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Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.
Kephart, Sally M; Hom, Nancy; Lee, Kelly K.
Afiliación
  • Kephart SM; Department of Medicinal Chemistry, University of Washington, Seattle, WA, USA.
  • Hom N; Department of Medicinal Chemistry, University of Washington, Seattle, WA, USA.
  • Lee KK; Department of Medicinal Chemistry, University of Washington, Seattle, WA, USA; Biological Structure Physics and Design Graduate Program, University of Washington, Seattle, WA, USA. Electronic address: kklee@uw.edu.
Trends Biochem Sci ; 49(10): 916-931, 2024 Oct.
Article en En | MEDLINE | ID: mdl-39054240
ABSTRACT
Protein-mediated membrane fusion is the dynamic process where specialized protein machinery undergoes dramatic conformational changes that drive two membrane bilayers together, leading to lipid mixing and opening of a fusion pore between previously separate membrane-bound compartments. Membrane fusion is an essential stage of enveloped virus entry that results in viral genome delivery into host cells. Recent studies applying cryo-electron microscopy techniques in a time-resolved fashion provide unprecedented glimpses into the interaction of viral fusion proteins and membranes, revealing fusion intermediate states from the initiation of fusion to release of the viral genome. In combination with complementary structural, biophysical, and computation modeling approaches, these advances are shedding new light on the mechanics and dynamics of protein-mediated membrane fusion.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Microscopía por Crioelectrón / Internalización del Virus / Tomografía con Microscopio Electrónico / Fusión de Membrana Límite: Humans Idioma: En Revista: Trends Biochem Sci Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Microscopía por Crioelectrón / Internalización del Virus / Tomografía con Microscopio Electrónico / Fusión de Membrana Límite: Humans Idioma: En Revista: Trends Biochem Sci Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos