PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33326798-4 2020 The disulfide-bonded ACE2 microbody protein inhibits entry of SARS-CoV-2 spike protein pseudotyped virus and replication of live SARS-CoV-2 in vitro and in a mouse model. Disulfides 4-13 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 73-78 33431842-3 2021 To support ongoing vaccine development efforts, we report the structure-based design of soluble S trimers with increased yields and stabilities, based on introduction of single point mutations and disulfide-bridges. Disulfides 197-206 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 96-97 33409271-3 2020 The receptor-binding domain (RBD) of the 2019-nCoV spike (S) protein contains disulfide bonds and N-linked glycosylations, therefore, it is typically produced by secretion. Disulfides 78-87 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 51-56 33409271-3 2020 The receptor-binding domain (RBD) of the 2019-nCoV spike (S) protein contains disulfide bonds and N-linked glycosylations, therefore, it is typically produced by secretion. Disulfides 78-87 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 34780781-0 2022 Disulfide bonds play a critical role in the structure and function of the receptor-binding domain of the SARS-CoV-2 Spike antigen. Disulfides 0-9 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 116-121 32737467-5 2020 Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state. Disulfides 80-89 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 35-36 32737467-6 2020 Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer. Disulfides 18-27 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-1 32737467-6 2020 Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer. Disulfides 47-56 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-1 32656452-6 2020 In this study, the role of thiol-disulfide balance on the interactions between SARS-CoV/CoV-2 spike proteins and ACE2 was investigated using molecular dynamics simulations. Disulfides 33-42 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 94-99 32656452-7 2020 The study revealed that the binding affinity was significantly impaired when all of the disulfide bonds of both ACE2 and SARS-CoV/CoV-2 spike proteins were reduced to thiol groups. Disulfides 88-97 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 136-141 33250972-5 2020 High-resolution protein structures of S-proteins and ACE2 receptors highlighted the probability that two of these disulfide bonds are potentially redox-active, facilitating the primal interaction between the receptor and the spike protein. Disulfides 114-123 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 225-230 34780781-2 2022 The Spike proteins of coronaviruses, responsible for cell receptor binding and viral internalization, possess multiple and frequently conserved disulfide bonds raising the question about their role in these proteins. Disulfides 144-153 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 4-9 34780781-3 2022 Here, we present a detailed structural and functional investigation of the disulfide bonds of the SARS-CoV-2 Spike receptor-binding domain (RBD). Disulfides 75-84 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 109-114 34780781-5 2022 This flexibility is particularly prominent for the disulfide bond-containing surface loop (residues 456-490) that participates in the formation of the interaction surface with the Spike cell receptor ACE2. Disulfides 51-60 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 180-185 34780781-7 2022 Our research demonstrates the mechanism by which the disulfide bonds contribute to the molecular structure of the RBD of the Spike protein, allowing the RBD to execute its viral function. Disulfides 53-62 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 125-130 34558135-2 2021 The interaction between the SARS-CoV-2 spike protein and the human receptor angiotensin-converting enzyme 2, both of which contain several cysteine residues, is impacted by the disulfide-thiol balance in the host cell. Disulfides 177-186 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 39-44 34004056-0 2021 Disruption of disulfides within RBD of SARS-CoV-2 spike protein prevents fusion and represents a target for viral entry inhibition by registered drugs. Disulfides 14-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 50-55 35163624-0 2022 A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed in E. coli Using a SEP-Tag Produces Antisera Interacting with the Mammalian Cell Expressed Spike (S1) Protein. Disulfides 8-17 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 66-71 35163624-0 2022 A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed in E. coli Using a SEP-Tag Produces Antisera Interacting with the Mammalian Cell Expressed Spike (S1) Protein. Disulfides 8-17 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 181-186 35123263-0 2022 The function of SARS-CoV-2 spike protein is impaired by disulfide-bond disruption with mutation at cysteine-488 and by thiol-reactive N-acetyl-cysteine and glutathione. Disulfides 56-65 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 27-32