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Angela Tramonti
Researcher at Sapienza University of Rome
Publications - 64
Citations - 1733
Angela Tramonti is an academic researcher from Sapienza University of Rome. The author has contributed to research in topics: Gene & Serine hydroxymethyltransferase. The author has an hindex of 17, co-authored 54 publications receiving 1422 citations. Previous affiliations of Angela Tramonti include University of Camerino & National Research Council.
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Coping with low pH: molecular strategies in neutralophilic bacteria
TL;DR: The current knowledge of the molecular mechanisms adopted by a range of Gram-positive and Gram-negative bacteria for coping with acid stress is reviewed, paying particular attention to Escherichia coli extreme acid resistance mechanisms, the activity of which ensure survival and may be directly linked to virulence.
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The response to stationary‐phase stress conditions in Escherichia coli : role and regulation of the glutamic acid decarboxylase system
TL;DR: In vivo evidence is provided that gadC is co‐transcribed with gadB and that the functional glutamic acid‐dependent system requires the activities of both GadA/B and GadC, and that expression of gad genes is positively regulated by acidic shock, salt stress and stationary growth phase.
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Functional Characterization and Regulation of gadX, a Gene Encoding an AraC/XylS-Like Transcriptional Activator of the Escherichia coli Glutamic Acid Decarboxylase System
TL;DR: It is demonstrated that transcription of both gadA and gadBC is positively controlled by gadX, a gene downstream of gadA, encoding a transcriptional regulator belonging to the AraC/XylS family.
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GadX/GadW-dependent regulation of the Escherichia coli acid fitness island: transcriptional control at the gadY-gadW divergent promoters and identification of four novel 42 bp GadX/GadW-specific binding sites.
TL;DR: It is shown that gadW transcription occurs from two native promoters, which are affected by the transcription of the divergently transcribed and GadX‐dependent gadY small RNA, and from the gadX promoter.
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Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli.
TL;DR: The two isoforms were characterized biochemically and all evidence, including that from analysis of the complex pre-steady-state kinetic behavior of the enzymes, indicates that the functional properties of the two isoenzymes are identical.