کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10870701 | 1074018 | 2014 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Gap junction regulation by calmodulin
ترجمه فارسی عنوان
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موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
چکیده انگلیسی
Intracellular Ca2+ activated calmodulin (CaM) inhibits gap junction channels in the low nanomolar to high micromolar range of [Ca2+]i. This regulation plays an essential role in numerous cellular processes that include hearing, lens transparency, and synchronized contractions of the heart. Previous studies have indicated that gap junction mediated cell-to-cell communication was inhibited by CaM antagonists. More recent evidence indicates a direct role of CaM in regulating several members of the connexin family. Since the intracellular loop and carboxyl termini of connexins are largely “invisible” in electron microscopy and X-ray crystallographic structures due to disorder in these domains, peptide models encompassing the putative CaM binding sites of several intracellular domains of connexins have been used to identify the Ca2+-dependent CaM binding sites of these proteins. This approach has been used to determine the CaM binding affinities of peptides derived from a number of different connexin-subfamilies.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 588, Issue 8, 17 April 2014, Pages 1430-1438
Journal: FEBS Letters - Volume 588, Issue 8, 17 April 2014, Pages 1430-1438
نویسندگان
Juan Zou, Mani Salarian, Yanyi Chen, Richard Veenstra, Charles F. Louis, Jenny J. Yang,