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Recent years have witnessed the identification of numerous inborn errors of metabolism that affect secretory or plasma membrane proteins. In many instances, mutations causing minor changes in protein primary structure lead to intracellular retention of the affected proteins, suggesting that proper conformation is critical for protein transport as well as protein function. Using a mouse model that is phenotypic ally indistinguishable from the human patients with congenital goitrous hypothyroidism.
Kim, Paul MD has done his MD from University of Virginia, 1985. Dr. Kim is an Associate Professor of Medicine in the Division of Endocrinology and Metabolism, with membership in the American Society for Cell Biology, Endocrine Society, and American Thyroid Association. Kim’s recent publications are Kim PS, Arvan PR, Endoplasmic Reticulum Storage Diseases Endocrine Disorders of Protein Trafficking, and Endocrine Reviews.
A single amino acid change in the acetyl cholinesterase like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog cog mouse: A model of human ER storage diseases. Kim PS, Ding M, Menon S, Jung CG, Cheng JM, Miyamoto T, Li B, Furudate S, Agui T.  A missense mutation G2320R in the thyroglobulin gene causes non goitrous congenital primary hypothyroidism in the WIC rdw rat.  Molec Endo 14: 1944 to 53, 2000.

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