The collectrin‐like part of the<scp>SARS‐CoV‐1 and ‐2</scp>receptor<scp>ACE2</scp>is shed by the metalloproteinases<scp>ADAM10</scp>and<scp>ADAM17</scp>-Reference-Cited by-同舟云学术

The collectrin‐like part of theSARS‐CoV‐1 and ‐2receptorACE2is shed by the metalloproteinasesADAM10andADAM17

Published:2022-02-24 Issue:3 Volume:36 Page:
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:The FASEB Journal

Author:

Niehues Rabea Victoria¹,Wozniak Justyna¹,Wiersch Florian¹,Lilienthal Eva¹,Tacken Nikola¹,Schumertl Tim²,Garbers Christoph²^ORCID,Ludwig Andreas¹,Düsterhöft Stefan¹^ORCID

Affiliation:

1. Institute of Molecular Pharmacology Medical Faculty RWTH Aachen University Aachen Germany

2. Department of Pathology Medical Faculty Otto von Guericke University Magdeburg Magdeburg Germany

Funder

Medizinische Fakultät, RWTH Aachen University

Bundesministerium für Bildung und Forschung

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.202101521R

Reference92 articles.

1. A Novel Angiotensin-Converting Enzyme–Related Carboxypeptidase (ACE2) Converts Angiotensin I to Angiotensin 1-9

2. Multiple Functions of Angiotensin-Converting Enzyme 2 and Its Relevance in Cardiovascular Diseases

3. ACE2 mouse models: a toolbox for cardiovascular and pulmonary research

4. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus

5. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

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