J
Jeremy S. Rossman
Researcher at University of Kent
Publications - 39
Citations - 2370
Jeremy S. Rossman is an academic researcher from University of Kent. The author has contributed to research in topics: Virus & Membrane curvature. The author has an hindex of 17, co-authored 35 publications receiving 1992 citations. Previous affiliations of Jeremy S. Rossman include Uniformed Services University of the Health Sciences & Howard Hughes Medical Institute.
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Journal ArticleDOI
Influenza virus assembly and budding.
TL;DR: This review investigates the latest research on influenza virus budding in an attempt to provide a step-by-step analysis of the assembly and budding processes for influenza viruses.
Journal ArticleDOI
Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission
Jeremy S. Rossman,Jeremy S. Rossman,Xianghong Jing,George P. Leser,Robert A. Lamb,Robert A. Lamb +5 more
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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Discovery and Mechanism of Highly Efficient Cyclic Cell-Penetrating Peptides
Ziqing Qian,Agnieszka Martyna,Ryan L. Hard,Jiang Wang,George Appiah-Kubi,Christopher C. Coss,Mitch A. Phelps,Jeremy S. Rossman,Dehua Pei +8 more
TL;DR: Data suggest that cyclic CPPs exit the endosome by binding to the endOSomal membrane and inducing CPP-enriched lipid domains to bud off as small vesicles, which should provide a powerful system for intracellular delivery of therapeutic agents and chemical probes.
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Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation
Jeremy S. Rossman,Xianghong Jing,Xianghong Jing,George P. Leser,Victoria Balannik,Lawrence H. Pinto,Robert A. Lamb +6 more
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.
Journal ArticleDOI
Filamentous Influenza Virus Enters Cells Via Macropinocytosis
TL;DR: It is found that filamentous influenza viruses use macropinocytosis as the primary entry mechanism, and low pH triggers a conformational change in the M2 ion channel protein, altering membrane curvature and leading to a fragmentation of the filamentous virions.