Results 81 to 90 of about 231,680 (303)
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
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Molecular Oncology, EarlyView.Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +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
USP7 inhibits FOXO1 activity in chronic lymphocytic leukaemia cells enhancing cell survival
Molecular Oncology, EarlyView.CLL cells rely on BCR‐mediated signalling for survival and proliferation in part through suppression of FOXO1. FOXO1 activity is regulated by a plethora of post‐translational modifications including phosphorylation and ubiquitination. We demonstrated that dual inhibition of BCR signalling and the deubiquitinase USP7 activates FOXO1, modulating its ...
Hassan N.B. Almuhanna +8 more
wiley +1 more source
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
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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FEBS Open Bio, EarlyView.IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo +6 more
wiley +1 more source
WWP1 (WW domain containing E3 ubiquitin protein ligase 1) [PDF]
, 2008 Review on WWP1 (WW domain containing E3 ubiquitin protein ligase 1), with data on DNA, on the protein encoded, and where the gene is ...
Chen, C
core +1 more source
FEBS Open Bio, EarlyView.We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
wiley +1 more source
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