FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4313219302> ?p ?o ?g. }

• W4313219302 abstract "Abstract The coronavirus SARS-CoV-2 protects its RNA from being recognized by host immune responses by methylation of its 5’ end, also known as capping. This process is carried out by two enzymes, non-structural protein 16 (NSP16) containing 2’-O-methyltransferase and NSP14 through its N7 methyltransferase activity, which are essential for the replication of the viral genome as well as evading the host’s innate immunity. NSP10 acts as a crucial cofactor and stimulator of NSP14 and NSP16. To further understand the role of NSP10, we carried out a comprehensive analysis of >13 million globally collected whole-genome sequences (WGS) of SARS-CoV-2 obtained from the Global Initiative Sharing All Influenza Data (GISAID) and compared it with the reference genome Wuhan/WIV04/2019 to identify all currently known variants in NSP10. T12I, T102I, and A104V in NSP10 have been identified as the three most frequent variants and characterized using X-ray crystallography, biophysical assays and enhanced sampling simulations. In contrast to other proteins such as spike and NSP6, NSP10 is significantly less prone to mutation due to its crucial role in replication. The functional effects of the variants were examined for their impact on the binding affinity and stability of both NSP14-NSP10 and NSP16-NSP10 complexes. These results highlight the limited changes induced by variant evolution in NSP10 and reflect on the critical roles NSP10 plays during the SARS-CoV-2 life cycle. These results also indicate that there is limited capacity for the virus to overcome inhibitors targeting NSP10 via the generation of variants in inhibitor binding pockets. Significance Statement The SARS-CoV-2 proteins have constantly been evolving. These variants assist the virus to survive, adapt and evade the host immune responses. While the main focus has been on structural proteins like Spike, there is very limited structural and functional information on the effects of emerging mutations on other essential non-structural viral proteins. One such protein is NSP10, an essential cofactor for NSP14 and NSP16. This study demonstrates that NSP10 is more resistant to genetic variations than other SARS-CoV-2 non-structural proteins and that the presence of mutations conserve structural and dynamic changes in NSP10. The effects of naturally occurring mutations reflect the evolutionary relationship between structurally conserved essential cofactors, their function and the role they play in the survival of the virus." @default.
• W4313219302 created "2023-01-06" @default.
• W4313219302 creator A5008762219 @default.
• W4313219302 creator A5009988205 @default.
• W4313219302 creator A5011865422 @default.
• W4313219302 creator A5015085792 @default.
• W4313219302 creator A5026371769 @default.
• W4313219302 creator A5034680877 @default.
• W4313219302 creator A5037269329 @default.
• W4313219302 creator A5045751131 @default.
• W4313219302 creator A5046225712 @default.
• W4313219302 creator A5053107527 @default.
• W4313219302 creator A5078109776 @default.
• W4313219302 date "2022-12-26" @default.
• W4313219302 modified "2023-10-17" @default.
• W4313219302 title "Emerging variants of SARS-CoV-2 NSP10 highlight strong functional conservation of its binding to two non-structural proteins, NSP14 and NSP16" @default.
• W4313219302 cites W1487052430 @default.
• W4313219302 cites W1969955120 @default.
• W4313219302 cites W2007662810 @default.
• W4313219302 cites W2010076108 @default.
• W4313219302 cites W2028875836 @default.
• W4313219302 cites W2035266068 @default.
• W4313219302 cites W2038532826 @default.
• W4313219302 cites W2066951434 @default.
• W4313219302 cites W2074499728 @default.
• W4313219302 cites W2082586732 @default.
• W4313219302 cites W2093427616 @default.
• W4313219302 cites W2124026197 @default.
• W4313219302 cites W2143660875 @default.
• W4313219302 cites W2145605402 @default.
• W4313219302 cites W2147988069 @default.
• W4313219302 cites W2154197653 @default.
• W4313219302 cites W2180229411 @default.
• W4313219302 cites W2296686360 @default.
• W4313219302 cites W2306812407 @default.
• W4313219302 cites W2442161751 @default.
• W4313219302 cites W2587970647 @default.
• W4313219302 cites W2605343262 @default.
• W4313219302 cites W2613638456 @default.
• W4313219302 cites W2954012201 @default.
• W4313219302 cites W3004280078 @default.
• W4313219302 cites W3004896487 @default.
• W4313219302 cites W3007500173 @default.
• W4313219302 cites W3014708904 @default.
• W4313219302 cites W3044391874 @default.
• W4313219302 cites W3045327938 @default.
• W4313219302 cites W3083008290 @default.
• W4313219302 cites W3083866604 @default.
• W4313219302 cites W3091122177 @default.
• W4313219302 cites W3091637359 @default.
• W4313219302 cites W3125590130 @default.
• W4313219302 cites W3147842526 @default.
• W4313219302 cites W3159182925 @default.
• W4313219302 cites W3162610282 @default.
• W4313219302 cites W3165479483 @default.
• W4313219302 cites W3197432239 @default.
• W4313219302 cites W3202880756 @default.
• W4313219302 cites W3217300869 @default.
• W4313219302 cites W4200137031 @default.
• W4313219302 cites W4200485684 @default.
• W4313219302 cites W4220707716 @default.
• W4313219302 cites W4292360241 @default.
• W4313219302 cites W4294927110 @default.
• W4313219302 doi "https://doi.org/10.1101/2022.12.23.521761" @default.
• W4313219302 hasPublicationYear "2022" @default.
• W4313219302 type Work @default.
• W4313219302 citedByCount "1" @default.
• W4313219302 countsByYear W43132193022023 @default.
• W4313219302 crossrefType "posted-content" @default.
• W4313219302 hasAuthorship W4313219302A5008762219 @default.
• W4313219302 hasAuthorship W4313219302A5009988205 @default.
• W4313219302 hasAuthorship W4313219302A5011865422 @default.
• W4313219302 hasAuthorship W4313219302A5015085792 @default.
• W4313219302 hasAuthorship W4313219302A5026371769 @default.
• W4313219302 hasAuthorship W4313219302A5034680877 @default.
• W4313219302 hasAuthorship W4313219302A5037269329 @default.
• W4313219302 hasAuthorship W4313219302A5045751131 @default.
• W4313219302 hasAuthorship W4313219302A5046225712 @default.
• W4313219302 hasAuthorship W4313219302A5053107527 @default.
• W4313219302 hasAuthorship W4313219302A5078109776 @default.
• W4313219302 hasBestOaLocation W43132193021 @default.
• W4313219302 hasConcept C104317684 @default.
• W4313219302 hasConcept C126831891 @default.
• W4313219302 hasConcept C140704245 @default.
• W4313219302 hasConcept C141231307 @default.
• W4313219302 hasConcept C181199279 @default.
• W4313219302 hasConcept C2522874641 @default.
• W4313219302 hasConcept C33288867 @default.
• W4313219302 hasConcept C54355233 @default.
• W4313219302 hasConcept C552990157 @default.
• W4313219302 hasConcept C55493867 @default.
• W4313219302 hasConcept C86803240 @default.
• W4313219302 hasConcept C91965660 @default.
• W4313219302 hasConceptScore W4313219302C104317684 @default.
• W4313219302 hasConceptScore W4313219302C126831891 @default.
• W4313219302 hasConceptScore W4313219302C140704245 @default.
• W4313219302 hasConceptScore W4313219302C141231307 @default.
• W4313219302 hasConceptScore W4313219302C181199279 @default.
• W4313219302 hasConceptScore W4313219302C2522874641 @default.
• W4313219302 hasConceptScore W4313219302C33288867 @default.

• next