Results 31 to 40 of about 117,989 (312)

A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae

Frontiers in Microbiology, 2018
Ubiquitination is an essential protein modification in eukaryotic cells, which is reversible. Deubiquitinating enzymes (DUBs) catalyze deubiquitination process to reverse ubiquitination, maintain ubiquitin homeostasis or promote protein degradation by ...
Zhao Wang, Hong Zhang, Caiyun Liu, Junjie Xing, Xiao-Lin Chen, Xiao-Lin Chen   +5 more
doaj   +1 more source

K63-linked polyubiquitin chains bind to DNA to facilitate DNA damage repair

Science Signaling, 2018
Mutations in the DNA-interacting patch of ubiquitin sensitize cells to DNA-damaging agents. DNA-bound ubiquitin coordinates DNA repair Ubiquitylation is a posttranslational modification that reversibly alters protein stability, activity, interactions, or
Pengda Liu, Wenjian Gan, Siyuan Su, Arthur V. Hauenstein, T. Fu, B. Brasher, C. Schwerdtfeger, A. Liang, Ming Xu, Wenyi Wei   +9 more
semanticscholar   +1 more source

The Pepper RING Finger E3 Ligase, CaDIR1, Regulates the Drought Stress Response via ABA-Mediated Signaling

Frontiers in Plant Science, 2017
Drought stress from soil or air limits plant growth and development, leading to a reduction in crop productivity. Several E3 ligases positively or negatively regulate the drought stress response.
Sang-Wook Han, Sung Chul Lee, Hyunhee Joo, Chae Woo Lim   +3 more
doaj   +1 more source

The Ubiquitination Machinery of the Ubiquitin System [PDF]

The Arabidopsis Book, 2014
The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as well as proteins that bind to ubiquitinated proteins leading them to their final fate.
openaire   +4 more sources

Ubiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate [PDF]

Biochemistry, 2011
Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer
Jonathan N, Pruneda, Kate E, Stoll, Laura J, Bolton, Peter S, Brzovic, Rachel E, Klevit   +4 more
openaire   +2 more sources

Integrative genomic analysis identifies associations of molecular alterations to APOBEC and BRCA1/2 mutational signatures in breast cancer

Molecular Genetics & Genomic Medicine, 2019
Background The observed mutations in cancer are the result of ~30 mutational processes, which stamp particular mutational signatures (MS). Nevertheless, it is still not clear which genomic alterations correlate to several MS.
Victor Trevino
doaj   +1 more source

Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler

Nature Chemical Biology, 2020
Virtually all aspects of cell biology are regulated by a ubiquitin code where distinct ubiquitin chain architectures guide the binding events and itineraries of modified substrates.
Joanna Liwocha, David T. Krist, Gerbrand J. van der Heden van Noort, Fynn M. Hansen, V. Truong, Ozge Karayel, Nicholas Purser, D. Houston, N. Burton, M. Bostock, M. Sattler, M. Mann, J. Harrison, Gary Kleiger, H. Ovaa, B. Schulman   +15 more
semanticscholar   +1 more source

A simple and high-sensitivity method for analysis of ubiquitination and polyubiquitination based on wheat cell-free protein synthesis

BMC Plant Biology, 2009
Background Ubiquitination is mediated by the sequential action of at least three enzymes: the E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme) and E3 (ubiquitin ligase) proteins. Polyubiquitination of target proteins is also implicated
Seki Motoaki, Nozawa Akira, Takahashi Hirotaka, Shinozaki Kazuo, Endo Yaeta, Sawasaki Tatsuya   +5 more
doaj   +1 more source

A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi

Nature Communications, 2020
Ubiquitin mediated signaling contributes critically to host cell defenses during pathogen infection. Many pathogens manipulate the ubiquitin system to evade these defenses.
Jason M. Berk, Chris C. Lim, J. Ronau, J. Ronau, A. Chaudhuri, Hongli Chen, J. Beckmann, J. Beckmann, J. P. Loria, Y. Xiong, M. Hochstrasser   +10 more
semanticscholar   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source