Marcus D. Hartmann

This paper expands the known ligand space of Cereblon by identifying new chemically distinct ligands that bind through non-canonical mechanisms.

The paper investigates the relationship between chaperone structure and substrate secretion order in bacterial type III secretion systems, finding that chaperone structure alone does not determine secretion hierarchy.

The paper investigates conformational diversity in poly-HAMP arrays and shows that axial helix rotation may be a conserved mechanism for signal transduction across different HAMP-containing systems.

This study characterizes HLp, a bacterial histone that forms tetramers and wraps ~60 base pairs of DNA, revealing a new mode of histone-DNA interaction in bacteria.

This study shows that the archaeal histone HTkC forms highly compact DNA structures, doubling the compaction level of hypernucleosomes and highlighting its role in chromatin organization.

The paper identifies pteridines, including lumazine dehydroxyxanthopterin B2, as natural ligands of CutA that modulate copper binding and redox homeostasis in E. coli and Synechococcus elongatus.

Structure providers for 18 CASP16 nucleic acid targets find blind predictions capture secondary structure but miss non-canonical interactions, backbone kinks, ligand sites, and intermolecular interfaces.

The paper identifies a synthetic small molecule, C26, that inhibits HilD, a key regulator of Salmonella secretion systems, thereby preventing bacterial invasion of host cells.

The paper compares the binding kinetics and structural features of silent and stimulatory flagellin variants with TLR5, identifying structural differences that explain their distinct immune responses.

This study investigates the DNA-binding properties of bacterial histone HBb in Bdellovibrio bacteriovorus, revealing its ability to bend DNA in a sequence-independent manner, similar to archaeal and eukaryotic histones.

The paper uses AlphaFold2 to classify prokaryotic histones into 17 groups and identifies a new histone superfamily that bridges DNA instead of wrapping it.

This study identifies SbtB as a redox-regulated apyrase that modulates bicarbonate transporter SbtA activity in cyanobacteria by integrating metabolic and carbon status signals.

This paper evaluates CASP14 models for molecular replacement using a new metric, reLLG, which is independent of diffraction data and shows AlphaFold2 models outperform others.