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Protein Misfolding and Misprocessing in Complex Disease

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

Document Type: Review Article

Affiliations: Yale University, School of Medicine, New Haven, CT., 06520.

Publication date: 2005-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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