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Liangyi Chen

Researcher at Peking University

Publications -  180
Citations -  4974

Liangyi Chen is an academic researcher from Peking University. The author has contributed to research in topics: Microscopy & Exocytosis. The author has an hindex of 29, co-authored 162 publications receiving 3631 citations. Previous affiliations of Liangyi Chen include McGovern Institute for Brain Research & Chinese Academy of Sciences.

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Fast high-resolution miniature two-photon microscopy for brain imaging in freely behaving mice

TL;DR: The design and application of a fast high-resolution, miniaturized two-photon microscope (FHIRM-TPM), capable of imaging commonly used biosensors at high spatiotemporal resolution, and its robustness is demonstrated with hour-long recordings of neuronal activities at the level of spines in mice experiencing vigorous body movements.
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Fast, long-term, super-resolution imaging with Hessian structured illumination microscopy.

TL;DR: A deconvolution algorithm for structured illumination microscopy based on Hessian matrixes (Hessian-SIM), which attains artifact-minimized SR images with less than 10% of the photon dose used by conventional SIM while substantially outperforming current algorithms at low signal intensities.
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Functional stoichiometry of the unitary calcium-release-activated calcium channel

TL;DR: It is concluded that the subunit stoichiometry in an active CRAC channel is four Orai1 molecules and two STIM1 molecules, and that four ORAi1 subunits form the assembled channel.
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Mapping the interacting domains of STIM1 and Orai1 in Ca2+ release-activated Ca2+ channel activation.

TL;DR: It is demonstrated that the coiled-coil domain in the C termini of STIM1 is crucial for its aggregation and a highly conserved region in the N terminus of Orai1 (amino acids 74–90) that is necessary for CRAC channel opening is identified.
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Aggregation of STIM1 underneath the plasma membrane induces clustering of Orai1.

TL;DR: It is proposed that store depletion causes aggregation and translocation of STIM1 in close apposition to the plasma membrane, which in turn recruits Orai1 in the plasma membranes to the sites ofSTIM1 aggregates to assemble functional units of CRAC channels in a stoichiometric manner.