Results 41 to 50 of about 77,894 (293)
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
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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
Developing as assay to screen inhibitors for various ATP-dependent ligases [PDF]
, 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.
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SUMO chain-induced dimerization activates RNF4 [PDF]
, 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
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Cereblon versus VHL: Hijacking E3 Ligases Against Each Other Using PROTACs [PDF]
, 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
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BMC 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
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Functional analysis of proteasome-associated ubiquitin ligases in plants [PDF]
, 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
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SUMO-targeted ubiquitin ligases [PDF]
, 2014 Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability
Dohmen, R. Jürgen +1 more
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Molecular Medicine, 2023 The homologous to the E6-AP carboxyl terminus (HECT)-type E3 ubiquitin ligases are the selective executers in the protein ubiquitination, playing a vital role in modulation of the protein function and stability. Evidence shows the regulatory role of HECT-
Rui Zhang, Shaoqing Shi
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The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]
, 2013 Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
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