Download Calreticulin: Second Edition by Paul Eggleton, Marek Michalak (auth.), Paul Eggleton Ph.D., PDF

By Paul Eggleton, Marek Michalak (auth.), Paul Eggleton Ph.D., Marek Michalak Ph.D. (eds.)

The publication makes a speciality of the most recent discoveries on calreticulin, calnexin and different endoplasmic reticulum proteins. Calreticulin has been implicated to impact different mobile functionality and play a task in lots of pathologies together with protein folding issues, cardiac pathologies, melanoma and autoimmunity. This e-book comprises contributions from the area leaders within the zone of endoplasmic reticulum functionality, protein folding, Calcium homeostasis and autoimmunity. It increases many interesting questions on calreticulin, calnexin and the endoplasmic reticulum and provides a distinct chance to gain the importance of those calcium-binding chaperones. The booklet is exclusive in each appreciate and we aren't conscious of the other book concentrating on those features of endoplasmic reticulum biology. as a result of a valuable position of endoplasmic reticulum, calreticulin and calnexin in almost all mobile features, the booklet may be of curiosity to every body within the organic sciences.

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J Cell Sci 1995; 109:271-6. 43. Schrag JD, Bergeron JJ, Li Y er aI. T he Srrucrure of calnexin, an ER chaperone involved in qualiry comrol of prot ein folding . Mol Cell 200 1; 8:633-44 . CHAPTER 3 AChaperone System for Glycoprotein Folding: The Calnexin/Calreticulin Cycle Lars Ellgaard and Ari Helenius Abstract T he endo plasmic ret iculum (ER) conta ins a particul arly wide range of mol ecular cha pero nes and other protein s th at assist the folding and qu ality cont rol of newly synthesized prot ein.

Different sorting of Lys-Asp-Glu-Leu proteins in rat liver. J Bioi Chern 1992; 267:10631 -7. 22. Johnson SJ. Characterization of the Structure and Pathophysiological Roles of Human Calreticulin . D. Phil. The sis 2001. 23. Hojrup P, Roepsrorff 1', Houen G . Human placental calreticulin characterization of domain structure and post-translational modifications . Eur J Biochem 2001 ; 268:2558-65. 24. Houen G, Koch C. Human placental calreticulin: purification, characterization and association with other proreins.

27• 8 The features by which GT senses the folding status of its substrates have been srudied in vitro using isolated GT. f" If the protein to which the glycan is bound is folded to its native conformation, the glycan is not reglucosylated. If it is in a random coil conformation, the glycan also fails to be reglucosylared indicating that GT preferentially recognizes parrially folded polypeptides. 3o•31 This is in agreement with in vivo experiments demonstrating that GT reglucosylates glycoproteins in late stages offolding.

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