کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1257541 | 971567 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expanding the functional diversity of proteins through cysteine oxidation
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی (عمومی)
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چکیده انگلیسی
The polarizable sulfur atom in cysteine is subject to numerous post-translational oxidative modifications in the cellular milieu, which regulates a wide variety of biological phenomena such as catalysis, metal binding, protein turnover, and signal transduction. The application of chemical rationale to describe the features of different cysteine oxoforms affords a unique perspective on this rapidly expanding field. Moreover, a chemical framework broadens our understanding of the functional roles that specific cysteine oxidation states can play and facilitates the development of mechanistic proposals, which can be tested in both biochemical and cellular studies.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Chemical Biology - Volume 12, Issue 6, December 2008, Pages 746–754
Journal: Current Opinion in Chemical Biology - Volume 12, Issue 6, December 2008, Pages 746–754
نویسندگان
Khalilah G Reddie, Kate S Carroll,