Results 41 to 50 of about 129,362 (255)

Strategies to Target Specific Components of the Ubiquitin Conjugation/Deconjugation Machinery

Frontiers in Chemistry, 2020
The regulation of ubiquitination status in the cell is controlled by ubiquitin ligases acting in tandem with deubiquitinating enzymes. Ubiquitination controls many key processes in the cell from division to death making its tight regulation key to ...
Neil C. Taylor, Joanna F. McGouran
doaj   +1 more source

E3-ubiquitin ligases and recent progress in osteoimmunology

Frontiers in Immunology, 2023
Ubiquitin-mediated proteasomal degradation is a post-transcriptional protein modification that is comprised of various components including the 76-amino acid protein ubiquitin (Ub), Ub-activating enzyme (E1), Ub-conjugating enzyme (E2), ubiquitin ligase (
Yosuke Asano, Yoshinori Matsumoto, Yoshinori Matsumoto, Jun Wada, Robert Rottapel, Robert Rottapel, Robert Rottapel, Robert Rottapel, Robert Rottapel   +8 more
doaj   +1 more source

Temperature dependence of circular DNA topological states [PDF]

PHYSICAL REVIEW E 79, 041926 (2009), 2009
Circular double stranded DNA has different topological states which are defined by their linking numbers. Equilibrium distribution of linking numbers can be obtained by closing a linear DNA into a circle by ligase. Using Monte Carlo simulation, we predict the temperature dependence of the linking number distribution of small circular DNAs.
arxiv   +1 more source

Role of RING-Type E3 Ubiquitin Ligases in Inflammatory Signalling and Inflammatory Bowel Disease

Mediators of Inflammation, 2020
Ubiquitination is a three-step enzymatic cascade for posttranslational protein modification. It includes the ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3).
Liguo Zhu, Ying Li, Longyuan Zhou, Guang Yang, Ying Wang, Jing Han, Li Li, Shenghong Zhang   +7 more
doaj   +1 more source

Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]

PLoS ONE, 2013
The ubiquitin-signaling pathway utilizes E1 activating, E2 conjugating, and E3 ligase enzymes to sequentially transfer the small modifier protein ubiquitin to a substrate protein.
Donald E Spratt, Pascal Mercier, Gary S Shaw   +2 more
doaj   +1 more source

Randomness and optimality in enhanced DNA ligation with crowding effects [PDF]

Phys. Rev. Research 2, 013360 (2020), 2019
Enzymatic ligation is essential for the synthesis of long DNA. However, the number of ligated products exponentially decays as the DNA synthesis proceeds in a random manner. The controlling of ligation randomness is of importance to suppress exponential decay and demonstrate an efficient synthesis of long DNA. Here, we report the analysis of randomness
arxiv   +1 more source

Arabidopsis EIN3-binding F-box 1 and 2 form ubiquitin-protein ligases that repress ethylene action and promote growth by directing EIN3 degradation.

Proceedings of the National Academy of Sciences of the United States of America, 2004
Ubiquitination of various intracellular proteins by ubiquitin-protein ligases (or E3s) plays an essential role in eukaryotic cell regulation primarily through its ability to selectively target proteins for degradation by the 26S proteasome. Skp1, Cullin,
J. Gagne, Jan A. Smalle, D. Gingerich, Joseph M. Walker, S. Yoo, S. Yanagisawa, R. Vierstra   +6 more
semanticscholar   +1 more source

PRKN (arkin RBR E3 ubiquitin protein ligase ) [PDF]

Atlas of Genetics and Cytogenetics in Oncology and Haematology, 2018
PARK2 (also known as Parkin RBR E3 ubiquitin protein ligase) is one of the largest genes in our genome. It undergoes an extensive alternative splicing both at transcript and protein level, producing multiple transcript variants and distinct protein isoforms.
La, Cognata, Valentina, Cavallaro, Sebastiano   +1 more
openaire   +2 more sources

Biochemical function of typical and variant Arabidopsis thaliana U-box E3 ubiquitin-protein ligases.

Biochemical Journal, 2008
The variance of the U-box domain in 64 Arabidopsis thaliana (thale cress) E3s (ubiquitin-protein ligases) was used to examine the interactions between E3s and E2s (ubiquitin-conjugating enzymes).
Jakob Wiborg, C. O'Shea, K. Skriver
semanticscholar   +1 more source

Binding Sites of Ubiquitin-Protein Ligase

Journal of Biological Chemistry, 1989
It was found previously that the enzyme ubiquitin-protein ligase (E3) contains specific protein substrate binding sites that are responsible for the selection of proteins for degradation by the ubiquitin system. In the present study, we have tried to gain more insight into the mode of action of E3 by the characterization of other binding sites of this ...
Avram Hershko, Hannah Heller, Yuval Reiss   +2 more
openaire   +3 more sources