Evidence map›Paper›PMID 37893156›Full record

ArticleBiomedicines2023

In Silico Approaches to Developing Novel Glycogen Synthase Kinase 3β (GSK-3β).

Shuchi Goyal, Manjinder Singh, Divya Thirumal, Pratibha Sharma, Somdutt Mujwar, Krishna Kumar Mishra, Thakur Gurjeet Singh, Ravinder Singh, Varinder Singh, Tanveer Singh and 1 more

Open access · goldAbstract read
In one paragraph

Article in Biomedicines, 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 18% 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, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

11 authors at 4 institutions in 3 countries.

Shuchi GoyalChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.ORCID 0000-0001-9096-3043
Manjinder SinghChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.
Divya ThirumalChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.ORCID 0000-0002-7927-6821
Pratibha SharmaChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.
Somdutt MujwarChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.ORCID 0000-0003-4037-5475
Krishna Kumar MishraChitkara University Institute of Engineering and Technology, Chitkara University, Rajpura 140401, Punjab, India.
Thakur Gurjeet SinghChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.ORCID 0000-0003-2979-1590
Ravinder SinghChitkara College of Pharmacy, Chitkara University, Rajpura 140401, Punjab, India.
Varinder SinghDepartment of Pharmaceutical Sciences and Technology, Maharaja Ranjit Singh Punjab Technical University, Bathinda 151001, Punjab, India.ORCID 0000-0001-6061-3640
Tanveer SinghDepartment of Neuroscience and Experimental Therapeutics, College of Medicine, Texas A & M Health Science Center, Bryan, TX 77807, USA.
Sheikh F AhmadDepartment of Pharmacology and Toxicology, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia.ORCID 0000-0002-8282-3726
Chitkara University · INTexas A&M Health Science Center · USKing Saud University · SAMaharaja Ranjit Singh Punjab Technical University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is caused by plaque agglomeration and entanglement in several areas of the neural cells, which leads to apoptosis. The main etiology of AD is senile dementia, which is linked to amyloid-beta (Aβ) deregulation and tau perivascular pathogeny. Hyperphosphorylated tau has a propensity for microtubules, which elevate the instability and tau-protein congregates, leading to accumulation of neurofibrillary tangles (NFTs). Tau hyperphosphorylation is susceptible to GSK-3, which has led to an emerging hypothesis regarding the pathogenesis of AD. Accordingly, attempts have been made to conduct investigations and achieve further advancements on new analogues capable of inhibiting the GSK-3 protein, which are currently in the clinical trials. In this analysis, we have evaluated certain GSK-3 inhibitor variants utilising scaffolding and framework devised techniques with pharmacological characteristics, accompanied by computational screenings (pharmacokinetics and docking). The structure-based designed analogues interacted effectively with the active amino acids of GSK-3β target protein. The in silico pharmacokinetic studies revealed their drug-like properties. The analogues with best interactions and binding scores will be considered in the future to completely demonstrate their potential relevance as viable GSK-3 inhibitors.

Indexed as

Alzheimer’s diseaseamyloid-betadockingGSK-3βmolecular dynamicsmorphingneurofibrillary tanglesscaffold

Identifiers

PMID37893156
PMCPMC10604233
OpenAlexW4387618406

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.