Evidence map›Paper›PMID 38204437›Full record

ArticleIn silico pharmacology2024

Inhibition of Uridine 5'-diphospho-glucuronosyltransferases A10 and B7 by vitamins: insights from in silico and in vitro studies.

Sonal Pande, Chirag A Patel, Tejas M Dhameliya, Jayesh Beladiya, Palak Parikh, Radhika Kachhadiya, Sandip Dholakia

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In one paragraph

Article in In silico pharmacology, 2024. 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
1.4field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

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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

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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, 3 citations in OpenAlex.

  1. Article
4 · The record

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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 2 institutions in 1 country.

Sonal PandeGujarat Technological University, Ahmedabad, India.
Chirag A PatelDepartment of Pharmacology, L. M. College of Pharmacy, Navrangpura, Ahmedabad, 380009 India.
Tejas M DhameliyaDepartment of Pharmaceutical Chemistry, Institute of Pharmacy, Nirma University, Ahmedabad, Gujarat 382 481 India.
Jayesh BeladiyaDepartment of Pharmacology, L. M. College of Pharmacy, Navrangpura, Ahmedabad, 380009 India.
Palak ParikhDepartment of Pharmaceutical Chemistry, L. M. College of Pharmacy, Ahmedabad, 38009 India.
Radhika KachhadiyaDepartment of Pharmaceutical Chemistry, L. M. College of Pharmacy, Ahmedabad, 38009 India.
Sandip DholakiaDepartment of Pharmaceutical Chemistry, L. M. College of Pharmacy, Ahmedabad, 38009 India.
B.J. Medical College · INNirma University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uridine 5'-diphospho-glucuronosyltransferases (UGTs) have been considered as a family of enzymes responsible for the glucuronidation process, a crucial phase II detoxification reaction. Among the various UGT isoforms, UGTs A10 and B7 have garnered significant attention due to their broad substrate specificity and involvement in the metabolism of numerous compounds. Recent studies have suggested that certain vitamins may exert inhibitory effects on UGT activity, thereby influencing the metabolism of drugs, environmental toxins, and endogenous substances, ultimately impacting their biological activities. In the present study, the inhibition potential of vitamins (A, B1, B2, B3, B5, B6, B7, B9, D3, E, and C) on UGT1A10 and UGT2B7 was determined using in silico and in vitro approaches. A 3-dimensional model of UGT1A10 and UGT2B7 enzymes was built using Swiss Model, ITASSER, and ROSETTA and verified using Ramachandran plot and SAVES tools. Molecular docking studies revealed that vitamins interact with UGT1A10 and UGT2B7 enzymes by binding within the active site pocket and interacting with residues. Among all vitamins, the highest binding affinity predicted by molecular docking was - 8.61 kcal/mol with vitamin B1. The in vitro studies results demonstrated the inhibition of the glucuronidation activity of UGTs by vitamins A, B1, B2, B6, B9, C, D, and E, with IC Supplementary Information: The online version contains supplementary material available at 10.1007/s40203-023-00182-0.

Indexed as

DockingIn-vitro assaySchrodingerUGTsVitamins

Identifiers

PMID38204437
PMCPMC10774253
OpenAlexW4390673216

What OpenQuestion holds

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Registered trials

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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.