کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6597304 | 1423853 | 2017 | 24 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry
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موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
مهندسی شیمی (عمومی)
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Fe-S clusters are cofactors that participate in diverse and essential biological processes. Mitochondria contain a complete machinery for Fe-S cluster assembly. Cysteine desulfurase (Nfs1) is required generation of a form of activated sulfur and is essential for the initial Fe-S cluster assembly step. Using mass-spectometry we identified proteins that were copurified with Nfs1 using a pull-down strategy, including a novel protein kinase. Furthermore, we were able to identify phosphorylation sites on the Nfs1 protein. These data and analyses support the research article “Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria” by Rocha et al. (in press) [1].
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Data in Brief - Volume 15, December 2017, Pages 775-799
Journal: Data in Brief - Volume 15, December 2017, Pages 775-799
نویسندگان
Agostinho G. Rocha, Simon A.B. Knight, Alok Pandey, Heeyong Yoon, Jayashree Pain, Debkumar Pain, Andrew Dancis,