Morin, a matrix metalloproteinase 9 inhibitor, attenuates endothelial-to-mesenchymal transition in atherosclerosis by downregulating Notch-1 signaling

Morin acts as an MMP-9 inhibitor to disrupt EndMT in atherosclerosis by limiting the activation of Notch-1 signaling. This study underscores morin's potential utility in the development of anti-atherosclerotic medication. Please cite this article as: He Y, Qin XX, Liu MW, Sun W. Morin, a matrix metalloproteinase 9 inhibitor, attenuates endothelial-to-mesenchymal transition in atherosclerosis by downregulating Notch-1 Signaling. J Integr Med. 2024; 22(6): 684-696.

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Publication Details

Journal
Journal of Integrative Medicine
Published
2024-11-01
DOI
https://doi.org/10.1016/j.joim.2024.11.002
Citations
8
Primary Topic
Protease and Inhibitor Mechanisms
Type
article
Field-Weighted Citation Impact
2.28
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article

Morin, a matrix metalloproteinase 9 inhibitor, attenuates endothelial-to-mesenchymal transition in atherosclerosis by downregulating Notch-1 signaling

Yuan He, Wei Sun, Mingwei Liu, Xiao-Xuan Qin
8 citations
Journal of Integrative Medicine
Protease and Inhibitor Mechanisms
2.28
article

Morin, a matrix metalloproteinase 9 inhibitor, attenuates endothelial-to-mesenchymal transition in atherosclerosis by downregulating Notch-1 signaling

Yuan He, Wei Sun, Mingwei Liu, Xiao-Xuan Qin
article en
8 citations

Abstract

Morin acts as an MMP-9 inhibitor to disrupt EndMT in atherosclerosis by limiting the activation of Notch-1 signaling. This study underscores morin's potential utility in the development of anti-atherosclerotic medication. Please cite this article as: He Y, Qin XX, Liu MW, Sun W. Morin, a matrix metalloproteinase 9 inhibitor, attenuates endothelial-to-mesenchymal transition in atherosclerosis by downregulating Notch-1 Signaling. J Integr Med. 2024; 22(6): 684-696.

Journal of Integrative MedicineVol. 22(6)
Jiangsu Provincial Hospital of Traditional Chinese Medicine (CN), Nanjing Medical University (CN)
Openalex Percentile: Top 11%
Protease and Inhibitor Mechanisms
2.28
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