L. Lehtiö

This study shows that dimerization of PARP15 is necessary for NAD+ binding and automodification, supported by structural and biochemical evidence.

The paper investigates the effect of the PKHD1L1 splice donor variant rs17368310 on female fertility, showing reduced child count in homozygous carriers across Finnish and Mexican populations.

The paper identifies a dual thiobarbiturate-indole inhibitor of the chikungunya virus macrodomain through screening and structural analysis, showing high selectivity over related proteins.

The paper develops a FRET-based assay to identify small molecules that inhibit collagen prolyl 4-hydroxylases by targeting their peptide-substrate-binding domain, leading to the discovery of a selective inhibitor.

The paper identifies a Tankyrase scaffolding inhibitor, S8 (ARCher-142), that selectively targets the ARC4 peptide binding domain with 8 µM potency.

This paper develops a FRET-based high-throughput screening assay to identify DarG inhibitors in M. tuberculosis and identifies pranlukast as a selective inhibitor.

This study identifies serine residues in PARP2's N-terminus as targets of automodification, showing their role in PARP2 release from DNA damage sites via PARylation.

The paper identifies 15 inhibitors of bacterial Arr enzymes that ADP-ribosylate rifamycin antibiotics, with structural insights into their selectivity.

This study identifies pyrrolo-pyrimidine-based Mac1 inhibitors that inhibit MHV and SARS-CoV-2 replication, with some compounds showing IFN-dependent antiviral activity.

This study identifies C-8 position substitutions in quinazolin-4-ones that enhance the potency and selectivity of tankyrase inhibitors by improving interactions with TNKS2.

This study investigates the evolutionary origin and conservation of tankyrases across species, showing their presence in choanoflagellates and conservation of core functions despite varying interaction partners.

This paper shows that the SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signaling in human cells.