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Ubiquitin modifications [PDF]

open access: yesCell Research, 2016
Protein ubiquitination is a dynamic multifaceted post-translational modification involved in nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid protein ubiquitin is subjected to further modifications, creating a multitude of distinct signals with distinct cellular outcomes, referred to as the 'ubiquitin code ...
David Komander
exaly   +3 more sources
Some of the next articles are maybe not open access.

NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly

Nature, 2020
Spencer Hill   +2 more
exaly  

The unravelling of the ubiquitin system

Nature Reviews Molecular Cell Biology, 2015
Aaron Ciechanover
exaly  

The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy

Trends in Biochemical Sciences, 2017
Aaron Ciechanover, Yong Tae Kwon
exaly  

SCF ubiquitin ligase-targeted therapies

Nature Reviews Drug Discovery, 2014
Julia Pagan   +2 more
exaly  

Principles of Ubiquitin-Dependent Signaling

Annual Review of Cell and Developmental Biology, 2018
Eugene Oh, Michael Rape
exaly  

Perilous journey: a tour of the ubiquitin–proteasome system

Trends in Cell Biology, 2014
Thibault Mayor, Gary Kleiger
exaly  

Ubiquitin and its kin: how close are the family ties?

Trends in Cell Biology, 2000
Stefan Jentsch
exaly  

Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules

Acta Crystallographica Section D: Biological Crystallography, 2014
Hermann Schindelin
exaly  

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