Results 21 to 30 of about 27,758 (248)

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

open access: yesMolecular Cell, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome. The proteasome subunits Rpn10 and Rpn13 are known to bind ubiquitin, but genetic and biochemical data suggest the existence of at least one ...
Paraskevopoulos, Konstantinos   +11 more
openaire   +3 more sources

Protein Degradation of RNA Polymerase II-Association Factor 1(PAF1) Is Controlled by CNOT4 and 26S Proteasome. [PDF]

open access: yesPLoS ONE, 2015
The PAF complex (PAFc) participates in various steps of the transcriptional process, from initiation to termination, by interacting with and recruiting various proteins to the proper locus for each step. PAFc is an evolutionarily conserved, multi-protein
Hwa-Young Sun   +3 more
doaj   +1 more source

Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis

open access: yesBiomolecules, 2023
The 26S proteasome is the largest and most complicated protease known, and changes to proteasome assembly or function contribute to numerous human diseases.
Daniel Betancourt   +2 more
doaj   +1 more source

Regulation of repair by the 26S proteasome [PDF]

open access: yesBioMed Research International, 2002
Cellular processes such as transcription and DNA repair may be regulated through diverse mechanisms, including RNA synthesis, protein synthesis, posttranslational modification and protein degradation. The 26S proteasome, which is responsible for degrading a broad spectrum of proteins, has been shown to interact with several nucleotide excision repair ...
Sweder, K., Madura, K.
openaire   +2 more sources

Ubiquitin Receptor RPN13 Mediates the Inhibitory Interaction of Diphenyldihaloketones CLEFMA and EF24 With the 26S Proteasome

open access: yesFrontiers in Chemistry, 2018
The proteasome is a validated target in drug discovery for diseases associated with unusual proteasomal activity. Here we report that two diphenyldihaloketones, CLEFMA and EF24, inhibit the peptidase activity of the 26S proteasome.
Geeta Rao   +6 more
doaj   +1 more source

Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain. [PDF]

open access: yesPLoS ONE, 2013
Proteostasis is critical for the maintenance of life. In neuronal cells an imbalance between protein synthesis and degradation is thought to be involved in the pathogenesis of neurodegenerative diseases during aging.
Carolin Giannini   +7 more
doaj   +1 more source

Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution.

open access: yesPLoS ONE, 2015
Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization.
Diego Sbardella   +9 more
doaj   +1 more source

Early cysteine-dependent inactivation of 26S proteasomes does not involve particle disassembly

open access: yesRedox Biology, 2018
Under oxidative stress 26S proteasomes suffer reversible disassembly into its 20S and 19S subunits, a process mediated by HSP70. This inhibits the degradation of polyubiquitinated proteins by the 26S proteasome and allows the degradation of oxidized ...
Martín Hugo   +7 more
doaj   +1 more source

Dietary apigenin potentiates the inhibitory effect of interferon-α on cancer cell viability through inhibition of 26S proteasome-mediated interferon receptor degradation

open access: yesFood & Nutrition Research, 2016
Background: Type I interferons (IFN-α/β) have broad and potent immunoregulatory and antiproliferative activities. However, it is still known whether the dietary flavonoids exhibit their antiviral and anticancer properties by modulating the function of ...
Sheng Li   +7 more
doaj   +1 more source

Molecular and cellular dynamics of the 26S proteasome

open access: yesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2021
In eukaryotic cells, the ubiquitin-proteasome system serves to remove proteins that are either dysfunctional or no longer needed. The 26S proteasome is a 2.5 MDa multisubunit complex comprising the 20S core particle, where degradation is executed, and one or two regulatory particles which prepare substrates for degradation.
Sakata, Eri   +2 more
openaire   +4 more sources

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