ArticleInternational journal of molecular sciences2022
Association Mechanism and Conformational Changes in Trypsin on Its Interaction with Atrazine: A Multi- Spectroscopic and Biochemical Study with Computational Approach.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 40 citations in OpenAlex.
- Influence of carboxymethyl chitosan chain length on its interaction with vitamin C and curcumin: molecular docking and molecular dynamic approach.Journal of molecular modeling · 2025Article
- Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods.Heliyon · 2024Article
- Comparison of the Effects on Bovine Serum Albumin Induced by Different Forms of Vanadium.Biological trace element research · 2023Article
- Anticancer Potential of Sulfonamide Moieties via In-Vitro and In-Silico Approaches: Comparative Investigations for Future Drug Development.International journal of molecular sciences · 2023Article
- Toxicity Study and Binding Analysis of Newly Synthesized AntifungalInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Atrazine (ATR) is a herbicide globally used to eliminate undesired weeds. Herbicide usage leads to various adverse effects on human health and the environment. The primary source of herbicides in humans is the food laced with the herbicides. The ATR binding to trypsin (TYP) was investigated in this study to explore its binding potential and toxicity. In vitro interaction of ATR with TYP was studied using multi-spectroscopic methods, molecular docking, and enzyme kinetics to explore the mechanism of binding for the TYP-ATR system. The TYP-ATR complex revealed binding constants (10
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Registered trials
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