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pro vyhledávání: '"Liliane Vinet"'
Autor:
Liliane Vinet, Frédéric Delom, Nathalie Baudry, Pierre Carayon, Pierre-Jean Lejeune, Bernard Mallet
Publikováno v:
Biochemical and Biophysical Research Communications. 242:292-296
Thyroglobulin (Tg), the prothyroid hormone, is stored in the lumen of the thyroid follicles as soluble dimers and tetramers and insoluble multimers. Soluble Tg is well characterized with regards to structure and role, but insoluble Tg (i-Tg) is not.
Publikováno v:
Biochemical and biophysical research communications. 255(2)
Reactive oxygen species (ROS) are involved in many pathological processes through modifications of structure and activity of proteins. ROS also participate in physiological pathways such as thyroid hormone biosynthesis, which proceeds through oxidati
Publikováno v:
Molecular and cellular endocrinology. 81(1-3)
The 22 kDa fragment (Asn1—Met171) purified from iodine-poor human thyroglobulin (hTg) is capable by itself to synthesize thyroxine at Tyr5, the preferential hormonogenic acceptor site of the protein, after iodination in vitro. To identify the corre
Publikováno v:
FEBS Letters. 242:414-418
At moderate iodination levels (20 iodine atoms/mol) human thyroglobulin (hTg) produces after reduction a hormone-rich peptide of 26 kDa which contains the preferential hormonogenic ‘acceptor’ tyrosine (Tyr 5) of the protein. The site of cleavage
Autor:
Pierre Carayon, Liliane Vinet, Nathalie Baudry, Bernard Mallet, Pierre-Jean Lejeune, Patricia Niccoli
Publikováno v:
FEBS Letters. (2-3):223-226
Formation of dityrosine bridges is a ubiquitous process mainly attributed to oxidative stress leading to protein degradation and cellular damages. Here we show that dityrosine formation is involved in a physiological process, thyroid hormone synthesi