Evidence map›Paper›PMID 31182591›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β

Chun-Ming Zhang, Keiichi Yamaguchi, Masatomo So, Kenji Sasahara, Toru Ito, Suguru Yamamoto, Ichiei Narita, József Kardos, Hironobu Naiki, Yuji Goto

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Plasma Proteomic Profile of Chemotherapy-Induced Severe Neutropenia: A Pilot Discovery Phase Study.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Inorganic Polyphosphate and Human Diseases.Progress in molecular and subcellular biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. The Protein Scaffolding Functions of Polyphosphate.Journal of molecular biology · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021
    Article
  17. Article
  18. Article
  19. Article
  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

10 authors at 4 institutions in 2 countries.

Chun-Ming ZhangInstitute for Protein Research, Osaka University, Suita, 565-0871 Osaka, Japan.
Keiichi YamaguchiInstitute for Protein Research, Osaka University, Suita, 565-0871 Osaka, Japan.
Masatomo SoInstitute for Protein Research, Osaka University, Suita, 565-0871 Osaka, Japan.ORCID 0000-0002-4815-4995
Kenji SasaharaInstitute for Protein Research, Osaka University, Suita, 565-0871 Osaka, Japan.
Toru ItoDivision of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Sciences, 951-8510 Niigata, Japan.
Suguru YamamotoDivision of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Sciences, 951-8510 Niigata, Japan.
Ichiei NaritaDivision of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Sciences, 951-8510 Niigata, Japan.
József KardosELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Eötvös Loránd University, 1117 Budapest, Hungary.
Hironobu NaikiFaculty of Medical Sciences, University of Fukui, Matsuoka, 910-1193 Fukui, Japan.
Yuji GotoInstitute for Protein Research, Osaka University, Suita, 565-0871 Osaka, Japan; gtyj8126@protein.osaka-u.ac.jp.ORCID 0000-0003-1221-1270
Protein Research Foundation · JPNiigata University · JPEötvös Loránd University · HUUniversity of Fukui · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyphosphate (polyP), which is found in various microorganisms and human cells, is an anionic biopolymer consisting of inorganic phosphates linked by high-energy phosphate bonds. Previous studies revealed that polyPs strongly promoted the amyloid formation of several amyloidogenic proteins; however, the mechanism of polyP-induced amyloid formation remains unclear. In the present study using β

Indexed as

Amyloidbeta 2-MicroglobulinHumansHydrogen-Ion ConcentrationPolymerizationPolyphosphatesStatic ElectricityAmyloidbeta 2-MicroglobulinPolyphosphatesamorphous aggregationamyloid fibrillationdialysis-related amyloidosispolyphosphatessupersaturation

Identifiers

PMID31182591
PMCPMC6600944
OpenAlexW2950003090

What OpenQuestion holds

Textmetadata
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.