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Luz-Maria Guzman

Researcher at Harvard University

Publications -  5
Citations -  5372

Luz-Maria Guzman is an academic researcher from Harvard University. The author has contributed to research in topics: Fusion protein & Cell division. The author has an hindex of 5, co-authored 5 publications receiving 5084 citations.

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Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.

TL;DR: The tight regulation of the PBAD promoter is exploited to study the phenotypes of null mutations of essential genes and the use of pBAD vectors as an expression system is explored.
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FtsL, an Essential Cytoplasmic Membrane Protein Involved in Cell Division in Escherichia coli

TL;DR: Under certain growth conditions, depletion of FtsL or expression of the largest ftsL-phoA fusion produced a variety of cell morphologies, including Y-shaped bacteria, indicating a possible general weakening of the cell wall.
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Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole.

TL;DR: It is concluded that immunofluorescence microscopy can be used to localize proteins whose abundance is as low as approximately 100 molecules per cell and that spatial and temporal regulation of FtsI activity in septum formation is achieved, at least in part, by timed localization of the protein to the division site.
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Genetic Footprinting in Bacteria

TL;DR: The ability of recombinant proteins to complement mutagenized hosts has been evaluated by genetic footprinting using a bacteriophage lambda transposon delivery system and demonstrates the utility of this technology for rapidly discovering genes that affect the fitness of E. coli under a variety of growth conditions.
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Functional activity of eukaryotic signal sequences in Escherichia coli: the ovalbumin family of serine protease inhibitors.

TL;DR: It is shown here that the same internal domain that promotes an inefficient translocation of murine PAI-2 in mammalian cells is a weak signal sequence in Escherichia coli, and mutations that improve the activity of the PAi-2 signal sequence and that convert the N-terminal regions of maspin and PI-10 into efficient signal sequences have been characterized.