Biochemical and Structural Studies of Conserved Maf Proteins Revealed Nucleotide Pyrophosphatases with a Preference for Modified Nucleotides. Read more about Biochemical and Structural Studies of Conserved Maf Proteins Revealed Nucleotide Pyrophosphatases with a Preference for Modified Nucleotides.
Structural determinants for ERK5 (MAPK7) and leucine rich repeat kinase 2 activities of benzo[e]pyrimido-[5,4-b]diazepine-6(11H)-ones. Read more about Structural determinants for ERK5 (MAPK7) and leucine rich repeat kinase 2 activities of benzo[e]pyrimido-[5,4-b]diazepine-6(11H)-ones.
RVX-208, an inhibitor of BET transcriptional regulators with selectivity for the second bromodomain. Read more about RVX-208, an inhibitor of BET transcriptional regulators with selectivity for the second bromodomain.
Maintenance of muscle myosin levels in adult C. elegans requires both the double bromodomain protein BET-1 and sumoylation. Read more about Maintenance of muscle myosin levels in adult C. elegans requires both the double bromodomain protein BET-1 and sumoylation.
Targeting low-druggability bromodomains: Fragment based screening and inhibitor design against the BAZ2B bromodomain. Read more about Targeting low-druggability bromodomains: Fragment based screening and inhibitor design against the BAZ2B bromodomain.
A versatile spectrophotometric protein tyrosine phosphatase assay based on 3-nitrophosphotyrosine containing substrates. Read more about A versatile spectrophotometric protein tyrosine phosphatase assay based on 3-nitrophosphotyrosine containing substrates.
[1,2,4]Triazolo[4,3-a]phthalazines: inhibitors of diverse bromodomains. Read more about [1,2,4]Triazolo[4,3-a]phthalazines: inhibitors of diverse bromodomains.
Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases. Read more about Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases.
Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations. Read more about Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations.
