Results 61 to 70 of about 47,588 (257)

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular 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

TRIM5α as an E3 ubiquitin ligase

open access: yesThe 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]

open access: yesCellular 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

USP7 inhibits FOXO1 activity in chronic lymphocytic leukaemia cells enhancing cell survival

open access: yesMolecular 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

Effects of IGFBP4 deficiency on human preadipocyte proliferation and differentiation through the IGF1R/AKT pathway

open access: yesFEBS 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

E3 ubiquitin ligases in T‐cell tolerance [PDF]

open access: yesEuropean 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
openaire   +2 more sources

Purification and preparation of Marchantia polymorpha Auxin Response Factor 2 for phase separation studies

open access: yesFEBS 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

Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function

open access: yeseLife, 2019
The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation.
Ann Feke   +6 more
doaj   +1 more source

E3 Ubiquitin Ligases in Neurological Diseases: Focus on Gigaxonin and Autophagy

open access: yesFrontiers in Physiology, 2020
Ubiquitination is a dynamic post-translational modification that regulates the fate of proteins and therefore modulates a myriad of cellular functions.
Léa Lescouzères, Pascale Bomont
doaj   +1 more source

Threonine 348 regulates the subcellular localization of PTEN

open access: yesFEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

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