Protein Misfolding and Misprocessing in Complex Disease

Title: Protein Misfolding and Misprocessing in Complex Disease

Volume: 12 Issue: 6

Author(s): A. Fadiel, K. D. Eichenbaum, A. Hamza, O. Tuncalp, J. Luk and F. Naftolin

Affiliation:

Keywords: endoplasmic reticulum, retrograde transport, ubiquitinproteasome system, er-associated degradation (erad), unfolded protein response (upr), chaperones

Abstract: Scientists from over 20 major research centers recently convened to discuss advances and new discoveries in “Protein MisFolding and MisProcessing in Disease.” Understanding protein mechanisms the underlying etiology of complex diseases lies in analyzing the associated biochemical mechanisms, which include folding patterns, processing patterns, chaperone regulators, stress pathways, and signal transduction.

Cite this article as:

Fadiel A., Eichenbaum D. K., Hamza A., Tuncalp O., Luk J. and Naftolin F., Protein Misfolding and Misprocessing in Complex Disease, Protein & Peptide Letters 2005; 12 (6) . https://dx.doi.org/10.2174/0929866054395743

DOI https://dx.doi.org/10.2174/0929866054395743	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305