, but it bound to chemically-damaged-DNA with a moderate affinity (1.2 µM) also in an entropically-driven process. The Nupr1 protein bound to chemically-damaged-DNA with a slightly larger affinity (0.4 µM), but in an enthalpically-driven process. Nupr1 showed different interacting regions in the formed complexes with Nupr1 or DNA; however, they were always disordered ("fuzzy"), as shown by NMR. These results underline a stochastic description of the functionality of the Nupr1 and its other interacting partners.
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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.