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Hongfeng Gao

Researcher at Helen Wills Neuroscience Institute

Publications -  6
Citations -  1314

Hongfeng Gao is an academic researcher from Helen Wills Neuroscience Institute. The author has contributed to research in topics: Axon & Neurite. The author has an hindex of 6, co-authored 6 publications receiving 1215 citations. Previous affiliations of Hongfeng Gao include University of California, San Francisco.

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Bioactive Nanofibers: Synergistic Effects of Nanotopography and Chemical Signaling on Cell Guidance

TL;DR: Aligned and bioactive nan ofibrous scaffolds are developed by immobilizing extracellular matrix protein and growth factor onto nanofibers, which simulated the physical and biochemical properties of native matrix fibrils, which induced neurite outgrowth and enhanced skin cell migration during wound healing.
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Differential Activity-Dependent Secretion of Brain-Derived Neurotrophic Factor from Axon and Dendrite

TL;DR: A novel mechanism by which differential exocytosis of BDNF-containing vesicles may regulate BDNF–TrkB signaling between connected neurons is revealed, consistent with the BDNF function as a retrograde factor.
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Local and Long-Range Reciprocal Regulation of cAMP and cGMP in Axon/Dendrite Formation

TL;DR: It is found that localized cAMP and cGMP activities in undifferentiated neurites of cultured hippocampal neurons promote and suppress axon formation, respectively, and exert opposite effects on dendrite formation.
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Semaphorin3A regulates neuronal polarization by suppressing axon formation and promoting dendrite growth.

TL;DR: Sema3A regulates the earliest step of neuronal morphogenesis by polarizing axon/dendrite formation in cultured hippocampal neurons by downregulation of PKA-dependent phosphorylation of axon determinants LKB1 and GSK-3β.
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Phosphorylation of E3 Ligase Smurf1 Switches Its Substrate Preference in Support of Axon Development

TL;DR: It is reported that protein kinase A (PKA)-dependent phosphorylation of Smurf1 can switch its substrate preference between two proteins of opposing actions on axon development, contributing to selective protein degradation required for localized cellular function.