Histone exchange

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Radboud University/Radboud UMC, Faculty of Science, Department of Molecular Biology, Radboud Institute for Molecular Life Sciences, Nijmegen, the Netherlands (1)
1 Max-Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse 14, 35043 Marburg, Germany 2 University of Marburg, Center for Synthetic Microbiology (SYNMIKRO) & Departments of Chemistry and Biology, Karl-von-Frisch Strasse 14, 35043 Marburg, Germany (1)
Penn Epigenetics Institute Department of Biochemistry and Biophysics Smilow Center for Translational Research University of Pennsylvania School of Medicine (1)
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Max-Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Am Klopferspitz 18, 82152 Martinsried, Germany (1)
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Department of Genetics, Harvard Medical School, Boston MA 02115 USA (1)
School of Life Sciences, The Chinese University of Hong Kong, Sha Tin, N.T., Hong Kong; State Key Laboratory of Agrobiotechnology, and School of Life Sciences, The Chinese University of Hong Kong, Shatin N.T., Hong Kong (1)
Hubrecht Institute, KNAW (Royal Netherlands Academy of Arts and Sciences), Utrecht, The Netherlands (1)
School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia (1)

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Fam170a deficiency causes male infertility by impairing histone-to-protamine exchange during mouse spermiogenesis

Families with sequence similarity 170 members A (Fam170a) deficiency caused abnormal sperm nuclear morphology and male infertility in mice, mirroring the observation of very low Fam170a transcription in sperm of infertile men with teratozoospermia.Fam170a directly interacted with the deubiquitinatin...

ORGANISM(S): Mus Musculus

2024-11-10 | PXD057721 |

Regulators of histone exchange

PRJNA927495 | ENA

Forebrain Hindbrain histone H4 Mus musculus P25 P47

Quantitative top down analysis of histone H4 proteoforms in the mouse forebrain and hindbrain at 25 and 47 days of age.

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

MSV000090249 | MassIVE

Phosphorylation regulates the chromatin remodeler SMARCAD1 in nucleosome binding, ATP hydrolysis, and histone exchange

Maintaining the dynamic structure of chromatin is critical for regulating the cellular processes that require access to the DNA template, such as DNA damage repair, transcription, and replication. Histone chaperones and ATP-dependent chromatin remodeling factors facilitate transitions in chromatin s...

ORGANISM(S): Homo sapiens (Human)

2025-05-07 | PXD055413 | Pride