Evidence map›Paper›PMID 37115110›Full record

ReviewChemical reviews2023

Regulation of Biomolecular Condensates by Poly(ADP-ribose).

Kevin Rhine, Hana M Odeh, James Shorter, Sua Myong

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. NADThe Journal of general virology · 2026
    Review
  4. Targeting the NADTrends in molecular medicine · 2026
    Review
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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

4 authors at 2 institutions in 1 country.

Kevin RhineProgram in Cell, Molecular, Developmental Biology, and Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, United States.
Hana M OdehDepartment of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania 19104, United States.
James ShorterDepartment of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0001-5269-8533
Sua MyongProgram in Cell, Molecular, Developmental Biology, and Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, United States.ORCID 0000-0001-9098-3423
Johns Hopkins University · USUniversity of Pennsylvania · US

Funding

Defining the mechanistic basis of a prion disaggregaseR01GM099836 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SHORTER, JAMES · 2013 to 2024
$3.9M
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
Molecular Assembly and Disassembly of RNA-Protein Complexes Implicated in ALS/FTDRF1NS113636 · NINDS · JOHNS HOPKINS UNIVERSITY · PI MYONG, SUA · 2019 to 2019
$2.0M
Mechanisms of Protein Disaggregation and Turnover by AAA+ ChaperonesR01GM138690 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SOUTHWORTH, DANIEL RYLAND · 2021 to 2024
$1.9M
Engineering therapeutic TRIM11 disaggregases for Alzheimer's Disease-Related Dementias (ADRDs)R21AG079609 · NIA · UNIVERSITY OF PENNSYLVANIA · PI SHORTER, JAMES · 2022 to 2022
$447k
Programming human protein disaggregases against FTDR21AG065854 · NIA · UNIVERSITY OF PENNSYLVANIA · PI SHORTER, JAMES · 2020 to 2020
$446k
Elucidating the molecular mechanism underlying ALS/FTD-linked FUS mutations with single-molecule resolutionF31NS113439 · NINDS · JOHNS HOPKINS UNIVERSITY · PI RHINE, KEVIN · 2020 to 2021
$92k
NIA NIH HHS R21 AG065854NIA NIH HHS R21 AG079609NIA NIH HHS RF1 AG071326NIGMS NIH HHS R01 GM099836NIGMS NIH HHS R01 GM138690NINDS NIH HHS F31 NS113439NINDS NIH HHS RF1 NS113636
6 · The paper itself

Abstract

Biomolecular condensates are reversible compartments that form through a process called phase separation. Post-translational modifications like ADP-ribosylation can nucleate the formation of these condensates by accelerating the self-association of proteins. Poly(ADP-ribose) (PAR) chains are remarkably transient modifications with turnover rates on the order of minutes, yet they can be required for the formation of granules in response to oxidative stress, DNA damage, and other stimuli. Moreover, accumulation of PAR is linked with adverse phase transitions in neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. In this review, we provide a primer on how PAR is synthesized and regulated, the diverse structures and chemistries of ADP-ribosylation modifications, and protein-PAR interactions. We review substantial progress in recent efforts to determine the molecular mechanism of PAR-mediated phase separation, and we further delineate how inhibitors of PAR polymerases may be effective treatments for neurodegenerative pathologies. Finally, we highlight the need for rigorous biochemical interrogation of ADP-ribosylation in vivo and in vitro to clarify the exact pathway from PARylation to condensate formation.

Indexed as

Poly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesBiomolecular CondensatesPoly ADP RibosylationProtein Processing, Post-TranslationalPoly Adenosine Diphosphate RibosePoly(ADP-ribose) Polymerases

Identifiers

PMID37115110
PMCPMC10524010
OpenAlexW4367319294

What OpenQuestion holds

Textmetadata
LicenceTDM
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.