Evidence map›Paper›PMID 31276123›Full record

ArticleChemical communications (Cambridge, England)2019

Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core.

Santu Bera, Elad Arad, Lee Schnaider, Shira Shaham-Niv, Valeria Castelletto, Yossef Peretz, Dor Zaguri, Raz Jelinek, Ehud Gazit, Ian W Hamley

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical communications (Cambridge, England), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022
    Article
  4. Review
  5. 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 3 institutions in 3 countries.

Santu BeraDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. ehudg@post.tau.ac.il.ORCID http://orcid.org/0000-0002-4830-552X
Elad AradDepartment of Chemistry & Ilse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, Beer Sheva 8410501, Israel.
Lee SchnaiderDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. ehudg@post.tau.ac.il.
Shira Shaham-NivDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. ehudg@post.tau.ac.il.ORCID http://orcid.org/0000-0001-8451-2625
Valeria CastellettoDepartment of Chemistry, University of Reading, Reading RG6 6AD, UK. I.W.Hamley@reading.ac.uk.
Yossef PeretzDepartment of Chemistry & Ilse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, Beer Sheva 8410501, Israel.
Dor ZaguriDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. ehudg@post.tau.ac.il.
Raz JelinekDepartment of Chemistry & Ilse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, Beer Sheva 8410501, Israel.ORCID http://orcid.org/0000-0002-0336-1384
Ehud GazitDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. ehudg@post.tau.ac.il.ORCID http://orcid.org/0000-0001-5764-1720
Ian W HamleyDepartment of Chemistry, University of Reading, Reading RG6 6AD, UK. I.W.Hamley@reading.ac.uk.ORCID http://orcid.org/0000-0002-4549-0926
Tel Aviv University · ILBen-Gurion University of the Negev · ILReading Museum · GB

Funding

European Research Council 694426
6 · The paper itself

Abstract

The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.

Indexed as

Amino Acid SequenceAmyloid beta-PeptidesAnimalsCell Line, TumorCholesterolHumansKineticsLipid BilayersPeptide FragmentsPhosphatidylcholinesProtein Conformation, beta-StrandProtein MultimerizationRatsSphingomyelins1,2-oleoylphosphatidylcholineAmyloid beta-Peptidesamyloid beta-protein (16-22)CholesterolLipid BilayersPeptide FragmentsPhosphatidylcholinesSphingomyelins

Identifiers

PMID31276123
PMCPMC7616937
OpenAlexW2954548293

What OpenQuestion holds

Textmetadata
LicenceTDM
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.