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Tumor Necrosis Factor-α Convertase (ADAM17) Mediates Regulated Ectodomain Shedding of the Severe-acute Respiratory Syndrome-Coronavirus (SARS-CoV) Receptor, Angiotensin-converting Enzyme-2 (ACE2)*
Direct evidence is provided for the involvement of ADAM17 in the regulated ectodomain shedding of ACE2 by using inhibitors with differing potency toward different members of the ADAM (a disintegrin and metalloproteinase) family of proteases. Expand
Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism.
In the RAS (renin-angiotensin system), Ang I (angiotensin I) is cleaved by ACE (angiotensin-converting enzyme) to form Ang II (angiotensin II), which has effects on blood pressure, fluid andExpand
The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function
Knowledge of the complete genomes of Caenorhabditis elegans and Drosophila melanogaster allows the full complement of NEP‐like activities to be analysed in a single organism, and reveals the power of functional genomics. Expand
Shedding light on ADAM metalloproteinases.
The recent studies have begun to elucidate the substrate specificity and the mechanisms that control ADAM-mediated shedding events that regulate, for example, growth-factor and Notch signalling, and the processing of the amyloid precursor protein. Expand
The angiotensin-converting enzyme gene family: genomics and pharmacology.
The gene that encodes collectrin, a homologue of ACEH, is upregulated in response to renal injury, which indicates that there is more to ACE-like function than simple peptide hydrolysis. Expand
The emerging role of ACE2 in physiology and disease†
The renin–angiotensin–aldosterone system (RAAS) is a key regulator of systemic blood pressure and renal function and a key player in renal and cardiovascular disease. However, itsExpand
Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein
A mechanism by which the cellular production of the neurotoxic Aβ is regulated by PrPC is regulated and may have implications for both Alzheimer's and prion diseases. Expand
Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
  • A. Turner, K. Tanzawa
  • Chemistry, Medicine
  • FASEB journal : official publication of the…
  • 1 April 1997
A wide range of biologically active peptide substrates has been described for NEP, of which the enkephalins and the atrial natriuretic peptide family have assumed greatest significance. Expand
Molecular pharmacology of endothelin converting enzymes.
The current evidence supporting a metallopeptidase ECE as the physiological regulator of endothelin production is described and its sensitivity to inhibition by the fungal metabolite phosphoramidon and subsequent cloning of the enzyme indicate it to be a type II integral membrane protein homologous with neural endopeptIDase-24.11. Expand
Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein*
Data indicate that although PrPC can be shed through the action of ADAM family members, modulation of PrPC or PrPSc ectodomain shedding does not regulate prion conversion. Expand