Evidence map›Paper›PMID 28827331›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Prion protein

Enrico Caldarulo, Alessandro Barducci, Kurt Wüthrich, Michele Parrinello

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023
    Review
  4. Article
  5. Computer Simulations Aimed at Exploring Protein Aggregation and Dissociation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  6. Article
  7. Article
  8. MetNeuropathology and applied neurobiology · 2021
    Article
  9. Article
  10. Bifurcated Hydrogen Bonds and the Fold Switching of Lymphotactin.The journal of physical chemistry. B · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. 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

4 authors at 3 institutions in 3 countries.

Enrico CaldaruloDepartment of Chemistry and Applied Biosciences, Eidgenössische Technische Hochschule Zurich, CH-8093 Zurich, Switzerland.
Alessandro BarducciCentre de Biochimie Structurale, INSERM, CNRS, Université de Montpellier, FR-34090 Montpellier, France.ORCID 0000-0002-1911-8039
Kurt WüthrichInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, CH-8093 Zurich, Switzerland.
Michele ParrinelloDepartment of Chemistry and Applied Biosciences, Eidgenössische Technische Hochschule Zurich, CH-8093 Zurich, Switzerland; michele.parrinello@phys.chem.ethz.ch.
ETH Zurich · CHCentre National de la Recherche Scientifique · FRScripps Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In transmissible spongiform encephalopathies (TSEs), which are lethal neurodegenerative diseases that affect humans and a wide range of other mammalian species, the normal "cellular" prion protein ([Formula: see text]) is transformed into amyloid aggregates representing the "scrapie form" of the protein ([Formula: see text]). Continued research on this system is of keen interest, since new information on the physiological function of [Formula: see text] in healthy organisms is emerging, as well as new data on the mechanism of the transformation of [Formula: see text] to [Formula: see text] In this paper we used two different approaches: a combination of the well-tempered ensemble (WTE) and parallel tempering (PT) schemes and metadynamics (MetaD) to characterize the conformational free-energy surface of [Formula: see text] The focus of the data analysis was on an 11-residue polypeptide segment in mouse [Formula: see text](121-231) that includes the [Formula: see text]2-[Formula: see text]2 loop of residues 167-170, for which a correlation between structure and susceptibility to prion disease has previously been described. This study includes wild-type mouse [Formula: see text] and a variant with the single-residue replacement Y169A. The resulting detailed conformational landscapes complement in an integrative manner the available experimental data on [Formula: see text], providing quantitative insights into the nature of the structural transition-related function of the [Formula: see text]2-[Formula: see text]2 loop.

Indexed as

Amino Acid SubstitutionAnimalsHumansMiceMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularPrion DiseasesProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandPrPC ProteinsPrPC Proteinsmetadynamicsprionβ2–α2 loop

Identifiers

PMID28827331
PMCPMC5594700
OpenAlexW2745333017

What OpenQuestion holds

Textmetadata
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.