2018
DOI: 10.1080/08927022.2018.1447108
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Correlation between experimentally indicated and atomistically simulated roles of EGFR N-glycosylation

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Cited by 10 publications
(5 citation statements)
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“…The average RMSD values also show that the gmRBDfN system is the most stable. This observation was expected as several other experimental, computational, and structural studies have reported that glycosylation contributes to increasing the stability of protein structures ( Solá and Griebenow, 2009 ; Azimzadeh Irani, 2018 ; Azimzadeh Irani and Ejtehadi, 2019 ; Motamedi et al, 2021 ).…”
Section: Resultssupporting
confidence: 80%
See 1 more Smart Citation
“…The average RMSD values also show that the gmRBDfN system is the most stable. This observation was expected as several other experimental, computational, and structural studies have reported that glycosylation contributes to increasing the stability of protein structures ( Solá and Griebenow, 2009 ; Azimzadeh Irani, 2018 ; Azimzadeh Irani and Ejtehadi, 2019 ; Motamedi et al, 2021 ).…”
Section: Resultssupporting
confidence: 80%
“…Glycosylation is the most common posttranslational modification that occurs for the virus, and the SARS-CoV-2 proteins, especially the S protein and its receptor ACE2, are densely glycosylated ( Shajahan et al, 2020 ; Woo et al, 2020 ; Gong et al, 2021 ; Guo et al, 2021 ). In several studies, glycosylation has been shown to be essential for protein folding, stability, and ligand binding ( Azimzadeh Irani et al, 2017 ; Azimzadeh Irani, 2018 ; Azimzadeh Irani and Ejtehadi, 2020 ; Motamedi et al, 2021 ; Rahnama et al, 2021 ). Both N-glycosylation and O-glycosylation occur on the spike protein of SARS-CoV-2, and the latter has a significant effect on virus function and infectivity ( Xu et al, 2020 ; Yasunori et al, 2020 ; Antonopoulos et al, 2021 ; Bagdonaite et al, 2021 ; Reis et al, 2021 ; Zhang et al, 2021 ).…”
Section: Introductionmentioning
confidence: 99%
“…The locations of glycosylated Asparagine residues are shown, one highlighted inside a grey box. Taken, with permission, from Irani [93]. ( e ) A molecular dynamic (MD) simulation of the sEGFR started from the structure in d. The connecting point between the extracellular and the transmembrane helices is marked by a circle.…”
Section: Figurementioning
confidence: 99%
“…38 Molecular dynamic simulations of glycosylation at N361 of EGFR showed large changes in side-chains, differences which were magnified in the presence of EGF ligand. 25,26,41,42 These simulations also suggested that glycosylation sugars at N361 may interact with the opposing EGFR dimer. 25,36 However, the functional relevance of how glycosylation of EGFR at N361 impacts EGFR protein and cellular behaviors remains unclear.…”
Section: Introductionmentioning
confidence: 80%