Results 11 to 20 of about 39,918 (341)

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   +3 more sources

Creation of a Pluripotent Ubiquitin-Conjugating Enzyme [PDF]

open access: greenMolecular 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.
Christopher P. Ptak   +5 more
openalex   +4 more sources

The lysine deprotonation mechanism in a ubiquitin conjugating enzyme [PDF]

open access: goldThe Journal of Physical Chemistry B
Ubiquitination is a biochemical reaction in which a small protein, ubiquitin (Ub), is covalently linked to a lysine on a target protein. This type of post-translational modification can signal for protein degradation, DNA repair, or inflammation response.
Alexis J. Wathan   +3 more
openalex   +3 more sources

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

open access: yes, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
A Arrigoni   +104 more
core   +14 more sources

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

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

open access: yesBiochemistry, 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   +4 more
openaire   +2 more sources

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

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

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