Evidence map›Paper›PMID 37985663›Full record

ReviewJournal of enzyme inhibition and medicinal chemistry2023

The multifaceted nature of plant acid phosphatases: purification, biochemical features, and applications.

Lokesh Sharma, Amol Kahandal, Anant Kanagare, Atul Kulkarni, Chandrakant K Tagad

Open access · goldAbstract readReview
In one paragraph

Review in Journal of enzyme inhibition and medicinal chemistry, 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
6.4field-weighted citation impact, top 4% 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, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Transcriptome analysis ofMicrobiology spectrum · 2026
    Article
  4. OftenFrontiers in microbiology · 2025
    Article
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

5 authors at 3 institutions in 3 countries.

Lokesh SharmaSchool of Bioengineering Sciences & Research, MIT Art, Design and Technology University, Pune, India.
Amol KahandalSchool of Bioengineering Sciences & Research, MIT Art, Design and Technology University, Pune, India.
Anant KanagareDepartment of Chemistry, Deogiri College, Aurangabad, India.
Atul KulkarniSymbiosis Centre for Nanoscience and Nanotechnology, Symbiosis International (Deemed University), Lavale, India.ORCID 0000-0003-1696-4982
Chandrakant K TagadSchool of Bioengineering Sciences & Research, MIT Art, Design and Technology University, Pune, India.
MIT Art, Design and Technology University · INGovernment Medical College · INSymbiosis International University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acid phosphatases (EC 3.1.3.2) are the enzymes that catalyse transphosphorylation reactions and promotes the hydrolysis of numerous orthophosphate esters in acidic media, as a crucial element for the metabolism of phosphate in tissues. Inorganic phosphate (Pi) utilisation and scavenging, as well as the turnover of Pi-rich sources found in plant vacuoles, are major processes in which intracellular and secretory acid phosphatases function. Therefore, a thorough understanding of these enzymes' structural characteristics, specificity, and physiochemical properties is required to comprehend the function of acid phosphatases in plant energy metabolism. Furthermore, acid phosphatases are gaining increasing importance in industrial biotechnology due to their involvement in transphosphorylation processes and their ability to reduce phosphate levels in food products. Hence, this review aims to provide a comprehensive overview of the purification methods employed for isolating acid phosphatases from diverse plant sources, as well as their structural and functional properties. Additionally, the review explores the potential applications of these enzymes in various fields.

Indexed as

Acid PhosphatasePlantsHydrolysisPhosphatesAcid PhosphatasePhosphatesapplicationsbiochemical propertiesPlant acid phosphatasespurification

Identifiers

PMID37985663
PMCPMC11003492
OpenAlexW4388850374

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.