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Renate Lux

Researcher at University of California, Los Angeles

Publications -  97
Citations -  4992

Renate Lux is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Myxococcus xanthus & Fusobacterium nucleatum. The author has an hindex of 35, co-authored 87 publications receiving 4107 citations. Previous affiliations of Renate Lux include University of Osnabrück.

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Interspecies Interactions within Oral Microbial Communities

TL;DR: This review describes some of the interesting interspecies-interaction scenarios in oral microbial communities, which indicate that the whole is much more than the simple sum of its parts, since the interactions between different parts resulted in many new physiological functions which cannot be observed with individual components.
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Cultivation of a human-associated TM7 phylotype reveals a reduced genome and epibiotic parasitic lifestyle

TL;DR: This first completed genome for a human-associated TM7 phylotype revealed a complete lack of amino acid biosynthetic capacity, and comparative genomics analyses with uncultivated environmental TM7 assemblies show remarkable conserved gene synteny and only minimal gene loss/gain that may have occurred as TM7x adapted to conditions within the human host.
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Extracellular polysaccharides mediate pilus retraction during social motility of Myxococcus xanthus

TL;DR: It is suggested that the interaction of type IV pili with amine-containing polysaccharides on cell and slime-trail surfaces may trigger pilus retraction, resulting in S-motility and Slime-trailing behaviors.
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The Fusobacterium nucleatum outer membrane protein RadD is an arginine‐inhibitable adhesin required for inter‐species adherence and the structured architecture of multispecies biofilm

TL;DR: Findings indicate that radD is responsible for arginine‐inhibitable adherence of F.’nucleatum and provides definitive molecular evidence that F.Nucleatum adhesins play a vital role in inter‐species adherence and multispecies biofilm formation.
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Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli.

TL;DR: It is found that in mutant strains HPr-like proteins could substitute for HPr in transport but did not mediate chemotactic signaling, suggesting the following model for signal transduction in PTS-dependent chemotaxis.