Results 81 to 90 of about 574,104 (383)

YOD1/TRAF6 association balances p62-dependent IL-1 signaling to NF-κB

eLife, 2017
The ubiquitin ligase TRAF6 is a key regulator of canonical IκB kinase (IKK)/NF-κB signaling in response to interleukin-1 (IL-1) stimulation. Here, we identified the deubiquitinating enzyme YOD1 (OTUD2) as a novel interactor of TRAF6 in human cells.
Gisela Schimmack, Kenji Schorpp, Kerstin Kutzner, Torben Gehring, Jara Kerstin Brenke, Kamyar Hadian, Daniel Krappmann   +6 more
doaj   +1 more source

Identification of ubiquitin Ser57 kinases regulating the oxidative stress response in yeast

eLife, 2020
Ubiquitination regulates many different cellular processes, including protein quality control, membrane trafficking, and stress responses. The diversity of ubiquitin functions in the cell is partly due to its ability to form chains with distinct linkages
Nathaniel L Hepowit, Kevin N Pereira, Jessica M Tumolo, Walter J Chazin, Jason A MacGurn   +4 more
doaj   +1 more source

echinus, required for interommatidial cell sorting and cell death in the Drosophila pupal retina, encodes a protein with homology to ubiquitin-specific proteases [PDF]

, 2007
Background: Programmed cell death is used to remove excess cells between ommatidia in the Drosophila pupal retina. This death is required to establish the crystalline, hexagonal packing of ommatidia that characterizes the adult fly eye.
Bosdet, Ian, Copeland, Jeffrey M., Freeman, J. Douglas, Gorski, Sharon M., Guo, Ming, Hay, Bruce A.   +5 more
core   +4 more sources

Structure and Ubiquitin Binding of the Ubiquitin-interacting Motif [PDF]

Journal of Biological Chemistry, 2003
Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules.
Daniel S. Higginson, Steven L. Alam, Christopher P. Hill, Bin Wang, Howard Robinson, Wesley I. Sundquist, Robert D. Fisher   +6 more
openaire   +3 more sources

TOMM20 as a driver of cancer aggressiveness via oxidative phosphorylation, maintenance of a reduced state, and resistance to apoptosis

Molecular Oncology, EarlyView.
TOMM20 increases cancer aggressiveness by maintaining a reduced state with increased NADH and NADPH levels, oxidative phosphorylation (OXPHOS), and apoptosis resistance while reducing reactive oxygen species (ROS) levels. Conversely, CRISPR‐Cas9 knockdown of TOMM20 alters these cancer‐aggressive traits.
Ranakul Islam, Megan E. Roche, Zhao Lin, Diana Whitaker‐Menezes, Victor Diaz‐Barros, Eurico Serrano, Maria Paula Martinez Cantarin, Nancy J. Philp, Atrayee Basu Mallick, Ubaldo Martinez‐Outschoorn   +9 more
wiley   +1 more source

Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3

eLife, 2013
Ubiquitination by HECT E3 enzymes regulates myriad processes, including tumor suppression, transcription, protein trafficking, and degradation. HECT E3s use a two-step mechanism to ligate ubiquitin to target proteins.
Hari B Kamadurai, Yu Qiu, Alan Deng, Joseph S Harrison, Chris MacDonald, Marcelo Actis, Patrick Rodrigues, Darcie J Miller, Judith Souphron, Steven M Lewis, Igor Kurinov, Naoaki Fujii, Michal Hammel, Robert Piper, Brian Kuhlman, Brenda A Schulman   +15 more
doaj   +1 more source

Ubiquitin carboxyl-terminal hydrolases are required for period maintenance of the circadian clock at high temperature in Arabidopsis [PDF]

, 2019
Protein ubiquitylation participates in a number of essential cellular processes including signal transduction and transcription, often by initiating the degradation of specific substrates through the 26S proteasome. Within the ubiquitin-proteasome system,
Coupland, George, Furutani-Hayama, Ikuyo, Hayama, Ryosuke, Mizoguchi, Tsuyoshi, Valverde Albacete, Federico, Vierstra, Richard D., Yang, Peizhen   +6 more
core   +1 more source

Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding

Science, 2019
Protein unfolding, one substrate at a time Ubiquitin marks proteins for degradation by the proteasome. However, many substrates cannot be directly degraded because they are well folded or are located in cell membranes or in multimeric complexes.
E. C. Twomey, Zhejian Ji, T. Wales, N. Bodnar, S. Ficarro, J. Marto, J. Engen, T. Rapoport   +7 more
semanticscholar   +1 more source

Plasma lipidomic and metabolomic profiles in high‐grade glioma patients before and after 72‐h presurgery water‐only fasting

Molecular Oncology, EarlyView.
Presurgery 72‐h fasting in GB patients leads to adaptations of plasma lipids and polar metabolites. Fasting reduces lysophosphatidylcholines and increases free fatty acids, shifts triglycerides toward long‐chain TGs and increases branched‐chain amino acids, alpha aminobutyric acid, and uric acid.
Iris Divé, Lisa Hahnefeld, Katharina J. Wenger, Donat Kögel, Joachim Steinbach, Gerd Geisslinger, Michael W. Ronellenfitsch, Irmgard Tegeder   +7 more
wiley   +1 more source

Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome

eLife, 2018
ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein–DNA interactions.
Ramasubramanian Sundaramoorthy, Amanda L Hughes, Hassane El-Mkami, David G Norman, Helder Ferreira, Tom Owen-Hughes   +5 more
doaj   +1 more source