Results 41 to 50 of about 30,210 (297)

Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation. [PDF]

PLoS ONE, 2015
The ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) directly targets its substrates for proteasomal degradation by becoming covalently attached via its C-terminal diglycine motif to internal lysine residues of its substrate proteins.
Johanna Bialas, Marcus Groettrup, Annette Aichem   +2 more
doaj   +1 more source

The deubiquitinating enzyme 13 retards non-alcoholic steatohepatitis via blocking inactive rhomboid protein 2-dependent pathway

Acta Pharmaceutica Sinica B, 2023
Nowadays potential preclinical drugs for the treatment of nonalcoholic steatohepatitis (NASH) have failed to achieve expected therapeutic efficacy because the pathogenic mechanisms are underestimated.
Minxuan Xu, Jun Tan, Liancai Zhu, Chenxu Ge, Wei Dong, Xianling Dai, Qin Kuang, Shaoyu Zhong, Lili Lai, Chao Yi, Qiang Li, Deshuai Lou, Linfeng Hu, Xi Liu, Gang Kuang, Jing Luo, Jing Feng, Bochu Wang   +17 more
doaj   +1 more source

The Emerging Role and Mechanism of E2/E3 Hybrid Enzyme UBE2O in Human Diseases

Biomedicines
The ubiquitin–proteasome system (UPS) plays a pivotal role in determining protein fate, regulating signal transduction, and maintaining cellular homeostasis. Protein ubiquitination, a key post-translational modification, is orchestrated by the sequential
Qian Cheng, Zuyin Li, Yongjian Li, Lei Chen, Dingbao Chen, Jiye Zhu   +5 more
doaj   +1 more source

The role of histone modifications in transcription regulation upon DNA damage

FEBS Letters, EarlyView.
This review discusses the critical role of histone modifications in regulating gene expression during the DNA damage response (DDR). By modulating chromatin structure and recruiting repair factors, these post‐translational modifications fine‐tune transcriptional programmes to maintain genomic stability.
Angelina Job Kolady, Siyao Wang
wiley   +1 more source

Determinants of Functionality in the Ubiquitin Conjugating Enzyme Family [PDF]

Structure, 2004
The E2 enzymes are key enzymes in the ubiquitin and ubiquitin-like protein ligation pathways. To understand the functionality of the different E2 enzymes, we analyzed 190 protein sequences and 211 structures and electrostatic potentials. Key findings include: The ScUbc1 orthologs are defined by a C-terminal UBA domain. An N-terminal sequence motif that
Winn, Peter J., Religa, Tomasz L., Battey, James N.D., Banerjee, Amit, Wade, Rebecca C.   +4 more
openaire   +2 more sources

Cell density–dependent nuclear‐cytoplasmic shuttling of SETDB1 integrates with Hippo signaling to regulate YAP1‐mediated transcription

FEBS Letters, EarlyView.
At low cell density, SETDB1 and YAP1 accumulate in the nucleus. As cell density increases, the Hippo pathway is gradually activated, and SETDB1 is associated with increased YAP1 phosphorylation. At high cell density, phosphorylated YAP1 is sequestered in the cytoplasm, while SETDB1 becomes polyubiquitinated and degraded by the ubiquitin–proteasome ...
Jaemin Eom, Jaewoong Jang, Jung Sun Park, Yong‐Kook Kang   +3 more
wiley   +1 more source

Activity-based protein profiling reveals both canonical and novel ubiquitin pathway enzymes in Plasmodium.

PLoS Pathogens
The ubiquitin-proteasome system (UPS) is essential for Plasmodium falciparum survival and represents a potential target for antimalarial therapies. We utilised a ubiquitin- activity based probe (Ub-Dha) to capture active components of the ubiquitin ...
Cameron Smith, Mohsen Hajisadeghian, Gerbrand J van der Heden van Noort, Michael J Deery, Adán Pinto-Fernández, Benedikt M Kessler, Katerina Artavanis-Tsakonas   +6 more
doaj   +1 more source

Ubiquitin control of S phase: a new role for the ubiquitin conjugating enzyme, UbcH7

Cell Division, 2009
Events within and transitions between the phases of the eukaryotic cell cycle are tightly controlled by transcriptional and post-translational processes. Prominent among them is a profound role for the ubiquitin proteasome proteolytic pathway. The timely
Taylor Allen, Whitcomb Elizabeth A
doaj   +1 more source

β‐TrCP overexpression enhances cisplatin sensitivity by depleting BRCA1

Molecular Oncology, EarlyView.
Low levels of β‐TrCP (Panel A) allow the accumulation of BRCA1 and CtIP, which facilitate the repair of cisplatin‐induced DNA damage via homologous recombination (HR) and promote tumor cell survival. In contrast, high β‐TrCP expression (Panel B) leads to BRCA1 and CtIP degradation, impairing HR repair, resulting in persistent DNA damage and apoptosis ...
Rocío Jiménez‐Guerrero, Alejandro Belmonte‐Fernández, Mónica González‐Moreno, Laura Rodríguez‐Cordero, Begoña Pérez‐Valderrama, Joaquín Herrero‐Ruíz, Francisco Romero, Carmen Sáez, Miguel Á. Japón   +8 more
wiley   +1 more source

Proteasome inhibitors: new class of antitumor agents

Biomolecules & Biomedicine, 2003
The ubiquitin-proteasome pathway is the principal pathway for intracellular protein degradation1,2 (Fig 1). This pathway selectively degrades an extensive number of short-lived regulatory proteins involved in the control of normal cellular processes. In
Gordan Srkalović
doaj   +1 more source