Background and activities

Education, training, experience

Research interests

We are working to determine how mutations in DNA repair genes result in disease

DNA in our cells is constantly damaged by internal and external factors. To maintain genomic stability, the cells developed multiple DNA repair pathways. Mutations in DNA repair genes lead to disorders in human. Non-Homologous DNA End-Joining (NHEJ) fixes the DNA double strand breaks (DSB) throughout the cell cycle. NHEJ is required for development of immune and nervous systems and to suppress various cancers.

NHEJ includes core factors Ku70, Ku80, XRCC4 and Ligase 4. There are also accessory factors such as DNA-PKcs, Artemis, XLF/Cernunnos, XLS/PAXX, APLF. We are looking for new NHEJ factors as well.

In response to DNA damage, there is a complex process that include activation of multiple enzymes and modifications of proteins, including the histones surrounding the DSBs. This process is called DNA damage response (DDR) pathway. It includes protein kinases ATM and DNA-PKcs, scaffold proteins MDC1 and 53BP1, ubiquitin-ligases RNF8 and RNF168, and many other proteins. During the DDR, histones are phosphorylated, ubiquitilated, methylated, acetylated, SUMOylated, NEDDylated etc (Nature, 2011; PNAS, 2012a; PNAS, 2012b; PLoS Genetics, 2013; DNA repair, 2014; DNA repair, 2017). We are attempting to understand the complexity of DDR, as well as its role in development of immune and nervous systems, and in cancer suppression.

Both NHEJ and DDR pathways are involved in immune system development, including the V(D)J recombination in developing B and T lymphocytes, and the Class Switch Recombination (CSR) in mature B cells (Nature, 2011; PNAS, 2012a; PNAS, 2012b; PNAS, 2013; DNA repair, 2014).


Projects in my group are funded by Young Research Talent grant from Research Council of Norway, Norwegian Cancer Society and the joined program of the Health Authority of Central Norway - NTNU.

We are working on the following projects:

Grants, Fellowships and Awards

Research group

Currently my team includes


  • Kimiko Teyama, Medical exchange student from Oita University, Japan (Currently: Oita University, Japan)
  • Alisa Dewan, MSc student, Molecular Medicine, NTNU (Project score A. Currently: University of Oslo)
  • Stefano Bradamante, BSc, Stuff Engineer (Currently: Engineer at Comparative Medicine, NTNU)

Invited presentations and lectures

  • 2017: NTNU-KAIST Symposium "Molecular mechanisms underlying carcinogenesis and neurodegeneration", Trondheim, Norway
  • 2017: DNA and RNA dynamics workshop, Trondheim, Norway (organizer, chairman, speaker)
  • 2017: Norwegian Biochemical Society meeting, Oppdale, Norway
  • 2017: Norwegian Biochemical Society meeting, Gol, Norway
  • 2016: Symposium "DNA repair, Epigenetics and Translational medicine", Trondheim, Norway
  • 2016: European Commission, final interview of ERC starting grant, Brussels, Belgium
  • 2016: Norwegian Biochemical Society meeting, Åre, Sweden
  • 2016: Helsinki University, Biomedicum Helsinki Seminar, Finland
  • 2016: Norwegian Biochemical Society Annual Meeting, Tromsø, Norway
  • 2016: NTNU, Trondheim, Norway
  • 2015: Tomas Lindahl conference on DNA Repair, Oslo, Norway

Tips for grad students:



The full list of publications can be found at:

Dewan A, Xing M, Lundbæk MB, Gago‐Fuentes R, Beck C, Aas PA, Liabakk NB, Sæterstad S, Phong C, Kavli B, Oksenych V. (2018). Robust DNA repair in PAXX‐deficient mammalian cells. FEBS Open Bio (accepted)

Gago‐Fuentes R, Xing M, Sæterstad S, Sarno A, Dewan A, Beck C, Bradamante S, Bjørås M, Oksenych V. (2018). Normal development of mice lacking PAXX, the paralogue of XRCC4 and XLF. FEBS Open Bio (accepted)

Xing M, Bjørås M, Daniel JA, Alt FW, Oksenych V. (2017) Synthetic lethality between murine DNA repair factors XLF and DNA-PKcs is rescued by inactivation of Ku70. DNA Repair (Amst.) 57: 133-138

Bulanova D et al. (2017) Antiviral Properties of Chemical Inhibitors of Cellular Anti-Apoptotic Bcl-2 Proteins. Viruses 9(10). pii: E271

Kumar V, Alt FW, Oksenych V.* (2014) Functional overlaps between XLF and the ATM-dependent DNA double strand break response**. DNA Repair (Amst.) 16:11-22

Oksenych V, Zhovmer A, Ziani S, Mari PO, Eberova J, Nardo T, Stefanini M, Giglia-Mari G, Egly JM, Coin F. (2013) Histone methyltransferase DOT1L drives recovery of gene expression after a genotoxic attack. PLoS Genet 9(7):e1003611

Oksenych V, Kumar V, Liu X, Guo C, Schwer B, Zha S, Alt FW. (2013) Functional redundancy between the XLF and DNA-PKcs DNA repair factors in V(D)J recombination and nonhomologous DNA end joining. Proc Natl Acad Sci USA 110(6):2234-9

Oksenych V, Alt FW, Kumar V, Schwer B, Wesemann DR, Hansen E, Patel H, Su A, Guo C. (2012) Functional redundancy between repair factor XLF and damage response mediator 53BP1 in V(D)J recombination and DNA repair. Proc Natl Acad Sci USA 109(7):2455-60

Boboila C*, Oksenych V*, Gostissa M, Wang JH, Zha S, Zhang Y, Chai H, Lee CS, Jankovic M, Saez LMA, Nussenzweig MC, McKinnon PJ, Alt FW, Schwer B.* (2012) Robust chromosomal DNA repair via alternative end-joining in the absence of X-ray repair cross-complementing protein 1 (XRCC1). Proc Natl Acad Sci USA 109(7):2473-8

Zha S, Guo C, Boboila C, Oksenych V, Cheng HL, Zhang Y, Wesemann DR, Yuen G, Patel H, Goff PH, Dubois RL, Alt FW. (2011) ATM Damage Response and XLF Repair Factor are Functionally Redundant In Joining DNA Breaks. Nature 469(7329):250-4

Zhovmer A, Oksenych V, Coin F. Two sides of the same coin: TFIIH complexes in transcription and DNA repair (2010) ScientificWorldJournal 10:633-43

Oksenych V, Coin F. (2010) The long unwinding road: XPB and XPD helicases in damaged DNA opening. Cell Cycle 9(1):90-6

Oksenych V, De Jesus BB, Zhovmer A, Egly JM, Coin F. (2009) Molecular insights into the recruitment of TFIIH to sites of DNA damage. EMBO J 28(19):2971-80

Coin F, Oksenych V, Mocquet V, Groh S, Blattner C, Egly JM. (2008) Nucleotide excision repair driven by the dissociation of CAK from TFIIH. Mol Cell 31(1):9-20

Coin F, Oksenych V, Egly JM. (2007) Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol Cell 26(2):245-56