Birthe Brandt Kragelund

This study investigates how alternative splicing of intrinsically disordered regions in the fungal circadian protein FRQ affects temperature-dependent clock function.

This paper identifies a direct interaction between the RecBCD complex and the DNA sliding clamp in E. coli, showing its role in DNA repair and survival after DNA damage.

This study examines how charge patterning affects the conformational behavior and dynamics of intrinsically disordered proteins using experimental techniques and simulations.

The paper develops SurpHer, a genetically encoded ratiometric pH sensor, and demonstrates its use in imaging extracellular pH dynamics in human cells and tumor microenvironments.

This study investigates how ligand binding affects the dynamics of the bacterial DNA sliding clamp beta-clamp using NMR and hydrogen-deuterium exchange mass spectrometry, revealing dynamic allosteric effects.

The paper presents the cryo-EM structure of HsNHE6, revealing its dimeric architecture, ion-binding site, and lipid-stabilized gate, along with insights into its disordered C-terminus and functional roles in ion exchange and disease.

This study identifies the mumps virus SH protein as a pentameric viroporin and shows it functions as a chloride channel inhibited by BIT225.

This study uses cryo-EM to analyze the structural changes in C3 during hydrolysis, revealing a dynamic opening in the macroglobulin ring that allows domain translocation.

The paper investigates the role of stereochemistry in disordered protein-protein interactions, finding that chirality is inconsequential in fully disordered complexes but essential when folding and binding are coupled.

The paper identifies an N-terminal region in AGO proteins that is accessible in the RNA-free state and mediates specific degradation through interaction with ATI1.

This study investigates the effects of replacing water with heavy water (D2O) on fission yeast, revealing pleiotropic effects and highlighting the cell integrity pathway's role in D2O tolerance.

This paper investigates the molecular properties of Arabidopsis autophagy cargo receptors ATI1 and ATI2, showing their intrinsically disordered regions and post-translational modifications upon ATG8 interaction.