. . "11"^^ . . "6"^^ . . . "The mature bovine cathepsin C (CC) molecule is composed of four identical monomers, each proteolytically processed into three chains. Five intrachain disulfides and three nonpaired cysteine residues per monomer were identified. Beside catalytic Cys234 in the active site, free-thiol Cys331 and Cys424 were characterized." . . "Vondr\u00E1\u0161ek, Ji\u0159\u00ED" . "Baudy\u0161, M." . "Kluh, Ivan" . . "Voburka, Zden\u011Bk" . "GB - Spojen\u00E9 kr\u00E1lovstv\u00ED Velk\u00E9 Brit\u00E1nie a Severn\u00EDho Irska" . . . "Protein Science" . "The mature bovine cathepsin C (CC) molecule is composed of four identical monomers, each proteolytically processed into three chains. Five intrachain disulfides and three nonpaired cysteine residues per monomer were identified. Beside catalytic Cys234 in the active site, free-thiol Cys331 and Cys424 were characterized."@en . . . . "Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I)." . "P(GA522/00/1553), P(GP203/01/D008), P(IAA4055006), P(LN00A032), Z(AV0Z4055905)" . . "[CDFC5F155667]" . . . "RIV/61388963:_____/02:57020120" . . "0"^^ . . "0"^^ . "Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I)."@en . . "Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I)." . "Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I)."@en . "Horn, Martin" . . "cathepsin C; cysteine protease"@en . "5"^^ . "933;943" . . . "646574" . . "11" . "RIV/61388963:_____/02:57020120!RIV/2003/AV0/A57003/N" . "0961-8368" . . "N/A" . "Mare\u0161, Michael" .