Evidence map›Paper›PMID 30130556›Full record

ArticleJournal of molecular biology2018

Polyphosphate Stabilizes Protein Unfolding Intermediates as Soluble Amyloid-like Oligomers.

Nicholas G Yoo, Siddhant Dogra, Ben A Meinen, Eric Tse, Janine Haefliger, Daniel R Southworth, Michael J Gray, Jan-Ulrik Dahl, Ursula Jakob

Abstract read
In one paragraph

Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.7field-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

50 citing papers in PubMed, 73 citations in OpenAlex.

  1. Inorganic polyphosphate chelates CaBiochemistry and biophysics reports · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Inorganic Polyphosphate and Human Diseases.Progress in molecular and subcellular biology · 2026
    Review
  10. Review
  11. Article
  12. Article
  13. Polyphosphate: a cellular Swiss army knife.Current opinion in biotechnology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. mSphere · 2024
    Article
  19. Article
  20. The Protein Scaffolding Functions of Polyphosphate.Journal of molecular biology · 2024
    Review
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

9 authors at 2 institutions in 1 country.

Nicholas G YooDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States; Biological Chemistry Department, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States.
Siddhant DograDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States; Biological Chemistry Department, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States.
Ben A MeinenHoward Hughes Medical Institute, University of Michigan, 2256 Biological Sciences Science Building, 1105 North University Ave, Ann Arbor, MI 48109, United States.
Eric TseInstitute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, CA 94158, United States.
Janine HaefligerDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States; Biological Chemistry Department, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States.
Daniel R SouthworthInstitute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, CA 94158, United States.
Michael J GrayDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States; Biological Chemistry Department, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States.
Jan-Ulrik DahlDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States; Biological Chemistry Department, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States.
Ursula JakobDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States; Biological Chemistry Department, University of Michigan, 830 N University Ave, Ann Arbor, MI 48109, United States. Electronic address: ujakob@umich.edu.
University of Michigan–Ann Arbor · USInstitute for Neurodegenerative Disorders · US

Funding

Role of Molecular Chaperones in Stress Response and DiseaseR35GM122506 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ursula H. Jakob · 2017 to 2026
$6.8M
Functional Analysis of the Intrinsically Disordered Chaperone Hsp33R01GM065318 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2003 to 2015
$3.9M
Polyphosphate - A Novel Member of the Proteostasis NetworkR01GM116582 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2015 to 2016
$913k
NIGMS NIH HHS R01 GM065318NIGMS NIH HHS R01 GM116582NIGMS NIH HHS R35 GM122506
6 · The paper itself

Abstract

Inorganic polyphosphate (polyP) constitutes one of the most conserved and ubiquitous molecules in biology. Recent work in bacteria demonstrated that polyP increases oxidative stress resistance by preventing stress-induced protein aggregation and promotes biofilm formation by stimulating functional amyloid formation. To gain insights into these two seemingly contradictory functions of polyP, we investigated the effects of polyP on the folding model lactate dehydrogenase. We discovered that the presence of polyP during the thermal unfolding process stabilizes folding intermediates of lactate dehydrogenase as soluble micro-β-aggregates with amyloid-like properties. Size and heterogeneity of the oligomers formed in this process were dependent on the polyP chain length, with longer chains forming smaller, more homogenous complexes. This ability of polyP to stabilize thermally unfolded proteins even upon exposure to extreme temperatures appears to contribute to the observed resistance of uropathogenic Escherichia coli toward severe heat shock treatment. These results suggest that the working mechanism of polyP is the same for both soluble and amyloidogenic proteins, with the ultimate outcome likely being determined by a combination of polyP chain length and the client protein itself. They help to explain how polyP can simultaneously function as general stress-protective chaperone and instigator of amyloidogenic processes in vivo.

Indexed as

Protein MultimerizationProtein UnfoldingAmyloidogenic ProteinsEscherichia coli ProteinsHot TemperatureL-Lactate DehydrogenaseOxidative StressPolyphosphatesProtein StabilitySolubilityAmyloidogenic ProteinsEscherichia coli ProteinsL-Lactate DehydrogenasePolyphosphatesamyloid-like aggregateschaperoneheat shockPolyphosphateprotein unfolding

Identifiers

PMID30130556
PMCPMC6186493
OpenAlexW2886250618

What OpenQuestion holds

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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.