Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase

Melamine consumption causes oxidative stress by an unknown mechanism. Therefore, it is of interest to analyze the interaction of melamine with two important proteins involved in oxidative stress biology namely, nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase. The molecular do...

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Autores principales: Rai, Nitish, Chowdhary, Sheemona, Kumar, Deepak, Bhattacharyya, Rajasri, Banerjee, Dibyajyoti
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10266370/
https://www.ncbi.nlm.nih.gov/pubmed/37323555
http://dx.doi.org/10.6026/97320630018718
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author Rai, Nitish
Chowdhary, Sheemona
Kumar, Deepak
Bhattacharyya, Rajasri
Banerjee, Dibyajyoti
author_facet Rai, Nitish
Chowdhary, Sheemona
Kumar, Deepak
Bhattacharyya, Rajasri
Banerjee, Dibyajyoti
author_sort Rai, Nitish
collection PubMed
description Melamine consumption causes oxidative stress by an unknown mechanism. Therefore, it is of interest to analyze the interaction of melamine with two important proteins involved in oxidative stress biology namely, nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase. The molecular docking data shows the melamine binding with these two proteins at critical residues. These interactions can be logically perceived for the causation of melamine induced oxidative stress.
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spelling pubmed-102663702023-06-15 Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase Rai, Nitish Chowdhary, Sheemona Kumar, Deepak Bhattacharyya, Rajasri Banerjee, Dibyajyoti Bioinformation Research Article Melamine consumption causes oxidative stress by an unknown mechanism. Therefore, it is of interest to analyze the interaction of melamine with two important proteins involved in oxidative stress biology namely, nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase. The molecular docking data shows the melamine binding with these two proteins at critical residues. These interactions can be logically perceived for the causation of melamine induced oxidative stress. Biomedical Informatics 2022-08-31 /pmc/articles/PMC10266370/ /pubmed/37323555 http://dx.doi.org/10.6026/97320630018718 Text en © 2022 Biomedical Informatics https://creativecommons.org/licenses/by/3.0/This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
spellingShingle Research Article
Rai, Nitish
Chowdhary, Sheemona
Kumar, Deepak
Bhattacharyya, Rajasri
Banerjee, Dibyajyoti
Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
title Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
title_full Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
title_fullStr Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
title_full_unstemmed Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
title_short Molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
title_sort molecular docking analysis of melamine with nuclear factor erythroid 2-related factor 2 and succinate dehydrogenase
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10266370/
https://www.ncbi.nlm.nih.gov/pubmed/37323555
http://dx.doi.org/10.6026/97320630018718
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