By Jiri Blazek

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Extra resources for Computational Fluid Dynamics: Principles and Applications (Referex Engineering)

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This complex multidomain assembly is thought to be responsible for the limited folding efficiency of wt CFTR. CFTR appears to have a significantly higher folding efficiency (60–100%) in epithelia, expressing the channel endogenously [10, 12]. The initial steps of biosynthetic processing, including the recognition, tagging and selective degradation of nonnative conformers of the wt and mutant CFTR, overlap at the ER and are summarized below. Reconstitution of CFTR biogenesis using in vitro transcription-translation assays and truncated molecules revealed that the transmembrane segments are cotranslationally inserted into the ER and undergo N-linked glycosylation [13, 14].

The nonclassical processing 23 route involves the direct vesicular transfer of CFTR between the ER and trans-Golgi network/endosomal compartments followed by syntaxin 13-dependent recycling through the Golgi compartment and is, therefore, insensitive to dominant negative Arf1, Rab1a/Rab2 and syntaxin 5 [44]. The nonclassical biosynthetic route is consistent with the negligible accumulation of CFTR in the Golgi compartment of BHK and CHO cells [44], while its presence in polarized epithelia remains to be established.

J Biol Chem 1999;274:2616–2624. Sheppard DN, Ostedgaard LS, Rich DP, Welsh MJ: The amino terminal portion of CFTR forms a regulated chloride channel. Cell 1994; 76:1091–1098. Chan KW, Csanady L, Nairn AC, Gadsby DC: Deletion analysis of CFTR channel R domain using severed molecules. Biophys J 1999;76: A405. 17 Akabas MH: Cystic fibrosis transmembrane conductance regulator: Structure and function of an epithelial chloride channel. J Biol Chem 2000;275:3729–3732. 18 Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM: The Hdj-2/Hsc 70 chaperone pair facilitates early steps in CFTR biogenesis.

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Computational Fluid Dynamics: Principles and Applications by Jiri Blazek
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