The isolated N terminus of Ring1B is a well-folded, monomeric fragment with native-like structure-Reference-Cited by-同舟云学术

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The isolated N terminus of Ring1B is a well-folded, monomeric fragment with native-like structure

Published:2013-11-26 Issue:1 Volume:27 Page:1-11
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Martinez-Gomez A. I.,Villegas S.,Aguado-Llera D.,Bacarizo J.,Camara-Artigas A.,Vidal M.,Neira J. L.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/27/1/1/4657705/gzt056.pdf

Reference34 articles.

1. Non-canonical residues of the marginally stable monomeric ubiquitin conjugase from goldfish are involved in binding to the C terminus of Ring 1B

2. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex

3. Ring1B Contains a Ubiquitin-Like Docking Module for Interaction with Cbx Proteins,

4. RING domains: master builders of molecular scaffolds?

5. Polycomb group proteins: navigators of lineage pathways led astray in cancer

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Citrullinating enzyme PADI4 and transcriptional repressor RING1B bind in cancer cells;International Journal of Biological Macromolecules;2024-08

2. The chondroitin sulfate/dermatan sulfate 4-O-endosulfatase from marine bacterium Vibrio sp FC509 is a dimeric species: Biophysical characterization of an endosulfatase;Biochimie;2016-12

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