Evidence map›Paper›PMID 36389229›Full record

ArticleFrontiers in neuroscience2022

Structural consequences of sequence variation in mammalian prion β2α2 loop segments.

Calina Glynn, Evelyn Hernandez, Marcus Gallagher-Jones, Jennifer Miao, Christina J Sigurdson, Jose A Rodriguez

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

Article in Frontiers in neuroscience, 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 47% 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, 3 citations in OpenAlex.

  1. Unravelling the Complexity of Amyloid Peptide Core Interfaces.Journal of chemical information and modeling · 2024
    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.

Calina GlynnDepartment of Chemistry and Biochemistry, STROBE NSF Science and Technology Center, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA, United States.
Evelyn HernandezDepartment of Chemistry and Biochemistry, STROBE NSF Science and Technology Center, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA, United States.
Marcus Gallagher-JonesDepartment of Chemistry and Biochemistry, STROBE NSF Science and Technology Center, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA, United States.
Jennifer MiaoDepartment of Chemistry and Biochemistry, STROBE NSF Science and Technology Center, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA, United States.
Christina J SigurdsonDepartment of Pathology and Medicine, University of California, San Diego, La Jolla, CA, United States.
Jose A RodriguezDepartment of Chemistry and Biochemistry, STROBE NSF Science and Technology Center, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA, United States.
University of California, Los Angeles · USUniversity of California, San Diego · US

Funding

Mechanisms of Prion Aggregation and Species BarriersR01NS069566 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ESKO, JEFFREY D, RAVITS, JOHN · 2011 to 2025
$5.7M
Mechanisms of Prion SpreadR01NS076896 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SIGURDSON, CHRISTINA · 2012 to 2021
$3.4M
Mechanisms of Prion Spread and Neuronal ToxicityR37NS076896 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Christina Sigurdson · 2023 to 2026
$2.6M
Molecular basis of prion protein-induced neurodegenerationRF1NS121992 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SIGURDSON, CHRISTINA · 2021 to 2023
$1.7M
Molecular basis of prion protein-induced neurodegenerationR01NS121992 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SIGURDSON, CHRISTINA · 2024 to 2025
$963k
NINDS NIH HHS R01 NS069566NINDS NIH HHS R01 NS076896NINDS NIH HHS R01 NS121992NINDS NIH HHS R37 NS076896NINDS NIH HHS RF1 NS121992
6 · The paper itself

Abstract

Sequence variation in the β2α2 loop, residues 165-175 of the mammalian prion protein (PrP), influences its structure. To better understand the consequences of sequence variation in this region of the protein, we biochemically and biophysically interrogate natural and artificial sequence variants of the β2α2 loop of mammalian PrP. Using microcrystal electron diffraction (MicroED), we determine atomic resolution structures of segments encompassing residues 168-176 from the β2α2 loop of PrP with sequences corresponding to human, mouse/cow, bank vole/hamster, rabbit/pig/guinea pig, and naked mole rat (elk-T174S) β2α2 loops, as well as synthetic β2α2 loop sequences. This collection of structures presents two dominant amyloid packing polymorphisms. In the first polymorph, denoted "clasped", side chains within a sheet form polar clasps by facing each other

Indexed as

cryoEMmicroEDprionstructuretransmission

Identifiers

PMID36389229
PMCPMC9645039
OpenAlexW4306943597

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.