Results 51 to 60 of about 1,442,074 (300)

Inhibition of dipeptidyl peptidase 7 impairs lysophagy in LLOMe‐treated HepG2 cells

open access: yesFEBS Letters, EarlyView.
DPP7 inhibition delays ubiquitin‐dependent lysophagy by attenuating ubiquitin accumulation and the recruitment of SQSTM1 and LC3 to damaged lysosomes, resulting in delayed clearance of damaged lysosomes and impaired restoration of lysosomal homeostasis. Created using FigureLabs (Certificate ID: FL‐PUB‐20260922‐Z99XNX).
Na Yeon Park   +8 more
wiley   +1 more source

CaMKII suppresses proteotoxicity by phosphorylating BAG3 in response to proteasomal dysfunction

open access: yesEMBO Reports
Protein quality control serves as the primary defense mechanism for cells against proteotoxicity induced by proteasome dysfunction. While cells can limit the build-up of ubiquitinated misfolded proteins during proteasome inhibition, the precise mechanism
Chenliang Zhang   +7 more
doaj   +1 more source

Inhibitory effects of pesticides on proteasome activity: Implication in Parkinson's disease

open access: yesNeurobiology of Disease, 2006
Epidemiological studies have suggested a correlation of pesticides and Parkinson's disease (PD) while genetic and biochemical studies have implicated the ubiquitin–proteasome system (UPS) in the pathogenesis of PD.
Xue-Feng Wang   +3 more
doaj   +1 more source

The Proteasome Inhibition Model of Parkinson’s Disease

open access: yesJournal of Parkinson’s Disease, 2016
The pathological hallmarks of Parkinson’s disease are the progressive loss of nigral dopaminergic neurons and the formation of intracellular inclusion bodies, termed Lewy bodies, in surviving neurons. Accumulation of proteins in large insoluble cytoplasmic aggregates has been proposed to result, partly, from a failure in the function of intracellular ...
Bentea, Eduard   +2 more
openaire   +3 more sources

Apoptosis induced by proteasome inhibition in human myoblast cultures [PDF]

open access: yes, 2009
Dysfunction of the ubiquitin-proteasome system has recently been implicated in the pathogenesis of some untreatable myodegenerative diseases characterized by the formation of ubiquitinated inclusions in skeletal muscles.
J Sassone   +6 more
core   +1 more source

The molecular network of the proteasome machinery inhibition response is orchestrated by HSP70, revealing vulnerabilities in cancer cells

open access: yes, 2022
Proteasome machinery is amajor proteostasis control system in human cells, actively compensated upon its inhibition. To understand this compensation, we compared global protein landscapes upon the proteasome inhibition with carfilzomib, in normal ...
Kolos, M.   +16 more
core   +1 more source

Going viral − Virus‐targeting nanobodies for research, diagnostics and therapy

open access: yesFEBS Letters, EarlyView.
The increasing prevalence of viral diseases represents a major threat for global human health. Nanobodies, small binding fragments derived from camelid heavy‐chain antibodies, offer versatile tools for viral research, diagnostics, and antiviral therapy.
Domenic Ebert, Ulrich Rothbauer
wiley   +1 more source

Dual Function of USP14 Deubiquitinase in Cellular Proteasomal Activity and Autophagic Flux

open access: yesCell Reports, 2018
Summary: The ubiquitin-proteasome system and the autophagy-lysosome system are two major intracellular proteolytic pathways in eukaryotes. Although several biochemical mechanisms underlying the crosstalk between them have been suggested, little is known ...
Eunkyoung Kim   +9 more
doaj   +1 more source

Changes in proteasome structure and function caused by HAMLET in tumor cells. [PDF]

open access: yesPLoS ONE, 2009
Proteasomes control the level of endogenous unfolded proteins by degrading them in the proteolytic core. Insufficient degradation due to altered protein structure or proteasome inhibition may trigger cell death.
Lotta Gustafsson   +5 more
doaj   +1 more source

How structural disorder and polyelectrolyte properties of prothymosin α enable its large interactome

open access: yesFEBS Letters, EarlyView.
In this review, complexes of the fully disordered and highly negatively charged prothymosin α are collected, described, and discussed. Linked to its poly‐electrostatic character, prothymosin α engages a large interactome through multiple different binding modes ranging from fully disordered complexes to short linear motif (SLiM)‐driven interactions ...
Ketty C. Tamburrini   +3 more
wiley   +1 more source

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