Results 21 to 30 of about 107,368 (305)

Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]

open access: yes, 2012
Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone   +2 more
core   +2 more sources

Thermostable DNA ligases from hyperthermophiles in biotechnology

open access: yesFrontiers in Microbiology, 2023
DNA ligase is an important enzyme ubiquitous in all three kingdoms of life that can ligate DNA strands, thus playing essential roles in DNA replication, repair and recombination in vivo.
Jingru Shi   +3 more
doaj   +1 more source

Ubiquitin-protein ligases [PDF]

open access: yesJournal of Cell Science, 2004
Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
P A, Robinson, H C, Ardley
openaire   +2 more sources

Bacterial DNA ligases [PDF]

open access: yesMolecular Microbiology, 2001
DNA ligases join breaks in the phosphodiester backbone of DNA molecules and are used in many essential reactions within the cell. All DNA ligases follow the same reaction mechanism, but they may use either ATP or NAD+ as a cofactor. All Bacteria (eubacteria) contain NAD+‐dependent DNA ligases, and the uniqueness of these enzymes to Bacteria makes them ...
Wilkinson, A, Day, J, Bowater, R
openaire   +3 more sources

DNA Ligase I, the Replicative DNA Ligase [PDF]

open access: yes, 2012
Multiple DNA ligation events are required to join the Okazaki fragments generated during lagging strand DNA synthesis. In eukaryotes, this is primarily carried out by members of the DNA ligase I family. The C-terminal catalytic region of these enzymes is composed of three domains: a DNA binding domain, an adenylation domain and an OB-fold domain.
Timothy R L, Howes, Alan E, Tomkinson
openaire   +2 more sources

E3-ligase knock down revealed differential titin degradation by autopagy and the ubiquitin proteasome system

open access: yesScientific Reports, 2021
The sarcomere protein titin is a major determinant of cardiomyocyte stiffness and ventricular distensibility. The constant mechanical stress on titin requires well-controlled protein quality control, the exact mechanisms of which have not yet been fully ...
Erik Müller   +5 more
doaj   +1 more source

Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins

open access: yesFrontiers in Immunology, 2021
Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins.
Haoran Cui   +7 more
doaj   +1 more source

Expanding PROTACtable genome universe of E3 ligases

open access: yesNature Communications, 2023
Proteolysis-targeting chimera (PROTAC) and other targeted protein degradation (TPD) molecules that induce degradation by the ubiquitin-proteasome system (UPS) offer new opportunities to engage targets that remain challenging to be inhibited by ...
Yuan Liu   +9 more
doaj   +1 more source

The role of Schizosaccharomyces pombe SUMO ligases in genome stability [PDF]

open access: yes, 2007
SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is ...
A. Skilton   +44 more
core   +2 more sources

Identification of a novel motif in DNA ligases exemplified by DNA ligase IV [PDF]

open access: yes, 2006
DNA ligase IV is an essential protein that functions in DNA non-homologous end-joining, the major mechanism that rejoins DNA double-strand breaks in mammalian cells. LIG4 syndrome represents a human disorder caused by mutations in DNA ligase IV that lead
Doherty, Aidan J   +5 more
core   +1 more source

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