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Xianghong Jing

Researcher at Northwestern University

Publications -  7
Citations -  1163

Xianghong Jing is an academic researcher from Northwestern University. The author has contributed to research in topics: Influenza A virus & Amantadine. The author has an hindex of 6, co-authored 6 publications receiving 1087 citations. Previous affiliations of Xianghong Jing include Food and Drug Administration.

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Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission

TL;DR: It is shown that M2 localizes to the neck of budding virions and that mutation of the M2 amphipathic helix results in failure of the virus to undergo membrane scission and virion release, suggesting that M1 mediates the final steps of budding for influenza viruses, bypassing the need for host ESCRT proteins.
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Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation

TL;DR: It is found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and it is speculated that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.
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Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel

TL;DR: Functional data suggest that amantadine/rimanadine binding outside of the channel pore is not the primary site associated with the pharmacological inhibition of the A/M2 ion channel.
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Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel

TL;DR: The conductance properties of truncation mutants expressed in Xenopus oocytes were examined and demonstrated that the determinants for folding, drug binding, and proton translocation are packaged in a remarkably small peptide that can be studied with confidence.
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Design and pharmacological characterization of inhibitors of amantadine-resistant mutants of the M2 ion channel of influenza A virus

TL;DR: These findings help to define the location and mechanism of binding of M2 channel-blocking drugs but also demonstrate the feasibility of discovering new inhibitors that target this binding site in a number of amantadine-resistant mutants.