Evidence map›Paper›PMID 38250434›Full record

ArticleFrontiers in bioinformatics2023

Protein-lipid interactions and protein anchoring modulate the modes of association of the globular domain of the Prion protein and Doppel protein to model membrane patches.

Patricia Soto, Davis T Thalhuber, Frank Luceri, Jamie Janos, Mason R Borgman, Noah M Greenwood, Sofia Acosta, Hunter Stoffel

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

Article in Frontiers in bioinformatics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 100% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 1 institution in 1 country.

Patricia SotoDepartment of Physics, Creighton University, Omaha, NE, United States.
Davis T ThalhuberDepartment of Physics, Creighton University, Omaha, NE, United States.
Frank LuceriOmaha Central High School, Omaha, NE, United States.
Jamie JanosDepartment of Chemistry and Biochemistry, Creighton University, Omaha, NE, United States.
Mason R BorgmanDepartment of Chemistry and Biochemistry, Creighton University, Omaha, NE, United States.
Noah M GreenwoodDepartment of Physics, Creighton University, Omaha, NE, United States.
Sofia AcostaOmaha North High School, Omaha, NE, United States.
Hunter StoffelOmaha Central High School, Omaha, NE, United States.
Creighton University · 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

The Prion protein is the molecular hallmark of the incurable prion diseases affecting mammals, including humans. The protein-only hypothesis states that the misfolding, accumulation, and deposition of the Prion protein play a critical role in toxicity. The cellular Prion protein (PrP

Indexed as

Doppel proteinmolecular dynamics simulationsperipheral membrane protein bindingPrion protein (PrP)protein-lipid interactions

Identifiers

PMID38250434
PMCPMC10796588
OpenAlexW4390610848

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.