About: Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain

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About: Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain
Creator	Clarke, Nicola Hooper, Nigel Lambert, Daniel Turner, Anthony
Source	Elsevier; Medline; PMC
abstract	Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin–angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-α converting enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors.
has issue date	2008-01-23(xsd:dateTime)
bibo:doi	10.1016/j.febslet.2007.11.085
bibo:pmid	18070603
has license	no-cc
sha1sum (hex)	91928facf53b5a9b8dea0f42a2ff0767dd2b94d0
schema:url	https://doi.org/10.1016/j.febslet.2007.11.085
resource representing a document's title	Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain
has PubMed Central identifier	PMC7094239
has PubMed identifier	18070603
schema:publication	FEBS Lett
resource representing a document's body	covid:91928facf53b5a9b8dea0f42a2ff0767dd2b94d0#body_text
is schema:about of	named entity 'involving' named entity 'cell' named entity 'protein' named entity 'ACE2' named entity 'CONVERTING' named entity 'PROCESS' named entity 'ECTODOMAIN' named entity 'STIMULATE' named entity 'SARS' named entity 'INVOLVING' named entity 'HAVE' named entity 'ECTODOMAIN' named entity 'ADAM17' named entity 'MEDIATED' named entity 'REGULATORY PROTEIN' named entity 'RECEPTOR' named entity 'ASSOCIATES' named entity 'INHIBITORS' named entity 'CAUSATIVE AGENT' named entity 'CALMODULIN' named entity 'DECREASED BY' named entity 'ANGIOTENSIN-CONVERTING ENZYME' named entity 'ACE2' named entity 'PREVIOUSLY' named entity 'ACUTE' named entity 'RESPONSE TO' named entity 'CALMODULIN' named entity 'ITS' named entity 'PROTEIN ' named entity 'CORONAVIRUS' named entity 'SHEDDING' named entity 'STUDY' named entity 'PHORBOL ESTERS' named entity 'SEVERE' named entity 'TNF-A' named entity 'SYNDROME' named entity 'METALLOPROTEINASE' named entity 'RENIN-ANGIOTENSIN SYSTEM' named entity 'SHEDDING' named entity 'RESPIRATORY' named entity 'THE CELL' named entity 'PARTIALLY' named entity 'CELL SURFACE' named entity 'INTERACTION' named entity 'IS A' named entity 'ENZYME' named entity 'ANGIOTENSIN-CONVERTING ENZYME' named entity 'process' named entity 'enzyme' named entity 'ACE2' named entity 'ACE2' named entity 'causative' named entity 'Angiotensin-converting enzyme' named entity 'ACE2' named entity 'TNF-a' named entity 'ADAM17' named entity 'renin-angiotensin' named entity 'ACE2' named entity 'calmodulin' named entity 'cell surface' named entity 'ACE2' named entity 'protein' named entity 'growth factors' named entity 'binding sites' named entity 'metalloproteinase' named entity 'Invitrogen' named entity 'plasma membrane' named entity 'pharmacological' named entity 'liver' named entity 'metallopeptidase' named entity 'ACE2' named entity 'kidney' named entity 'Cambridge University' named entity 'calmodulin' named entity 'cell surface' named entity 'plasma membrane' named entity 'enhanced chemiluminescence' named entity 'secondary antibody'

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