Evidence map›Paper›PMID 37126687›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Switch-like compaction of poly(ADP-ribose) upon cation binding.

Mohsen Badiee, Adam L Kenet, Laura R Ganser, Tapas Paul, Sua Myong, Anthony K L Leung

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  4. Modulation of histone tail electrostatic potentials in nucleosome core particles by acetylation and PARylation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Review
  7. Review
  8. Poly(ADP-ribose) binding sites on collagen I fibrils for nucleating intrafibrillar bone mineral.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
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  14. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Mohsen BadieeDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.ORCID 0000-0003-3722-4609
Adam L KenetDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.ORCID 0000-0003-2109-3480
Laura R GanserDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218.
Tapas PaulDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218.ORCID 0000-0001-7508-5676
Sua MyongDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218.ORCID 0000-0001-9098-3423
Anthony K L LeungDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.ORCID 0000-0001-5569-4036
Johns Hopkins University · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Role of ADP-Ribosylation in Stress Granules-Equipment SupplementR01GM104135 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Anthony K L Leung · 2015 to 2026
$4.2M
Defining the Role of Poly ADP-ribose in Biomolecular Condensation in ALS and FTLDRF1AG071326 · NIA · JOHNS HOPKINS UNIVERSITY · PI LEUNG, ANTHONY K L, MYONG, SUA · 2020 to 2020
$2.6M
NCI NIH HHS T32 CA009110NIA NIH HHS RF1 AG071326NIGMS NIH HHS R01 GM104135
6 · The paper itself

Abstract

Poly(ADP-ribose) (PAR) is a homopolymer of adenosine diphosphate ribose that is added to proteins as a posttranslational modification to regulate numerous cellular processes. PAR also serves as a scaffold for protein binding in macromolecular complexes, including biomolecular condensates. It remains unclear how PAR achieves specific molecular recognition. Here, we use single-molecule fluorescence resonance energy transfer (smFRET) to evaluate PAR flexibility under different cation conditions. We demonstrate that, compared to RNA and DNA, PAR has a longer persistence length and undergoes a sharper transition from extended to compact states in physiologically relevant concentrations of various cations (Na

Indexed as

Adenosine Diphosphate RibosePoly Adenosine Diphosphate RiboseCell Physiological PhenomenaProtein BindingProtein Processing, Post-TranslationalAdenosine Diphosphate RibosePoly Adenosine Diphosphate RibosePAR-binding proteinpersistence lengthpoly(ADP-ribose)single molecule FRET

Identifiers

PMID37126687
PMCPMC10175808
OpenAlexW4367623870

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.