Temperature adaptation of DNA ligases from psychrophilic organisms [PDF]
, 2019 DNA ligases operating at low temperatures have potential advantages for use in biotechnological applications. For this reason, we have characterized the temperature optima and thermal stabilities of three minimal Lig E-type ATP-dependent DNA ligase ...
Williamson, Adele Kim +2 more
core +1 more source
Regulation of SCF Ubiquitin Ligases by Jab1/Csn5 and the Cop9 Signalosome [PDF]
, 2006 SCF ubiquitin ligases regulate the ubiquitin-dependent proteolysis of a myriad of substrate proteins, including p27, Cyclin E, and IkBa. To further gain insight into SCF regulation and function, we purified SCF from mammalian cells and found the Cop9 ...
Cope, Gregory Allan
core +1 more source
Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity
Biomolecules, 2022 In recent years, researchers have leveraged the ubiquitin-proteasome system (UPS) to induce selective degradation of proteins by E3 ubiquitin ligases, which has great potential as novel therapeutics for human diseases, including cancer and ...
Bayonle Aminu +4 more
doaj +1 more source
Ubiquitin ligases in cancer: functions and clinical potentials
Cell Chemical Biology, 2021 Ubiquitylation, a highly regulated post-translational modification, controls many cellular pathways that are critical to cell homeostasis. Ubiquitin ligases recruit substrates and promote ubiquitin transfer onto targets, inducing proteasomal degradation ...
Shanshan Duan, M. Pagano
semanticscholar +1 more source
Characterisation of ATP-Dependent Mur Ligases Involved in the Biogenesis of Cell Wall Peptidoglycan in Mycobacterium tuberculosis [PDF]
, 2013 ATP-dependent Mur ligases (Mur synthetases) play essential roles in the biosynthesis of cell wall peptidoglycan (PG) as they catalyze the ligation of key amino acid residues to the stem peptide at the expense of ATP hydrolysis, thus representing ...
Nicholas H Keep +29 more
core +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 +7 more
doaj +1 more source
A capsid-encoded PPxY-motif facilitates adenovirus entry. [PDF]
, 2010 Viruses use cellular machinery to enter and infect cells. In this study we address the cell entry mechanisms of nonenveloped adenoviruses (Ads). We show that protein VI, an internal capsid protein, is rapidly exposed after cell surface attachment and ...
Segura-Morales, Carolina +28 more
core +1 more source
Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases [PDF]
, 2023 The acetylation-dependent (Ac/)N-degron pathway degrades proteins through recognition of their acetylated N-termini (Nt) by E3 ligases called Ac/N-recognins. To date, specific Ac/N-recognins have not been defined in plants.
Bailey, Mark +30 more
core +1 more source
Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
Frontiers in Plant Science, 2021 Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses.
Souleimen Jmii, Laurent Cappadocia
doaj +1 more source
NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
Current Opinion in Structural Biology, 2020 RING E3s comprise the largest family of ubiquitin (UB) and ubiquitin-like protein (UBL) ligases. RING E3s typically promote UB or UBL transfer from the active site of an associated E2 enzyme to a distally-recruited substrate.
K. Baek, D. C. Scott, B. Schulman
semanticscholar +1 more source