Structure-Function Relationship Study of a Secretory Amoebic Phosphatase: A Computational-Experimental Approach.

Celina Terán-Ramírez, Rosa E Mares-Alejandre, Ana L Estrada-González, Patricia L A Muñoz-Muñoz, Marco A Ramos-Ibarra

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact, top 98% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

Bioinformatics Approaches for Functional and Structural Annotation and Molecular Docking Study of a Hypothetical Protein From Staphylococcus aureus.BioMed research international · 2026
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 1 institution in 1 country.

Celina Terán-RamírezBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.

Rosa E Mares-AlejandreBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.ORCID 0000-0001-6102-6966

Ana L Estrada-GonzálezBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.

Patricia L A Muñoz-MuñozBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.

Marco A Ramos-IbarraBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.ORCID 0000-0002-8950-2079

Universidad Autónoma de Baja California · MX

Funding

Consejo Nacional de Ciencia y Tecnología CB-2010/01-155714Consejo Nacional de Ciencia y Tecnología CB-2019/01-170715Universidad Autónoma de Baja California CPI/300/2/N/112/1

6 · The paper itself

Abstract

Phosphatases are hydrolytic enzymes that cleave the phosphoester bond of numerous substrates containing phosphorylated residues. The typical classification divides them into acid or alkaline depending on the pH at which they have optimal activity. The histidine phosphatase (HP) superfamily is a large group of functionally diverse enzymes characterized by having an active-site His residue that becomes phosphorylated during catalysis. HP enzymes are relevant biomolecules due to their current and potential application in medicine and biotechnology.

Indexed as

Structure-Activity Relationship6-PhytaseBinding SitesCatalytic DomainDiphosphatesEntamoeba histolyticaHumansMolecular Docking SimulationPhosphoric Monoester HydrolasesProtein ConformationProtozoan ProteinsRecombinant Proteins6-PhytaseDiphosphatesPhosphoric Monoester HydrolasesProtozoan ProteinsRecombinant Proteinssodium pyrophosphateEntamoeba histolyticaHAP/phytase-like phosphatasehomology-based modelingrecombinant protein productionstructure–function characterization

Identifiers

PMID33671604

DOI10.3390/ijms22042164

PMCPMC7926622

OpenAlexW3133114803

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.