Results 91 to 100 of about 39,029 (256)
The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav +4 more
wiley +1 more source
Ubiquitination functions as an important posttranslational modification for orchestrating inflammatory immune responses and cell death during pathogenic infection.
Luyu Yang +4 more
doaj +1 more source
Background. Hyperglycemia plays a pivotal role in the development of diabetic nephropathy (DN) and may be related to epigenetic metabolic memory.
Chenlin Gao +7 more
doaj +1 more source
Quantitative proteomics reveals extensive lysine ubiquitination and transcription factor stability states in Arabidopsis [PDF]
Protein activity, abundance, and stability can be regulated by post-translational modification including ubiquitination. Ubiquitination is conserved among eukaryotes and plays a central role in modulating cellular function; yet, we lack comprehensive ...
Pu, Yunting +8 more
core
Ciliary/Flagellar Protein Ubiquitination
Cilia/flagella are conserved eukaryotic organelles that play an important role in the control of cell motility and detection of environmental cues. However, the molecular mechanisms underlying ciliary/flagellar assembly, maintenance, disassembly, and ...
Huan Long, Qiyu Wang, Kaiyao Huang
core +1 more source
The PAM pathway and its impact on cellular metabolism. Color‐coded key symbols represent Rapamycin (R, orange, targeting mTOR) and Dactolisib (D, green, targeting PI3K/mTOR), indicating their sites of action. Created with BioRenders.com. Glioblastoma resists therapy through interconnected survival programs.
Kai Zhao +23 more
wiley +1 more source
The Ligation Systems for Ubiquitin and Ubiquitin-like Proteins
Ubiquitin (Ub) is a highly conserved small protein present universally in eukaryotic cells, which is covalently attached to substrate proteins by a cascade system, consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. The modification of cellular proteins with Ub targets them for degradation by a large multisubunit protease ...
K, Tanaka, T, Suzuki, T, Chiba
openaire +2 more sources
The role of ubiquitination in health and disease
Ubiquitination is an enzymatic process characterized by the covalent attachment of ubiquitin to target proteins, thereby modulating their degradation, transportation, and signal transduction.
Yan Liao +4 more
doaj +1 more source
Bidirectional regulation of the ubiquitin-RNA modification axis in cancer
RNA modifications, dynamically regulated by RNA-modifying proteins (RMPs) acting as “writers”, “erasers”, and “readers”, play pivotal roles in governing gene expression and cellular fate.
Kailang Li +6 more
doaj +1 more source
Insights into non-proteinaceous ubiquitination [PDF]
Ubiquitination plays a key role in the regulation of numerous diverse cellular functions. This process involves the covalent attachment of ubiquitin to protein substrates by a cascade of enzymes.
Huang, Danny, Dearlove, Emily
core +1 more source

