Evidence map›Paper›PMID 36692648›Full record

ReviewApplied biochemistry and biotechnology2023

Exploring the Role of Glycolytic Enzymes PFKFB3 and GAPDH in the Modulation of Aβ and Neurodegeneration and Their Potential of Therapeutic Targets in Alzheimer's Disease.

Imran Ahmad, Ranjana Singh, Saurabh Pal, Soni Prajapati, Nidhi Sachan, Yusra Laiq, Hadiya Husain

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied biochemistry and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.

  1. Pooled it
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  12. Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023
    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

7 authors at 4 institutions in 1 country.

Imran Ahmad *Department of Biochemistry, King George's Medical University, Lucknow, 226003, Uttar Pradesh, India. imranahmadysbiochem@kgmcindia.edu.
Ranjana SinghDepartment of Biochemistry, King George's Medical University, Lucknow, 226003, Uttar Pradesh, India. ranjanasingh@kgmcindia.edu.
Saurabh Pal *Department of Biotechnology, Era's Lucknow Medical College & Hospital, Era University, Lucknow, 226003, Uttar Pradesh, India.
Soni PrajapatiDepartment of Biochemistry, King George's Medical University, Lucknow, 226003, Uttar Pradesh, India.
Nidhi SachanCell and Neurobiology Laboratory, Department of Biochemistry, Institute of Science, Banaras Hindu University, Varanasi, 221005, Uttar Pradesh, India.
Yusra LaiqDepartment of Biochemistry, King George's Medical University, Lucknow, 226003, Uttar Pradesh, India.
Hadiya HusainDepartment of Zoology, University of Lucknow, Lucknow, 226007, Uttar Pradesh, India.
King George's Medical University · INBanaras Hindu University · INEra's Lucknow Medical College and Hospital · INUniversity of Lucknow · IN

Funding

Indian Council of Medical Research R.12014/61/2020-HR
6 · The paper itself

Abstract

Alzheimer's disease (AD) is presently the 6th major cause of mortality across the globe. However, it is expected to rise rapidly, following cancer and heart disease, as a leading cause of death among the elderly peoples. AD is largely characterized by metabolic changes linked to glucose metabolism and age-induced mitochondrial failure. Recent research suggests that the glycolytic pathway is required for a range of neuronal functions in the brain including synaptic transmission, energy production, and redox balance; however, alteration in glycolytic pathways may play a significant role in the development of AD. Moreover, it is hypothesized that targeting the key enzymes involved in glucose metabolism may help to prevent or reduce the risk of neurodegenerative disorders. One of the major pro-glycolytic enzyme is 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3); it is normally absent in neurons but abundant in astrocytes. Similarly, another key of glycolysis is glyceraldehyde-3-phosphate dehydrogenase (GAPDH) which catalyzes the conversion of aldolase and glyceraldehyde 3 phosphates to 1,3 bisphosphoglycerate. GAPDH has been reported to interact with various neurodegenerative disease-associated proteins, including the amyloid-β protein precursor (AβPP). These findings indicate PFKFB3 and GAPDH as a promising therapeutic target to AD. Current review highlight the contributions of PFKFB3 and GAPDH in the modulation of Aβand AD pathogenesis and further explore the potential of PFKFB3 and GAPDH as therapeutic targets in AD.

Indexed as

Alzheimer DiseaseNeurodegenerative DiseasesAgedGlucoseGlyceraldehyde-3-Phosphate DehydrogenasesGlycolysisHumansPhosphofructokinase-2GlucoseGlyceraldehyde-3-Phosphate DehydrogenasesPFKFB3 protein, humanPhosphofructokinase-2Alzheimer’s diseaseAmyloid-βGAPDHPFKFB3Therapeutic target

Identifiers

PMID36692648
OpenAlexW4317829609

What OpenQuestion holds

Textmetadata
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.