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.
Keywords: endoplasmic reticulum, retrograde transport, ubiquitinproteasome system, er-associated degradation (erad), unfolded protein response (upr), chaperones
Protein & Peptide Letters
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.
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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 |
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