Evidence map›Paper›PMID 34311273›Full record

ReviewDNA repair2021

Biomolecular condensates at sites of DNA damage: More than just a phase.

Vincent Spegg, Matthias Altmeyer

Open access · hybridAbstract readReview
In one paragraph

Review in DNA repair, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed, 1 pooled it
5.8field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 1 synthesis or guideline pooled it, 94 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

2 authors at 1 institution in 1 country.

Vincent SpeggDepartment of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
Matthias AltmeyerDepartment of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland. Electronic address: matthias.altmeyer@uzh.ch.
University of Zurich · CH

Funding

European Research Council 714326
6 · The paper itself

Abstract

Protein recruitment to DNA break sites is an integral part of the DNA damage response (DDR). Elucidation of the hierarchy and temporal order with which DNA damage sensors as well as repair and signaling factors assemble around chromosome breaks has painted a complex picture of tightly regulated macromolecular interactions that build specialized compartments to facilitate repair and maintenance of genome integrity. While many of the underlying interactions, e.g. between repair factors and damage-induced histone marks, can be explained by lock-and-key or induced fit binding models assuming fixed stoichiometries, structurally less well defined interactions, such as the highly dynamic multivalent interactions implicated in phase separation, also participate in the formation of multi-protein assemblies in response to genotoxic stress. Although much remains to be learned about these types of cooperative and highly dynamic interactions and their functional roles, the rapidly growing interest in material properties of biomolecular condensates and in concepts from polymer chemistry and soft matter physics to understand biological processes at different scales holds great promises. Here, we discuss nuclear condensates in the context of genome integrity maintenance, highlighting the cooperative potential between clustered stoichiometric binding and phase separation. Rather than viewing them as opposing scenarios, their combined effects can balance structural specificity with favorable physicochemical properties relevant for the regulation and function of multilayered nuclear condensates.

Indexed as

DNA DamageDNA RepairAnimalsCell NucleusChromatinChromatin Assembly and DisassemblyDNADNA-Binding ProteinsEukaryotaHumansIntrinsically Disordered ProteinsTumor Suppressor p53-Binding Protein 1ChromatinDNADNA-Binding ProteinsIntrinsically Disordered ProteinsTumor Suppressor p53-Binding Protein 1Biomolecular condensatesDNA damage response (DDR)DNA repairGenome stabilityHigher-order assembliesIntrinsically disordered regions (IDR)Liquid-liquid phase separation (LLPS)Low complexity domains (LCD)Multivalent interactions

Identifiers

PMID34311273
PMCPMC7612016
OpenAlexW3186924676

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.