Results 51 to 60 of about 153,107 (330)

Developing as assay to screen inhibitors for various ATP-dependent ligases [PDF]

open access: yes, 2009
DNA ligases (EC.6.5.1.1) are key enzymes that catalyze the formation of phosphodiester bonds at single-stranded or double-stranded breaks between adjacent 5’-PO4 and 3’-OH groups of DNA. These enzymes are essential guardians of genomic integrity and have
Kaur, L.
core   +1 more source

New classes of E3 ligases illuminated by chemical probes [PDF]

open access: yes, 2022
Specificity in the ubiquitin system depends on E3 ligases, largely belonging to a handful of families discovered more than a decade ago. However, the last two years brought a quantum leap in the identification and/or mechanistic characterization of ...
Horn-Ghetko, D., Schulman, B.
core   +1 more source

SUMO chain-induced dimerization activates RNF4 [PDF]

open access: yes, 2014
Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Hay, Ronald T   +5 more
core   +1 more source

HECT E3 ubiquitin ligases – emerging insights into their biological roles and disease relevance

open access: yesJournal of Cell Science, 2020
Homologous to E6AP C-terminus (HECT) E3 ubiquitin ligases play a critical role in various cellular pathways, including but not limited to protein trafficking, subcellular localization, innate immune response, viral infections, DNA damage responses and ...
Yaya Wang   +4 more
semanticscholar   +1 more source

Cereblon versus VHL: Hijacking E3 Ligases Against Each Other Using PROTACs [PDF]

open access: yes, 2019
The von Hippel-Lindau (VHL) and cereblon (CRBN) proteins are substrate recognition subunits of two ubiquitously expressed and biologically important Cullin RING E3 ubiquitin ligase complexes.
Chiara, Maniaci   +4 more
core   +1 more source

Classification of barley U-box E3 ligases and their expression patterns in response to drought and pathogen stresses

open access: yesBMC Genomics, 2019
Background Controlled turnover of proteins as mediated by the ubiquitin proteasome system (UPS) is an important element in plant defense against environmental and pathogen stresses.
Moon Young Ryu   +11 more
doaj   +1 more source

Regulating Nrf2 activity: ubiquitin ligases and signaling molecules in redox homeostasis.

open access: yesTIBS -Trends in Biochemical Sciences. Regular ed
Transcription factor NF-E2 p45-related factor 2 (Nrf2) orchestrates defenses against oxidants and thiol-reactive electrophiles. It is controlled at the protein stability level by several E3 ubiquitin ligases (CRL3Keap1, CRL4DCAF11, SCFβ-TrCP, and Hrd1 ...
John D. Hayes   +2 more
semanticscholar   +1 more source

E3 Ubiquitin Ligases in Signaling, Disease, and Therapeutics

open access: yesTIBS -Trends in Biochemical Sciences. Regular ed
The ubiquitin–proteasome system (UPS) is a central regulator of protein turnover and signaling, with E3 ubiquitin ligases conferring substrate specificity and chain-type control.
Pirouz Ebadi   +2 more
semanticscholar   +1 more source

Functional analysis of proteasome-associated ubiquitin ligases in plants [PDF]

open access: yes, 2022
Degradation of intracellular proteins by the ubiquitin-proteasome system (UPS) is a sophisticated mechanism that begins with anchoring ubiquitin molecules to a substrate and ends with proteasome-dependent proteolysis.
Wang, Zhishuo
core   +1 more source

MAMMALIAN DNA LIGASES [PDF]

open access: yesAnnual Review of Biochemistry, 1992
DNA LIGASE I .... ... ....... ...... . . . . . .. . . . .. ........ . 255 Structure. . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 255 Gene Structure and Chromosome Mapping . . . . ......... . . . . . .. . . . . .
T, Lindahl, D E, Barnes
openaire   +2 more sources

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