Structure-Based Library Design and Fragment Screening for the Identification of Reversible Complement Factor D Protease Inhibitors-Reference-Cited by-同舟云学术

Structure-Based Library Design and Fragment Screening for the Identification of Reversible Complement Factor D Protease Inhibitors

Published:2017-02-20 Issue:5 Volume:60 Page:1946-1958
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Vulpetti Anna¹^ORCID,Randl Stefan¹,Rüdisser Simon¹,Ostermann Nils¹,Erbel Paul¹,Mac Sweeney Aengus¹,Zoller Thomas¹,Salem Bahaa¹,Gerhartz Bernd¹,Cumin Frederic¹,Hommel Ulrich¹,Dalvit Claudio¹,Lorthiois Edwige¹,Maibaum Jürgen¹

Affiliation:

1. Novartis Institutes for BioMedical Research, Novartis Pharma AG, Novartis Campus, CH-4056 Basel, Switzerland

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.6b01684

Reference57 articles.

1. Complement factor D, a novel serine protease

2. Structures of native and complexed complement factor D: implications of the atypical his57 conformation and self-inhibitory loop in the regulation of specific serine protease activity

3. Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D

4. Induced Fit Activation Mechanism of the Exceptionally Specific Serine Protease, Complement Factor D†

5. Structures of C3b in Complex with Factors B and D Give Insight into Complement Convertase Formation

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