Protein Misfolding and Misprocessing in Complex Disease

A. Fadiel; K. D. Eichenbaum; A. Hamza; O. Tuncalp; J. Luk; F. Naftolin

doi:10.2174/0929866054395743

ISSN: 0929-8665
E-ISSN: 1875-5305

Protein Misfolding and Misprocessing in Complex Disease
Authors: A. Fadiel¹, K. D. Eichenbaum², A. Hamza³, O. Tuncalp⁴, J. Luk⁵ and F. Naftolin⁶
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¹ Yale University, School of Medicine, New Haven, CT., 06520. ² Yale University, School of Medicine, New Haven, CT., 06520. ³ Yale University, School of Medicine, New Haven, CT., 06520. ⁴ Yale University, School of Medicine, New Haven, CT., 06520. ⁵ Yale University, School of Medicine, New Haven, CT., 06520. ⁶ Yale University, School of Medicine, New Haven, CT., 06520.
Source: Protein and Peptide Letters, Volume 12, Issue 6, Aug 2005, p. 499 - 506
DOI: https://doi.org/10.2174/0929866054395743
- Available online: 01 Aug 2005

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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2005-08-01

2025-09-02

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Article Type: Review Article

Keyword(s): chaperones; endoplasmic reticulum; er-associated degradation (erad); retrograde transport; ubiquitinproteasome system; unfolded protein response (upr)

Protein Misfolding and Misprocessing in Complex Disease

Abstract

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