Design of a fluorescent ligand targeting the S-adenosylmethionine binding site of the histone methyltransferase MLL1. Read more about Design of a fluorescent ligand targeting the S-adenosylmethionine binding site of the histone methyltransferase MLL1.
Structural basis for substrate recognition by the human N-terminal methyltransferase 1. Read more about Structural basis for substrate recognition by the human N-terminal methyltransferase 1.
Emerging Target Families: Intractable Targets. Read more about Emerging Target Families: Intractable Targets.
Generation of a selective small molecule inhibitor of the CBP/p300 bromodomain for leukemia therapy. Read more about Generation of a selective small molecule inhibitor of the CBP/p300 bromodomain for leukemia therapy.
Structural Chemistry of Human RNA Methyltransferases. Read more about Structural Chemistry of Human RNA Methyltransferases.
Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins. Read more about Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.
The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities. Read more about The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities.
Structures of the CDK12/CycK complex with AMP-PNP reveal a flexible C-terminal kinase extension important for ATP binding. Read more about Structures of the CDK12/CycK complex with AMP-PNP reveal a flexible C-terminal kinase extension important for ATP binding.
A Potent, Selective and Cell-active Inhibitor of Human Type I Protein Arginine Methyltransferases. Read more about A Potent, Selective and Cell-active Inhibitor of Human Type I Protein Arginine Methyltransferases.
Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing Studies. Read more about Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing Studies.