Results 81 to 90 of about 200,227 (256)

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

Drugging the Fbw7 E3 Ligase with a Fragment-Based Approach

open access: yes, 2019
Fbw7 is an important E3 ligase and one of the most commonly deregulated proteins in human cancers.
Salvatore Scaffidi   +3 more
core   +1 more source

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

Parkin is protective against proteotoxic stress in a transgenic zebrafish model [PDF]

open access: yes, 2010
Mutations in the gene encoding the E3 ubiquitin ligase parkin (PARK2) are responsible for the majority of autosomal recessive parkinsonism. Similarly to other knockout mouse models of PD-associated genes, parkin knockout mice do not show a substantial ...
van Bebber Frauke   +25 more
core   +2 more sources

TRAIP Mediates Alcohol‐Induced Liver Injury through Regulating β‐catenin Ubiquitin Degradation via Direct Interaction

open access: yesAdvanced Science, EarlyView.
This study reveals that NF‐κB1‐driven TRAIP upregulation in ALD correlates with disease severity. Mechanistically, TRAIP directly binds β‐catenin via its CC domain and promotes its K48‐linked ubiquitination and degradation, which is independent of the GSK3β/β‐TrCP pathway.
Zhan Wu   +13 more
wiley   +1 more source

Microglial Deubiquitinase OTUD7B Stabilizes STAT3 to Promote Neuroinflammation and Cognitive Decline in Alzheimer's Disease

open access: yesAdvanced Science, EarlyView.
. ABSTRACT Neuroinflammation driven by microglial activation is a defining feature of Alzheimer's disease (AD), yet the molecular mechanisms sustaining this proinflammatory state remain unclear. Here, we identify the deubiquitinase OTUD7B as a critical regulator of microglial activation and AD pathology.
Luyao Li   +15 more
wiley   +1 more source

Essential roles of the HECT E3 ubiquitin ligase Smurf2 in mitotic progression and fidelity.

open access: yes, 2009
Essential roles of the HECT E3 ubiquitin ligase Smurf2 in mitotic progression and ...
Evan. Osmundson (7973687)
core   +3 more sources

MG53/TRIM72: multi-organ repair protein and beyond

open access: yesFrontiers in Physiology
MG53, a member of the tripartite motif protein family, possesses multiple functionalities due to its classic membrane repair function, anti-inflammatory ability, and E3 ubiquitin ligase properties.
Yong-Fei Wang   +9 more
doaj   +1 more source

Loss of E3 Ubiquitin Ligase RINES via CpG Methylation Relieves Suppression of STAT3 and MYC, Facilitating Multiple Tumorigeneses

open access: yesAdvanced Science, EarlyView.
Dysregulated protein modifications drive tumorigenesis. RINES, an E3 ubiquitin ligase, represses tumor cell proliferation and metastasis by facilitating RING domain‐dependent, ubiquitin–proteasome‐mediated degradation of STAT3 and MYC, which consequently restrains cancer stemness and oncogenic progression.
Lili Li   +8 more
wiley   +1 more source

In vitro SUMOylation assay to study SUMO E3 ligase activity

open access: yes, 2018
[[abstract]]Small ubiquitin-like modifier (SUMO) modification is an important post-translational modification (PTM) that mediates signal transduction primarily through modulating protein-protein interactions.
Yang, WS;Campbell, M;Kung, HJ;Chang, PC
core   +1 more source

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