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 angiotensin converting enzyme 2 Homo sapiens 21-25 34155214-5 2021 Additional disulfide mutations caused the fixing of a closed ACE2 conformation to avoid off-target effects of protease activity, and also improved structural stability. Disulfides 11-20 angiotensin converting enzyme 2 Homo sapiens 61-65 34150335-3 2021 While groups such as disulfides in ACE2"s zinc metallopeptidase, and also in COVID-19"s spikes, facilitate such binding, it is worth exploring how similar complementary sites on materials such as polymers, metals, ceramics, fabrics, and biomaterials promote binding of viruses and bacteria and how they could be further engineered to prevent bioactivity, or to act as agents to collect viral payloads in filters or similar devices. Disulfides 21-31 angiotensin converting enzyme 2 Homo sapiens 35-39 34142531-2 2021 Based on the structure of the complex of the protein S receptor-binding domain (RBD) and ACE2, the design of chimeric molecules consisting of two 22-23-mer peptides linked to each other by disulfide bonds was carried out. Disulfides 189-198 angiotensin converting enzyme 2 Homo sapiens 89-93 35123263-3 2022 The cysteine residue at position 488, consisting of a disulfide bridge with cysteine 480 is located in an important structural loop at ACE2-binding surface of RBD, and is highly conserved among SARS-related coronaviruses. Disulfides 54-63 angiotensin converting enzyme 2 Homo sapiens 135-139 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 angiotensin converting enzyme 2 Homo sapiens 200-204 34780781-6 2022 In vitro, disulfide bond reducing agents affect the RBD secondary structure, lower its melting temperature from 52 C to 36-39 C and decrease its binding affinity to ACE2 by two orders of magnitude at 37 C. Consistent with these in vitro findings, the reducing agents tris(2-carboxyethyl)phosphine (TCEP) and dithiothreitol (DTT) were able to inhibit viral replication at low millimolar levels in cell-based assays. Disulfides 10-19 angiotensin converting enzyme 2 Homo sapiens 165-169 34538222-8 2021 Importantly, vaccination with peptide 446-480 or with a cyclic version of peptide 446-488 containing a disulfide bridge between cysteines 480 and 488, protected humanized K18-hACE2 mice from a lethal dose of SARS-CoV-2 (62.5 and 75% of protection; P<0.01 and P<0.001, respectively). Disulfides 103-112 angiotensin converting enzyme 2 Homo sapiens 175-180 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 angiotensin converting enzyme 2 Homo sapiens 76-107 34745440-2 2021 Based on the structure of the complex of the protein S receptor-binding domain (RBD) and ACE2, the design of chimeric molecules consisting of two 22-23-mer peptides linked to each other by disulfide bonds was carried out. Disulfides 189-198 angiotensin converting enzyme 2 Homo sapiens 89-93 33250972-4 2020 Our analysis of retrieved amino acid sequences deposited in data bases shows that S-proteins and ACE2 are rich in cysteine (Cys) residues, many of which are conserved in various SARS-related coronaviruses and participate in intra-molecular disulfide bonds. Disulfides 240-249 angiotensin converting enzyme 2 Homo sapiens 97-101 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 angiotensin converting enzyme 2 Homo sapiens 113-117 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 angiotensin converting enzyme 2 Homo sapiens 112-116 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 angiotensin converting enzyme 2 Homo sapiens 53-57 33250972-6 2020 Presence of redox-active disulfides in the interacting parts of S-protein, ACE2, and a ferredoxin-like fold domain in the transmembrane part of ACE2, strongly indicate the role of redox in COVID-19 pathogenesis and severity. Disulfides 25-35 angiotensin converting enzyme 2 Homo sapiens 75-79 33250972-6 2020 Presence of redox-active disulfides in the interacting parts of S-protein, ACE2, and a ferredoxin-like fold domain in the transmembrane part of ACE2, strongly indicate the role of redox in COVID-19 pathogenesis and severity. Disulfides 25-35 angiotensin converting enzyme 2 Homo sapiens 144-148 33250972-7 2020 Resistant animals lack a redox-active disulfide (Cys133-Cys141) in ACE2 sequences, further strengthening the redox hypothesis for infectivity. Disulfides 38-47 angiotensin converting enzyme 2 Homo sapiens 67-71