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Robert D. Fleischmann

Researcher at J. Craig Venter Institute

Publications -  68
Citations -  23631

Robert D. Fleischmann is an academic researcher from J. Craig Venter Institute. The author has contributed to research in topics: Genome & Gene. The author has an hindex of 38, co-authored 68 publications receiving 23105 citations. Previous affiliations of Robert D. Fleischmann include Human Genome Sciences & Philips.

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Investigating the genome diversity of B. cereus and evolutionary aspects of B. anthracis emergence.

TL;DR: The use of a multi-genome DNA microarray is reported to investigate the genome diversity of Bacillus cereus group members and elucidate the events associated with the emergence of Bacillin anthracis the causative agent of anthrax-a lethal zoonotic disease.
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Integral and peripheral association of proteins and protein complexes with Yersinia pestis inner and outer membranes

TL;DR: Since only 32 inner membrane (IM) proteins with two or more predicted transmembrane domains (TMDs) were profiled in 2D gels, a proteomic analysis by 2D-LC-MS/MS supported biologically meaningful assignments of many proteins to the membrane periphery.
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Characterizing the dynamic nature of the Yersinia pestis periplasmic proteome in response to nutrient exhaustion and temperature change

TL;DR: The data suggest that nutrient exhaustion in the stationary phase triggers cellular responses resulting in the induced expression of numerous ABC transporters, which are responsible for the import of solutes/nutrients.
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Improved quantitation and reproducibility in Mycobacterium tuberculosis DNA microarrays.

TL;DR: It is shown that optimizing the labeling protocol is a critical element in conducting microarray experiments and obtaining reproducible and interpretable data and variability between replicate features can be reduced by using more labeled cDNA.
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Recombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis

TL;DR: Multiple expression vectors, employing distinct fusion tags in a high throughput pipeline increased overall success rates in expression, solubility and purification of proteases.