The cholinesterase-like domain of thyroglobulin functions as an intramolecular chaperone

Journal of Clinical Investigation

Volumn 118, Issue 8, 2008, Pages 2950-2958

  Lee, Jaemin ^a   Di Jeso, Bruno ^b   Arvan, Peter ^a,c  

^a UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

^b UNIVERSITY OF SALENTO   (Italy)

^c UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHOLINESTERASE; PEPTIDE; THYROGLOBULIN;

ARTICLE; CELL TRANSPORT; CONTROLLED STUDY; HUMAN; HUMAN CELL; MUTATION; OXIDATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN SECRETION;

CELL LINE; CHOLINESTERASES; ENDOPLASMIC RETICULUM; HUMANS; KIDNEY; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDATION-REDUCTION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THYROGLOBULIN; TRANSFECTION;

EID: 48749132842     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI35164     Document Type: Article

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