A QSAR study on the inhibition mechanism of matrix metalloproteinase-12 by arylsulfone analogs based on molecular orbital calculations-Reference-Cited by-同舟云学术

A QSAR study on the inhibition mechanism of matrix metalloproteinase-12 by arylsulfone analogs based on molecular orbital calculations

Published:2015 Issue:3 Volume:13 Page:793-806
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Hitaoka Seiji¹²³⁴,Chuman Hiroshi⁵⁶⁷⁴,Yoshizawa Kazunari¹²³⁴

Affiliation:

1. Institute for Materials Chemistry and Engineering and International Research Center for Molecular System

2. Kyushu University

3. Fukuoka 819-0395

4. Japan

5. Institute of Health Biosciences

6. The University of Tokushima Graduate School

7. Tokushima 770-8505

Abstract

The inhibition mechanism of matrix metalloproteinase-12 by arylsulfone analogs is revealed using a comprehensive computational approach including docking simulations, molecular orbital calculations, and QSAR.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/OB/C4OB01843E

Reference95 articles.

1. Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

2. Matrix metalloproteinases: a tail of a frog that became a prince

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5. Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion

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