Stefan M.V. Freund

Mechanism and regulation of Bim1 interactions withthe S. cerevisiae outer kinetochore Ndc80 complex

The paper identifies a conserved interaction between Bim1 and the Ndc80 complex in S. cerevisiae, showing it enhances microtubule attachment strength and is regulated by phosphorylation.

Mechanism and regulation of the Bim1 interaction withthe outer kinetochore Ndc80 complex in S. cerevisiae

This study identifies a conserved interaction between Bim1 and the Ndc80 complex in S. cerevisiae, showing it enhances microtubule attachment strength and is regulated by phosphorylation.

Twelve phosphomimetic mutations induce the assembly of recombinant full-length human tau into paired helical filaments

This study identifies twelve phosphomimetic mutations in tau that induce the formation of paired helical filaments in vitro, mimicking Alzheimer's disease structures.

Phosphorylation-dependent tuning of mRNA deadenylation rates

The paper shows phosphorylation modulates deadenylation rates via multivalent interactions in RNA adaptors, enabling graded regulation of mRNA decay.

RNA-binding proteins provide specificity to the PAN2-PAN3 mRNA deadenylation complex

This study shows that the PAN2-PAN3 deadenylation complex can be recruited to specific mRNAs via RNA adaptors, adding to the specificity of mRNA degradation.

Molecular mechanism of Mad2 conformational conversion promoted by the Mad2-interaction motif of Cdc20

This study elucidates how the Cdc20MIM induces Mad2 conformational conversion by transiently exposing a binding site and facilitating structural changes.

Dynamics in Fip1 regulate eukaryotic mRNA 3'-end processing

This study investigates the dynamics of Fip1 in the CPF complex, showing its IDR remains highly dynamic and mediates conformational transitions during mRNA 3'-end processing.

TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control

The paper identifies TASOR as a pseudo-PARP essential for HUSH complex assembly and epigenetic repression of transposons.

An "invisible" ubiquitin conformation is required for efficient phosphorylation by PINK1

The paper shows that an 'invisible' conformation of ubiquitin enhances its phosphorylation by PINK1 through a dynamic equilibrium involving the Ser65 loop.