Results 151 to 160 of about 27,758 (248)

Structural Polymorphism of polyG Inclusions Revealed by In Situ Cryo‐Electron Tomography

open access: yesAdvanced Science, EarlyView.
Correlative cryo‐electron tomography in primary cortical neurons and NIID mouse brain tissue reveals that polyG inclusions are interconnected ribbon‐like assemblies rather than canonical amyloid fibrils. Multiple compartment‐specific ribbon states show distinct 26S proteasome accessibility, while cytoplasmic ribbons contact and deform ER‐like ...
Yunwen Qian   +12 more
wiley   +1 more source

NUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome. [PDF]

open access: yesNat Struct Mol Biol
Arkinson C   +7 more
europepmc   +1 more source

ZBTB11 Promotes Breast Cancer Progression by Activating FBXO28‐Mediated MST1 Degradation and Suppressing Hippo Signaling

open access: yesAdvanced Science, EarlyView.
ZBTB11 is identified as an oncogenic transcription factor that activates FBXO28 in breast cancer. FBXO28 promotes K48‐linked ubiquitination and degradation of MST1, suppressing Hippo signaling and enhancing epithelial–mesenchymal transition and metastasis. This transcription‐to‐ubiquitination cascade defines a prognostic biomarker axis and highlights a
An Xu   +10 more
wiley   +1 more source

PolyG Fibrils Coalesce Into Nuclear Ribbons That Engage Proteostasis Machinery in Neuronal Intranuclear Inclusion Disease

open access: yesAdvanced Science, EarlyView.
In NIID, expanded NOTCH2NLC repeats give rise to nuclear polyG inclusions. Tracer‐guided in situ cryo‐electron tomography enables cross‐scale structural analysis from mouse brain to native neuronal nuclei, revealing dense‐core/peripheral‐halo inclusions built from compact polyG ribbons.
Hui Dong   +13 more
wiley   +1 more source

SPSB1 Promotes Subcutaneous Adipose Hyperplasia in Facial Port‐Wine Stains by Controlling HDAC1 Degradation and Stability Through Two Distinct Proteolytic Pathways

open access: yesAdvanced Science, EarlyView.
In PWS‐ASPCs, FOSL1 drives the expression of SPSB1. SPSB1, as part of the ESC complex, further binds to HDAC1 and promotes K29‐linked and K48‐linked polyubiquitination of HDAC1. These modifications facilitate the degradation of HDAC1 through the ALP and UPS pathways, respectively.
Hongrui Chen   +5 more
wiley   +1 more source

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