In Silico Design, Synthesis, and Assays of Specific Substrates for Proteinase 3: Influence of Fluorogenic and Charged Groups-Reference-Cited by-同舟云学术

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In Silico Design, Synthesis, and Assays of Specific Substrates for Proteinase 3: Influence of Fluorogenic and Charged Groups

Published:2014-01-21 Issue:3 Volume:57 Page:1111-1115
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Narawane Shailesh¹,Budnjo Adnan²,Grauffel Cédric¹³,Haug Bengt Erik²,Reuter Nathalie¹³

Affiliation:

1. Department of Molecular Biology, University of Bergen, 5008, Bergen, Norway

2. Department of Chemistry and Centre for Pharmacy, University of Bergen, Allégaten 41, 5007, Bergen, Norway

3. Computational Biology Unit, Department of Informatics, University of Bergen, 5008, Bergen, Norway

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm401559r

Reference15 articles.

1. Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases

2. Three Wavelength Substrate System of Neutrophil Serine Proteinases

3. Structures of human proteinase 3 and neutrophil elastase - so similar yet so different

4. On the size of the active site in proteases. I. Papain

5. Influence of Charge Distribution at the Active Site Surface on the Substrate Specificity of Human Neutrophil Protease 3 and Elastase

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1. Expression and purification of human neutrophil proteinase 3 from insect cells and characterization of ligand binding;PLOS ONE;2024-06-25

2. Expression and purification of human neutrophil proteinase 3 from insect cells and characterization of ligand binding;2023-11-11

3. Human proteinase 3resistanceto inhibition extends to alpha‐2 macroglobulin;The FEBS Journal;2020-02-24

4. Iterative Optimization of the Cyclic Peptide SFTI-1 Yields Potent Inhibitors of Neutrophil Proteinase 3;ACS Medicinal Chemistry Letters;2019-07-19

5. Anthranilic Acid as a Versatile Fluorescent Tag and Linker for Functional Glycomics;Bioconjugate Chemistry;2018-11-01

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