Evidence map›Paper›PMID 28283568›Full record

ArticleThe Journal of biological chemistry2017

Nanostructure and stability of calcitonin amyloids.

Federica Rigoldi, Pierangelo Metrangolo, Alberto Redaelli, Alfonso Gautieri

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Federica RigoldiFrom the Dipartimento di Elettronica, Informazione e Bioingegneria, Politecnico di Milano, Piazza Leonardo da Vinci 32, 20133 Milano, Italy.
Pierangelo Metrangolothe Dipartimento di Chimica, Materiali e Ingegneria Chimica "Giulio Natta," Politecnico di Milano, Via L. Mancinelli 7, 20131 Milano, Italy, and.
Alberto RedaelliFrom the Dipartimento di Elettronica, Informazione e Bioingegneria, Politecnico di Milano, Piazza Leonardo da Vinci 32, 20133 Milano, Italy.
Alfonso GautieriFrom the Dipartimento di Elettronica, Informazione e Bioingegneria, Politecnico di Milano, Piazza Leonardo da Vinci 32, 20133 Milano, Italy, alfonso.gautieri@polimi.it.
Politecnico di Milano · ITVTT Technical Research Centre of Finland · FI

Funding

European Research Council 307108
6 · The paper itself

Abstract

Calcitonin is a 32-amino acid thyroid hormone that can form amyloid fibrils. The structural basis of the fibril formation and stabilization is still debated and poorly understood. The reason is that NMR data strongly suggest antiparallel β-sheet calcitonin assembly, whereas modeling studies on the short DFNKF peptide (corresponding to the sequence from Asp

Indexed as

Molecular Dynamics SimulationAmyloidCalcitoninHumansPeptidesProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryAmyloidCalcitoninPeptidesaggregationamyloidmolecular dynamicsprotein misfoldingprotein-protein interaction

Identifiers

PMID28283568
PMCPMC5418037
OpenAlexW2592668044

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.