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Yixian Zheng

Researcher at Carnegie Institution for Science

Publications -  120
Citations -  8217

Yixian Zheng is an academic researcher from Carnegie Institution for Science. The author has contributed to research in topics: Microtubule & Lamin. The author has an hindex of 46, co-authored 112 publications receiving 7449 citations. Previous affiliations of Yixian Zheng include Chinese Academy of Sciences & Johns Hopkins University.

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γ-Tubulin is present in Drosophila melanogaster and homo sapiens and is associated with the centrosome

TL;DR: The mipA gene of A. nidulans encodes a newly discovered member of the tubulin superfamily of proteins, gamma-tubulin, which is suggested to be a universal component of microtubule organizing centers and consistent with an earlier hypothesis that gamma- Tubulin is a minus-end nucleator of micro Tubulin assembly.
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Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran.

TL;DR: Ran, a small guanosine triphosphatase, is suggested to have additional functions beyond its well-characterized role in nuclear trafficking, and could be a key signaling molecule regulating microtubule polymerization during mitosis.
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A Ran signalling pathway mediated by the mitotic kinase Aurora A in spindle assembly

TL;DR: It is hypothesized that the Ran-GTP gradient established by the condensed chromosomes is translated into the Aurora A kinase gradient on the microtubules to regulate spindle assembly and dynamics.
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Role of Importin-β in Coupling Ran to Downstream Targets in Microtubule Assembly

TL;DR: It is shown that importin-β is an inhibitor of microtubule aster assembly in Xenopus egg extracts and that Ran regulates the interaction between importin -β and NuMA, which suggests that similar mechanisms regulate nuclear import during interphase and spindle assembly during mitosis.
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Characterization of Two Related Drosophila γ-tubulin Complexes that Differ in Their Ability to Nucleate Microtubules

TL;DR: Analysis of the nucleotide content of the γTuSC reveals that γ-tubulin binds preferentially to GDP over GTP, rendering γ -tubulin an unusual member of the tubulin superfamily.