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Q27620995-1B7F58EA-59CA-4D4E-A47C-B5EB4803D1DA
Q27620995-1B7F58EA-59CA-4D4E-A47C-B5EB4803D1DA
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27620995-1B7F58EA-59CA-4D4E-A47C-B5EB4803D1DA
New structural motifs on the chymotrypsin fold and their potential roles in complement factor B
P2860
Q27620995-1B7F58EA-59CA-4D4E-A47C-B5EB4803D1DA
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27620995-1B7F58EA-59CA-4D4E-A47C-B5EB4803D1DA
rank
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type
BestRank
Statement
wasDerivedFrom
19f5cb7c952020673b1362bbd159c3a1e8251cde
P2860
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D