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Lysine

Known as: (S)-?,?-diaminocaproic acid, (S)-2,6-diaminohexanoic acid, Lysine acid 
A nutritional supplement containing the biologically active L-isomer of the essential amino acid lysine, with potential anti-mucositis activity. Upon… Expand
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2018
Review
2018
Post-translational modification of lysine residues via reversible acylation occurs on proteins from diverse pathways, functions… Expand
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Review
2017
Review
2017
Epigenetic and metabolic alterations in cancer cells are highly intertwined. Oncogene-driven metabolic rewiring modifies the… Expand
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Review
2016
Review
2016
Transcriptional silencing in Saccharomyces cerevisiae occurs at several genomic sites including the silent mating-type loci… Expand
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Review
2016
Review
2016
The Bromodomain and Extra-Terminal Domain (BET) family of proteins is characterized by the presence of two tandem bromodomains… Expand
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Highly Cited
2010
Highly Cited
2010
Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulation, in particular through the… Expand
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Highly Cited
2009
Highly Cited
2009
Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression… Expand
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Highly Cited
2007
Highly Cited
2007
Homologs of the Saccharomyces cerevisiae Sir2 protein, sirtuins, promote longevity in many organisms. Studies of the sirtuin… Expand
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Highly Cited
2007
Highly Cited
2007
Mammals use DNA methylation for the heritable silencing of retrotransposons and imprinted genes and for the inactivation of the X… Expand
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Highly Cited
2001
Highly Cited
2001
Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing. The chromo domain of HP1… Expand
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Highly Cited
2001
Highly Cited
2001
The assembly of higher order chromatin structures has been linked to the covalent modifications of histone tails. We provide in… Expand
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