Protein neddylation: beyond cullin–RING ligases
RI Enchev, BA Schulman, M Peter - Nature reviews Molecular cell …, 2015 - nature.com
NEDD8 (neural precursor cell expressed developmentally downregulated protein 8) is a
ubiquitin-like protein that activates the largest ubiquitin E3 ligase family, the cullin–RING …
ubiquitin-like protein that activates the largest ubiquitin E3 ligase family, the cullin–RING …
Function and regulation of SUMO proteases
CM Hickey, NR Wilson, M Hochstrasser - Nature reviews Molecular cell …, 2012 - nature.com
Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins is highly dynamic,
and both SUMO–protein conjugation and cleavage can be regulated. Protein desumoylation …
and both SUMO–protein conjugation and cleavage can be regulated. Protein desumoylation …
Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
FE Reyes-Turcu, KH Ventii… - Annual review of …, 2009 - annualreviews.org
Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene
products, reverse the modification of proteins by a single ubiquitin (-like) protein, and …
products, reverse the modification of proteins by a single ubiquitin (-like) protein, and …
Protein posttranslational modifications: the chemistry of proteome diversifications
CT Walsh, S Garneau‐Tsodikova… - Angewandte Chemie …, 2005 - Wiley Online Library
The diversity of distinct covalent forms of proteins (the proteome) greatly exceeds the
number of proteins predicted by DNA coding capacities owing to directed posttranslational …
number of proteins predicted by DNA coding capacities owing to directed posttranslational …
A genomic and functional inventory of deubiquitinating enzymes
SMB Nijman, MPA Luna-Vargas, A Velds… - Cell, 2005 - cell.com
Posttranslational modification of proteins by the small molecule ubiquitin is a key regulatory
event, and the enzymes catalyzing these modifications have been the focus of many studies …
event, and the enzymes catalyzing these modifications have been the focus of many studies …
SUMO: a history of modification
RT Hay - Molecular cell, 2005 - cell.com
The small ubiquitin-like modifier (SUMO) is covalently linked to a variety of proteins and is
deconjugated by SUMO-specific proteases. A characteristic of SUMO modification is that the …
deconjugated by SUMO-specific proteases. A characteristic of SUMO modification is that the …
Protein modification by SUMO
ES Johnson - Annual review of biochemistry, 2004 - annualreviews.org
▪ Abstract Small ubiquitin-related modifier (SUMO) family proteins function by becoming
covalently attached to other proteins as post-translational modifications. SUMO modifies …
covalently attached to other proteins as post-translational modifications. SUMO modifies …
[HTML][HTML] Mechanism and function of deubiquitinating enzymes
AY Amerik, M Hochstrasser - … et Biophysica Acta (BBA)-Molecular Cell …, 2004 - Elsevier
Attachment of ubiquitin to proteins is a crucial step in many cellular regulatory mechanisms
and contributes to numerous biological processes, including embryonic development, the …
and contributes to numerous biological processes, including embryonic development, the …
On terminal alkynes that can react with active-site cysteine nucleophiles in proteases
Active-site directed probes are powerful in studies of enzymatic function. We report an active-
site directed probe based on a warhead so far considered unreactive. By replacing the C …
site directed probe based on a warhead so far considered unreactive. By replacing the C …
Modification in reverse: the SUMO proteases
D Mukhopadhyay, M Dasso - Trends in biochemical sciences, 2007 - cell.com
SUMOs (small ubiquitin-like modifiers) are ubiquitin-related proteins that become covalently
conjugated to cellular target proteins that are involved in a variety of processes. Frequently …
conjugated to cellular target proteins that are involved in a variety of processes. Frequently …