Article3 Biotech2021
Structural analysis of COVID-19 spike protein in recognizing the ACE2 receptor of different mammalian species and its susceptibility to viral infection.
Article in 3 Biotech, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Identification of new pharmacophore against SARS-CoV-2 spike protein by multi-fold computational and biochemical techniques.Scientific reports · 2024Article
- Synthesis of multivalent sialyllactose-conjugated PAMAM dendrimers: Binding to SARS-CoV-2 spike protein and influenza hemagglutinin.International journal of biological macromolecules · 2023Article
- Viral target and metabolism-based rationale for combined use of recently authorized small molecule COVID-19 medicines: Molnupiravir, nirmatrelvir, and remdesivir.Fundamental & clinical pharmacology · 2023Review
- Label-Free Saliva Test for Rapid Detection of Coronavirus Using Nanosensor-Enabled SERS.Bioengineering (Basel, Switzerland) · 2023Article
- SARS-CoV-2 Affects Both Humans and Animals: What Is the Potential Transmission Risk? A Literature Review.Microorganisms · 2023Review
- Computational prediction of the effect of mutations in the receptor-binding domain on the interaction between SARS-CoV-2 and human ACE2.Molecular diversity · 2022Article
- Genomic and structural mechanistic insight to reveal the differential infectivity of omicron and other variants of concern.Computers in biology and medicine · 2022Article
- GPS Tracking of Free-Roaming Cats (Viruses · 2022Article
- Structural modeling of Omicron spike protein and its complex with human ACE-2 receptor: Molecular basis for high transmissibility of the virus.Biochemical and biophysical research communications · 2022Article
- Tracking cryptic SARS-CoV-2 lineages detected in NYC wastewater.Nature communications · 2022Article
- Systems analysis shows that thermodynamic physiological and pharmacological fundamentals drive COVID-19 and response to treatment.Pharmacology research & perspectives · 2022Review
- Comparative Structural Analysis of Human ACE2 Receptor with Spike Protein of SARS-CoV-2 Variants: Implications to Understand Infectivity of the Virus.Advances and applications in bioinformatics and chemistry : AABC · 2022Article
- Fruit Bromelain-Derived Peptide Potentially Restrains the Attachment of SARS-CoV-2 Variants to hACE2: A Pharmacoinformatics Approach.Molecules (Basel, Switzerland) · 2022Article
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- Animal Transmission of SARS-CoV-2 and the Welfare of Animals during the COVID-19 Pandemic.Animals : an open access journal from MDPI · 2021Review
- An Analysis Based on Molecular Docking and Molecular Dynamics Simulation Study of Bromelain as Anti-SARS-CoV-2 Variants.Frontiers in pharmacology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pandemic COVID-19 was caused by a novel Coronavirus-2 (SARS-CoV-2) that infects humans through the binding of glycosylated SARS-CoV-2 spike 2 protein to the glycosylated ACE2 receptor. The spike 2 protein recognizes the N-terminal helices of the glycosylated metalloprotease domain in the human ACE2 receptor. To understand the susceptibility of animals for infection and transmission, we did sequence and structure-based molecular interaction analysis of 16 ACE2 receptors from different mammalian species with SARS-CoV-2 spike 2 receptor binding domain. Our comprehensive structure analysis revealed that the natural substitution of amino acid residues Gln24, His34, Phe40, Leu79 and Met82 in the N-terminal α1 and α2 helices of the ACE2 receptor results in loss of crucial network of hydrogen-bonded and hydrophobic interactions with receptor binding domain of SARS-CoV-2 spike protein. Another striking observation is the absence of N-glycosylation site Asn103 in all mammals and many species, lack more than one N-linked glycosylation site in the ACE2 receptor. Based on the loss of crucial interactions and the absence of N-linked glycosylation sites we categorized SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13205-020-02599-2.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.