Publisher Correction: Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis

By R. Kirchdoerfer, Nianshuang Wang, J. Pallesen, D. Wrapp, H. Turner, C. Cottrell, Kizzmekia S. Corbett, Barney S. Graham, J. McLellan, A. Ward. 2018

A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper

Citations in the corpus

• Elicitation of Potent Neutralizing Antibody Responses by Designed Protein Nanoparticle Vaccines for SARS-CoV-2 (2020, neutral): “…purified RBD-I53-50A proteins (~30 mg purified protein per liter Expi293F cells) were ~20-fold higher than for the prefusion-stabilized S-2P trimer (Kirchdoerfer et al., 2018; Pallesen et al., 2017; Walls et al., 2020; Wrapp et al., 2020) (~1.5 mg/L), and increased to ~60 mg/L following promoter…”
• Molecular Architecture of the SARS-CoV-2 Virus (2020, unknown): “The activation of S requires cleavage of S1/S2 by furin-like protease and undergoes the conformational change from prefusion to postfusion (Belouzard et al., 2009; Kirchdoerfer et al., 2018; Simmons et al., 2004; Simmons et al., 2013; Song et al., 2018).”