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