T
Thomas C. Marlovits
Researcher at University of Hamburg
Publications - 36
Citations - 2101
Thomas C. Marlovits is an academic researcher from University of Hamburg. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 12, co-authored 27 publications receiving 1765 citations. Previous affiliations of Thomas C. Marlovits include Austrian Academy of Sciences & Research Institute of Molecular Pathology.
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Journal ArticleDOI
Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells
TL;DR: One of the most exciting developments in the field of bacterial pathogenesis in recent years is the discovery that many pathogens utilize complex nanomachines to deliver bacterially encoded effector proteins into target eukaryotic cells.
Journal ArticleDOI
Structural insights into the assembly of the type III secretion needle complex.
Thomas C. Marlovits,Tomoko Kubori,Tomoko Kubori,Anand Sukhan,Anand Sukhan,Dennis R. Thomas,Dennis R. Thomas,Jorge E. Galán,Jorge E. Galán,Vinzenz M. Unger,Vinzenz M. Unger +10 more
TL;DR: Both the base and the fully assembled needle complex adopted multiple oligomeric states in vivo, and needle assembly was accompanied by recruitment of the protein PrgJ as a structural component of the base.
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Assembly of the inner rod determines needle length in the type III secretion injectisome
Thomas C. Marlovits,Tomoko Kubori,Tomoko Kubori,Tomoko Kubori,Maria Lara-Tejero,Dennis R. Thomas,Vinzenz M. Unger,Jorge E. Galán +7 more
TL;DR: Evidence is provided that, in Salmonella typhimurium, completion of the assembly of the inner rod determines the size of the needle substructure, which is fundamental to biology and which is regulated by the InvJ protein.
Journal ArticleDOI
Structure of a pathogenic type 3 secretion system in action
TL;DR: Cryo-EM was used to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport and showing that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.
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The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria
TL;DR: It is shown that the polytopic membrane protein FeoB, which is essential for Fe(II) uptake in bacteria, contains a guanine-nucleotide-specific nucleotide binding site, and the G4-motif, NXXD, responsible forGuanine nucleotide specificity, is identified, and it is found that GTP hydrolysis occurs very slowly.