ArticleProteomics2013
Histone H4 lysine 16 acetylated isoform synthesis opens new route to biophysical studies.
Article in Proteomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- The Non-Specific Lethal (NSL) Histone Acetyltransferase Complex Transcriptionally Regulates Yin Yang 1-Mediated Cell Proliferation in Human Cells.International journal of molecular sciences · 2022Article
- MOF Suppresses Replication Stress and Contributes to Resolution of Stalled Replication Forks.Molecular and cellular biology · 2018Article
- Differentiation of Human Induced Pluripotent or Embryonic Stem Cells Decreases the DNA Damage Repair by Homologous Recombination.Stem cell reports · 2017Article
- A multifaceted role for MOF histone modifying factor in genome maintenance.Mechanisms of ageing and development · 2017Review
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Abstract
Histone H4 lysine acetylation regulated by MOF (males absent on the first) was initially discovered as a dosage compensation epigenetic mark. Recent studies have revealed, however, that the epigenetic mark has a critical role in cellular function both during oogenesis as well as oncogenesis. Detailed molecular analysis of H4K16 isoforms and other posttranslational modified histones has been limited by the lack of means to prepare sufficient material for in vitro study. This paper describes an improved method to prepare acetylated H4K16 as well as other covalently modified histone H4 isoform for biophysical studies.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.