Limited proteolysis of human kidney angiotensin-converting enzyme and generation of catalytically active N- and C-terminal domains

scientific article published on 01 July 1997

Limited proteolysis of human kidney angiotensin-converting enzyme and generation of catalytically active N- and C-terminal domains is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1006/BBRC.1997.6841
P698PubMed publication ID9223417

P2093author name stringRiordan JF
Danilov SM
Sturrock ED
P433issue1
P921main subjectproteolysisQ33123
P304page(s)16-19
P577publication date1997-07-01
P1433published inBiochemical and Biophysical Research CommunicationsQ864228
P1476titleLimited proteolysis of human kidney angiotensin-converting enzyme and generation of catalytically active N- and C-terminal domains
P478volume236

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cites work (P2860)
Q24306614A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme
Q41906309A new high-resolution crystal structure of the Drosophila melanogaster angiotensin converting enzyme homologue, AnCE.
Q34195870ACE for all - a molecular perspective
Q43658440Arg(1098) is critical for the chloride dependence of human angiotensin I-converting enzyme C-domain catalytic activity.
Q27680712Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme
Q44560486Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme
Q73092337Monoclonal antibodies to denatured human ACE (CD 143), broad species specificity, reactivity on paraffin sections, and detection of subtle conformational changes in the C-terminal domain of ACE
Q27667064Novel mechanism of inhibition of human angiotensin-I-converting enzyme (ACE) by a highly specific phosphinic tripeptide
Q74404393Temperature-induced selective death of the C-domain within angiotensin-converting enzyme molecule
Q42928380The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity

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