Role of conserved regulatory loop residues in allosteric propagation of serine protease HtrA2
Author:
Funder
Department of Biotechnology
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases;Singh;Arch. Biochem. Biophys.,2011
2. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death;Suzuki;Mol. Cell,2001
3. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes;Suzuki;J. Biol. Chem.,2001
4. HtrA protease family as therapeutic targets;Joanna;Curr. Pharmaceut. Des.,2013
5. Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi;Li;Nat. Struct. Biol.,2002
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. cFLIP – An interacting partner and a novel substrate for pro-apoptotic serine protease HtrA2;Biochemistry and Biophysics Reports;2024-07
2. Corrigendum to “Role of conserved regulatory loop residues in allosteric propagation of serine protease HtrA2”;Biochemical and Biophysical Research Communications;2022-04
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