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Amy Peng

Researcher at Harvard University

Publications -  11
Citations -  2579

Amy Peng is an academic researcher from Harvard University. The author has contributed to research in topics: Bose–Einstein condensate & Angular momentum. The author has an hindex of 8, co-authored 11 publications receiving 2317 citations. Previous affiliations of Amy Peng include Washington University in St. Louis.

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A quantum gas microscope for detecting single atoms in a Hubbard-regime optical lattice

TL;DR: A quantum gas ‘microscope’ that bridges the two approaches to creating highly controllable quantum information systems, realizing a system in which atoms of a macroscopic ensemble are detected individually and a complete set of degrees of freedom for each of them is determined through preparation and measurement.
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Probing the Superfluid–to–Mott Insulator Transition at the Single-Atom Level

TL;DR: In this article, the authors used single atom-single lattice site imaging to investigate the Bose-Hubbard model on a microscopic level, enabling space and time-resolved characterization of the number statistics across the superfluid-Mott insulator quantum phase transition.
Journal Article

Probing the Superfluid to Mott Insulator Transition at the Single Atom Level

TL;DR: Single atom–single lattice site imaging is used to investigate the Bose-Hubbard model on a microscopic level and enables space- and time-resolved characterization of the number statistics across the superfluid–Mott insulator quantum phase transition.
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Initial clinical experience with remifentanil, a new opioid metabolized by esterases.

TL;DR: It is concluded that remifentanil was effective and well tolerated as a component of nitrous oxide-opioid-relaxant anesthesia and to determine the speed of recovery.
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Differential Motion Dynamics of Synaptic Vesicles Undergoing Spontaneous and Activity-Evoked Endocytosis

TL;DR: It is found that vesicles undergoing spontaneous and stimulated endocytosis differ in their dynamic behavior, particularly in the ability to engage in directed motion, and the data indicate that such motional differences depend on the myosin family of motor proteins, particularly myOSin II.