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Elio A. Abbondanzieri

Researcher at Delft University of Technology

Publications -  19
Citations -  2588

Elio A. Abbondanzieri is an academic researcher from Delft University of Technology. The author has contributed to research in topics: DNA & RNA polymerase. The author has an hindex of 14, co-authored 19 publications receiving 2417 citations. Previous affiliations of Elio A. Abbondanzieri include Harvard University & Stanford University.

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Direct observation of base-pair stepping by RNA polymerase

TL;DR: It is concluded that RNAP advances along DNA by a single base pair per nucleotide addition to the nascent RNA, and the force–velocity relationship for transcription at both saturating and sub-saturating nucleotide concentrations is determined.
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Backtracking by single RNA polymerase molecules observed at near-base-pair resolution

TL;DR: Backtracking events occurred infrequently at locations throughout the DNA template and were associated with pauses lasting 20 s to >30 min, whereas the accessory proteins GreA and GreB, which stimulate the cleavage of nascent RNA, decreased the duration of such pauses.
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Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking.

TL;DR: It is proposed that ubiquitous pauses in transcription do not result from the backtracking of RNAP along the DNA template, but are caused by a structural rearrangement within the enzyme.
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Passive All-Optical Force Clamp for High-Resolution Laser Trapping

TL;DR: A novel force clamp is developed that operates without feedback, taking advantage of the anharmonic region of the trapping potential where the differential stiffness vanishes, and is demonstrated by measuring the unfolding of DNA hairpins and the effect of trap stiffness on opening distance and transition rates.
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Dynamic binding orientations direct activity of HIV reverse transcriptase

TL;DR: Different orientational dynamics of reverse transcriptase observed on different substrates with a single-molecule assay indicate that the activities of reverse transcripts are determined by its binding orientation on substrates.