Results 11 to 20 of about 617,710 (283)

Evidence for a particulate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in rabbit brain.

open access: yesJournal of Biological Chemistry, 1991
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
core   +7 more sources

Ubiquitin conjugating enzymes participate in polyglutamine protein aggregation [PDF]

open access: yesBMC Cell Biology, 2007
Background Protein aggregation is a hallmark of several neurodegenerative diseases including Huntington's disease and Parkinson's disease. Proteins containing long, homopolymeric stretches of glutamine are especially prone to form aggregates. It has long
Caldwell Guy A   +7 more
doaj   +2 more sources

lemmingA encodes the Apc11 subunit of the APC/C in Drosophila melanogaster that forms a ternary complex with the E2-C type ubiquitin conjugating enzyme, Vihar and Morula/Apc2 [PDF]

open access: yes, 2012
Background: Ubiquitin-dependent protein degradation is a critical step in key cell cycle events, such as metaphase-anaphase transition and mitotic exit.
Pal, Margit   +6 more
core   +5 more sources

Quantitative proteome dataset profiling of UBC4 and UBC5 deletion strains in Saccharomyces cerevisiae

open access: yesData in Brief, 2022
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   +1 more source

Targeting neddylation E2s: a novel therapeutic strategy in cancer

open access: yesJournal of Hematology & Oncology, 2021
Ubiquitin-conjugating enzyme E2 M (UBE2M) and ubiquitin-conjugating enzyme E2 F (UBE2F) are the two NEDD8-conjugating enzymes of the neddylation pathway that take part in posttranslational modification and change the activity of target proteins.
Yi-Chao Zheng   +6 more
doaj   +1 more source

Robust high-throughput assays to assess discrete steps in ubiquitination and related cascades

open access: yesBMC Molecular and Cell Biology, 2020
Background Ubiquitination and ubiquitin-like protein post-translational modifications play an enormous number of roles in cellular processes. These modifications are constituted of multistep reaction cascades.
Gabriel Fenteany   +5 more
doaj   +1 more source

Mechanism and Disease Association With a Ubiquitin Conjugating E2 Enzyme: UBE2L3

open access: yesFrontiers in Immunology, 2022
Ubiquitin conjugating enzyme E2 is an important component of the post-translational protein ubiquitination pathway, which mediates the transfer of activated ubiquitin to substrate proteins.
Xiaoxia Zhang   +7 more
doaj   +1 more source

Creation of a Pluripotent Ubiquitin-Conjugating Enzyme [PDF]

open access: yesMolecular and Cellular Biology, 2001
We describe the creation of a pluripotent ubiquitin-conjugating enzyme (E2) generated through a single amino acid substitution within the catalytic domain of RAD6 (UBC2). This RAD6 derivative carries out the stress-related function of UBC4 and the cell cycle function of CDC34 while maintaining its own DNA repair function.
C, Ptak   +5 more
openaire   +2 more sources

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