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Anna Leder

@annaleder.bsky.social

130 followers 42 following 8 posts

PhD student in Hiller lab, University of Basel | studying molecular chaperones and protein folding homeostasis

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Anna Leder @annaleder.bsky.social · Aug 13

Thanks Elif!

Anna Leder @annaleder.bsky.social · Aug 12

Thank you very much @nicolasluxfawzi.bsky.social!

Anna Leder @annaleder.bsky.social · Aug 11

Thank you Elias!

Anna Leder @annaleder.bsky.social · Aug 11

Thanks Ben!

Anna Leder @annaleder.bsky.social · Aug 11

Great teamwork with @masgu.bsky.social and I am very thankful for the huge support by Sebastian @hillerlab.bsky.social and Anne @spanglab.bsky.social!

Anna Leder @annaleder.bsky.social · Aug 11

PDIA6 forms the scaffold of these phase separated condensates and we resolve the underlying calcium-dependent mechanism. Further chaperones - including Hsp70, Hsp40 and Hsp90 - are recruited into the condensates, where they enhance client proteins folding, functioning as “folding factories”.

Anna Leder @annaleder.bsky.social · Aug 11

Happy to share my first publication, where we present our discovery of multi-chaperone condensates that orchestrate protein folding in the endoplasmic reticulum!
www.nature.com/articles/s41...

Anna Leder @annaleder.bsky.social · Jun 2

Check out this amazing work on the functional cycle of Hsp70 BiP NBD at atomic resolution by @masgu.bsky.social

HillerLab @hillerlab.bsky.social · Jun 2

Introducing in-cyclo NMR, a breakthrough method led by first author @masgu.bsky.social at @biozentrum.unibas.ch! This method combines high-resolution NMR with ATP regeneration & phosphate removal to resolve kinetics & dynamics of molecular machines - all in one experiment! doi.org/10.1038/s414...

Mechanism of ATP hydrolysis in the Hsp70 BiP nucleotide-binding domain - Nature Communications

Mas et al introduce in-cyclo NMR to quantify all states and kinetic steps of Hsp70 chaperones ATPase cycle. In-cyclo NMR will enable studies of other molecular machines at an unprecedented level of de...