Botulinum neurotoxins: biology, pharmacology, and toxicology
M Pirazzini, O Rossetto, R Eleopra… - Pharmacological …, 2017 - ASPET
The study of botulinum neurotoxins (BoNT) is rapidly progressing in many aspects. Novel
BoNTs are being discovered owing to next generation sequencing, but their biologic and …
BoNTs are being discovered owing to next generation sequencing, but their biologic and …
Protein export through the bacterial Sec pathway
A Tsirigotaki, J De Geyter, A Economou… - Nature Reviews …, 2017 - nature.com
The general secretory (Sec) pathway comprises an essential, ubiquitous and universal
export machinery for most proteins that integrate into, or translocate through, the plasma …
export machinery for most proteins that integrate into, or translocate through, the plasma …
Crystal structure of a substrate-engaged SecY protein-translocation channel
Hydrophobic signal sequences target secretory polypeptides to a protein-conducting
channel formed by a heterotrimeric membrane protein complex, the prokaryotic SecY or …
channel formed by a heterotrimeric membrane protein complex, the prokaryotic SecY or …
[HTML][HTML] Co-translational targeting and translocation of proteins to the endoplasmic reticulum
Co-translational protein targeting to the endoplasmic reticulum (ER), represents an
evolutionary-conserved mechanism to target proteins into the secretory pathway. In this …
evolutionary-conserved mechanism to target proteins into the secretory pathway. In this …
[HTML][HTML] Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways
R Kudva, K Denks, P Kuhn, A Vogt, M Müller… - Research in …, 2013 - Elsevier
Gram negative bacteria possess a large variety of protein transport systems, by which
proteins that are synthesised in the cytosol are exported to destinations in the cell envelope …
proteins that are synthesised in the cytosol are exported to destinations in the cell envelope …
Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase
K Kumazaki, T Kishimoto, A Furukawa, H Mori… - Scientific reports, 2014 - nature.com
Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane
protein chaperone in cooperation with the Sec translocon and as an independent insertase …
protein chaperone in cooperation with the Sec translocon and as an independent insertase …
Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG–SecDF–YajC–YidC
RJ Schulze, J Komar, M Botte… - Proceedings of the …, 2014 - National Acad Sciences
The SecY/61 complex forms the protein-channel component of the ubiquitous protein
secretion and membrane protein insertion apparatus. The bacterial version SecYEG …
secretion and membrane protein insertion apparatus. The bacterial version SecYEG …
The dynamic SecYEG translocon
J Oswald, R Njenga, A Natriashvili… - Frontiers in Molecular …, 2021 - frontiersin.org
The spatial and temporal coordination of protein transport is an essential cornerstone of the
bacterial adaptation to different environmental conditions. By adjusting the protein …
bacterial adaptation to different environmental conditions. By adjusting the protein …
Structure of the SecY channel during initiation of protein translocation
Many secretory proteins are targeted by signal sequences to a protein-conducting channel,
formed by prokaryotic SecY or eukaryotic Sec61 complexes, and are translocated across the …
formed by prokaryotic SecY or eukaryotic Sec61 complexes, and are translocated across the …
Toward a structural understanding of co-translational protein translocation
RM Voorhees, RS Hegde - Current opinion in cell biology, 2016 - Elsevier
Highlights•Advances in cryo-electron microscopy allow analysis of low abundance native
complexes.•Near-atomic resolution structures of intermediates in co-translational …
complexes.•Near-atomic resolution structures of intermediates in co-translational …