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Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features.
Hassan, Sk Sarif; Ghosh, Shinjini; Attrish, Diksha; Choudhury, Pabitra Pal; Aljabali, Alaa A A; Uhal, Bruce D; Lundstrom, Kenneth; Rezaei, Nima; Uversky, Vladimir N; Seyran, Murat; Pizzol, Damiano; Adadi, Parise; Soares, Antonio; El-Aziz, Tarek Mohamed Abd; Kandimalla, Ramesh; Tambuwala, Murtaza M; Azad, Gajendra Kumar; Sherchan, Samendra P; Baetas-da-Cruz, Wagner; Takayama, Kazuo; Serrano-Aroca, Ángel; Chauhan, Gaurav; Palu, Giorgio; Brufsky, Adam M.
  • Hassan SS; Department of Mathematics, Pingla Thana Mahavidyalaya, Maligram 721140, India.
  • Ghosh S; Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata 700009, India.
  • Attrish D; Dr. B. R. Ambedkar Centre for Biomedical Research (ACBR), University of Delhi (North Campus), Delhi 110007, India.
  • Choudhury PP; Applied Statistics Unit, Indian Statistical Institute, Kolkata 700108, West Bengal, India.
  • Aljabali AAA; Department of Pharmaceutics and Pharmaceutical Technology, Yarmouk University-Faculty of Pharmacy, Irbid 566, Jordan.
  • Uhal BD; Department of Physiology, Michigan State University, East Lansing, MI 48824, USA.
  • Lundstrom K; PanTherapeutics, Rte de Lavaux 49, CH1095 Lutry, Switzerland.
  • Rezaei N; Research Center for Immunodeficiencies, Pediatrics Center of Excellence, Children's Medical Center, Tehran University of Medical Sciences, Tehran 1416753955, Iran.
  • Uversky VN; Network of Immunity in Infection, Malignancy and Autoimmunity (NIIMA), Universal Scientific Education and Research Network (USERN), SE-123 Stockholm, Sweden.
  • Seyran M; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.
  • Pizzol D; Doctoral studies in natural and technical sciences (SPL 44), University of Vienna, 1010 Wien, Austria.
  • Adadi P; Italian Agency for Development Cooperation-Khartoum, Sudan Street 33, Al Amarat, Khartoum 825109, Sudan.
  • Soares A; Department of Food Science, University of Otago, Dunedin 9054, New Zealand.
  • El-Aziz TMA; Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 77030, USA.
  • Kandimalla R; Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 77030, USA.
  • Tambuwala MM; Zoology Department, Faculty of Science, Minia University, El-Minia 61519, Egypt.
  • Azad GK; Applied Biology, CSIR-Indian Institute of Chemical Technology Uppal Road, Tarnaka, Hyderabad 500007, India.
  • Sherchan SP; Department of Biochemistry, Kakatiya Medical College, Warangal, Telangana 500022, India.
  • Baetas-da-Cruz W; School of Pharmacy and Pharmaceutical Science, Ulster University, Coleraine BT52 1SA, Northern Ireland, UK.
  • Takayama K; Department of Zoology, Patna University, Patna, Bihar 800005, India.
  • Serrano-Aroca Á; Department of Environmental Health Sciences, Tulane University, New Orleans, LA 70112, USA.
  • Chauhan G; Translational Laboratory in Molecular Physiology, Centre for Experimental Surgery, College of Medicine, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro 21941901, Brazil.
  • Palu G; Center for iPS Cell Research and Application, Kyoto University, Kyoto 606-8501, Japan.
  • Brufsky AM; Biomaterials and Bioengineering Lab, Translational Research Centre San Alberto Magno, Catholic University of Valencia San Vicente Mártir, c/Guillem de Castro 94, 46001 Valencia, Spain.
Molecules ; 25(24)2020 Dec 13.
Article in English | MEDLINE | ID: covidwho-971260
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
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ABSTRACT
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) that is engendering the severe coronavirus disease 2019 (COVID-19) pandemic. The spike (S) protein receptor-binding domain (RBD) of SARS-CoV-2 binds to the three sub-domains viz. amino acids (aa) 22-42, aa 79-84, and aa 330-393 of ACE2 on human cells to initiate entry. It was reported earlier that the receptor utilization capacity of ACE2 proteins from different species, such as cats, chimpanzees, dogs, and cattle, are different. A comprehensive analysis of ACE2 receptors of nineteen species was carried out in this study, and the findings propose a possible SARS-CoV-2 transmission flow across these nineteen species.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Limits: Animals / Humans Language: English Journal subject: Biology Year: 2020 Document Type: Article Affiliation country: Molecules25245906

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Limits: Animals / Humans Language: English Journal subject: Biology Year: 2020 Document Type: Article Affiliation country: Molecules25245906