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Reconstitution of the DTX3L-PARP9 complex reveals determinants for high affinity heterodimer formation and enzymatic function
View ORCID ProfileYashwanth Ashok, Carlos Vela-Rodriguez, Chunsong Yang, Heli I. Alanen, Fan Liu, View ORCID ProfileBryce M. Paschal, View ORCID ProfileLari Lehtiö
doi: https://doi.org/10.1101/2021.06.14.448324
Yashwanth Ashok
1Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland
Carlos Vela-Rodriguez
1Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland
Chunsong Yang
2Department of Biochemistry and Molecular genetics, University of Virginia, PO Box 800577, Charlottesville, VA22908, USA
Heli I. Alanen
1Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland
Fan Liu
3Department of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Deutschland
Bryce M. Paschal
2Department of Biochemistry and Molecular genetics, University of Virginia, PO Box 800577, Charlottesville, VA22908, USA
Lari Lehtiö
1Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland

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Posted October 13, 2021.
Reconstitution of the DTX3L-PARP9 complex reveals determinants for high affinity heterodimer formation and enzymatic function
Yashwanth Ashok, Carlos Vela-Rodriguez, Chunsong Yang, Heli I. Alanen, Fan Liu, Bryce M. Paschal, Lari Lehtiö
bioRxiv 2021.06.14.448324; doi: https://doi.org/10.1101/2021.06.14.448324
Reconstitution of the DTX3L-PARP9 complex reveals determinants for high affinity heterodimer formation and enzymatic function
Yashwanth Ashok, Carlos Vela-Rodriguez, Chunsong Yang, Heli I. Alanen, Fan Liu, Bryce M. Paschal, Lari Lehtiö
bioRxiv 2021.06.14.448324; doi: https://doi.org/10.1101/2021.06.14.448324
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