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The Plant Genome, Volume 19, Issue 2, June 2026.Abstract Polyploidization has played a key role in plant genome evolution. Eragrostis curvula (Schrad.) Ness, a perennial forage grass species of the Poaceae family, is an excellent model for investigating genome duplication due to its natural variation in ploidy levels.
D. F. Santoro +5 more
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Harnessing energy metabolism for enhanced bone defect repair: Mechanisms and therapeutic strategies
VIEW, Volume 7, Issue 3, June 2026.This review addresses the critical challenge of bone defect repair by focusing on the underexplored role of cellular energy metabolism. It synthesizes regulatory mechanisms in bone‐forming cells and sums up innovative strategies—leveraging cell derivatives, active factors, and biomimetic scaffolds—to modulate metabolism for enhanced regeneration.
Junting Li +5 more
wiley +1 more source
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Histone Acetyltransferase Complexes and Their Link to Transcription
Critical Reviews in Eukaryotic Gene Expression, 1999Early studies revealing the relationship between the state of histone acetylation and gene transcription were largely indirect. Increasing information regarding the enzymes that catalyze transcription linked acetylation is beginning to clarify this issue.
Leann J Howe +2 more
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Annual Review of Biochemistry, 2001
▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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Histone acetyltransferase complexes
Seminars in Cell & Developmental Biology, 1999Modification of histone amino terminal tails by acetylation has long been linked to the transcriptional capacity of genes in chromatin and to various aspects of chromatin dynamics. Over the last few years a flurry of reports have described the purification and identification of a large number of histone acetyltransferases.
P A, Grant, S L, Berger
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Fluorescent reporters of the histone acetyltransferase
Analytical Biochemistry, 2008Histone acetyltransferases (HATs) are important chromatin modifying enzymes that catalyze acetylation of specific lysine residues in histone and nonhistone substrates. They participate in multiple cellular processes such as transcriptional regulation and signal transduction.
Jiang, Wu, Yujun George, Zheng
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Structure and function of histone acetyltransferases
Cellular and Molecular Life Sciences, 2001Histone acetyltranferase (HAT) enzymes are the catalytic subunit of large multisubunit HAT complexes that acetylate the epsilon-amino group of specific lysine residues on histone tails to promote transcriptional activation. Recent structural and functional studies on the divergent HAT enzymes Gcn5/PCAF, Esa1 and Hat1 have provided new insights into the
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The MYST Family of Histone Acetyltransferases
2003Multiple chromatin modifying proteins and multisubunit complexes have been characterized in recent years. Histone acetyltransferase (HAT) activities have been the most thoroughly studied, both biochemically and functionally. This review sums up the current knowledge on a specific group of proteins that is extremely well conserved throughout evolution ...
R T, Utley, J, Côté
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