Results 11 to 20 of about 59,068 (260)
Orthogonal ubiquitin transfer identifies ubiquitination substrates under differential control by the two ubiquitin activating enzymes [PDF]
Nature Communications, 2017 The transfer of ubiquitin (UB) to cellular targets is mediated sequentially by three groups of enzymes, UB activating enzyme (E1), UB conjugating enzyme (E2) and UB ligase (E3).
Bo Zhao +2 more
exaly +3 more sources
The deubiquitinase USP35: from an oncogenic hub to a therapeutic target in human cancers [PDF]
Frontiers in OncologyUbiquitination is a critical post-translational modification in eukaryotic cells, mediated by a sequential enzymatic cascade involving E1 (activating), E2 (conjugating), and E3 (ligase) enzymes that catalyze the covalent conjugation of ubiquitin to ...
Bisheng Li +6 more
doaj +2 more sources
MALDI-TOF Mass Spectrometry for interrogating ubiquitin enzymes
Frontiers in Molecular Biosciences, 2023 The attachment of ubiquitin to a substrate (ubiquitination or ubiquitylation) impacts its lifetime and regulates its function within the cell. Several classes of enzymes oversee the attachment of ubiquitin to the substrate: an E1 activating enzyme that ...
Virginia De Cesare
doaj +1 more source
Decoding the ubiquitin-mediated pathway of arthropod disease vectors. [PDF]
PLoS ONE, 2013 Protein regulation by ubiquitin has been extensively described in model organisms. However, characterization of the ubiquitin machinery in disease vectors remains mostly unknown.
Anthony Choy +5 more
doaj +1 more source
Pleiotropic Roles of a KEAP1-Associated Deubiquitinase, OTUD1
Antioxidants, 2023 Protein ubiquitination, which is catalyzed by ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin ligases, is a crucial post-translational modification to regulate numerous cellular functions in a spatio–temporal-specific manner ...
Daisuke Oikawa +2 more
doaj +1 more source
Structural Diversity of Ubiquitin E3 Ligase
Molecules, 2021 The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes ...
Sachiko Toma-Fukai, Toshiyuki Shimizu
doaj +1 more source
Evolution of the ubiquitin-activating enzyme Uba1 (E1) [PDF]
Physica A: Statistical Mechanics and its Applications, 2017 Ubiquitin tags diseased proteins and initiates an enzyme conjugation cascade, which has three stages. The first-stage enzyme Uba1 (E1) has evolved only modestly from slime mold to humans, and is > 14 times larger than Ub. Here we use critical point thermodynamic scaling theory to connect Uba1 (E1) evolution from yeast and slime mold to fruit flies ...
Allan, Douglas C., Phillips, J. C.
openaire +2 more sources
Crystal Structure of a Fragment of Mouse Ubiquitin-activating Enzyme [PDF]
Journal of Biological Chemistry, 2005 Protein ubiquitination requires the sequential activity of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-ligase (E3). The ubiquitin-transfer machinery is hierarchically organized; for every ubiquitin-activating enzyme, there are several ubiquitin-conjugating enzymes, and most ubiquitin ...
Szczepanowski, R. +2 more
openaire +3 more sources
Interplay between the Ubiquitin Proteasome System and Ubiquitin-Mediated Autophagy in Plants
Cells, 2020 All eukaryotes rely on the ubiquitin-proteasome system (UPS) and autophagy to control the abundance of key regulatory proteins and maintain a healthy intracellular environment. In the UPS, damaged or superfluous proteins are ubiquitinated and degraded in
Tong Su +4 more
doaj +1 more source
Targeting the ubiquitin system by fragment-based drug discovery
Frontiers in Molecular Biosciences, 2022 The ubiquitin system contains a wealth of potential drug targets for many diseases and conditions, including neurodegenerative, immune, metabolic and developmental diseases, as well as multiple cancers.
Cassandra Kennedy +2 more
doaj +1 more source