Interactions of a new α-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition-Reference-Cited by-同舟云学术

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Interactions of a new α-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition

Published:2003-06-27 Issue:7 Volume:59 Page:1200-1205
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Selkti Mohamed,Tomas Alain,Gaucher Jean-François,Prangé Thierry,Fournié-Zaluski Marie-Claude,Chen Huixiong,Roques Bernard-Pierre

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2003/07/00/tm0002/tm0002.pdf

Cited by 15 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases;ACS Pharmacology & Translational Science;2022-11-28

2. Phosphinic Peptides as Potent Inhibitors of Zinc-Metalloproteases;Topics in Current Chemistry;2014

3. Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin;Angewandte Chemie International Edition;2013-01-02

4. Zerlegung des hydrophoben Effekts auf molekularer Ebene: Die Rolle von Wasser, Enthalpie und Entropie bei der Ligandenbindung an Thermolysin;Angewandte Chemie;2013-01-02

5. A three-component Mannich-type condensation leading to phosphinic dipeptides—extended transition state analogue inhibitors of aminopeptidases;Tetrahedron Letters;2011-06

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