Results 41 to 50 of about 27,758 (248)

Compensatory role of the Nrf2–ARE pathway against paraquat toxicity: Relevance of 26S proteasome activity

open access: yesJournal of Pharmacological Sciences, 2015
Oxidative stress and the ubiquitin–proteasome system play a key role in the pathogenesis of Parkinson disease. Although the herbicide paraquat is an environmental factor that is involved in the etiology of Parkinson disease, the role of 26S proteasome in
Yasuhiko Izumi   +6 more
doaj   +1 more source

The Cardiac 26S Proteasome [PDF]

open access: yesCirculation Research, 2006
See related articles, pages 362–371 and 372–380 The ubiquitin–proteasome system (UPS) is the main pathway for the nonlysosomal degradation of intracellular proteins, representing upwards of 80% of all intracellular proteins. A key component of the UPS is the 26S proteasome, a macromolecular multisubunit complex that has the responsibility of ...
openaire   +1 more source

Insights into the molecular architecture of the 26S proteasome [PDF]

open access: yesProceedings of the National Academy of Sciences, 2009
Cryo-electron microscopy in conjunction with advanced image analysis was used to analyze the structure of the 26S proteasome and to elucidate its variable features. We have been able to outline the boundaries of the ATPase module in the “base” part of the regulatory complex that can vary in its position and orientation relative to the 20S core particle.
Nickell, S.   +13 more
openaire   +3 more sources

Dimethyl fumarate combined with cisplatin at subcytotoxic doses sensitizes cervical cancer toward ferroptosis and apoptosis through GSH restriction and p53 (re)activation

open access: yesMolecular Oncology, EarlyView.
Dimethyl fumarate (DMF) reduces growth of HPV‐positive cervical cancer spheroids and induces ferroptosis in cervical cancer cells via blocking SLC7A11/Glutathione (GSH) axis. Combination of subcytotoxic doses of DMF and cisplatin (CDDP) further suppresses spheroid growth and drives cell death in 2D culture models.
Carolina Punziano   +6 more
wiley   +1 more source

The C-Terminus of the PSMA3 Proteasome Subunit Preferentially Traps Intrinsically Disordered Proteins for Degradation

open access: yesCells, 2022
The degradation of intrinsically disordered proteins (IDPs) by a non-26S proteasome process does not require proteasomal targeting by polyubiquitin.
Assaf Biran   +7 more
doaj   +1 more source

Transcriptional profiling of circulating extracellular vesicles from prebiopsy prostate cancer patients

open access: yesMolecular Oncology, EarlyView.
RNA profiling of circulating extracellular vesicles (EVs) from blood samples of men undergoing prostate biopsy identifies transcripts associated with clinically significant prostate cancer. Integrative analysis with public tumor datasets links EV‐derived gene signatures to tumor stage and progression‐free survival, highlighting CASP3, XRCC2, and RIT1 ...
Stefan Werner   +14 more
wiley   +1 more source

UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity [PDF]

open access: yesProceedings of the National Academy of Sciences, 2011
Protein degradation by the 26S proteasome is a fundamental process involved in a broad range of cellular activities, yet how proteasome activity is regulated remains poorly understood. We report here that ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) is a 26S proteasome phosphatase that regulates nuclear proteasome activity.
Xing, Guo   +6 more
openaire   +2 more sources

USP29‐regulated noncanonical stabilization of the hypoxia‐inducible factor‐α in aggressive prostate cancer

open access: yesMolecular Oncology, EarlyView.
We identify USP29 as the only DUB mirroring CA9 expression, a marker of hypoxia and HIF pathway activation associated with PCA aggressiveness. USP29 stabilizes HIF‐1α and HIF‐2α via a noncanonical mechanism that is independent of PHD/pVHL activity yet relies on proteasomal regulation, establishing USP29 as a previously unrecognized regulator of hypoxic
Amelie S Schober   +16 more
wiley   +1 more source

Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity

open access: yesiScience
Summary: In addition to the degradation of cell-cycle proteins, short-lived, damaged, or unfolded proteins are constantly cleared from cells by the proteasome.
Gabriel Ruiz-Romero   +4 more
doaj   +1 more source

Phosphorylation of ATPase subunits of the 26S proteasome

open access: yesFEBS Letters, 1998
The 26S proteasome complex plays a major role in the non‐lysosomal degradation of intracellular proteins. Purified 26S proteasomes give a pattern of more than 40 spots on 2D‐PAGE gels. The positions of subunits have been identified by mass spectrometry of tryptic peptides and by immunoblotting with subunit‐specific antipeptide antibodies.
Mason, Grant G.F.   +3 more
openaire   +3 more sources

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