Results 1 to 10 of about 27,627 (205)

The role of ubiquitin-conjugating enzyme in the process of spermatogenesis. [PDF]

Reprod Biol Endocrinol
The ubiquitination is crucial for controlling cellular homeostasis and protein modification, in which ubiquitin-conjugating enzyme (E2) acts as the central player in the ubiquitination system. Ubiquitin-conjugating enzymes, which have special domains that catalyse substrates, have sequence discrepancies and modulate various pathophysiological processes
Lv P, Liu J, Liu X.
europepmc   +4 more sources

Ubiquitin-conjugating enzyme E2C (UBE2C) is a prognostic indicator for cholangiocarcinoma. [PDF]

Eur J Med Res, 2023
AbstractCholangiocarcinoma is the most common malignant bile duct tumor in Southeast Asia. The special location of cholangiocarcinoma leads to it being difficult to diagnose. Currently, the progress in clinical prognosis outcomes remains abysmal owing to the lack of definitive diagnostic criteria.
Ong KH, Lai HY, Sun DP, Chen TJ, Huang SK, Tian YF, Chou CL, Shiue YL, Chan TC, Li CF, Kuo YH.   +10 more
europepmc   +5 more sources

Ubiquitin-Conjugating Enzymes in Cancer [PDF]

Cells, 2021
The ubiquitin-mediated degradation system is responsible for controlling various tumor-promoting processes, including DNA repair, cell cycle arrest, cell proliferation, apoptosis, angiogenesis, migration and invasion, metastasis, and drug resistance.
Quyen Thu Bui, Jeong Hee Hong, Minseok Kwak, Ji Yeon Lee, Peter Chang-Whan Lee   +4 more
openaire   +5 more sources

Creation of a Pluripotent Ubiquitin-Conjugating Enzyme [PDF]

Molecular 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, Chantelle Gwozd, J. Torin Huzil, Todd J. Gwozd, Grace Garen, Michael J. Ellison   +5 more
openalex   +4 more sources

Preferential Interaction of Sentrin with a Ubiquitin-conjugating Enzyme, Ubc9 [PDF]

Journal of Biological Chemistry, 1997
Sentrin is a ubiquitin-like molecule that has been shown to interact with the death domains of Fas and tumor necrosis factor receptor 1 (TNFR1), PML, Rad51, Rad52, and RanGAP1. We have reported previously that sentrin can be conjugated to other proteins in a manner analogous to protein ubiquitination (Kamitani, T., Nguyen, H. P., and Yeh, E. T.
Limin Gong, Tetsu Kamitani, Kenichi Fujise, Laura S. Caskey, Edward T.H. Yeh   +4 more
openalex   +4 more sources

Cyclization of Polyubiquitin by the E2-25K Ubiquitin Conjugating Enzyme [PDF]

Journal of Biological Chemistry, 2000
For most substrates of ubiquitin (Ub)-dependent degradation, recognition by the proteasome is mediated by a covalently attached signal assembled from multiple ubiquitins linked to each other via the C terminus of one Ub and the epsilon-amine of Lys(48) of another Ub.
Tingting Yao, Robert E. Cohen
openalex   +4 more sources

Regulation of lysosome integrity and lysophagy by the ubiquitin-conjugating enzyme UBE2QL1. [PDF]

Autophagy, 2020
Lysosomal membrane permeabilization or full rupture of lysosomes is a common and severe stress condition that is relevant for degenerative disease, infection and cancer. Cells respond with extensive ubiquitination of damaged lysosomes, which triggers selective macroautophagy/autophagy of the whole organelle, termed lysophagy.
Kravic B, Behrends C, Meyer H.
europepmc   +6 more sources

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

Biochemistry, 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
Rachel E. Klevit, Jonathan N. Pruneda, Peter S. Brzovic, Kate E. Stoll, Laura Bolton   +4 more
openaire   +3 more sources

Solution Structure of the Ubiquitin-conjugating Enzyme UbcH5B [PDF]

Journal of Molecular Biology, 2004
The ubiquitination pathway is the main pathway for protein degradation in eukaryotic cells. The attachment of ubiquitin to a substrate protein is catalyzed by three types of enzymes, namely a ubiquitin activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3). Here, the structure of the human ubiquitin-conjugating enzyme (
Houben, K, Dominguez, C, van Schaik FM, Timmers, HT, Bonvin, AM, Boelens, R   +5 more
openaire   +6 more sources

Determinants of Functionality in the Ubiquitin Conjugating Enzyme Family [PDF]

Structure, 2004
The E2 enzymes are key enzymes in the ubiquitin and ubiquitin-like protein ligation pathways. To understand the functionality of the different E2 enzymes, we analyzed 190 protein sequences and 211 structures and electrostatic potentials. Key findings include: The ScUbc1 orthologs are defined by a C-terminal UBA domain. An N-terminal sequence motif that
Peter J. Winn, Amit Banerjee, James N.D. Battey, Tomasz L. Religa, Rebecca C. Wade   +4 more
openaire   +3 more sources