Naringin dihydrochalcone potentially binds to catalytic domain of matrix metalloproteinase-2: molecular docking, MM-GBSA, and molecular dynamics simulation approach-Reference-Cited by-同舟云学术

Naringin dihydrochalcone potentially binds to catalytic domain of matrix metalloproteinase-2: molecular docking, MM-GBSA, and molecular dynamics simulation approach

Published:2022-09-01 Issue:11 Volume:37 Page:1851-1855
ISSN:1478-6419
Container-title:Natural Product Research
language:en
Short-container-title:Natural Product Research

Author:

Singh Atul Kumar¹,Kumar Shashank¹

Affiliation:

1. Molecular Signaling & Drug Discovery Laboratory, Department of Biochemistry, Central University of Punjab, Bathinda, Punjab, India

Publisher

Informa UK Limited

Subject

Organic Chemistry,Plant Science,Biochemistry,Analytical Chemistry

Link

https://www.tandfonline.com/doi/pdf/10.1080/14786419.2022.2118746

Reference11 articles.

1. Enzymatic inhibitory activity of Ficus deltoidea leaf extract on matrix metalloproteinase-2, 8 and 9

2. Halting Tumor Progression via Novel Non-Hydroxamate Triazole-Based Mannich Bases MMP-2/9 Inhibitors; Design, Microwave-Assisted Synthesis, and Biological Evaluation

3. MMP-Inhibitory Effects of Flavonoid Glycosides from Edible Medicinal Halophyte Limonium tetragonum

4. Inhibitors of gelatinases (MMP-2 and MMP-9) for the management of hematological malignancies

5. Recent insights into natural product inhibitors of matrix metalloproteinases

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