Fluorine Scan of Inhibitors of the Cysteine Protease Human Cathepsin L: Dipolar and Quadrupolar Effects in the π-Stacking of Fluorinated Phenyl Rings on Peptide Amide Bonds-Reference-Cited by-同舟云学术

Fluorine Scan of Inhibitors of the Cysteine Protease Human Cathepsin L: Dipolar and Quadrupolar Effects in the π-Stacking of Fluorinated Phenyl Rings on Peptide Amide Bonds

Published:2016-04-20 Issue:10 Volume:11 Page:1042-1047
ISSN:1860-7179
Container-title:ChemMedChem
language:en
Short-container-title:ChemMedChem

Author:

Giroud Maude¹,Harder Michael¹,Kuhn Bernd²,Haap Wolfgang²,Trapp Nils¹,Schweizer W. Bernd¹,Schirmeister Tanja³,Diederich François¹

Affiliation:

1. Laboratorium für Organische Chemie; ETH Zürich; Wolfgang-Pauli-Strasse 10, HCI 8093 Zürich Switzerland

2. Small Molecule Research; Roche Innovation Center Basel; F. Hoffmann-La Roche AG; Grenzacherstrasse 124, Building 92 4070 Basel Switzerland

3. Institut für Pharmazie und Biochemie; Johannes Gutenberg-Universität Mainz; Staudinger Weg 5 55128 Mainz Germany

Funder

F. Hoffmann-La Roche, Basel

ETH Research Council

Publisher

Wiley

Subject

Organic Chemistry,General Pharmacology, Toxicology and Pharmaceutics,Molecular Medicine,Drug Discovery,Biochemistry,Pharmacology

Reference65 articles.

1. Plasma levels of cathepsins L, K, and V and risks of abdominal aortic aneurysms: A randomized population-based study

2. Cathepsin L is involved in proliferation and invasion of ovarian cancer cells

3. Cathepsin L targeting in cancer treatment

4. Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response

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