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HP1 oligomerization compensates for low-affinity H3K9me recognition and provides a tunable mechanism for heterochromatin-specific localization
View ORCID ProfileSaikat Biswas, View ORCID ProfileJoshua D. Karslake, View ORCID ProfileZiyuan Chen, View ORCID ProfileAli Farhat, View ORCID ProfilePeter L. Freddolino, View ORCID ProfileJulie S. Biteen, View ORCID ProfileKaushik Ragunathan
doi: https://doi.org/10.1101/2021.01.26.428151
Saikat Biswas
1Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109 USA
Joshua D. Karslake
2Department of Biophysics, University of Michigan, Ann Arbor, MI 48104 USA
Ziyuan Chen
2Department of Biophysics, University of Michigan, Ann Arbor, MI 48104 USA
Ali Farhat
3Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109 USA
Peter L. Freddolino
1Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109 USA
3Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109 USA
Julie S. Biteen
2Department of Biophysics, University of Michigan, Ann Arbor, MI 48104 USA
4Department of Chemistry, University of Michigan, Ann Arbor, MI 48104 USA
Kaushik Ragunathan
1Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109 USA

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Posted May 17, 2021.
HP1 oligomerization compensates for low-affinity H3K9me recognition and provides a tunable mechanism for heterochromatin-specific localization
Saikat Biswas, Joshua D. Karslake, Ziyuan Chen, Ali Farhat, Peter L. Freddolino, Julie S. Biteen, Kaushik Ragunathan
bioRxiv 2021.01.26.428151; doi: https://doi.org/10.1101/2021.01.26.428151
HP1 oligomerization compensates for low-affinity H3K9me recognition and provides a tunable mechanism for heterochromatin-specific localization
Saikat Biswas, Joshua D. Karslake, Ziyuan Chen, Ali Farhat, Peter L. Freddolino, Julie S. Biteen, Kaushik Ragunathan
bioRxiv 2021.01.26.428151; doi: https://doi.org/10.1101/2021.01.26.428151
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