Ubiquitin-like protein conjugation: structures, chemistry, and mechanism
L Cappadocia, CD Lima - Chemical reviews, 2018 - ACS Publications
Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …
Protein analysis by shotgun/bottom-up proteomics
According to Genome Sequencing Project statistics (http://www. ncbi. nlm. nih.
gov/genomes/static/gpstat. html), as of February 16, 2012, complete gene sequences have …
gov/genomes/static/gpstat. html), as of February 16, 2012, complete gene sequences have …
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 …
[HTML][HTML] Systematic and quantitative assessment of the ubiquitin-modified proteome
Despite the diverse biological pathways known to be regulated by ubiquitylation, global
identification of substrates that are targeted for ubiquitylation has remained a challenge. To …
identification of substrates that are targeted for ubiquitylation has remained a challenge. To …
Affinity‐purification coupled to mass spectrometry: Basic principles and strategies
WH Dunham, M Mullin, AC Gingras - Proteomics, 2012 - Wiley Online Library
Identifying the interactions established by a protein of interest can be a critical step in
understanding its function. This is especially true when an unknown protein of interest is …
understanding its function. This is especially true when an unknown protein of interest is …
[HTML][HTML] Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation
DM Duda, LA Borg, DC Scott, HW Hunt, M Hammel… - Cell, 2008 - cell.com
Cullin-RING ligases (CRLs) comprise the largest ubiquitin E3 subclass, in which a central
cullin subunit links a substrate-binding adaptor with an E2-binding RING. Covalent …
cullin subunit links a substrate-binding adaptor with an E2-binding RING. Covalent …
RBR E3 ubiquitin ligases: new structures, new insights, new questions
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double
RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain …
RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain …
Ubiquitin-like proteins
AG van der Veen, HL Ploegh - Annual review of biochemistry, 2012 - annualreviews.org
The eukaryotic ubiquitin family encompasses nearly 20 proteins that are involved in the
posttranslational modification of various macromolecules. The ubiquitin-like proteins (UBLs) …
posttranslational modification of various macromolecules. The ubiquitin-like proteins (UBLs) …
Targeting Cullin–RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation
In the last decade, the ubiquitin–proteasome system has emerged as a valid target for the
development of novel therapeutics. E3 ubiquitin ligases are particularly attractive targets …
development of novel therapeutics. E3 ubiquitin ligases are particularly attractive targets …
Function and regulation of protein neddylation
G Rabut, M Peter - EMBO reports, 2008 - embopress.org
Neddylation is the post‐translational protein modification that is most closely related to
ubiquitination. However, ubiquitination is known to regulate a myriad of processes in …
ubiquitination. However, ubiquitination is known to regulate a myriad of processes in …