Evidence map›Paper›PMID 36138837›Full record

ArticleBiology2022

Evidence of Orientation-Dependent Early States of Prion Protein Misfolded Structures from Single Molecule Force Spectroscopy.

Andrea Raspadori, Valentina Vignali, Anna Murello, Gabriele Giachin, Bruno Samorì, Motomasa Tanaka, Carlos Bustamante, Giampaolo Zuccheri, Giuseppe Legname

Open access · goldAbstract read
In one paragraph

Article in Biology, 2022. 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
0.3field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

9 authors at 6 institutions in 3 countries.

Andrea RaspadoriDepartment of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy.
Valentina VignaliDipartimento di Farmacia e Biotecnologie, Alma Mater Studiorum Università di Bologna, 40126 Bologna, Italy.
Anna MurelloDipartimento di Farmacia e Biotecnologie, Alma Mater Studiorum Università di Bologna, 40126 Bologna, Italy.
Gabriele GiachinDepartment of Chemical Sciences (DiSC), University of Padua, 35131 Padova, Italy.ORCID 0000-0001-7550-0307
Bruno SamorìDipartimento di Farmacia e Biotecnologie, Alma Mater Studiorum Università di Bologna, 40126 Bologna, Italy.
Motomasa TanakaLaboratory for Protein Conformation Diseases, RIKEN Brain Science Institute, Wako 351-0198, Saitama, Japan.ORCID 0000-0002-2994-7703
Carlos BustamanteQB3 Institute, University of California, 642 Stanley Hall #3220, Berkeley, CA 94720-3220, USA.
Giampaolo ZuccheriDipartimento di Farmacia e Biotecnologie, Alma Mater Studiorum Università di Bologna, 40126 Bologna, Italy.ORCID 0000-0003-4777-5391
Giuseppe LegnameDepartment of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy.
University of Bologna · ITScuola Internazionale Superiore di Studi Avanzati · ITIstituto Nanoscienze · ITRIKEN Center for Brain Science · JPUniversity of California, Berkeley · USUniversity of Padua · IT

Funding

International Human Frontier Science Program Organization RGP0010/2011
6 · The paper itself

Abstract

Prion diseases are neurodegenerative disorders characterized by the presence of oligomers and amyloid fibrils. These are the result of protein aggregation processes of the cellular prion protein (PrP

Indexed as

atomic force microscopyintrinsically disordered proteinsprionsprotein misfoldingsingle molecule force spectroscopy

Identifiers

PMID36138837
PMCPMC9495685
OpenAlexW4296252759

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.