Rolf Lutz
Heidelberg University
7 Papers
24 Citations
Rolf Lutz is an academic researcher from Heidelberg University. The author has contributed to research in topics: Plasmodium falciparum & Malaria vaccine. The author has an hindex of 6, co-authored 7 publications.
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Papers
Independent and Tight Regulation of Transcriptional Units in Escherichia Coli Via the LacR/O, the TetR/O and AraC/I1-I2 Regulatory Elements
Rolf Lutz,Hermann Bujard +1 more
TL;DR: Controlling the expression of the genes encoding luciferase, the low abundance E.coli protein DnaJ and restriction endonuclease Cfr9I not only demonstrates that high levels of expression can be achieved but also suggests that under conditions of optimal repression only around one mRNA every 3rd generation is produced.
Dissecting the functional program of Escherichia coli promoters: the combined mode of action of Lac repressor and AraC activator.
TL;DR: A three step model of transcription initiation which reveals mechanisms of AraC and LacR action is yielded which shows three distinct rate limiting steps at which AraC can exert its function.
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Interactions between merozoite surface proteins 1, 6, and 7 of the malaria parasite Plasmodium falciparum.
Christian W. Kauth,Ute Woehlbier,Michaela Kern,Zeleke Mekonnen,Rolf Lutz,Norbert Mücke,Jörg Langowski,Hermann Bujard +7 more
TL;DR: The findings raise interesting questions with regard to proteolysis-mediated mechanisms of maturation of the MSP-1-MSP-6-M SP-7 complex and to the mode by which antibodies directed against this complex interfere with parasite multiplication.
92
The merozoite surface protein 1 complex of human malaria parasite Plasmodium falciparum: interactions and arrangements of subunits.
TL;DR: The data indicate that the conformation assumed by the reassembled complex as well as by the heterologously produced 190-kDa precursor corresponds to the native one, and this work proposes a first structural model for the MSP-1 complex.
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Expression and purification of Plasmodium falciparum MSP-142: A malaria vaccine candidate
TL;DR: Cloned and expressed two synthetic DNA sequences encoding the two prototypic MSP-1(42) variants in E. coli meet key criteria of preparations for clinical use and conformational studies suggest proper folding of the proteins, particularly in the region containing two EGF-like domains.
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