Results 71 to 80 of about 223,344 (207)
Overexpression of a soybean ariadne-like ubiquitin ligase gene GmARI1 enhances aluminum tolerance in Arabidopsis. [PDF]
PLoS ONE, 2014 Ariadne (ARI) subfamily of RBR (Ring Between Ring fingers) proteins have been found as a group of putative E3 ubiquitin ligases containing RING (Really Interesting New Gene) finger domains in fruitfly, mouse, human and Arabidopsis.
Xiaolian Zhang +8 more
doaj +1 more source
In vitro Protein Ubiquitination Assays
Bio-Protocol, 2013 Ubiquitin can be added to substrate protein as a protein tag by the concerted actions of ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2) and ubiquitin protein ligase (E3).
Qingzhen Zhao, Qi Xie
doaj +1 more source
Characterisation of the Cullin-3 mutation that causes a severe form of familial hypertension and hyperkalaemia [PDF]
, 2015 Deletion of exon 9 from Cullin-3 (CUL3, residues 403-459: CUL3Δ403-459) causes pseudohypoaldosteronism type IIE (PHA2E), a severe form of familial hyperkalaemia and hypertension (FHHt).
Nichola L Figg +35 more
core +1 more source
TRIM5α as an E3 ubiquitin ligase
The FASEB Journal, 2009 Human immunodeficiency virus type1 (HIV‐1) efficiently infects susceptible cells and causes acquired immunodeficiency syndrome (AIDS) in humans. Although HIV can also enter the cells of Old World monkeys, it encounters a block before reverse transcription.
Makoto Tanaka +2 more
openaire +1 more source
E3 ubiquitin ligases in B-cell malignancies [PDF]
Cellular Immunology, 2019 Ubiquitylation is a post-translational modification (PTM) that controls various cellular signaling pathways. It is orchestrated by a three-step enzymatic cascade know as the ubiquitin proteasome system (UPS). E3 ligases dictate the specificity to the substrates, primarily leading to proteasome-dependent degradation.
Jaewoo Choi, Luca Busino
openaire +2 more sources
Data for positive selection test and co-evolutionary analysis on mammalian cereblon
Data in Brief, 2019 Cereblon (CRBN) is a substrate recognition subunit of the CRL4 E3 ubiquitin ligase complex, directly binding to specific substrates for poly-ubiquitination followed by proteasome-dependent degradation of proteins.
Wataru Onodera +2 more
doaj +1 more source
Unbiased identification of substrates for the Epac1-inducible E3 ubiquitin ligase component SOCS-3
, 2012 The anti-inflammatory effects of the prototypical second messenger cAMP have been extensively documented in multiple cell types. One mechanism by which these effects are achieved is via Epac1 (exchange protein directly activated by cAMP 1)-dependent ...
Williams, Jamie J.L., Palmer, Timothy M.
core +1 more source
E3 ubiquitin ligases in T‐cell tolerance [PDF]
European Journal of Immunology, 2009 AbstractThe immune system uses several mechanisms of central and peripheral tolerance in order to prevent the activation of T lymphocytes toward self‐antigens. Although the importance of immune self‐tolerance has been established for a long time, some essential cellular and molecular mechanisms of T‐cell tolerance have only been recently revealed. Once
Magdalena, Paolino, Josef M, Penninger
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Nature Communications, 2017 Protein stability modulation by E3 ubiquitin ligases is an important layer of functional regulation, but screening for E3 ligase-substrate interactions is time-consuming and costly.
Yang Li +12 more
doaj +1 more source
Role of E3 ubiquitin ligases in lung cancer
World Journal of Clinical Oncology, 2013 E3 ubiquitin ligases are a large family of proteins that catalyze the ubiquitination of many protein substrates for targeted degradation by the 26S proteasome. Therefore, E3 ubiquitin ligases play an essential role in a variety of biological processes including cell cycle regulation, proliferation and apoptosis.
Snoek, B.C. +3 more
openaire +2 more sources