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Angiotensin-Converting Enzyme-2
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistr...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7150073/ http://dx.doi.org/10.1016/B978-0-12-382219-2.00100-9 |
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author | Clarke, Nicola E. Hooper, Nigel M. Turner, Anthony J. |
author_facet | Clarke, Nicola E. Hooper, Nigel M. Turner, Anthony J. |
author_sort | Clarke, Nicola E. |
collection | PubMed |
description | The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing features for a specific peptidase. The subject of Chapter 100 is Angiotensin-Converting Enzyme-2. Keywords: Angiotensin, angiotensin-converting enzyme 2 (ACE2), apelin, bradykinin, carboxypeptidase, cardiovascular, collectrin, renin-angiotensin system, SARS virus, shedding, transmembrane, vasoactive, zinc-binding motif. |
format | Online Article Text |
id | pubmed-7150073 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71500732020-04-13 Angiotensin-Converting Enzyme-2 Clarke, Nicola E. Hooper, Nigel M. Turner, Anthony J. Handbook of Proteolytic Enzymes Article The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing features for a specific peptidase. The subject of Chapter 100 is Angiotensin-Converting Enzyme-2. Keywords: Angiotensin, angiotensin-converting enzyme 2 (ACE2), apelin, bradykinin, carboxypeptidase, cardiovascular, collectrin, renin-angiotensin system, SARS virus, shedding, transmembrane, vasoactive, zinc-binding motif. 2013 2012-11-09 /pmc/articles/PMC7150073/ http://dx.doi.org/10.1016/B978-0-12-382219-2.00100-9 Text en Copyright © 2013 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Clarke, Nicola E. Hooper, Nigel M. Turner, Anthony J. Angiotensin-Converting Enzyme-2 |
title | Angiotensin-Converting Enzyme-2 |
title_full | Angiotensin-Converting Enzyme-2 |
title_fullStr | Angiotensin-Converting Enzyme-2 |
title_full_unstemmed | Angiotensin-Converting Enzyme-2 |
title_short | Angiotensin-Converting Enzyme-2 |
title_sort | angiotensin-converting enzyme-2 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7150073/ http://dx.doi.org/10.1016/B978-0-12-382219-2.00100-9 |
work_keys_str_mv | AT clarkenicolae angiotensinconvertingenzyme2 AT hoopernigelm angiotensinconvertingenzyme2 AT turneranthonyj angiotensinconvertingenzyme2 |