Evidence map›Paper›PMID 24560923›Full record

ArticleMolecular cell2014

Polyphosphate is a primordial chaperone.

Michael J Gray, Wei-Yun Wholey, Nico O Wagner, Claudia M Cremers, Antje Mueller-Schickert, Nathaniel T Hock, Adam G Krieger, Erica M Smith, Robert A Bender, James C A Bardwell and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 231 papers.

0numbers the graph read from it
0cells of the map it votes in
231citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

231 citing papers in PubMed, 363 citations in OpenAlex.

  1. Inorganic polyphosphate chelates CaBiochemistry and biophysics reports · 2026
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  5. The roles and synthesis of inorganic polyphosphate inbioRxiv : the preprint server for biology · 2026
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  12. Polyphosphate synthesis is essential for phosphate and ATP homeostasis during nutrient upshift.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. Article
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171 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Michael J GrayDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Wei-Yun WholeyDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Cellular and Molecular Biology Program, University of Michigan, Ann Arbor, MI 48109, USA.
Nico O WagnerDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Claudia M CremersDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Antje Mueller-SchickertDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Nathaniel T HockDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Adam G KriegerDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Erica M SmithDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Robert A BenderDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
James C A BardwellDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Cellular and Molecular Biology Program, University of Michigan, Ann Arbor, MI 48109, USA; Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Ursula JakobDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Cellular and Molecular Biology Program, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: ujakob@umich.edu.
University of Michigan–Ann Arbor · US

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
Functional Analysis of the Intrinsically Disordered Chaperone Hsp33R01GM065318 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2003 to 2015
$3.9M
Characterization of bleach-specific transcriptional regulators in bacteriaR21AI097893 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2012 to 2013
$417k
Cellular stress response to the oxidizing effects of bleachF32GM096613 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GRAY, MICHAEL JEFFREY · 2011 to 2012
$101k
Howard Hughes Medical InstituteNIAID NIH HHS AI097893NIAID NIH HHS R21 AI097893NIGMS NIH HHS F32 GM096613NIGMS NIH HHS F32-GM096613NIGMS NIH HHS GM065318NIGMS NIH HHS R01 GM065318NIGMS NIH HHS T32 GM007315NIGMS NIH HHS T32-GM007315
6 · The paper itself

Abstract

Composed of up to 1,000 phospho-anhydride bond-linked phosphate monomers, inorganic polyphosphate (polyP) is one of the most ancient, conserved, and enigmatic molecules in biology. Here we demonstrate that polyP functions as a hitherto unrecognized chaperone. We show that polyP stabilizes proteins in vivo, diminishes the need for other chaperone systems to survive proteotoxic stress conditions, and protects a wide variety of proteins against stress-induced unfolding and aggregation. In vitro studies reveal that polyP has protein-like chaperone qualities, binds to unfolding proteins with high affinity in an ATP-independent manner, and supports their productive refolding once nonstress conditions are restored. Our results uncover a universally important function for polyP and suggest that these long chains of inorganic phosphate may have served as one of nature's first chaperones, a role that continues to the present day.

Indexed as

Catalytic DomainCircular DichroismDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsHot TemperatureHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsLuciferasesMolecular ChaperonesOxidation-ReductionOxidative StressOxygenPhenotypePolyphosphatesDnaJ protein, E colidnaK protein, E coliEscherichia coli ProteinsGrpE protein, E coliHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsLuciferasesMolecular ChaperonesOxygenPolyphosphates

Identifiers

PMID24560923
PMCPMC3996911
OpenAlexW2100876879

What OpenQuestion holds

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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.