By Philippe Taupin

ISBN-10: 160456010X

ISBN-13: 9781604560107

ISBN-10: 1606927485

ISBN-13: 9781606927489

This publication goals at providing an summary of the present wisdom of cystatins and molecles of the cystatin superfamily, their constitution, physio-and pathological functionality in addition to the course that examine is at the moment aiming for in constructing healing remedies in line with cysteine proteinases and similar molecules. Its objective is to offer the reader a device that serves as a reference within the box of protease inhibitor, their physio-and pathological capabilities and healing strength. It additionally goals at making obtainable to a broader viewers, that doesn't have quick access to clinical courses, a resource of information and data. To acheive this aim, the publication goals at masking largely, systematically, concisely, and extensive, the multifacets of the function of cystatins and molecules of the cystatin superfamily in physiopathology, and emphasize on their healing potentials. Figures, self-explantory schemas and diagrams give a contribution to clarifying and help the knowledge provided.

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Extra info for The Cystatin Superfamily of Proteinase Inhibitors

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1973) Some properties of a ficin-papain inhibitor from avian egg white. Arch Biochem Biophys. 158, 623-32. Anastasi A, Brown MA, Kembhavi AA, Nicklin MJ, Sayers CA, Sunter DC, Barrett AJ. (1983) Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. Biochem J. 211, 12938. Turk V, Brzin J, Longer M, Ritonja A, Eropkin M, Borchart U, Machleidt W. (1983) Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white.

Three-dimensional domain swapping is a process for forming dimeric, oligomeric and multimeric proteins. In three-dimensional domain swapping, one domain, a flexible domain, of a multi-domain molecule takes the place of the same domain in another similar molecule. In turn, the flexible domain from the latter molecule takes the same place in another molecule, leading to the formation of multimeric proteins. Multimeric proteins can be either closedended (a) or open-ended (b). One of the requirements for three-dimensional domain swapping is the existence of a flexible domain, capable of unfolding and taking the same place in another similar molecule.

J Biol Chem. 262, 9688-94. Arai S, Watanabe H, Kondo H, Emori Y, Abe K. (1991) Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-ValVal-Ala-Gly region conserved among cystatin superfamily members. J Biochem (Tokyo). 109, 294-8. Saitoh E, Isemura S, Sanada K, Ohnishi K. (1991) Cystatins of family II are harboring two domains which retain inhibitory activities against the proteinases. Biochem Biophys Res Commun. 175, 1070-5. Hall A, Dalboge H, Grubb A, Abrahamson M.

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The Cystatin Superfamily of Proteinase Inhibitors by Philippe Taupin


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