DFT Studies of the Ring-Opening Mechanism of SB-3CT, a Potent Inhibitor of Matrix Metalloproteinase 2-Reference-Cited by-同舟云学术

DFT Studies of the Ring-Opening Mechanism of SB-3CT, a Potent Inhibitor of Matrix Metalloproteinase 2

Published:2009-05-14 Issue:12 Volume:11 Page:2559-2562
ISSN:1523-7060
Container-title:Organic Letters
language:en
Short-container-title:Org. Lett.

Author:

Tao Peng¹,Fisher Jed F.¹,Mobashery Shahriar¹,Schlegel H. Bernhard¹

Affiliation:

1. Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, and Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ol9008393

Reference23 articles.

1. Partial purification and characterization of a neutral protease which cleaves type IV collagen

2. Potent and Selective Mechanism-Based Inhibition of Gelatinases

3. X-ray Absorption Studies of Human Matrix Metalloproteinase-2 (MMP-2) Bound to a Highly Selective Mechanism-based Inhibitor

4. Pronounced Diversity in Electronic and Chemical Properties between the Catalytic Zinc Sites of Tumor Necrosis Factor-α-converting Enzyme and Matrix Metalloproteinases despite Their High Structural Similarity

5. Potent Mechanism-based Inhibitors for Matrix Metalloproteinases

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