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Review Article
Mechanisms of Disease
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Volume 339:1688-1695 December 3, 1998 Number 23
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Folding of Secretory and Membrane Proteins
Galina Kuznetsov, Ph.D., and Sanjay K. Nigam, M.D.

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Genetic errors may result in abnormal synthesis of proteins, abnormal folding and processing of proteins after they are synthesized, or changes in the functional properties of proteins. Although the synthesis of proteins begins in the cytoplasm, many are destined to be expressed on the cell surface (e.g., surface-recognition molecules, ion channels, receptors, and adhesion molecules) or secreted (e.g., hormones, growth factors, extracellular matrix proteins, and proteolytic enzymes). Newly synthesized membrane and secretory proteins are transported into the endoplasmic reticulum, the internal membranous network of the cell, in a largely unfolded state. When they leave the endoplasmic reticulum to move through . . . [Full Text of this Article]

Molecular Chaperones in the Endoplasmic Reticulum

Synthesis of Molecular Chaperones

The Role of Chaperones in the Maturation of Newly Synthesized Proteins

The Fate of Misfolded Proteins

Ischemia as an Example of Stress That Causes Abnormal Protein Folding

Inherited Alterations in Protein Folding and Assembly

Cystic Fibrosis

Alpha1-Antitrypsin Deficiency

Conclusions


Source Information

From the Renal Division, Department of Medicine, Brigham and Women's Hospital, and Harvard Medical School, Boston (G.K., S.K.N.); and the Eisai Research Institute, Andover, Mass. (G.K.).

Address reprint requests to Dr. Nigam at the Harvard Institutes of Medicine, 77 Ave. Louis Pasteur, Boston, MA 02115.

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