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200 00$aWereld en Zending
210   $a[Amsterdam]$c[publisher not identified]$d1972-
215   $a1 online resource
300   $a"Tijdschrift voor opbouw van de missionaire gemeente," (varies).
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200 10$aFoldases catalyzing the formation and isomerization of disulfide bonds in proteins /$fNatalya K. Nagradova
205   $a1st ed.
210   $aNew York $cNova Biomedical Books$dc2009
215   $a1 online resource (85 p.)
300   $aDescription based upon print version of record.
311 08$a1-60692-466-4 
320   $aIncludes bibliographical references (p. [61]-68) and index.
327   $a""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 ""
327   $a""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 ""
330   $aOne 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).
606   $aProtein disulfide isomerase
606   $aProtein folding
615  0$aProtein disulfide isomerase.
615  0$aProtein folding.
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