Evidence map›Paper›PMID 37717490›Full record

ReviewCurrent opinion in structural biology2023

Conformational inhibitors of protein aggregation.

María Del Carmen Fernández Ramírez, Shumaila Afrin, Lorena Saelices

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 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
0.3field-weighted citation impact, top 36% 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, 2 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

3 authors at 2 institutions in 1 country.

María Del Carmen Fernández RamírezCenter for Alzheimer's and Neurodegenerative Diseases, Department of Biophysics, Peter O'Donnell Jr Brain Institute, University of Texas Southwestern Medical Center (UTSW), Dallas, TX, USA. Electronic address: https://twitter.com/FernandezR_MC.
Shumaila AfrinCenter for Alzheimer's and Neurodegenerative Diseases, Department of Biophysics, Peter O'Donnell Jr Brain Institute, University of Texas Southwestern Medical Center (UTSW), Dallas, TX, USA. Electronic address: https://twitter.com/Shumyla44.
Lorena SaelicesCenter for Alzheimer's and Neurodegenerative Diseases, Department of Biophysics, Peter O'Donnell Jr Brain Institute, University of Texas Southwestern Medical Center (UTSW), Dallas, TX, USA. Electronic address: Lorena.SaelicesGomez@UTSouthwestern.edu.
Southwestern Medical Center · USTwitter (United States) · US

Funding

Closing the gap between structural biology and translational science for amyloid diseasesDP2HL163810 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI SAELICES GOMEZ, LORENA · 2021 to 2024
$2.5M
NHLBI NIH HHS DP2 HL163810
6 · The paper itself

Abstract

Amyloidoses are fatal conditions associated with the aggregation of proteins into amyloid fibrils that deposit systemically and/or locally. Possibly because the causal mechanism of protein aggregation and deposition is not fully understood, this group of diseases remains uncurable. Advances in structural biology, such as the use of nuclear magnetic resonance and cryo-electron microscopy, have enabled the study of the structures and the conformational nature of the proteins whose aggregation is associated with the underlying pathogenesis of amyloidosis. As a result, the last years of research have translated into the development of directed therapeutic strategies that target the specific conformations of precursors, fibrils, and intermediary species. Current efforts include the use of small molecules, peptides, and antibodies. This review summarizes the recent progress in developing strategies that target specific protein conformations for the treatment of amyloidoses.

Indexed as

AmyloidosisProtein AggregatesAmyloidCryoelectron MicroscopyHumansProtein ConformationAmyloidProtein AggregatesAmyloidAmyloidosisConformational inhibitorsProtein aggregation

Identifiers

PMID37717490
PMCPMC12452704
OpenAlexW4386766068

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.