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E. Pardon

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Open access Sep 2026

Chaperone-inspired nanobodies enable pathway-selective control of Tau self-assembly

Selective control of pathogenic protein self-assembly remains a major challenge for intrinsically disordered amyloid-forming proteins such as Tau. Here we show that nanobodies originally raised against the chaperone S100B unexpectedly cross-react with Tau as potential pathway-selective modulators of Tau self-assembly...

Margarida C. Simões, Joana Saavedra, Isabel Cardoso et al. · 0 citations
Sep 2026

Characterizing two nanobodies for SMAD4.

Two nanobodies, NbS4A1 and NbS4A7, are reported, which target the 3D structure of the human SMAD4-MH2 domain with high affinity and specificity and will enable the study of folded SMAD complexes with cofactors and/or DNA in different experimental contexts.

Miriam Condeminas, C. Torner, Radoslaw Pluta et al. · 0 citations
Open access Aug 2026

Molecular arrangement and modulation of extrasynaptic αβδ GABAA receptors

Key insights are provided into the stoichiometry, arrangement and molecular modes of GABA activation and δ-selective modulation of these critical regulators of neuronal excitability of GABAA αβδ receptors.

Stephanie A. Nestorow, Wan-Na Chen, D. Bertrand et al. · 0 citations
Open access Aug 2026

Distinct mechanisms of antibody-mediated HCV neutralization revealed by nanobody-guided epitope mapping

This study illustrates how alternative antibody repertoires can reveal functionally important antigenic surfaces that are underrepresented in conventional human antibody responses, providing new opportunities for the rational design of next-generation HCV vaccine immunogens.

Haneen Tarabih, Jenna Weisz, Itai Yechezkel et al. · 0 citations
Open access Aug 2026

Structural insights into the polytopic Escherichia coli phosphoglycosyl transferase WbaP.

The 3.0 Å cryo-electron microscopy apo-structure of the PGT enzyme WbaP from Escherichia coli, a UDP-galactose:undecaprenolphosphate galactose-1-phosphoryl transferase, provides new insights into the PGT family of enzymes.

M. Weckener, Audrey Le Bas, Philip N. Ward et al. · 0 citations

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