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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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Membrane insertion of—and membrane potential sensing by—semiconductor voltage nanosensors: Feasibility demonstration

TL;DR: A rationally designed peptide is used to functionalize membrane voltage nanosensors, imparting them with the ability to self-insert into a lipid membrane with a desired orientation, with a single-particle sensitivity.
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Three-Dimensional Localization of pORF65 in Kaposi's Sarcoma-Associated Herpesvirus Capsid

TL;DR: The lack of horn-shaped densities on the hexons indicates that KSHV SCP exhibits structural features that are substantially different from those of HSV-1 SCP, which suggests a possible role in mediating capsid interactions with the tegument and cytoskeletal proteins during infection.
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Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation.

TL;DR: It is shown that monomeric and dimeric receptors activate distinct conformational changes in G and implications for receptor-activated virus entry are discussed, providing insights into the pathway of receptor- activated virus entry.
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A putative ATPase mediates RNA transcription and capping in a dsRNA virus.

TL;DR: A role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus is supported.
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Tetrahymena Telomerase Holoenzyme Assembly, Activation, and Inhibition by Domains of the p50 Central Hub

TL;DR: It is shown that the p50-bound RNP catalytic core has a relatively low rate of tandem repeat synthesis but high processivity of repeat addition, indicative of high stability of enzyme-product interaction.