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Liming Ying

Researcher at National Institutes of Health

Publications -  91
Citations -  4685

Liming Ying is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Förster resonance energy transfer & G-quadruplex. The author has an hindex of 35, co-authored 86 publications receiving 4130 citations. Previous affiliations of Liming Ying include Peking University & University College London.

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Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

TL;DR: The fundamental characteristics that enable toxic α-synuclein oligomers to perturb biological membranes and disrupt cellular function are identified; these include a highly lipophilic element that promotes strong membrane interactions and a structured region that inserts into lipid bilayers and disrupts their integrity.
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Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer

TL;DR: The structure and unfolding kinetics of the human telomeric intramolecular G quadruplex are investigated by using single-molecule fluorescence resonance energy transfer and it is concluded that under near-physiological conditions these structures can interconvert on a minute time scale.
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A CRISPR–Cas9-triggered strand displacement amplification method for ultrasensitive DNA detection

TL;DR: CRISDA is a powerful isothermal tool for ultrasensitive and specific detection of nucleic acids in point-of-care diagnostics and field analyses.
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Ultrasensitive coincidence fluorescence detection of single DNA molecules.

TL;DR: This work demonstrates that it can detect 100 fM dual-labeled DNA diluted in 1 microM unlabeled DNA, which was not possible with single color detection, and can be used to detect rare molecules in complex mixtures.
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Non-Arrhenius kinetics for the loop closure of a DNA hairpin

TL;DR: The kinetics of closing the loop show non-Arrhenius behavior, in agreement with theoretical prediction and other experimental measurements on peptide folding, and intrachain interactions, especially stacking interaction in the loop, might increase the roughness of the free energy surface of the DNA hairpin-loop.