Results 11 to 20 of about 27,539 (236)

Deciphering histone 2A deubiquitination [PDF]

open access: yesGenome Biology, 2008
Three recent papers have identified distinct enzymes that can remove ubiquitin from mammalian histone 2A (H2A). Functions in transcriptional activation, DNA repair and control of the cell cycle have been proposed for these enzymes.
Michael J, Clague   +2 more
openaire   +2 more sources

The Mechanism of Ubiquitination or Deubiquitination Modifications in Regulating Solid Tumor Radiosensitivity

open access: yesBiomedicines, 2023
Radiotherapy, a treatment method employing radiation to eradicate tumor cells and subsequently reduce or eliminate tumor masses, is widely applied in the management of numerous patients with tumors.
Mengyun Zhang, Yingjie Shao, Wendong Gu
doaj   +1 more source

USP13: Multiple Functions and Target Inhibition

open access: yesFrontiers in Cell and Developmental Biology, 2022
As a deubiquitination (DUB) enzyme, ubiquitin-specific protease 13 (USP13) is involved in a myriad of cellular processes, such as mitochondrial energy metabolism, autophagy, DNA damage response, and endoplasmic reticulum-associated degradation (ERAD), by
Xiaolong Li   +11 more
doaj   +1 more source

VHL protein‐interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF‐1α [PDF]

open access: yesEMBO reports, 2005
Hypoxia‐inducible factor (HIF)‐1α is a short‐lived protein and is ubiquitinated and degraded through the von Hippel–Lindau protein (pVHL)–E3 ubiquitin ligase pathway at normoxia. Deubiquitination, by reversing ubiquitination, has been recognized as an important regulatory step in ubiquitination‐related processes.
Zaibo, Li   +3 more
openaire   +2 more sources

Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins [PDF]

open access: yes, 2008
Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail.
Deshaies, Raymond J.   +6 more
core   +6 more sources

The Proteasomal Deubiquitinating Enzyme PSMD14 Regulates Macroautophagy by Controlling Golgi-to-ER Retrograde Transport [PDF]

open access: yes, 2020
Ubiquitination regulates several biological processes, however the role of specific members of the ubiquitinome on intracellular membrane trafficking is not yet fully understood.
Arias-Muñoz, Eloisa   +16 more
core   +2 more sources

Ubiquitin-specific peptidase 10, a deubiquitinating enzyme: Assessing its role in tumor prognosis and immune response

open access: yesFrontiers in Oncology, 2022
Ubiquitin-specific peptidase 10 (USP10) is a member of the ubiquitin-specific protease family that removes the ubiquitin chain from ubiquitin-conjugated protein substrates.
Ziqi Ye   +7 more
doaj   +1 more source

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation. [PDF]

open access: yes, 2019
The 26S proteasome is essential for proteostasis and the regulation of vital processes through ATP-dependent degradation of ubiquitinated substrates. To accomplish the multi-step degradation process, the proteasomes regulatory particle, consisting of lid
Aufderheide   +42 more
core   +1 more source

The emerging role of Deubiquitinases (DUBs) in parasites: A foresight review

open access: yesFrontiers in Cellular and Infection Microbiology, 2022
Before the discovery of the proteasome complex, the lysosomes with acidic proteases and caspases in apoptotic pathways were thought to be the only pathways for the degradation of damaged, unfolded, and aged proteins. However, the discovery of 26S and 20S
Prakash Kumar   +4 more
doaj   +1 more source

The Molecular Basis of Spinocerebellar Ataxia Type 7

open access: yesFrontiers in Neuroscience, 2022
Spinocerebellar ataxia (SCA) type 7 (SCA7) is caused by a CAG trinucleotide repeat expansion in the ataxin 7 (ATXN7) gene, which results in polyglutamine expansion at the amino terminus of the ATXN7 protein.
Rituparna Goswami   +12 more
doaj   +1 more source

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