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The Interplay of Furin Cleavage and D614G in Modulating SARS-CoV-2 Spike Protein Dynamics

https://doi.org/10.1101/2025.01.27.635166

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

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Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant

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ESCRT recruitment to SARS-CoV-2 spike induces virus-like particles that improve mRNA vaccines

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Real-Time Conformational Dynamics of SARS-CoV-2 Spikes on Virus Particles

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The ABC transporter MsbA in a dozen environments

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Monoclonal antibody therapies against SARS-CoV-2

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Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein

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STRUCTURE AND ENZYMATIC BREAK-DOWN OF PROTEINS

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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

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Distinct conformational states of SARS-CoV-2 spike protein

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Structural impact on SARS-CoV-2 spike protein by D614G substitution

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Broadly neutralizing antibodies target the coronavirus fusion peptide

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Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion

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MultiSero: An Open-Source Multiplex-ELISA Platform for Measuring Antibody Responses to Infection

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What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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SARS CoV-2 spike adopts distinct conformational ensembles in situ

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Production of SARS-CoV-2 virus-like particles as a vaccine candidate in stable cell lines through inducible E and M protein expression

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An integrated workflow for structural virology with a 100 keV electron microscope

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