Evidence map›Paper›PMID 38003389›Full record

ArticleInternational journal of molecular sciences2023

The Unfolded Protein Response in a Murine Model of Alzheimer's Disease: Looking for Predictors.

Giulia Sita, Agnese Graziosi, Camilla Corrieri, Luca Ghelli, Sabrina Angelini, Pietro Cortelli, Patrizia Hrelia, Fabiana Morroni

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Alzheimer's Disease: Cellular and Pharmacological Aspects.Geriatrics (Basel, Switzerland) · 2024
    Review
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.

Giulia SitaDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.ORCID 0000-0001-6627-7078
Agnese GraziosiDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.ORCID 0000-0002-4992-7902
Camilla CorrieriDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.
Luca GhelliDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.
Sabrina AngeliniDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.ORCID 0000-0002-1609-0421
Pietro CortelliDepartment of Biomedical and NeuroMotor Sciences-DiBiNeM, Alma Mater Studiorum University of Bologna, Via Altura 3, 40139 Bologna, Italy.ORCID 0000-0002-3633-8818
Patrizia HreliaDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.ORCID 0000-0002-8415-3711
Fabiana MorroniDepartment of Pharmacy and BioTechnology-FaBiT, Alma Mater Studiorum University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.ORCID 0000-0001-6494-5968
University of Bologna · IT

Funding

Fondazione del Monte di Bologna e RavennaMinistero dell'Istruzione, dell'Università e della Ricerca (MIUR) 2017MYJ5THMinistero dell'Università e della Ricerca (MUR) 20202THZAWPNRR PE12 - MNESYS PE000006University of Bologna RFO 2019University of Bologna RFO 2020University of Bologna RFO 2021University of Bologna RFO 2022
6 · The paper itself

Abstract

Alzheimer's disease (AD) represents the most frequent type of dementia worldwide, and aging is the most important risk factor for the sporadic form of the pathology. The endoplasmic reticulum (ER), the main cellular actor involved in proteostasis, appears significantly compromised in AD due to the accumulation of the β-amyloid (Aβ) protein and the phosphorylated Tau protein. Increasing protein misfolding activates a specific cellular response known as Unfolded Protein Response (UPR), which orchestrates the recovery of ER function. The aim of the present study was to investigate the role of UPR in a murine model of AD induced by intracerebroventricular (i.c.v.) injection of Aβ

Indexed as

Alzheimer DiseaseAnimalsDisease Models, AnimalEndoplasmic Reticulum StressEndoribonucleasesMicePhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesUnfolded Protein ResponseEndoribonucleasesPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesagingAlzheimer’s diseaseAβ oligomersneurodegenerationUPR

Identifiers

PMID38003389
PMCPMC10671834
OpenAlexW4388635494

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.