Extended cleavage specificity of sheep mast cell protease-2: A classical chymase with preference to aromatic P1 substrate residues-Reference-Cited by-同舟云学术

Extended cleavage specificity of sheep mast cell protease-2: A classical chymase with preference to aromatic P1 substrate residues

Published:2019-03 Issue: Volume:92 Page:160-169
ISSN:0145-305X
Container-title:Developmental & Comparative Immunology
language:en
Short-container-title:Developmental & Comparative Immunology

Author:

Fu Zhirong,Akula Srinivas^ORCID,Thorpe Michael,Chahal Gurdeep^ORCID,de Garavilla Lawrence,Kervinen Jukka,Hellman Lars^ORCID

Funder

Consejo Superior de Investigaciones Científicas

Publisher

Elsevier BV

Subject

Developmental Biology,Immunology

Reference42 articles.

1. Mutations in Arg143 and Lys192 of the human mast cell chymase markedly affect the activity of five potent human chymase inhibitors;Ahooghalandari;PLoS One,2013

2. Granule associated serine proteases of hematopoietic cells - an analysis of their appearance and diversification during vertebrate evolution;Akula;PLoS One,2015

3. The extended substrate specificity of the human mast cell chymase reveals a serine protease with well-defined substrate recognition profile;Andersson;Int. Immunol.,2009

4. The extended cleavage specificity of the rodent beta-chymases rMCP-1 and mMCP-4 reveal major functional similarities to the human mast cell chymase;Andersson;Mol. Immunol.,2008

5. Extended cleavage specificity of mMCP-1, the major mucosal mast cell protease in mouse-High specificity indicates high substrate selectivity;Andersson;Mol. Immunol.,2008

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