Results 21 to 30 of about 77,898 (323)

Inactivating UBE2M impacts the DNA damage response and genome integrity involving multiple cullin ligases. [PDF]

PLoS ONE, 2014
Protein neddylation is involved in a wide variety of cellular processes. Here we show that the DNA damage response is perturbed in cells inactivated with an E2 Nedd8 conjugating enzyme UBE2M, measured by RAD51 foci formation kinetics and cell based DNA ...
Scott Cukras, Nicholas Morffy, Takbum Ohn, Younghoon Kee   +3 more
doaj   +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, Julia Fux, Evan Mallette, Nathaniel Petersen, Wei Zhang   +4 more
doaj   +1 more source

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

Thoracic 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, Yuxin Wang, Yuan Cui, Zhike Chen, Yu Li, Jian Yang, Yang Yang, Tengfei Chen, Dian Xia, Chang Li, Chun Xu, Cheng Ding, Jun Zhao   +12 more
doaj   +1 more source

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

Frontiers 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, Haiqi Xu, Jiaqi Xu, Saien Lu, Shilong You, Xinyue Huang, Naijin Zhang, Lijun Zhang   +7 more
doaj   +1 more source

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

, 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, Arabshahi, Bebenek, Begley, Bellacosa, Blondal, Blondal, Cherepanov, Cherepanov, Clepet, Della, Desmond R. Bullard, Doherty, Engler, Fareed, Higgins, Ho, Ho, Kaufmann, Keppetipola, Kornberg, Kuhn, Lavesa-Curto, Lehman, Markham, Martins, Martins, Miller, Moore, Nandakumar, Nandakumar, Nandakumar, Nick McElhinny, Omari, Pascal, Pitcher, Pitcher, Richard P. Bowater, Rossi, Ruiz, Runnels, Rydberg, Sambrook, Sekiguchi, Shuman, Shuman, Snopek, Sriskanda, Stuart, Timson, Tomkinson, Wang, Wang, Weiss, Wilkinson, Wilkinson, Wilkinson, Wood, Wood, Worthey, Yin, Yin   +61 more
core   +4 more sources

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

PLoS 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, Melanie Gonzalez, Marie-Helene Miquel Kabbaj, Akash Gunjan   +3 more
doaj   +1 more source

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

, 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, Alexandra Bonner, Altschul, Andrew Hemmings, Andrew Smith, Baer, Bork, Brotz-Oesterhelt, Callebaut, Derbyshire, Dermody, Desmond Bullard, Doherty, Doherty, Doherty, Feng, Gajiwala, Georlette, Georlette, Glover, Gong, Grawunder, Guex, Gunther, Halligan, Heather Sayer, Herrmann, Huyton, Jeon, Joo, Kaczmarek, Kodama, Krishnan, Lavesa-Curto, Lee, Legrain, Lehman, Manuel Lavesa-Curto, Masson, Odell, Pascal, Richard Bowater, Sambrook, Shuman, Singleton, Sriskanda, Sriskanda, Sriskanda, Sriskanda, Subramanya, Timson, Timson, Wieland, Wilkinson, Wilkinson, Williams, Yamane, Yamane, Zhang, Zimmerman   +59 more
core   +1 more source

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

, 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., Brzostek, Anna, Dziadek, Jarosław, Korycka-Machala, Malgorzata, Rumijowska-Galewicz, Anna, Rychta, Ewelina, Sayer, Heather R.   +6 more
core   +2 more sources

CRL Ubiquitin Ligases and DNA Damage Response

Frontiers 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

Mammalian DNA ligases. Catalytic domain and size of DNA ligase I. [PDF]

Journal of Biological Chemistry, 1990
DNA ligase I is the major DNA ligase activity in proliferating mammalian cells. The protein has been purified to apparent homogeneity from calf thymus. It has a monomeric structure and a blocked N-terminal residue. DNA ligase I is a 125-kDa polypeptide as estimated by sodium dodecyl sulfate-gel electrophoresis and by gel chromatography under denaturing
Dana D. Lasko, Tomas Lindahl, Alan E. Tomkinson, Graham Daly   +3 more
openaire   +2 more sources