Results 61 to 70 of about 76,539 (287)
Transcriptional regulation of the 26S proteasome by Nrf1
The 26S proteasome is a large protease complex that selectively degrades ubiquitinated proteins. It comprises 33 distinct subunits, each of which differ in function and structure, and which cannot be substituted by the other subunits. Owing to its complicated structure, the biogenesis of the 26S proteasome is elaborately regulated at the transcription,
KOIZUMI, Shun +2 more
openaire +3 more sources
Oncogenic DMTF1β promotes cancer cell motility by regulating autophagy through ULK1 stabilization
In the current study, we demonstrate that the oncogene DMTF1β regulates ULK1 stability by reducing its proteasomal degradation in cancer cells. This stabilization enables ULK1 to induce autophagy, which in turn facilitates cancer cell migration. Consequently, reduced DMTF1β levels lead to decreased autophagy and impaired cancer cell migration.
Jun Xu +13 more
wiley +1 more source
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
ADP‐ribosylation: An emerging regulator of the epigenome
ADP‐ribosylation has emerged as a dynamic epigenetic signaling mechanism that modifies histones and chromatin‐associated proteins. Through coordinated PARylation and MARylation, it integrates with other histone modifications to regulate chromatin structure, transcription factor activity, and gene expression, influencing genome function and disease ...
Cristel V. Camacho +2 more
wiley +1 more source
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
In vitro Reconstitution Assays of Arabidopsis 20S Proteasome
The majority of cellular proteins are degraded by the 26S proteasome in eukaryotes. However, intrinsically disordered proteins (IDPs), which contain large portions of unstructured regions and are inherently unstable, are degraded via the ubiquitin ...
Yanjun Li +4 more
doaj +1 more source
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
Accurate and noninvasive prostate cancer detection using plasma‐derived extracellular vesicle RNA
Plasma extracellular vesicles were captured with WGA‐conjugated magnetic beads and profiled for RNA biomarkers. A three‐RNA panel (NM_024955, NR_047469, and NR_002564) distinguished prostate cancer from healthy controls and benign prostatic hyperplasia, supporting a simple, noninvasive approach to improve prostate cancer detection.
Hanping Wei, Haoran Wu, Wei Feng
wiley +1 more source
Summary: The 26S proteasome is the central ATP-dependent protease in eukaryotes and is essential for organismal health. Proteasome assembly is mediated by several dedicated, evolutionarily conserved chaperone proteins.
Antonia A. Nemec +4 more
doaj +1 more source
Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules (PSG) and survival in stationary phase. [PDF]
Decline of proteasome activity has been reported in mammals, flies and yeasts during aging. In the yeast Saccharomyces cerevisiae, the reduction of proteolysis in stationary phase is correlated with disassembly of the 26S proteasomes into their 20S and ...
Rémy Saunier +3 more
doaj +1 more source

