Evidence map›Paper›PMID 36892160›Full record

ArticlePrion2023

Insight into the conserved structural dynamics of the C-terminus of mammal PrPC identifies structural core and possible structural role of pharmacological chaperones.

Patricia Soto, Garrett M Gloeb, Kaitlin A Tsuchida, Austin A Charles, Noah M Greenwood, Heidi Hendrickson

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Prion, 2023. 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
0.2field-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

1 citing paper in PubMed, 1 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

6 authors at 2 institutions in 1 country.

Patricia SotoPhysics department, Creighton University, Omaha, NE, USA.ORCID 0000-0002-3255-9226
Garrett M GloebChemistry department, Creighton University, Omaha, NE, USA.
Kaitlin A TsuchidaPhysics department, Creighton University, Omaha, NE, USA.
Austin A CharlesChemistry department, Creighton University, Omaha, NE, USA.
Noah M GreenwoodPhysics department, Creighton University, Omaha, NE, USA.
Heidi HendricksonChemistry department, Lafayette College, Easton, PA, USA.
Creighton University · USLafayette College · US

Funding

UNMC Structural Biology CoreP20GM103427 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PAUL L SORGEN · 2012 to 2026
$59.2M
NIGMS NIH HHS P20 GM103427
6 · The paper itself

Abstract

Misfolding of the prion protein is central to prion disease aetiology. Although understanding the dynamics of the native fold helps to decipher the conformational conversion mechanism, a complete depiction of distal but coupled prion protein sites common across species is lacking. To fill this gap, we used normal mode analysis and network analysis to examine a collection of prion protein structures deposited on the protein data bank. Our study identified a core of conserved residues that sustains the connectivity across the C-terminus of the prion protein. We propose how a well-characterized pharmacological chaperone may stabilize the fold. Also, we provide insight into the effect on the native fold of initial misfolding pathways identified by others using kinetics studies.

Indexed as

Prion DiseasesPrion ProteinsAnimalsMammalsProtein FoldingPrion ProteinsCollective motionsnetwork analysisnormal mode analysisPrion proteinstructural dynamics

Identifiers

PMID36892160
PMCPMC10012922
OpenAlexW4323653682

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.