Structure of the yeast Bre1 RING domain-Reference-Cited by-同舟云学术

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Structure of the yeast Bre1 RING domain

Published:2015-04-29 Issue:6 Volume:83 Page:1185-1190
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Kumar Pankaj¹,Wolberger Cynthia¹

Affiliation:

1. Department of Biophysics and Biophysical ChemistryJohns Hopkins University School of Medicine725 North Wolfe StreetBaltimore Maryland21205

Funder

National Institute of General Medical Sciences

National Cancer Institute

Advanced Photon Source

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24812

Reference33 articles.

1. Building ubiquitin chains: E2 enzymes at work

2. New insights into ubiquitin E3 ligase mechanism

3. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

4. BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer

5. Structure of a RING E3 Trapped in Action Reveals Ligation Mechanism for the Ubiquitin-like Protein NEDD8

Cited by 22 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. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure;Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms;2024-06

2. In Silico Analysis of Protein–Protein Interactions of Putative Endoplasmic Reticulum Metallopeptidase 1 in Schizosaccharomyces pombe;Current Issues in Molecular Biology;2024-05-12

3. Structure of the human Bre1 complex bound to the nucleosome;Nature Communications;2024-03-22

4. Structural basis for the role of C-terminus acidic tail of Saccharomyces cerevisiae ubiquitin-conjugating enzyme (Rad6) in E3 ligase (Bre1) mediated recognition of histones;International Journal of Biological Macromolecules;2024-01

5. Mechanism of histone H2B monoubiquitination by Bre1;Nature Structural & Molecular Biology;2023-10-23

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