The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation - ScienceDirect
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Cryo–electron microscopy structure of the H3-H4 octasome: A nucleosome-like particle without histones H2A and H2B | PNAS
Histones H3 and H4 require their relevant amino-tails for efficient nuclear import and replication-coupled chromatin assembly in vivo | Scientific Reports
Distinct H3/H4 – histone chaperone complexes are marked by specific H3/H4 posttranslational modifications
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MCM2 binding to histones H3–H4 and ASF1 supports a tetramer-to-dimer model for histone inheritance at the replication fork | Nature Structural & Molecular Biology
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A unique binding mode enables MCM2 to chaperone histones H3–H4 at replication forks | Nature Structural & Molecular Biology
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