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Cell cycle and checkpoint regulation of histone H3K56 acetylation by Hst3 and Hst4
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Dynamic range of mass accuracy in LTQ Orbitrap hybrid mass spectrometer
Alexander Makarov et al.
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Alejandro Vaquero et al.
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F Picard et al.
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N Suka et al.
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Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
A Kimura et al.
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A core nucleosome surface crucial for transcriptional silencing
JH Park et al.
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HH Ng et al.
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Dot1p modulates silencing in yeast by methylation of the nucleosome core
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JY Luo et al.
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H Vaziri et al.
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Mass analysis at the advent of the 21st century
SA McLuckey et al.
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The silencing protein SIR2 and its homologs are MAD-dependent protein deacetylases
J Landry et al.
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S Imai et al.
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