Zinc-Binding B-Box Domains with RING Folds Serve Critical Roles in the Protein Ubiquitination Pathways in Plants and Animals-Reference-Cited by-同舟云学术

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Zinc-Binding B-Box Domains with RING Folds Serve Critical Roles in the Protein Ubiquitination Pathways in Plants and Animals

Published:2019-06-19 Issue: Volume: Page:
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Container-title:Ubiquitin Proteasome System - Current Insights into Mechanism Cellular Regulation and Disease
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Author:

Anthony Massiah Michael

Publisher

IntechOpen

Link

http://www.intechopen.com/download/pdf/66768

Reference144 articles.

1. Klug A. The discovery of zinc fingers and their development for practical applications in gene regulation and genome manipulation. Quarterly Reviews of Biophysics. 2010;43:1-21

2. Massiah MA, Blake PR, Summers MF. Nucleic Acid Interactive Protein Domains that Require Zinc. New York, NY: Oxford University Press; 1998

3. Berg JM. Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules. The Journal of Biological Chemistry. 1990;265:6513-6516

4. Wright KM, Wu K, Babatunde O, Du H, Massiah MA. XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding. PLoS One. 2014;9:e107537

5. Zhao Y, Zeng C, Massiah MA. Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain. PLoS One. 2015;10:e0124377

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