Evidence map›Paper›PMID 35480736›Full record

ArticleRSC advances2021

Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin.

Vasantha Gowda, Michal Biler, Andrei Filippov, Malisa V Mantonico, Eirini Ornithopoulou, Mathieu Linares, Oleg N Antzutkin, Christofer Lendel

Abstract read
In one paragraph

Article in RSC advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
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  3. Article
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  5. Article
  6. Article
  7. A new fibrillization mechanism of β-lactoglobulin in glycine solutions.International journal of biological macromolecules · 2022
    Article
  8. Article
  9. 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

8 authors.

Vasantha GowdaDept. of Chemistry, KTH Royal Institute of Technology Stockholm Sweden lendel@kth.se.ORCID https://orcid.org/0000-0001-9577-6845
Michal BilerDept. of Theoretical Chemistry, KTH Royal Institute of Technology Stockholm Sweden.ORCID https://orcid.org/0000-0003-3809-6928
Andrei FilippovChemistry of Interfaces, Luleå University of Technology Sweden.ORCID https://orcid.org/0000-0002-6810-1882
Malisa V MantonicoDept. of Chemistry, KTH Royal Institute of Technology Stockholm Sweden lendel@kth.se.
Eirini OrnithopoulouDept. of Chemistry, KTH Royal Institute of Technology Stockholm Sweden lendel@kth.se.
Mathieu LinaresDept. of Theoretical Chemistry, KTH Royal Institute of Technology Stockholm Sweden.
Oleg N AntzutkinChemistry of Interfaces, Luleå University of Technology Sweden.ORCID https://orcid.org/0000-0003-1067-7990
Christofer LendelDept. of Chemistry, KTH Royal Institute of Technology Stockholm Sweden lendel@kth.se.ORCID https://orcid.org/0000-0001-9238-7246

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein nanofibrils (PNFs) represent a promising class of biobased nanomaterials for biomedical and materials science applications. In the design of such materials, a fundamental understanding of the structure-function relationship at both molecular and nanoscale levels is essential. Here we report investigations of the nanoscale morphology and molecular arrangement of amyloid-like PNFs of a synthetic peptide fragment consisting of residues 11-20 of the protein β-lactoglobulin (β-LG

Identifiers

PMID35480736
PMCPMC9037834

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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.