Evolutionarily Conserved Functional Mechanics across Pepsin-like and Retroviral Aspartic Proteases-Reference-Cited by-同舟云学术

Evolutionarily Conserved Functional Mechanics across Pepsin-like and Retroviral Aspartic Proteases

Published:2005-02-26 Issue:11 Volume:127 Page:3734-3742
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cascella Michele¹,Micheletti Cristian¹,Rothlisberger Ursula¹,Carloni Paolo¹

Affiliation:

1. Contribution from the International School for Advanced Studies (SISSA/ISAS) and INFMDEMOCRITOS Modeling Center for Research in Atomistic Simulation, Via Beirut 2−4, 34014 Trieste, Italy, and Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja044608%2B

Reference85 articles.

1. Follow the Protons: A Low-Barrier Hydrogen Bond Unifies the Mechanisms of the Aspartic Proteases

2. The Structure and Function of the Aspartic Proteinases

3. Structure and function of plant aspartic proteinases

4. [8] Procathepsin E and cathepsin E

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