Results 31 to 40 of about 39,918 (341)
Structural Diversity of Ubiquitin E3 Ligase
Molecules, 2021 The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes ...
Sachiko Toma-Fukai, Toshiyuki Shimizu
doaj +1 more source
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
core +2 more sources
Cell Reports, 2019 Summary: Ubiquitin and ubiquitin-like chains are finely balanced by conjugating and de-conjugating enzymes. Alterations in this balance trigger the response to stress conditions and are often observed in pathologies.
Aymeric P. Bailly +8 more
doaj +1 more source
Regulation of alphaherpesvirus infections by the ICP0 family of proteins [PDF]
, 2013 Immediate-early protein ICP0 of herpes simplex virus type 1 (HSV-1) is important for the regulation of lytic and latent viral infection. Like the related proteins expressed by other alphaherpesviruses, ICP0 has a zinc-stabilized RING finger domain that ...
Boutell, Chris, Everett, Roger
core +1 more source
The HIP2~ubiquitin conjugate forms a non-compact monomeric thioester during di-ubiquitin synthesis. [PDF]
PLoS ONE, 2015 Polyubiquitination is a post-translational event used to control the degradation of damaged or unwanted proteins by modifying the target protein with a chain of ubiquitin molecules.
Benjamin W Cook +3 more
doaj +1 more source
Pleiotropic Roles of a KEAP1-Associated Deubiquitinase, OTUD1
Antioxidants, 2023 Protein ubiquitination, which is catalyzed by ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin ligases, is a crucial post-translational modification to regulate numerous cellular functions in a spatio–temporal-specific manner ...
Daisuke Oikawa +2 more
doaj +1 more source
TULIP2: An Improved Method for the Identification of Ubiquitin E3-Specific Targets
Frontiers in Chemistry, 2019 Protein modification by Ubiquitin or Ubiquitin-like modifiers is mediated by an enzyme cascade composed of E1, E2, and E3 enzymes. E1s, or ubiquitin-activating enzymes, perform ubiquitin activation. Next, ubiquitin is transferred to ubiquitin-conjugating
Daniel Salas-Lloret +2 more
doaj +1 more source
The MALDI TOF E2/E3 ligase assay as universal tool for drug discovery in the ubiquitin pathway [PDF]
, 2017 In many diseases, components of the ubiquitin system - such as E2/E3 ligases and deubiquitylases - are dysregulated. The ubiquitin system has therefore become an emergent target for the treatment of a number of diseases, including cancer ...
Barlow, Victoria +5 more
core +5 more sources
UBE2G1 governs the destruction of cereblon neomorphic substrates
eLife, 2018 The cereblon modulating agents (CMs) including lenalidomide, pomalidomide and CC-220 repurpose the Cul4-RBX1-DDB1-CRBN (CRL4CRBN) E3 ubiquitin ligase complex to induce the degradation of specific neomorphic substrates via polyubiquitination in ...
Gang Lu +17 more
doaj +1 more source
Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation [PDF]
, 2018 The E3 ligase parkin ubiquitinates outer mitochondrial membrane proteins during oxidative stress and is linked to early-onset Parkinson’s disease. Parkin is autoinhibited but is activated by the kinase PINK1 that phosphorylates ubiquitin leading to ...
Aguirre, Jacob D. +9 more
core +1 more source