Results 31 to 40 of about 79,069 (319)

Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity

open access: yesBiomolecules, 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

Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae. [PDF]

open access: yesPLoS ONE, 2012
Core histone proteins are essential for packaging the genomic DNA into chromatin in all eukaryotes. Since multiple genes encode these histone proteins, there is potential for generating more histones than what is required for chromatin assembly.
Rakesh Kumar Singh   +3 more
doaj   +1 more source

The regulatory roles of the E3 ubiquitin ligase NEDD4 family in DNA damage response

open access: yesFrontiers in Physiology, 2022
E3 ubiquitin ligases, an important part of ubiquitin proteasome system, catalyze the covalent binding of ubiquitin to target substrates, which plays a role in protein ubiquitination and regulates different biological process. DNA damage response (DDR) is
Xinxin Lu   +7 more
doaj   +1 more source

Direct comparison of nick-joining activity of the nucleic acid ligases from bacteriophage T4 [PDF]

open access: yes, 2006
The genome of bacteriophage T4 encodes three polynucleotide ligases, which seal the backbone of nucleic acids during infection of host bacteria. The T4Dnl (T4 DNA ligase) and two RNA ligases [T4Rnl1 (T4 RNA ligase 1) and T4Rnl2] join a diverse array of ...
Amitsur   +61 more
core   +4 more sources

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

open access: yesDNA Repair, 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 to impaired but not ablated activity.
Penny A. Jeggo   +5 more
openaire   +3 more sources

Comprehensive analysis of the expression and prognosis for RBR E3 ubiquitin ligases in lung adenocarcinoma

open access: yesThoracic Cancer, 2022
Background Lung adenocarcinoma (LUAD) is the most common subtype of non‐small cell lung cancer and has a poor prognosis. RBR E3 ubiquitin ligases are a special class of E3 ubiquitin ligases which contain three zinc‐bing domains that catalyze ubiquitin to
Hao Ding   +12 more
doaj   +1 more source

Analysis of ligation and DNA binding by Escherichia coli DNA ligase (LigA). [PDF]

open access: yes, 2005
NAD+-dependent DNA ligases are essential enzymes in bacteria, with the most widely studied of this class of enzymes being LigA from Escherichia coli. NAD+-dependent DNA ligases comprise several discrete structural domains, including a BRCT domain at the ...
Adam Wilkinson   +59 more
core   +1 more source

Evaluation of NAD(+)-dependent DNA ligase of mycobacteria as a potential target for antibiotics [PDF]

open access: yes, 2007
Mycobacteria contain genes for several DNA ligases, including ligA, which encodes a NAD+-dependent enzyme that has been postulated to be a target for novel antibacterial compounds.
Bowater, Richard P.   +6 more
core   +2 more sources

CRL Ubiquitin Ligases and DNA Damage Response

open access: yesFrontiers in Oncology, 2012
Cullin/RING ubiquitin ligases (CRL) comprise the largest subfamily of ubiquitin ligases and are involved in various biological processes. One of the main functions of CRLs is to regulate DNA damage response, a fundamental signaling cascade to maintain ...
Jianping eJin, Ju-Mei eLi
doaj   +1 more source

The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]

open access: yes, 2018
Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren   +4 more
core   +1 more source

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