H3–H4 histone chaperones and cancer - ScienceDirect
Histone H3-H4 tetramer found to be a copper reductase enzyme
Distinct H3/H4 – histone chaperone complexes are marked by specific H3/H4 posttranslational modifications
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The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation - ScienceDirect
Histone - Wikipedia
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Insights into the molecular architecture and histone H3-H4 deposition mechanism of yeast Chromatin assembly factor 1 | eLife
Histone H3/H4 Tetramer, Recombinant Human Protein
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POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication - ScienceDirect
The histone H3-H4 tetramer is a copper reductase enzyme | Science
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Cryo–electron microscopy structure of the H3-H4 octasome: A nucleosome-like particle without histones H2A and H2B | PNAS
Models for loss of histone marks. (A) Splitting of the H3/H4... | Download Scientific Diagram
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Nuclear import and chaperoning of monomeric histones H3 and H4 is mediated by Imp5, NASP and the HAT1 complex | bioRxiv
Histone H3/H4 Tetramer, Recombinant Human Protein
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Inheritance of Histone (H3/H4): A Binary Choice?: Trends in Biochemical Sciences
