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Armindo Salvador

As seen in: Nature, MDPI
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Articles

Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins

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By Jannik Zimmermann, Lukas Lang, Julia Malo Pueyo, Mareike Riedel, Khadija Wahni, Dylan Stobbe, Laura Leiskau, Christopher Lux, Steven Janvier, Didier Vertommen, Svenja Lenhard, Helena Castro, Volkhard Helms, Ana María Tomás, Johannes Herrmann, Armindo Salvador, Timo Mühlhaus, Jan Riemer, Joris Messens, Marcel Deponte, Bruce Morgan Verified, Elham Aref, Frank Hannemann, Sudharshini Thangamuragan
| Nature Verified
Abstract Peroxiredoxins are thiol peroxidases, which detoxify peroxides, relay redox signals and act as chaperones. In eukaryotes, multiple peroxiredoxin-1 (Prx1)/AhpC-type isoforms frequently co-exist in the same subcellular compartment, yet have been assumed to assemble only as homo-oligomeric complexes. Here we show that hetero-oligomerization is a conserved and functionally relevant property of Prx1/AhpC-type peroxiredoxins.
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Ligand’s Partition to the Lipid Bilayer Should Be Accounted for When Estimating Their Affinity to Proteins

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By Maria Moreno, Maria João, Armindo Salvador
| MDPI
This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
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