Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease
The activity of metabolic enzymes is controlled by three principle levels: the amount of enzyme, the...
In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chr...
In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chr...
Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme...
Abstract Lysine acetylation is a post-translational mod-ification that critically regulates gene tra...
Lysine acetylation is a post-translational modification that critically regulates gene transcription...
Lysine acetylation is a widespread and versatile protein post-translational modification. Lysine ace...
Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulatio...
Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulatio...
AbstractAcetylation is one of the major post-translational protein modifications in the cell, with m...
Acetylation is a post-translational modification that occurs on thousands of proteins located in man...
Abstract The biochemical landscape of lysine acetylation has expanded from a small number of protein...
Post-translational protein modification represents a fundamental tool within the control of protein ...
Post-translational protein modification represents a fundamental tool within the control of protein ...
The activity of metabolic enzymes is controlled by three principle levels: the amount of enzyme, the...
The activity of metabolic enzymes is controlled by three principle levels: the amount of enzyme, the...
In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chr...
In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chr...
Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme...
Abstract Lysine acetylation is a post-translational mod-ification that critically regulates gene tra...
Lysine acetylation is a post-translational modification that critically regulates gene transcription...
Lysine acetylation is a widespread and versatile protein post-translational modification. Lysine ace...
Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulatio...
Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulatio...
AbstractAcetylation is one of the major post-translational protein modifications in the cell, with m...
Acetylation is a post-translational modification that occurs on thousands of proteins located in man...
Abstract The biochemical landscape of lysine acetylation has expanded from a small number of protein...
Post-translational protein modification represents a fundamental tool within the control of protein ...
Post-translational protein modification represents a fundamental tool within the control of protein ...
The activity of metabolic enzymes is controlled by three principle levels: the amount of enzyme, the...
The activity of metabolic enzymes is controlled by three principle levels: the amount of enzyme, the...
In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chr...
In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chr...