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Publisher Correction: A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells

James A. Thomas
Michele S. Y. Tan
Michael J. Blackman
Amendments and Corrections06 Mar 2018
Nature Microbiology

Volume: 3, P: 523
Author Correction: In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque

Tina Drobnič
Eli J. Cohen
Morgan Beeby
Amendments and CorrectionsOpen Access14 Jul 2025
Nature Microbiology

Volume: 10, P: 2092
In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque

In situ cryoEM and modelling of the Campylobacter jejuni flagellar motor characterize the periplasmic scaffold and the structural basis for increased torque generation.

Tina Drobnič
Eli J. Cohen
Morgan Beeby
ResearchOpen Access01 Jul 2025
Nature Microbiology

Volume: 10, P: 1723-1740
Trapping of the transport-segment DNA by the ATPase domains of a type II topoisomerase

Type 2 topoisomerases alter DNA supercoiling by an ATP-dependent reaction involving DNA passage through a cleaved DNA duplex. Here the authors present the crystal structure of the ParE ATPase domains of S. pneumoniae topoisomerase IV, in complex with a captured DNA oligonucleotide.

Ivan Laponogov
Xiao-Su Pan
Mark R. Sanderson
ResearchOpen Access03 Jul 2018
Nature Communications

Volume: 9, P: 1-14
A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells

To exit from infected red blood cells, malaria parasites rely on the sequential action of different proteases, such as SUB1 and SERA6, in a process that culminates with the disassembly of the host cell’s cytoskeleton and rupture of the cell membrane.

James A. Thomas
Michele S. Y. Tan
Michael J. Blackman
Research19 Feb 2018
Nature Microbiology

Volume: 3, P: 447-455