FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4306318232> ?p ?o ?g. }

• W4306318232 abstract "Abstract The Omicron variant (BA.1) and its sub-variants of the SARS-CoV-2 virus which causes the COVID-19 disease continues to spread across the United States and the World at large. As new sub-variants of SARS-CoV-2 continue to proliferate, a reliable computational method of quickly determining the potential infectivity of these new variants is needed to assess their potential threat. In the present study, we have tested and validated an efficient computational protocol, which includes an efficient energy minimization and subsequent molecular mechanics/Poisson Boltzmann surface area (MM-PBSA) calculation of the binding free energy between the SARS-CoV-2 spike protein and human angiotensin converting enzyme-2 (ACE2), to predict the binding affinities of these spike/ACE2 complexes based upon the calculated binding free energies and a previously calibrated linear correlation relationship. The predicted binding affinities are in good agreement with available experimental data including those for Omicron variants, suggesting that the predictions based on this protocol should be reasonable. Further, we have investigated several hundred potential mutations of both the wildtype and Omicron variants of the SARS-CoV-2 spike protein. Based on the predicted binding affinity data, we have identified several mutations that have the potential to vastly increase the binding affinity of the spike protein to ACE2 within both the wildtype and Omicron variants. Author Summary As well known, the coronavirus responsible for COVID-19 disease enters human cells through its spike protein binding with a human receptor protein known as angiotensin converting enzyme-2. So, the binding affinity between the spike protein and angiotensin converting enzyme-2 contributes to the infectivity of the coronavirus and its variants. In this study, we demonstrated that a generally applicable, fast and easy-to-use computational protocol was able to accurately predict the binding affinity of angiotensin converting enzyme-2 with spike protein of the currently known variants of the coronavirus. Hence, we believe that this computational protocol may be used to reliably predict the binding affinity of angiotensin converting enzyme-2 with spike protein of new variants to be identified in the future. Using this computational protocol, we have further examined a number of possible single mutations on the spike protein of both the wildtype and Omicron variants and predicted their binding affinity with angiotensin converting enzyme-2, demonstrating that several mutations have the potential to vastly increase the binding affinity of the spike protein to angiotensin converting enzyme-2." @default.
• W4306318232 created "2022-10-16" @default.
• W4306318232 creator A5037378495 @default.
• W4306318232 creator A5069992998 @default.
• W4306318232 date "2022-10-14" @default.
• W4306318232 modified "2023-10-18" @default.
• W4306318232 title "Computational Prediction of Binding Affinities of Human Angiotensin Converting Enzyme-2 with SARS-CoV-2 Spike Protein Variants: Omicron Variants and Potentially Deleterious Mutations" @default.
• W4306318232 cites W1965011325 @default.
• W4306318232 cites W2012443018 @default.
• W4306318232 cites W2065838297 @default.
• W4306318232 cites W2095719702 @default.
• W4306318232 cites W2167557712 @default.
• W4306318232 cites W2470899874 @default.
• W4306318232 cites W2554019130 @default.
• W4306318232 cites W2803029512 @default.
• W4306318232 cites W2808844862 @default.
• W4306318232 cites W2936076700 @default.
• W4306318232 cites W2938770575 @default.
• W4306318232 cites W3012841297 @default.
• W4306318232 cites W3030688226 @default.
• W4306318232 cites W3034673010 @default.
• W4306318232 cites W3084236163 @default.
• W4306318232 cites W3090312226 @default.
• W4306318232 cites W3104727101 @default.
• W4306318232 cites W3112362785 @default.
• W4306318232 cites W3113473864 @default.
• W4306318232 cites W3132966328 @default.
• W4306318232 cites W3133973522 @default.
• W4306318232 cites W3156241083 @default.
• W4306318232 cites W3165790948 @default.
• W4306318232 cites W3174394849 @default.
• W4306318232 cites W3193496380 @default.
• W4306318232 cites W3194545253 @default.
• W4306318232 cites W3194891808 @default.
• W4306318232 cites W3195621233 @default.
• W4306318232 cites W4200509137 @default.
• W4306318232 cites W4205815466 @default.
• W4306318232 cites W4206737621 @default.
• W4306318232 cites W4220696284 @default.
• W4306318232 cites W4225312017 @default.
• W4306318232 cites W769759530 @default.
• W4306318232 doi "https://doi.org/10.1101/2022.10.14.512203" @default.
• W4306318232 hasPublicationYear "2022" @default.
• W4306318232 type Work @default.
• W4306318232 citedByCount "0" @default.
• W4306318232 crossrefType "posted-content" @default.
• W4306318232 hasAuthorship W4306318232A5037378495 @default.
• W4306318232 hasAuthorship W4306318232A5069992998 @default.
• W4306318232 hasBestOaLocation W43063182321 @default.
• W4306318232 hasConcept C12554922 @default.
• W4306318232 hasConcept C147597530 @default.
• W4306318232 hasConcept C162324750 @default.
• W4306318232 hasConcept C170493617 @default.
• W4306318232 hasConcept C185592680 @default.
• W4306318232 hasConcept C187736073 @default.
• W4306318232 hasConcept C2780283098 @default.
• W4306318232 hasConcept C2781390188 @default.
• W4306318232 hasConcept C3018795828 @default.
• W4306318232 hasConcept C54355233 @default.
• W4306318232 hasConcept C55493867 @default.
• W4306318232 hasConcept C59593255 @default.
• W4306318232 hasConcept C70721500 @default.
• W4306318232 hasConcept C86803240 @default.
• W4306318232 hasConceptScore W4306318232C12554922 @default.
• W4306318232 hasConceptScore W4306318232C147597530 @default.
• W4306318232 hasConceptScore W4306318232C162324750 @default.
• W4306318232 hasConceptScore W4306318232C170493617 @default.
• W4306318232 hasConceptScore W4306318232C185592680 @default.
• W4306318232 hasConceptScore W4306318232C187736073 @default.
• W4306318232 hasConceptScore W4306318232C2780283098 @default.
• W4306318232 hasConceptScore W4306318232C2781390188 @default.
• W4306318232 hasConceptScore W4306318232C3018795828 @default.
• W4306318232 hasConceptScore W4306318232C54355233 @default.
• W4306318232 hasConceptScore W4306318232C55493867 @default.
• W4306318232 hasConceptScore W4306318232C59593255 @default.
• W4306318232 hasConceptScore W4306318232C70721500 @default.
• W4306318232 hasConceptScore W4306318232C86803240 @default.
• W4306318232 hasLocation W43063182321 @default.
• W4306318232 hasOpenAccess W4306318232 @default.
• W4306318232 hasPrimaryLocation W43063182321 @default.
• W4306318232 hasRelatedWork W1976430096 @default.
• W4306318232 hasRelatedWork W2018888195 @default.
• W4306318232 hasRelatedWork W2125501431 @default.
• W4306318232 hasRelatedWork W2139920520 @default.
• W4306318232 hasRelatedWork W2564621143 @default.
• W4306318232 hasRelatedWork W2969740023 @default.
• W4306318232 hasRelatedWork W3169615991 @default.
• W4306318232 hasRelatedWork W3170371354 @default.
• W4306318232 hasRelatedWork W3196360555 @default.
• W4306318232 hasRelatedWork W4206693359 @default.
• W4306318232 isParatext "false" @default.
• W4306318232 isRetracted "false" @default.
• W4306318232 workType "article" @default.