Evidence map›Paper›PMID 39120652›Full record

ArticleBiomolecular NMR assignments2024

Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy.

Natalia Rodina, Riddhiman Sarkar, Dimitrios Tsakalos, Saba Suladze, Zheng Niu, Bernd Reif

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Article in Biomolecular NMR assignments, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. 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

6 authors.

Natalia RodinaDepartment of Bioscience, TUM School of Natural Sciences, Technical University of Munich, Munich, Germany.
Riddhiman SarkarDepartment of Bioscience, TUM School of Natural Sciences, Technical University of Munich, Munich, Germany.
Dimitrios TsakalosDepartment of Bioscience, TUM School of Natural Sciences, Technical University of Munich, Munich, Germany.
Saba SuladzeDepartment of Bioscience, TUM School of Natural Sciences, Technical University of Munich, Munich, Germany.
Zheng NiuSchool of Pharmacy, Henan University, Kaifeng, China.
Bernd ReifDepartment of Bioscience, TUM School of Natural Sciences, Technical University of Munich, Munich, Germany. reif@tum.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid fibrils from Alzheimer's amyloid-beta peptides (Aβ) are found to be polymorphic. So far, 14 Aβ40 fibril structures have been determined. The mechanism of why one particular protein sequence adopts so many different three-dimensional structures is yet not understood. In this work, we describe the assignment of the NMR chemical shifts of two Alzheimer's disease fibril polymorphs, P1 and P2, which are formed by the amyloid-beta peptide Aβ40. The assignment is based on

Indexed as

Amyloid beta-PeptidesPeptide FragmentsAmyloidAutomationNuclear Magnetic Resonance, BiomolecularAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsAbeta peptideAmyloid fibrilsAssignmentAutomated assignmentCarbon-detectionSolid-state NMR

Identifiers

PMID39120652
PMCPMC11511749

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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.