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Reposted by Tobias Raisch

IMPRS for Living Matter @imprs-lm.bsky.social · 30/09/2026

Are you ready to submit your application? Deadline extended: 4 October, 2026 For more information and to apply: www.imprs-lm.mpg.de/join/apply/ #IMPRS-LM #PhDpositions #FullyFunded #LifeScience

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Reposted by Tobias Raisch

IMPRS for Living Matter @imprs-lm.bsky.social · 09/09/2026

10 #fullyfunded #PhDpositions @imprs-lm.bsky.social! If you are eager to contribute to groundbreaking discoveries in the areas of #biochemistry, #structuralbiology, #biophysics, #cellbiology, #chemicalbiology and #syntheticbiology don’t miss your chance and APPLY NOW! Deadline: October 1, 2026

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Reposted by Tobias Raisch

IMPRS for Living Matter @imprs-lm.bsky.social · 05/03/2026

Are you passionate about interdisciplinary research and eager to contribute to groundbreaking discoveries in the areas of #biochemistry, #structuralbiology, #biophysics, #cellbiology, #chemicalbiology and #syntheticbiology? Apply NOW for a #fullyfunded #PhDpositions @IMPRS-LM. Deadline: April 6

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Reposted by Tobias Raisch

Hannah Garner @hannahgarner.bsky.social · 20/11/2025

Excited to share this highlight of a beautiful study into how myeloperoxidase acts as a chromatin transformer

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Reposted by Tobias Raisch

Max Planck Institute for Infection Biology @mpiib-berlin.mpg.de · 19/09/2025

📃 New paper alert! The Zychlinsky Lab and @raunser-lab.bsky.social identified the first protein that converts chromatin into an immune effector: Myeloperoxidase transforms chromatin into neutrophil extracellular traps. Now published in @nature.com: www.nature.com/articles/s41...

nature.com

Myeloperoxidase transforms chromatin into neutrophil extracellular traps - Nature

Myeloperoxidase, a highly expressed neutrophil protein, disassembles nucleosomes, facilitating neutrophil extracellular trap (NET) formation, and binds stably to NETs extracellularly.

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Tobias Raisch @traisch.bsky.social · 18/09/2025

We just published this paper of which I am immensely proud: www.nature.com/articles/s41... In the study, we uncover how the enzyme MPO disassembles #nucleosomes in a process called NETosis, a funky mechanism of #neutrophils to kill #pathogens that you might have never heard of. Let's dive in... 🧵

nature.com

Myeloperoxidase transforms chromatin into neutrophil extracellular traps - Nature

Myeloperoxidase, a highly expressed neutrophil protein, disassembles nucleosomes, facilitating neutrophil extracellular trap (NET) formation, and binds stably to NETs extracellularly.

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Tobias Raisch @traisch.bsky.social · 01/07/2025

I have an open postdoc position in my group at @mpi-dortmund.bsky.social @maxplanck.de! If you are passionate about structural biology and/or membrane proteins, apply today! The position is initially funded for two years, starting from this October. Deadline for application is on July 15th.

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Tobias Raisch @traisch.bsky.social · 04/11/2023

1/3 Today I can proudly present the first preprint from my project group! biorxiv.org/content/10.1... We determined the CryoEM structure of the Slo1 potassium channel in complex with the regulatory subunit γ1 and propose a mechanism of how γ1 can activate Slo1.

Figure 1 of the linked preprint showing an overview of the structure of the Slo1-γ1 complex.

A) Schematic representation of γ subunit domain organization
B) Cartoon scheme of γ1 helix binding across the Slo1 voltage sensor
C) EM density showing γ1 transmembrane helices binding to Slo1
D) Same depicting the molecular model as cartoon
E) Closeup of one γ1 transmembrane segment including transmembrane helix, extracellular hook and intracellular polybasic stretch binding to a Slo1 voltage-seonsor

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Tobias Raisch @traisch.bsky.social · 16/10/2023

Together with Stefan Raunser, I wrote a little review on neurotoxic insecticides acting on ion channels. We focus on structures and mechanisms and try to reveal similarities in modes of action between chemically diverse compounds. In the end, many act surprisingly similar! rdcu.be/doHyK

Figure 1 from the linked paper. It shows the main targets of neurotoxic insecticides, which are mainly ion channels belonging either to the pentameric ligand-gated ion channel family or the tetrameric voltage-gated ion channel family.

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