id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-307894-pfsztifl	Clarke, Nicola E.	Chapter 100 Angiotensin-Converting Enzyme-2	2013-12-31		.txt	text/plain	2801	162	46	Keywords: Angiotensin, angiotensin-converting enzyme 2 (ACE2), apelin, bradykinin, carboxypeptidase, cardiovascular, collectrin, renin-angiotensin system, SARS virus, shedding, transmembrane, vasoactive, zinc-binding motif. Despite high similarity in sequence to ACE, particularly around the active site, ACE2 functions as a carboxypeptidase, rather than a peptidyl dipeptidase, cleaving the C-terminal amino acid from susceptible substrates. Key active site residues of ACE2 ( Figure 100 .1) were identified by site-directed mutagenesis based on the structure of the single domain testicular form of ACE [15] . Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements., chloride dependence Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase Substrate-based design of the first class of angiotensin-converting enzyme-related carboxypeptidase (ACE2) inhibitors Residues affecting the chloride regulation and substrate selectivity of the angiotensinconverting enzymes (ACE and ACE2) identified by site-directed mutagenesis Increased angiotensin-(1À7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2	./cache/cord-307894-pfsztifl.txt	./txt/cord-307894-pfsztifl.txt