Evidence map›Paper›PMID 38254616›Full record

ReviewBiomolecules2023

Updates on Aβ Processing by Hsp90, BRICHOS, and Newly Reported Distinctive Chaperones.

Mohammed Iqbal, Shea-Lorane Lewis, Shivani Padhye, Umesh Kumar Jinwal

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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

4 authors at 1 institution in 1 country.

Mohammed IqbalDepartment of Pharmaceutical Sciences, USF-Health Taneja College of Pharmacy, University of South Florida, Tampa, FL 33612, USA.
Shea-Lorane LewisDepartment of Pharmaceutical Sciences, USF-Health Taneja College of Pharmacy, University of South Florida, Tampa, FL 33612, USA.
Shivani PadhyeDepartment of Pharmaceutical Sciences, USF-Health Taneja College of Pharmacy, University of South Florida, Tampa, FL 33612, USA.
Umesh Kumar JinwalDepartment of Pharmaceutical Sciences, USF-Health Taneja College of Pharmacy, University of South Florida, Tampa, FL 33612, USA.
University of South Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is an extremely devastating neurodegenerative disease, and there is no cure for it. AD is specified as the misfolding and aggregation of amyloid-β protein (Aβ) and abnormalities in hyperphosphorylated tau protein. Current approaches to treat Alzheimer's disease have had some success in slowing down the disease's progression. However, attempts to find a cure have been largely unsuccessful, most likely due to the complexity associated with AD pathogenesis. Hence, a shift in focus to better understand the molecular mechanism of Aβ processing and to consider alternative options such as chaperone proteins seems promising. Chaperone proteins act as molecular caretakers to facilitate cellular homeostasis under standard conditions. Chaperone proteins like heat shock proteins (Hsps) serve a pivotal role in correctly folding amyloid peptides, inhibiting mitochondrial dysfunction, and peptide aggregation. For instance, Hsp90 plays a significant role in maintaining cellular homeostasis through its protein folding mechanisms. In this review, we analyze the most recent studies from 2020 to 2023 and provide updates on Aβ regulation by Hsp90, BRICHOS domain chaperone, and distinctive newly reported chaperones.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesHSP90 Heat-Shock ProteinsNeurodegenerative DiseasesHeat-Shock ProteinsHumansMolecular ChaperonesAmyloid beta-PeptidesHeat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesAlzheimer’s diseaseamyloid-β proteinartificial chaperoneBRICHOS domain chaperonechemical chaperoneengineerable chaperoneHsp90

Identifiers

PMID38254616
PMCPMC10812967
OpenAlexW4390111937

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.