Results 21 to 30 of about 230,401 (303)
Self‐regulating ubiquitin ligases [PDF]
The EMBO Journal, 2017 Occasional auto‐modification of ubiquitin ligases typically leads to their proteasomal destruction, but new findings published in The EMBO Journal now show that in the case of Rsp5/Nedd4, auto‐ubiquitylation instead triggers oligomerization and concomitant reduction of ligase activity.
Spencer Hill, Gary Kleiger
openaire +2 more sources
The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]
, 2013 Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
core +1 more source
PLoS Genetics, 2023 The tumor suppressor BRCA1-BARD1 complex regulates many cellular processes; of critical importance to its tumor suppressor function is its role in genome integrity.
Qianyan Li +4 more
doaj +1 more source
The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover. [PDF]
PLoS ONE, 2012 The HIV1 protein Vpr assembles with and acts through an ubiquitin ligase complex that includes DDB1 and cullin 4 (CRL4) to cause G2 cell cycle arrest and to promote degradation of both uracil DNA glycosylase 2 (UNG2) and single-strand selective mono ...
Xiaoyun Wen +4 more
doaj +1 more source
Dysregulation of ubiquitin ligases in cancer [PDF]
Drug Resistance Updates, 2015 Ubiquitin ligases (UBLs) are critical components of the ubiquitin proteasome system (UPS), which governs fundamental processes regulating normal cellular homeostasis, metabolism, and cell cycle in response to external stress signals and DNA damage. Among multiple steps of the UPS system required to regulate protein ubiquitination and stability, UBLs ...
Jianfei, Qi, Ze'ev A, Ronai
openaire +2 more sources
Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4 [PDF]
, 2014 The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response.
Simpson, P +15 more
core +1 more source
Cell, 2016 Ubiquitination is a post-translational modification of proteins involved in a variety of cellular processes. Ubiquitination requires the sequential action of three enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases).
Morreale, Francesca Ester, Walden, Helen
openaire +2 more sources
Tag Team Ubiquitin Ligases [PDF]
Cell, 2016 Cullin-RING (CRL) and RING1-IBR-RING2 (RBR) are two distinct types of ubiquitin ligases. In this issue, Scott et al. show that CRLs activate the RBR enzyme ARIH1 to initiate ubiquitin chains on CRL substrates, thereby marking an unexpected and important advance in our understanding of both enzymes.
Kleiger, Gary, Deshaies, Raymond
openaire +3 more sources
A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence [PDF]
, 2011 Intrinsic antiviral resistance represents the first line of intracellular defence against virus infection. During herpes simplex virus type-1 (HSV-1) infection this response can lead to the repression of viral gene expression but is counteracted by the ...
Delphine Cuchet-Lourenço +21 more
core +1 more source
A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders
Frontiers in Genetics, 2018 Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George +4 more
doaj +1 more source