[HTML][HTML] Regulation of translesion DNA synthesis: posttranslational modification of lysine residues in key proteins

J McIntyre, R Woodgate - DNA repair, 2015 - Elsevier
Posttranslational modification of proteins often controls various aspects of their cellular
function. Indeed, over the past decade or so, it has been discovered that posttranslational …

[HTML][HTML] Ubiquitin—omics reveals novel networks and associations with human disease

BM Kessler - Current opinion in chemical biology, 2013 - Elsevier
Human neurodegenerative and infectious diseases and tumorigenesis are associated with
alterations in ubiquitin pathways. Over 10% of the genome encode for genes that either bind …

The application of targeted mass spectrometry‐based strategies to the detection and localization of post‐translational modifications

N Chicooree, RD Unwin… - Mass spectrometry …, 2015 - Wiley Online Library
This review describes some of the more interesting and imaginative ways in which mass
spectrometry has been utilized to study a number of important post‐translational …

SUMO proteomics to decipher the SUMO‐modified proteome regulated by various diseases

W Yang, W Paschen - Proteomics, 2015 - Wiley Online Library
Small ubiquitin‐like modifier (SUMO1–3) conjugation is a posttranslational protein
modification whereby SUMOs are conjugated to lysine residues of target proteins. SUMO …

Proteomics strategies to identify SUMO targets and acceptor sites: a survey of RNA-binding proteins SUMOylation

G Filosa, SML Barabino, A Bachi - Neuromolecular medicine, 2013 - Springer
SUMOylation is a protein posttranslational modification that participates in the regulation of
numerous biological processes within the cells. Small ubiquitin-like modifier (SUMO) …

Mass spectral enhanced detection of Ubls using SWATH acquisition: MEDUSA—simultaneous quantification of SUMO and ubiquitin-derived isopeptides

JR Griffiths, N Chicooree, Y Connolly… - Journal of The …, 2014 - ACS Publications
Protein modification by ubiquitination and SUMOylation occur throughout the cell and are
responsible for numerous cellular functions such as apoptosis, DNA replication and repair …

The strategies for identification and quantification of SUMOylation

Y Zhang, Y Li, B Tang, C Zhang - Chemical Communications, 2017 - pubs.rsc.org
SUMOylation is a post-translational modification that plays critical roles in a multitude of
cellular processes including transcription, cellular localization, DNA repair and cell cycle …

A chemical and enzymatic approach to study site-specific sumoylation

CP Albuquerque, E Yeung, S Ma, T Fu, KD Corbett… - PLoS …, 2015 - journals.plos.org
A variety of cellular pathways are regulated by protein modifications with ubiquitin-family
proteins. SUMO, the S mall U biquitin-like MO difier, is covalently attached to lysine on target …

The S. pombe Translation Initiation Factor eIF4G Is Sumoylated and Associates with the SUMO Protease Ulp2

J Jongjitwimol, M Feng, L Zhou, O Wilkinson, L Small… - PLoS …, 2014 - journals.plos.org
SUMO is a small post-translational modifier, that is attached to lysine residues in target
proteins. It acts by altering protein-protein interactions, protein localisation and protein …

Preparing to read the ubiquitin code: a middle‐out strategy for characterization of all lysine‐linked diubiquitins

AE Lee, CA Castañeda, Y Wang… - Journal of Mass …, 2014 - Wiley Online Library
Multiple studies demonstrate that ubiquitination of proteins codes for regulation of cell
differentiation, apoptosis, endocytosis and many other cellular functions. There is great …