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Histone H3 threonine 11 phosphorylation is catalyzed directly by the meiosis-specific kinase Mek1 and provides a molecular readout of Mek1 activity in vivo
Ryan Kniewel, Hajime Murakami, Yan Liu, Nancy M. Hollingsworth, Scott Keeney
doi: https://doi.org/10.1101/106245
Ryan Kniewel
1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA
2Weill Cornell Graduate School of Medical Sciences, New York, New York, USA
Hajime Murakami
1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA
Yan Liu
3Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA
Nancy M. Hollingsworth
3Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA
Scott Keeney
1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA
2Weill Cornell Graduate School of Medical Sciences, New York, New York, USA
4Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York, New York, USA
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Posted February 06, 2017.
Histone H3 threonine 11 phosphorylation is catalyzed directly by the meiosis-specific kinase Mek1 and provides a molecular readout of Mek1 activity in vivo
Ryan Kniewel, Hajime Murakami, Yan Liu, Nancy M. Hollingsworth, Scott Keeney
bioRxiv 106245; doi: https://doi.org/10.1101/106245
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