Petr Man

De novo EHMT2 variants cause an autosomal dominant EHMT2-related Kleefstra syndrome via loss of G9a methyltransferase activity.

The paper identifies de novo EHMT2 variants causing an autosomal dominant Kleefstra syndrome by impairing G9a methyltransferase activity, mimicking EHMT1 haploinsufficiency.

Molecular mechanism of exchange coupling in CLC chloride/proton antiporters

The paper provides a mechanistic model for the 2:1 Cl-/H+ exchange in CLC transporters using structural and computational methods.

Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex

This study identifies the structural basis of allosteric regulation in the human cis-prenyltransferase complex using a combination of experimental and computational methods.

New structural insights into the control of the retinoic acid receptors RAR/RXR by DNA, ligands and transcriptional coregulators

This study reveals how DNA sequence and ligand binding influence the structural dynamics of RAR/RXR-coregulator complexes through integrative structural analysis.

A somatic multiple myeloma mutation unravels a mechanism of oligomerization-mediated product inhibition in GGPPS

The paper identifies a mutation in GGPPS that disrupts inter-dimer interactions, leading to increased substrate affinity and product release, revealing product inhibition as a regulatory mechanism in GGPPS.

Nanobodies as therapies for loss-of-function misfolding diseases.

This study develops and characterizes six nanobodies as potential therapeutics for PH1 by targeting misfolded AGT variants, showing high affinity and functional enhancement in cellular models.

Active site tyrosine residues in human NQO1 homodimer are critical for non-synchronous enzyme catalysis at the two active sites.

This study investigates the role of Tyr126 and Tyr128 in human NQO1 catalysis, showing their critical impact on enzyme activity and non-synchronous catalysis.

Post-proline cleaving enzymes also show specificity to reduced cysteine.

The paper shows that post-proline cleaving enzymes also specifically cleave after reduced cysteine, revealing previously undetected activity due to alkylation blocking.