Evidence map›Paper›PMID 28267202›Full record

ArticleFEBS letters2017

The role of histidines in amyloid β fibril assembly.

Kristoffer Brännström, Tohidul Islam, Linda Sandblad, Anders Olofsson

Open access · hybridAbstract readComparative Study
In one paragraph

Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. Multivariate effects of pH, salt, and ZnCommunications chemistry · 2022
    Article
  5. One- and Two-Photon Excited Autofluorescence of Lysozyme Amyloids.The journal of physical chemistry letters · 2022
    Article
  6. Article
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  9. Differences in the free energies between the excited states of AProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
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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 1 institution in 1 country.

Kristoffer BrännströmDepartment of Medical Biochemistry and Biophysics, Umeå University, Sweden.
Tohidul IslamDepartment of Medical Biochemistry and Biophysics, Umeå University, Sweden.
Linda SandbladDepartment of Molecular Biology, Umeå University, Sweden.
Anders OlofssonDepartment of Medical Biochemistry and Biophysics, Umeå University, Sweden.
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Low pH has a strong stabilising effect on the fibrillar assembly of amyloid β, which is associated with Alzheimer's disease. The stabilising effect is already pronounced at pH 6.0, suggesting that protonation of histidines might mediate this effect. Through the systematic substitution of the three native histidines in Aβ for alanines, we have evaluated their role in fibril stability. Using surface plasmon resonance, we show that at neutral pH the fibrillar forms of all His-Ala variants are destabilised by a factor of 4-12 compared to wild-type Aβ. However, none of the His-Ala Aβ variants impair the stabilising effect of the fibril at low pH.

Indexed as

Amino Acid SubstitutionAmyloidAmyloid beta-PeptidesHistidineHumansHydrogen-Ion ConcentrationKineticsMicroscopy, Electron, TransmissionMutationPeptide FragmentsProtein Aggregation, PathologicalProtein StabilityRecombinant ProteinsSurface Plasmon ResonanceAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)HistidinePeptide FragmentsRecombinant Proteinsabetaamyloidfibrilhistidinestabilitysurface plasmon resonance

Identifiers

PMID28267202
PMCPMC5434815
OpenAlexW2592044709

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.