Dissecting the role of protein phosphorylation: a chemical biology toolbox

T Bilbrough, E Piemontese, O Seitz - Chemical Society Reviews, 2022 - pubs.rsc.org
Protein phosphorylation is a crucial regulator of protein and cellular function, yet, despite
identifying an enormous number of phosphorylation sites, the role of most is still unclear …

Deubiquitinases: From mechanisms to their inhibition by small molecules

SM Lange, LA Armstrong, Y Kulathu - Molecular cell, 2022 - cell.com
Deubiquitinases (DUBs) are specialized proteases that remove ubiquitin from substrates or
cleave within ubiquitin chains to regulate ubiquitylation and therefore play important roles in …

Breaking the chains: deubiquitylating enzyme specificity begets function

MJ Clague, S Urbé, D Komander - Nature reviews Molecular cell …, 2019 - nature.com
The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases)
maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from …

Structure and function of the 26S proteasome

JAM Bard, EA Goodall, ER Greene… - Annual review of …, 2018 - annualreviews.org
As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …

Mechanisms of deubiquitinase specificity and regulation

TET Mevissen, D Komander - Annual review of biochemistry, 2017 - annualreviews.org
Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …

An overview of cancer treatment modalities

Z Abbas, S Rehman - Neoplasm, 2018 - books.google.com
Cancer is a global issue majorly affecting developing countries. According to a survey, 63%
of deaths due to cancer are reported from developing countries. There are different …

The ubiquitin code

D Komander, M Rape - Annual review of biochemistry, 2012 - annualreviews.org
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation,
controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a …

Targeting metalloenzymes for therapeutic intervention

AY Chen, RN Adamek, BL Dick, CV Credille… - Chemical …, 2018 - ACS Publications
Metalloenzymes are central to a wide range of essential biological activities, including
nucleic acid modification, protein degradation, and many others. The role of metalloenzymes …

Atypical ubiquitylation—the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages

Y Kulathu, D Komander - Nature reviews Molecular cell biology, 2012 - nature.com
Ubiquitylation is one of the most abundant and versatile post-translational modifications
(PTMs) in cells. Its versatility arises from the ability of ubiquitin to form eight structurally and …

Breaking the chains: structure and function of the deubiquitinases

D Komander, MJ Clague, S Urbé - Nature reviews Molecular cell …, 2009 - nature.com
Ubiquitylation is a reversible protein modification that is implicated in many cellular
functions. Recently, much progress has been made in the characterization of a superfamily …