Monitoring Human Neutrophil Activation by a Proteinase 3 Near-Infrared Fluorescence Substrate-Based Probe-Reference-Cited by-同舟云学术

Monitoring Human Neutrophil Activation by a Proteinase 3 Near-Infrared Fluorescence Substrate-Based Probe

Published:2021-07-16 Issue:8 Volume:32 Page:1782-1790
ISSN:1043-1802
Container-title:Bioconjugate Chemistry
language:en
Short-container-title:Bioconjugate Chem.

Author:

Saidi Ahlame¹²,Wartenberg Mylène¹²,Madinier Jean-Baptiste³,Ilango Guy⁴,Seren Seda¹²,Korkmaz Brice¹²^ORCID,Lecaille Fabien¹²,Aucagne Vincent³,Lalmanach Gilles¹²^ORCID

Affiliation:

1. Université de Tours, Tours 37032, France

2. UMR 1100, Research Center for Respiratory Diseases (CEPR), Team: “Proteolytic Mechanisms in Inflammation”, INSERM, Tours 37032, France

3. Center for Molecular Biophysics (CBM), Team: “Molecular, Structural and Chemical Biology″, CNRS UPR 4301, Orléans 45071, France

4. IBiSA Electron Microscopy Platform, Université de Tours, Tours 37032, France

Funder

Conseil RÃ©gional du Centre-Val de Loire

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Pharmaceutical Science,Pharmacology,Biomedical Engineering,Bioengineering,Biotechnology

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.bioconjchem.1c00267

Reference50 articles.

1. Neutrophil serine proteases: specific regulators of inflammation

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

3. NSP4, an elastase-related protease in human neutrophils with arginine specificity

4. An ancient mechanism of arginine-specific substrate cleavage: What's ‘up’ with NSP4?

5. Therapeutic targeting of cathepsin C: from pathophysiology to treatment

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