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Histone acetyltransferases: challenges in targeting bi-substrate enzymes
Hannah Wapenaar,
Frank J Dekker
Biopharmaceuticals, Discovery, Design and Delivery
Synthesis and Analysis
Chemische en Farmaceutische Biologie
Onderzoeksoutput
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peer review
181
Citaten (Scopus)
431
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Gewicht
Alfabetische volgorde
Biochemistry, Genetics and Molecular Biology
Histone Acetyltransferase
100%
Enzyme Substrate
100%
Enzyme
15%
Small Molecule
15%
Lysine
10%
Histone
10%
Coenzyme A
5%
Epigenetics
5%
Protein-Protein Interaction
5%
Transcription Factors
5%
Catalytic Mechanism
5%
Enzyme Inhibition
5%
Biological Activity
5%
In Vitro Study
5%
Acetylation
5%
Antioxidant Activity
5%
Enzyme Kinetics
5%
Nuclear Receptor
5%
Non-Histone Protein
5%
Pharmacology, Toxicology and Pharmaceutical Science
Histone Acetyltransferase
100%
Lysine
10%
Histone
10%
Disease
5%
Inflammatory Disease
5%
Malignant Neoplasm
5%
Acetic Acid Derivative
5%
Neurologic Disease
5%
Antioxidant Capacity
5%
Natural Product
5%
Biological Activity
5%
Enzyme Inhibition
5%
Acetyl-CoA
5%
Transcription Factors
5%
Cell Nucleus Receptor
5%
Cell Protein
5%
Enzyme Kinetics
5%
Nonhistone Protein
5%
Chemistry
Histone
100%
Coenzyme A
4%
Cofactor
4%
Occurrence in Nature
4%
Antioxidant Capacity
4%
Acetyl
4%
Lysine
4%
Bioactivity
4%
Enzyme Kinetics
4%
Acetylation
4%
Acetyl Group
4%
Protein Interaction
4%
Lysine Residue
4%
Inhibition of Enzyme
4%
Keyphrases
Bisubstrate Inhibitor
10%
Natural Product Derivatives
10%
Chemical-protein Interaction
10%
Histone Transcription
10%