ACTIVITY-BASED PROBES TO UTILIZE THE PROTEOLYTIC ACTIVITY OF CATHEPSIN G IN BIOLOGICAL SAMPLES
| dc.contributor.author | Burster, Timo | |
| dc.contributor.author | Gärtner, Fabian | |
| dc.contributor.author | Knippschild, Uwe | |
| dc.contributor.author | Zhanapiya, Anuar | |
| dc.date.accessioned | 2021-12-13T12:48:41Z | |
| dc.date.available | 2021-12-13T12:48:41Z | |
| dc.date.issued | 2021-02-25 | |
| dc.description.abstract | Neutrophils, migrating to the site of infection, are able to release serine proteases after being activated. These serine proteases comprise cathepsin G (CatG), neutrophil elastase protease 3 (PR3), and neutrophil serine protease 4 (NSP4). A disadvantage of the uncontrolled proteolytic activity of proteases is the outcome of various human diseases, including cardiovascular diseases, thrombosis, and autoimmune diseases. Activity-based probes (ABPs) are used to determine the proteolytic activity of proteases, containing a set of three essential elements: Warhead, recognition sequence, and the reporter tag for detection of the covalent enzyme activity–based probe complex. ... | en_US |
| dc.identifier.citation | Burster T, Gärtner F, Knippschild U and Zhanapiya A (2021) Activity-Based Probes to Utilize the Proteolytic Activity of Cathepsin G in Biological Samples. Front. Chem. 9:628295. doi: 10.3389/fchem.2021.628295 | en_US |
| dc.identifier.uri | http://nur.nu.edu.kz/handle/123456789/5923 | |
| dc.language.iso | en | en_US |
| dc.publisher | Front. Chem. | en_US |
| dc.rights | Attribution-NonCommercial-ShareAlike 3.0 United States | * |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/3.0/us/ | * |
| dc.subject | immune cells | en_US |
| dc.subject | serine proteases | en_US |
| dc.subject | activity-based probes | en_US |
| dc.title | ACTIVITY-BASED PROBES TO UTILIZE THE PROTEOLYTIC ACTIVITY OF CATHEPSIN G IN BIOLOGICAL SAMPLES | en_US |
| dc.type | Article | en_US |
| workflow.import.source | science |