Giulio Romano / Lorenzo Bonoldi

• Record Nr.: UNISA990001407330203316
• Autore: BONOLDI, Lorenzo
• Pubbl/distr/stampa: Milano : Skira, 2008
• ISBN: 978-88-6130-557-1
• Descrizione fisica: 95 p. : ill. ; 17 cm
• Collana: SkiraMiniARTbooks
• Disciplina: 759.5
• Soggetti: Giulio : Romano
• Collocazione: XII.2.B. 1526
• Lingua di pubblicazione: Italiano
• Formato: Materiale a stampa
• Livello bibliografico: Monografia

Foldases catalyzing the formation and isomerization of disulfide bonds in proteins / / Natalya K. Nagradova

• Record Nr.: UNINA9910964442303321
• Autore: Nagradova N. K (Natalia Konstantinovna)
• Pubbl/distr/stampa: New York, : Nova Biomedical Books, c2009
• ISBN: 1-60741-689-1
• Edizione: [1st ed.]
• Descrizione fisica: 1 online resource (85 p.)
• Disciplina: 572/.633
• Soggetti: Protein disulfide isomerase; Protein folding
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references (p. [61]-68) and index.
• Nota di contenuto: ""FOLDASES CATALYZING THE FORMATION AND ISOMERIZATION OF DISULFIDE BONDS IN PROTEINS""; ""Contents""; ""Preface ""; ; ""Introduction ""; ""Eukaryotic Protein Disulfide Isomerase (PDI)""; ""1.1. The Role of Protein Disulfide Isomerase in the Endoplasmic Reticulum""; ""1.2. Modular Organization of the PDI Molecule and the Role of Different Domains""; ""1.3. Functional Properties of PDI Active Centers. The pKa Values of Essential Cysteine Residues ""; ""1.4. Disulfide Isomerization: The Essential Function of PDI ""; ""1.5. Dithiol Oxidation Catalyzed by PDI ""; ""1.6. The Role of Glutathione in Oxidative Protein Folding in Endoplasmic Reticulum """"Disulfide Bond Formation and Isomerization in Prokaryotes ""; ""2.1. A Pathway for Disulfide Bond Formation in the Periplasm ""; ""2.2. Similarities in Prokaryotic and Eukaryotic Disulfide Bond-Forming Pathways ""; ""2.3. A Pathway for Disulfide Bond Isomerization in the Periplasm ""; ""Conclusion ""; ""References ""; ""Index ""
• Sommario/riassunto: One of the rate-limiting steps in the folding pathways of many secretory proteins is the formation of correct disulfide bonds between cysteine residues. In eukaryotes, both disulfide bond formation and isomerisation which shuffles incorrectly formed disulfides are catalysed by protein disulfide isomerase (PDI).