Evidence map›Paper›PMID 34291085›Full record

ArticleFrontiers in molecular biosciences2021

Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.

Alessio Bonucci, Martina Palomino-Schätzlein, Paula Malo de Molina, Arantxa Arbe, Roberta Pierattelli, Bruno Rizzuti, Juan L Iovanna, José L Neira

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.2field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. The intrinsically disordered protein NUPR1 binds to phospholipids.Protein science : a publication of the Protein Society · 2025
    Article
  3. Pitfalls of Using ANS Dye Under Molecular Crowding Conditions.International journal of molecular sciences · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Ultrafast Spectroscopy Reveals Slow Water Dynamics in Biocondensates.Journal of the American Chemical Society · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 3 countries.

Alessio BonucciCERM & Department of Chemistry "Ugo Schiff", University of Florence, Sesto Fiorentino (Florence), Italy.
Martina Palomino-SchätzleinNMR Laboratory, Centro de Investigación Príncipe Felipe, Valencia, Spain.
Paula Malo de MolinaCentro de Física de Materiales (CFM), CSIC-UPV/EHU, San Sebastián, Spain.
Arantxa ArbeCentro de Física de Materiales (CFM), CSIC-UPV/EHU, San Sebastián, Spain.
Roberta PierattelliCERM & Department of Chemistry "Ugo Schiff", University of Florence, Sesto Fiorentino (Florence), Italy.
Bruno RizzutiCNR-NANOTEC, Licryl-UOS Cosenza and CEMIF.Cal, Department of Physics, University of Calabria, Rende, Italy.
Juan L IovannaCentre de Recherche en Cancérologie de Marseille (CRCM), INSERM U1068, CNRS UMR 7258, Aix-Marseille Université and Institut Paoli-Calmettes, Parc Scientifique et Technologique de Luminy, Marseille, France.
José L NeiraInstituto de Biocomputación y Física de Sistemas Complejos (BIFI), Joint Units IQFR-CSIC-BIFI and GBsC-CSIC-BIFI, Universidad de Zaragoza, Zaragoza, Spain.
Material Physics Center · ESUniversidad de Zaragoza · ESUniversity of Florence · ITCentre National de la Recherche Scientifique · FRCentro de Investigacion Principe Felipe · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intracellular environment is crowded with macromolecules, including sugars, proteins and nucleic acids. In the cytoplasm, crowding effects are capable of excluding up to 40% of the volume available to any macromolecule when compared to dilute conditions. NUPR1 is an intrinsically disordered protein (IDP) involved in cell-cycle regulation, stress-cell response, apoptosis processes, DNA binding and repair, chromatin remodeling and transcription. Simulations of molecular crowding predict that IDPs can adopt compact states, as well as more extended conformations under crowding conditions. In this work, we analyzed the conformation and dynamics of NUPR1 in the presence of two synthetic polymers, Ficoll-70 and Dextran-40, which mimic crowding effects in the cells, at two different concentrations (50 and 150 mg/ml). The study was carried out by using a multi-spectroscopic approach, including: site-directed spin labelling electron paramagnetic resonance spectroscopy (SDSL-EPR), nuclear magnetic resonance spectroscopy (NMR), circular dichroism (CD), small angle X-ray scattering (SAXS) and dynamic light scattering (DLS). SDSL-EPR spectra of two spin-labelled mutants indicate that there was binding with the crowders and that the local dynamics of the C and N termini of NUPR1 were partially affected by the crowders. However, the overall disordered nature of NUPR1 did not change substantially in the presence of the crowders, as shown by circular dichroism CD and NMR, and further confirmed by EPR. The changes in the dynamics of the paramagnetic probes appear to be related to preferred local conformations and thus crowding agents partially affect some specific regions, further pinpointing that NUPR1 flexibility has a key physiological role in its activity.

Indexed as

crowderselectron paramagnetic resonanceintrinsically disordered proteinNMRnuclear protein 1spin labelling

Identifiers

PMID34291085
PMCPMC8287036
OpenAlexW3185740880

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.