Evidence map›Paper›PMID 35924280›Full record

ArticleJournal of structural biology: X2022

SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study.

Arpita Sundaria, Falk Liberta, Dilan Savran, Riddhiman Sarkar, Natalia Rodina, Carsten Peters, Nadine Schwierz, Christian Haupt, Matthias Schmidt, Bernd Reif

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

Article in Journal of structural biology: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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 4 institutions in 1 country.

Arpita SundariaBayerisches NMR Zentrum (BNMRZ) at the Department of Chemistry, Technische Universität München (TUM), Lichtenbergstr. 4, 85747 Garching, Germany.
Falk LibertaInstitute of Protein Biochemistry, Ulm University, Helmholtzstr. 8/1, 89081 Ulm, Germany.
Dilan SavranInstitute of Physics, Computational Biology, University of Augsburg, Universitätsstraße 1, 86159 Augsburg, Germany.
Riddhiman SarkarBayerisches NMR Zentrum (BNMRZ) at the Department of Chemistry, Technische Universität München (TUM), Lichtenbergstr. 4, 85747 Garching, Germany.
Natalia RodinaBayerisches NMR Zentrum (BNMRZ) at the Department of Chemistry, Technische Universität München (TUM), Lichtenbergstr. 4, 85747 Garching, Germany.
Carsten PetersCenter for Protein Assemblies, Department of Chemistry, Technische Universität München (TUM), Ernst-Otto-Fischer Str. 8, 85747 Garching, Germany.
Nadine SchwierzInstitute of Physics, Computational Biology, University of Augsburg, Universitätsstraße 1, 86159 Augsburg, Germany.
Christian HauptInstitute of Protein Biochemistry, Ulm University, Helmholtzstr. 8/1, 89081 Ulm, Germany.
Matthias SchmidtInstitute of Protein Biochemistry, Ulm University, Helmholtzstr. 8/1, 89081 Ulm, Germany.
Bernd ReifBayerisches NMR Zentrum (BNMRZ) at the Department of Chemistry, Technische Universität München (TUM), Lichtenbergstr. 4, 85747 Garching, Germany.
Helmholtz-Institute Ulm · DETechnical University of Munich · DEHelmholtz Zentrum München · DEUniversity of Augsburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AA amyloidosis is one of the most prevalent forms of systemic amyloidosis and affects both humans and other vertebrates. In this study, we compare MAS solid-state NMR data with a recent cryo-EM study of fibrils involving full-length murine SAA1.1. We address the question whether the specific requirements for the reconstitution of an amyloid fibril structure by cryo-EM can potentially yield a bias towards a particular fibril polymorph. We employ fibril seeds extracted from

Indexed as

Amyloid fibrilsCryo electron microscopy (EM)Magic Angle Spinning (MAS)Solid-state NMRStructure

Identifiers

PMID35924280
PMCPMC9340516
OpenAlexW4286260943

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.