Evidence map›Paper›PMID 34517052›Full record

ArticleBiochimie2021

Novel quaternary structures of the human prion protein globular domain.

Leandro Oliveira Bortot, Victor Lopes Rangel, Francesca A Pavlovici, Kamel El Omari, Armin Wagner, Jose Brandao-Neto, Romain Talon, Frank von Delft, Andrew G Reidenbach, Sonia M Vallabh and 3 more

Open access · greenAbstract read
In one paragraph

Article in Biochimie, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Identification of the Highly Polymorphic Prion Protein Gene (Animals : an open access journal from MDPI · 2025
    Article
  2. Article
  3. Article
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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

13 authors at 5 institutions in 4 countries.

Leandro Oliveira BortotLaboratory of Protein Crystallography, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
Victor Lopes RangelLaboratory of Protein Crystallography, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
Francesca A PavloviciChemical Biology and Therapeutics Science Program, Broad Institute of MIT and Harvard, Cambridge, MA, 02142, USA.
Kamel El OmariDiamond Light Source, Harwell Science and Innovation Campus, Didcot, United Kingdom.
Armin WagnerDiamond Light Source, Harwell Science and Innovation Campus, Didcot, United Kingdom.
Jose Brandao-NetoDiamond Light Source, Harwell Science and Innovation Campus, Didcot, United Kingdom.
Romain TalonDiamond Light Source, Harwell Science and Innovation Campus, Didcot, United Kingdom.
Frank von DelftDiamond Light Source, Harwell Science and Innovation Campus, Didcot, United Kingdom; Structural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Headington, OX3 7DQ, UK; Department of Biochemistry, University of Johannesburg, Auckland Park, 2006, South Africa.
Andrew G ReidenbachChemical Biology and Therapeutics Science Program, Broad Institute of MIT and Harvard, Cambridge, MA, 02142, USA.
Sonia M VallabhChemical Biology and Therapeutics Science Program, Broad Institute of MIT and Harvard, Cambridge, MA, 02142, USA.
Eric Vallabh MinikelChemical Biology and Therapeutics Science Program, Broad Institute of MIT and Harvard, Cambridge, MA, 02142, USA.
Stuart SchreiberChemical Biology and Therapeutics Science Program, Broad Institute of MIT and Harvard, Cambridge, MA, 02142, USA; Department of Chemistry & Chemical Biology, Harvard University, Cambridge, MA, 02138, USA.
Maria Cristina NonatoLaboratory of Protein Crystallography, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil. Electronic address: cristy@fcfrp.usp.br.
Broad Institute · USDiamond Light Source · GBUniversidade de São Paulo · BRUniversidade de Ribeirão Preto · BRUniversity of Johannesburg · ZA

Funding

Studies of Materials with Physiological PropertiesR35GM127045 · NIGMS · BROAD INSTITUTE, INC. · PI SCHREIBER, STUART L · 2018 to 2022
$3.2M
Developing in vitro assays to identify small molecules that inhibit human prionsF31AI122592 · NIAID · HARVARD MEDICAL SCHOOL · PI MINIKEL, ERIC VALLABH · 2016 to 2018
$99k
NIAID NIH HHS F31 AI122592NIGMS NIH HHS R35 GM127045
6 · The paper itself

Abstract

Prion disease is caused by the misfolding of the cellular prion protein, PrP

Indexed as

Crystallography, X-RayHumansProtein DomainsProtein Structure, QuaternaryPrPC ProteinsPrPC ProteinsAmyloidAnomalous scatteringPrionX-ray crystallography

Identifiers

PMID34517052
PMCPMC8627497
OpenAlexW3200437637

What OpenQuestion holds

Textmetadata
LicenceTDM
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.