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Z. Hong Zhou

Researcher at University of California, Los Angeles

Publications -  251
Citations -  13342

Z. Hong Zhou is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Capsid & Biology. The author has an hindex of 58, co-authored 225 publications receiving 11143 citations. Previous affiliations of Z. Hong Zhou include University of Texas Health Science Center at Houston & University of Science and Technology of China.

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In situ Structure of Viral RNA by Cryo Electron Tomography with Volta Phase Plate, Energy Filtering and Direct Electron Counting

TL;DR: In this paper, the power of averaging low-contrast, high-resolution images of as many as one million purified particles of the same homogeneous complex to overcome low contrast problem to obtain structures suitable for functional interpretation was demonstrated at near atomic resolution for proteins in an icosahedral virus.
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Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission

TL;DR: In this paper , the authors determined the native structure of SGS1 by the cryoID approach, showing that the 3364 amino acid protein has a Tc toxin-like Rhs/YD shell, four receptor domains, and a set of C-terminal daisy-chained helices.
Posted ContentDOI

Membrane insertion of- and membrane potential sensing by semiconductor voltage nanosensors: feasibility demonstration

TL;DR: In this paper, the authors developed membrane voltage nanosensors that are based on inorganic semiconductor nanoparticles, which self-insert into the cell membrane and optically record the membrane potential via the quantum confined Stark effect, with single-particle sensitivity.
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On The Unique Structural Organization of the Saccharomyces Cerevisiae Pyruvate Dehydrogenase Complex

TL;DR: The structure of the truncated 60-mer core (tE2) and complexes of the tE2 associated with a binding protein (BP), and the BP associated with its dihydrohpoamide dehydrogenase (BP'E3) and the intact E2 associated both BP and E1 were determined in this paper.
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CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics

TL;DR: In this article , the authors report the cryogenic electron microscopy (cryoEM) structures and assembly of different oligomeric isomers of endogenous PCC from the parasitic protozoan Leishmania tarentolae (LtPCC).