Evidence map›Paper›PMID 31941036›Full record

ReviewBiomolecules2020

Osmolytes: A Possible Therapeutic Molecule for Ameliorating the Neurodegeneration Caused by Protein Misfolding and Aggregation.

Neetu Kushwah, Vishal Jain, Dhananjay Yadav

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.

  1. Pooled it
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  14. Taurine Stabilizing Effect on Lysozyme.Life (Basel, Switzerland) · 2022
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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 3 institutions in 3 countries.

Neetu KushwahFunctional Genomics Unit, CSIR-institute of genomics and integrative biology, Mall road, Delhi 110007, India.
Vishal JainDepartment of ECE, Carnegie Mellon University, Pittsburgh, PA 15289, USA.
Dhananjay YadavDepartment of Medical Biotechnology, Yeungnam University, Gyeongsan 712-749, Korea.ORCID 0000-0003-4047-7236
Carnegie Mellon University · USInstitute of Genomics and Integrative Biology · INYeungnam University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most of the neurological disorders in the brain are caused by the abnormal buildup of misfolded or aggregated proteins. Osmolytes are low molecular weight organic molecules usually built up in tissues at a quite high amount during stress or any pathological condition. These molecules help in providing stability to the aggregated proteins and protect these proteins from misfolding. Alzheimer's disease (AD) is the uttermost universal neurological disorder that can be described by the deposition of neurofibrillary tangles, aggregated/misfolded protein produced by the amyloid β-protein (Aβ). Osmolytes provide stability to the folded, functional form of a protein and alter the folding balance away from aggregation and/or degradation of the protein. Moreover, they are identified as chemical chaperones. Brain osmolytes enhance the pace of Aβ aggregation, combine with the nearby water molecules more promptly, and avert the aggregation/misfolding of proteins by providing stability to them. Therefore, osmolytes can be employed as therapeutic targets and may assist in potential drug design for many neurodegenerative and other diseases.

Indexed as

Protein FoldingAlzheimer DiseaseAmino AcidsAmyloid beta-PeptidesAnimalsBrainCarbohydrate MetabolismDrug DiscoveryExcipientsHumansMethylaminesNeurodegenerative DiseasesProtein AggregatesProtein Aggregation, PathologicalUreaAmino AcidsAmyloid beta-PeptidesExcipientsMethylaminesProtein AggregatesUreaAlzheimer’sAβ aggregationosmolytesprotein folding/misfolding

Identifiers

PMID31941036
PMCPMC7022651
OpenAlexW2999966139

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.