Evidence map›Paper›PMID 30769878›Full record

ArticleBiomolecules2019

The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism.

Sandi Brudar, Barbara Hribar-Lee

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions.International journal of molecular sciences · 2022
    Pooled it
  2. Article
  3. Article
  4. The influence of glycine onZeitschrift fur physikalische Chemie (Frankfurt am Main, Germany) · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation.Chembiochem : a European journal of chemical biology · 2020
    Article
  16. Review
  17. Buffer Influence on the Amino Acid Silica Interaction.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020
    Article
  18. 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

2 authors at 1 institution in 1 country.

Sandi BrudarFaculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia. sandi.brudar@fkkt.uni-lj.si.
Barbara Hribar-LeeFaculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia. barbara.hribar@fkkt.uni-lj.si.ORCID 0000-0002-9029-588X
University of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid fibrils, highly ordered protein aggregates, play an important role in the onset of several neurological disorders. Many studies have assessed amyloid fibril formation under specific solution conditions, but they all lack an important phenomena in biological solutions-buffer specific effects. We have focused on the formation of hen egg-white lysozyme (HEWL) fibrils in aqueous solutions of different buffers in both acidic and basic pH range. By means of UV-Vis spectroscopy, fluorescence measurements and CD spectroscopy, we have managed to show that fibrillization of HEWL is affected by buffer identity (glycine, TRIS, phosphate, KCl-HCl, cacodylate, HEPES, acetate), solution pH, sample incubation (agitated vs. static) and added excipients (NaCl and PEG). HEWL only forms amyloid fibrils at pH = 2.0 under agitated conditions in glycine and KCl-HCl buffers of high enough ionic strength. Phosphate buffer on the other hand stabilizes the HEWL molecules. Similar stabilization effect was achieved by addition of PEG12000 molecules to the solution.

Indexed as

AcetatesAmyloidAnimalsBuffersCacodylic AcidGlycineHydrochloric AcidHydrogen-Ion ConcentrationMuramidasePhosphatesPotassium ChlorideAcetatesAmyloidBuffersCacodylic AcidGlycinehen egg lysozymeHydrochloric AcidMuramidasePhosphatesPotassium Chlorideamyloid fibrilsbuffer-specific effectslysozyme

Identifiers

PMID30769878
PMCPMC6406783
OpenAlexW2911834686

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.