Petri Kursula

This paper introduces sdAb(mNG), a high-affinity nanobody that enables versatile applications for mNG-tagged proteins, including imaging, immunoprecipitation, and in vivo manipulation.

This paper identifies FABP8/PMP2 as a defining feature of human and old-world monkey CNS myelin, revealing molecular heterogeneity in myelin sheaths and its role in cholesterol enrichment.

The paper presents a structural analysis of the AXL-tilvestamab complex using cryo-EM and SAXS, providing a low-resolution 3D model and insights for optimizing binding affinity.

This study maps the paratope residues of tilvestamab, an anti-AXL antibody, identifying twelve critical residues and Glu2 on AXL essential for binding.

This study investigates how myelin proteins P0, MBP, and P2 interact with lipid membranes and each other, revealing both synergistic and competitive effects on membrane structure and stability.

This study identifies Arc/Arg3.1 as a regulator of PABPN1 nuclear speckles through direct binding, impacting mRNA processing during neuronal activity.

This study identifies NDRG1 as a DNA repair protein that links pancreatic cancer stroma to chemoresistance by enhancing DNA damage repair through R-loop resolution.

This paper develops nanobodies against CNPase, showing distinct epitopes and functional applications in imaging and as intrabodies.

This paper investigates how the cytoplasmic tail of P0 affects lipid membrane morphology and describes the production of full-length P0 for further study.

The paper develops and validates Arc nanobodies to study Arc protein dynamics and function, showing their ability to bind Arc and enable live-cell labeling and purification.

This paper presents the crystal structure of a homodimeric actin capping protein from Plasmodium berghei and describes its atypical regulatory effects on actin dynamics.

This study identifies GADL1 as a multifunctional enzyme involved in β-alanine and carnosine production, showing its tissue-specific roles and associations with physiological traits in mice and humans.

The paper identifies β4 integrin as a binding partner for the C-terminal region of periaxin, revealing its role in linking Schwann cells to the basal lamina in myelination.