PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30670593-4 2019 Ficolin-3, the most abundant lectin pathway initiator in humans, circulates as disulfide-linked multimers of a monomer. Disulfides 79-88 ficolin 3 Homo sapiens 0-9 30670593-5 2019 ERp57 attenuated ficolin-3 ligand recognition and complement activation by cleaving intermolecular disulfide bonds in large ficolin-3 multimers, thereby reducing multimer size and ligand-binding affinity. Disulfides 99-108 ficolin 3 Homo sapiens 17-26 30670593-5 2019 ERp57 attenuated ficolin-3 ligand recognition and complement activation by cleaving intermolecular disulfide bonds in large ficolin-3 multimers, thereby reducing multimer size and ligand-binding affinity. Disulfides 99-108 ficolin 3 Homo sapiens 124-133 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 27-36 ficolin 3 Homo sapiens 56-65 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 27-36 ficolin 3 Homo sapiens 176-185 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 27-36 ficolin 3 Homo sapiens 176-185 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 84-93 ficolin 3 Homo sapiens 176-185 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 84-93 ficolin 3 Homo sapiens 176-185 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 84-93 ficolin 3 Homo sapiens 176-185 30670593-6 2019 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57. Disulfides 84-93 ficolin 3 Homo sapiens 176-185