SARS-CoV-2 Recombinant Proteins
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A sharp tool for nucleic acid extraction and removing impurities (unnecessary protein and nuclease) from SARS-CoV2-virus samples-Protease K (Large quantity of spot supply)
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SARS-CoV-2 Antigens Structural Protein
SARS-CoV-2 structural proteins have important functions in pathogenesis as well as infectious virus assembly. These include spike protein (S protein), envelope protein (E protein), membrane protein (M protein) and nucleocapsid protein (N protein), which are all encoded by the 3’-end of the virus genome.
SARS-CoV-2 Antigens Non-Structural Protein
The recently sequenced genomes of SARS-CoV-2 strains combined with the comparative analysis of the SARS-CoV genome organization and transcription allowed us to construct a tentative list of gene products. It was suggested that SARS-CoV-2 had 16 predicted non-structural proteins (referred to nsp1-nsp16) constituting polyproteins pp1a and pp1ab, which were translated from ORF1a and ORF1ab of the virus genome.
SARS-CoV-2 Entry Receptors
The invasion of host cells is the most important part of coronavirus (CoV) infection. The envelope spike (S) glycoprotein is responsible for CoV cell entry and host-to-host transmission. For productive entry into host cells, viruses attach to specific cell surface receptor molecules. This is the case of CoV, whose use of distinct entry receptor molecules is responsible for their broad host range and tissue tropism.
SARS-CoV-2 Cytokine Storm
After the virus invades the body, if the body cannot produce enough specific immune response to effectively remove the virus, it will continue to strengthen the non-specific inflammatory response to eliminate the virus in an inefficient way. This not only cannot effectively remove the virus but will aggravate infection, tissue ischemia and hypoxia and even necrosis, and eventually lead to non-specific inflammatory response out of control to trigger cytokine storms.
SARS-CoV-2 Research Articles The Hottest
- 1. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Science. 458 Citations
- 2. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
Cell. 1375 Citations
- 3.Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine
Cellular & Molecular Immunology. 125 Citations
- 4.Structural basis of receptor recognition by SARS-CoV-2
Nature. 173 Citations
- 5.Molecular immune pathogenesis and diagnosis of COVID-19
Journal of Pharmaceutical Analysis. 151 Citations
- 6.Evidence of the COVID-19 Virus Targeting the CNS: Tissue Distribution, Host−Virus Interaction, and Proposed Neurotropic Mechanisms
ACS chemical neuroscience. 256 Citations
- 7. Prediction of the SARS-CoV-2 (2019-nCoV) 3C-like protease (3CL pro) structure: virtual screening reveals velpatasvir, ledipasvir, and other drug repurposing candidates
F1000Research. 66 Citations
- 8. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion
Cell research. 54 Citations
- 1. The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
Iscience. 26 June 2020
- 2.Pathogenesis of SARS-CoV-2 in Transgenic Mice Expressing Human Angiotensin-Converting Enzyme 2
Cell. 21 May 2020
- 3. Key residues of the receptor binding motif in the spike protein of SARS-CoV-2 that interact with ACE2 and neutralizing antibodies
Cellular & Molecular. 15 May 2020
- 4.Site-specific glycan analysis of the SARS-CoV-2 spike
Science. 04 May 2020
- 5.A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Science. 08 May 2020
- 6.TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes
Science Immunology. 13 May 2020
- 7. Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19
Cell. 28 May 2020
- 8. Human neutralizing antibodies elicited by SARS-CoV-2 infection
Nature. 26 May 2020