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The ubiquitin-proteasome system is required for African swine fever replication. [PDF]
Several viruses manipulate the ubiquitin-proteasome system (UPS) to initiate a productive infection. Determined viral proteins are able to change the host's ubiquitin machinery and some viruses even encode their own ubiquitinating or deubiquitinating ...
Lucía Barrado-Gil+4 more
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Structural Diversity of Ubiquitin E3 Ligase
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
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Conjugate ubiquitin was previously found in the nucleus, cytoplasm, and membranes of eukaryotic cells while the enzymes of the ubiquitin-conjugating system appear to be cytoplasmic. We have prepared the mitochondrial fraction from rabbit brain by discontinuous density gradient ultracentrifugation and by Western blotting, using a specific antibody ...
MAGNANI, MAURO+4 more
openaire +5 more sources
An Allosteric Inhibitor of the Human Cdc34 Ubiquitin-Conjugating Enzyme [PDF]
In the ubiquitin-proteasome system (UPS), E2 enzymes mediate the conjugation of ubiquitin to substrates and thereby control protein stability and interactions. The E2 enzyme hCdc34 catalyzes the ubiquitination of hundreds of proteins in conjunction with the cullin-RING (CRL) superfamily of E3 enzymes.
Xiaojing Tang+29 more
openaire +3 more sources
The Ubiquitin-Proteasome System (UPS) regulates many cellular processes in eukaryotic cells. Ubiquitylation by the UPS mainly directs proteins to proteasomal degradation, but it can also have non-degradative functions, such as regulating protein activity
Valentina Rossio, Joao A Paulo
doaj
TULIP2: An Improved Method for the Identification of Ubiquitin E3-Specific Targets
Protein modification by Ubiquitin or Ubiquitin-like modifiers is mediated by an enzyme cascade composed of E1, E2, and E3 enzymes. E1s, or ubiquitin-activating enzymes, perform ubiquitin activation. Next, ubiquitin is transferred to ubiquitin-conjugating
Daniel Salas-Lloret+2 more
doaj +1 more source
The HIP2~ubiquitin conjugate forms a non-compact monomeric thioester during di-ubiquitin synthesis. [PDF]
Polyubiquitination is a post-translational event used to control the degradation of damaged or unwanted proteins by modifying the target protein with a chain of ubiquitin molecules.
Benjamin W Cook+3 more
doaj +1 more source
BackgroundProtein ubiquitination is a ubiquitous mechanism in eukaryotes. In Arabidopsis, ubiquitin modification is mainly mediated by two ubiquitin activating enzymes (E1s), 37 ubiquitin conjugating enzymes (E2s), and more than 1300 predicted ubiquitin ...
Abdelaziz Ramadan+6 more
semanticscholar +1 more source
UBE2G1 governs the destruction of cereblon neomorphic substrates
The cereblon modulating agents (CMs) including lenalidomide, pomalidomide and CC-220 repurpose the Cul4-RBX1-DDB1-CRBN (CRL4CRBN) E3 ubiquitin ligase complex to induce the degradation of specific neomorphic substrates via polyubiquitination in ...
Gang Lu+17 more
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