SARS_CoV_2 mutation literature information.


  A comprehensive overview of identified mutations in SARS CoV-2 spike glycoprotein among Iranian patients.
 PMID: 34896524       2022       Gene
Table: N501T


  Insights into the structural and dynamical changes of spike glycoprotein mutations associated with SARS-CoV-2 host receptor binding.
 PMID: 32851910       2022       Journal of biomolecular structure & dynamics
Table: N501T
Discussion: Interestingly, in our study too, the RBD mutations L455Y, F486L, Q493N, and N501T were observed to have the highest deviations as compared to the WT structure.
Discussion: Most of the mutations like F486L, Q493N, L455Y, and Q498Y are known to interact and N501T was found in forming a hydrogen bond with ACE2 in the viral entry to the host cells.


  Analysis of SARS-COV2 spike protein variants among Iraqi isolates.
 PMID: 34754982       2022       Gene reports
Result: However, N501T reduces the binding affinity of spike protein to the human ACE2.


  SARS-CoV-2 spike evolutionary behaviors; simulation of N501Y mutation outcomes in terms of immunogenicity and structural characteristic.
 PMID: 34783057       2022       Journal of cellular biochemistry
Conclusion: So far, many mutations (E484K, Q493N, and N501T) have been identified in the RBD domain of this protein.


  Computational modelling of potentially emerging SARS-CoV-2 spike protein RBDs mutations with higher binding affinity towards ACE2: A structural modelling study.
 PMID: 34979405       2022       Computers in biology and medicine
Result: 3 A, and the structures of N501I, N501T and N501V mutants are given in.
Result: According to these values, the N501I and N501T are strong binders of ACE2 than N501V, which is comparable to the wild type.
Result: By achieving a stable structural state red colour, these conformational levels were shown to be closer to each other, notably in wild type, N501I, and N501T, and were regarded an energetically stable conformational state.


  Aggregation of high-frequency RBD mutations of SARS-CoV-2 with three VOCs did not cause significant antigenic drift.
 PMID: 35032057       2022       Journal of medical virology
Introduction: As of March 2021, the 15 most commonly observed mutations in the RBD were as follows: V367F, P384L, K417N, N439K, L452R, Y453F, S477N, S477R, T478K, E484K, S494P, N501T, N501Y, A520S, and A522S, which were located at 13 sites in the RBD.
Result: The neutralization results for the possible VOC single variants showed that the N501Y mutation escap


  Impact of B.1.617 and RBD SARS-CoV-2 variants on vaccine efficacy: An in-silico approach.
 PMID: 35370005       2022       Indian journal of medical microbiology
Table: N501T
Discussion: A few mutants' viz.L455Y, Q493N, R408I, Q498Y, F486L, N501T within the RBD region (319-591), and D936Y& A930V within HR1 site (912-984) have also been studied by in silico analysis to investigate the basic structure of spike glycoprotein.


  Evolutionary history of the SARS-CoV-2 Gamma variant of concern (P.1): a perfect storm.
 PMID: 35266951       2022       Genetics and molecular biology
Introduction: The first strain of SARS-CoV-2 identified in Wuhan, China, in December 2019, was also characterized as having five critical amino acid differences in its RBD when compared with SARS-CoV (L455Y, F486L, Q493N, S494D, N501T; SARS-CoV-2 and SARS-CoV aa respectively; Wan et al., 2020).


  Tracking cryptic SARS-CoV-2 lineages detected in NYC wastewater.
 PMID: 35115523       2022       Nature communications
Figure: WNY1 = E484A/F486P/S494P/Q498Y/H519N/F572N, WNY2 = Q493K/S494P/Q498Y/H519N/T572N, WNY3 = K417T/K444T/E484A/F590Y/Q498H, WNY4 = K417T/N439K/K444N/Y449R/L452R/N460K/S477N/Delta484/


  The basis of mink susceptibility to SARS-CoV-2 infection.
 PMID: 35396646       2022       Journal of applied genetics
Table: N501T
Figure: Abbreviations stand for: CT, cytoplasmic domain; D614G, mutation in the S protein; F486L, mutation in the S protein; FP, fusion peptide; HR1, heptapeptide repeat sequence 1; HR2, heptapeptide repeat sequence 2; N501T, mutation in the S protein; NDT, N-terminal domain; PRRA, polybasic cleavage site; RBD, receptor-binding domain; S1, S1 subunit of the S protein; S2, S2 subunit of the S protein; TM, transmembrane domain; Y453F, mutation in the S protein.
Discussion: According to Welkers et al., each of the three mut



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