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Anna Ahn

Researcher at Yeshiva University

Publications -  6
Citations -  344

Anna Ahn is an academic researcher from Yeshiva University. The author has contributed to research in topics: Semliki Forest virus & Lipid bilayer fusion. The author has an hindex of 6, co-authored 6 publications receiving 336 citations. Previous affiliations of Anna Ahn include New York Medical College & Albert Einstein College of Medicine.

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Journal ArticleDOI

The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains

TL;DR: Detergent extraction and gradient floatation experiments are used to demonstrate that E1* associated selectively with detergent-resistant membrane domains (DRMs or rafts) and monoclonal antibody studies demonstrated that raft association was mediated by the proposed E1 fusion peptide.
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Formation and Characterization of the Trimeric Form of the Fusion Protein of Semliki Forest Virus

TL;DR: Data from a sensitive fluorescence assay and protein structure predictions suggest a model in which the less stable native E1 subunit specifically responds to low pH to form the more stable E1 homotrimer via conformational changes different from those of the coiled-coil type of fusion proteins.
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Multistep Regulation of Membrane Insertion of the Fusion Peptide of Semliki Forest Virus

TL;DR: Study of the class II fusion protein E1 from the alphavirus Semliki Forest virus shows that the membrane insertion of the E1 fusion peptide is regulated by additional low-pH-dependent steps after exposure, perhaps involving an E1-cholesterol interaction.
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An Epitope of the Semliki Forest Virus Fusion Protein Exposed during Virus-Membrane Fusion

TL;DR: Characterization of monoclonal antibodies specific for the acid conformation of E1 localize an E1 region that is normally hidden in the neutral pH structure and becomes exposed as part of the reorganization of the spike protein to its fusion-active conformation.
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Purification and Crystallization Reveal Two Types of Interactions of the Fusion Protein Homotrimer of Semliki Forest Virus

TL;DR: Determination of the structure will provide the first high-resolution views of both the low-pH-induced trimeric conformation and the target membrane-interacting region of the alphavirus fusion protein.