Protein Misfolding Diseases: Current and Emerging Principles by Marina Ramirez-Alvarado, Jeffery W. Kelly, Christopher M.

By Marina Ramirez-Alvarado, Jeffery W. Kelly, Christopher M. Dobson

An more and more getting older inhabitants will upload to the variety of members struggling with amyloid. Protein Misfolding illnesses presents a scientific review of the present and rising remedies for most of these protein misfolding ailments, together with Alzheimer's, Parkinson's, and Mad Cow. The ebook emphasizes therapeutics in an amyloid disorder context to assist scholars, college, medical researchers, and medical professionals operating with protein misfolding ailments bridge the distance among uncomplicated technology and pharmaceutical purposes to protein misfolding illness.

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Additional info for Protein Misfolding Diseases: Current and Emerging Principles and Therapies (Wiley Series in Protein and Peptide Science)

Sample text

All proteins that transit the secretory pathway in eukaryotic cells first enter the endoplasmic reticulum (ER), where they fold and assemble into multisubunit complexes prior to transit to the Golgi compartment [1]. Quality control is a surveillance mechanism that permits only properly folded proteins to exit the ER en route to other intracellular organelles and the cell surface. Misfolded proteins are either retained within the ER lumen in a complex with molecular chaperones or are directed toward degradation through the 26S proteasome in a process called ER-associated degradation (ERAD) or through autophagy.

PROTEIN FOLDING AND QUALITY CONTROL IN THE ER Protein folding and maturation in vivo is a highly assisted process. The ER lumen contains molecular chaperones, folding enzymes, and quality control UPR SIGNALING 23 factors that assist in folding and trafficking of newly synthesized polypeptides. Nascent polypeptide chains enter the ER lumen through a proteinaceous channel, the Sec 61 translocon complex. The nascent chains of most translocated polypeptides are subject to addition of a preassembled oligosaccharide core (N-acetylglucosamine2–mannose9–glucose3) (Glc3Man9GlcNac2) to selective asparagine (N) residues.

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