Evidence map›Paper›PMID 28882996›Full record

ArticleScience (New York, N.Y.)2017

Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.

Lothar Gremer, Daniel Schölzel, Carla Schenk, Elke Reinartz, Jörg Labahn, Raimond B G Ravelli, Markus Tusche, Carmen Lopez-Iglesias, Wolfgang Hoyer, Henrike Heise and 2 more

Registry-linked trialOpen access · bronzeAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03977025 (Evaluation of Alzheimer's Biomarkers in Cerebrospinal Fluid and Peripheral Blood of Elderly Patients Undergoing Surgery in the HCUCH.), which is not on this map. Cited by 504 papers.

0numbers the graph read from it
0cells of the map it votes in
504citing papers in PubMed
63.6field-weighted citation impact, top 1% 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.

NCT03977025 unknown statusnot on this mapstarted 2019, after this paper: background citation

Evaluation of Alzheimer's Biomarkers in Cerebrospinal Fluid and Peripheral Blood of Elderly Patients Undergoing Surgery in the HCUCH.

TypeobservationalSponsorUniversity of ChileRan2019 to 2020Enrolled30ConditionsAlzheimer DiseaseArmsLumbar punction
3 · Its place in the literature

Who cites it

504 citing papers in PubMed, 1,037 citations in OpenAlex.

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444 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Lothar GremerInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0001-7065-5027
Daniel SchölzelInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.
Carla SchenkInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.
Elke ReinartzInstitut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany.
Jörg LabahnInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-0648-8145
Raimond B G RavelliThe Maastricht Multimodal Molecular Imaging Institute, Maastricht University, Universiteitssingel 50, 6229 ER Maastricht, Netherlands.ORCID 0000-0001-6056-5888
Markus TuscheInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.
Carmen Lopez-IglesiasThe Maastricht Multimodal Molecular Imaging Institute, Maastricht University, Universiteitssingel 50, 6229 ER Maastricht, Netherlands.
Wolfgang HoyerInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0003-4301-5416
Henrike HeiseInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-9081-3894
Dieter WillboldInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany. gu.schroeder@fz-juelich.de d.willbold@fz-juelich.de.ORCID 0000-0002-0065-7366
Gunnar F SchröderInstitute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany. gu.schroeder@fz-juelich.de d.willbold@fz-juelich.de.ORCID 0000-0003-1803-5431
Forschungszentrum Jülich · DEMaastricht University · NLHeinrich Heine University Düsseldorf · DE

Funding

European Research Council
6 · The paper itself

Abstract

Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's disease patients. We present the structure of an Aβ(1-42) fibril composed of two intertwined protofilaments determined by cryo-electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. The backbone of all 42 residues and nearly all side chains are well resolved in the EM density map, including the entire N terminus, which is part of the cross-β structure resulting in an overall "LS"-shaped topology of individual subunits. The dimer interface protects the hydrophobic C termini from the solvent. The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed "groove" and "ridge," leading to different binding pathways on both fibril ends, which has implications for fibril growth.

Indexed as

Amyloid beta-PeptidesCryoelectron MicroscopyHumansNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein MultimerizationProtein Structure, SecondaryX-Ray DiffractionAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide Fragments

Identifiers

PMID28882996
PMCPMC6080689
OpenAlexW2753860285

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

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.