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Cited by 283

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Maturation-Dependent HIV-1 Surface Protein Redistribution Revealed by Fluorescence Nanoscopy

Open access
Chojnacki, Jakub, Staudt, Thorsten, Glass, Bärbel, Bingen, Pit, Engelhardt, Johann, Anders, Maria, Schneider, Jale, Müller, Barbara, Hell, Stefan W., Kräusslich, Hans-Georg·2012·Science

Abstract

Switching on HIV: Newly assembled human immunodeficiency virus (HIV) virions bud from the host cell as immature particles. Proteolysis of the Gag protein, which forms a structural lattice below the viral membrane, leads to the formation of mature infectious HIV. Fusion of mature HIV virions with a target cell is mediated by viral envelope (Env) proteins that occur in trimeric “spikes” on the surface of the virion. Chojnacki et al. (p. 524 ) used subdiffraction microscopy to show that the spikes were dispersed on the immature virion but clustered into a single focus on the mature virion. The clustering was important for infectivity. Coupling Gag proteolysis with clustering may ensure that only particles whose interior has switched to the entry mode are competent for membrane fusion.

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Metadata

Authors
Chojnacki, J., Staudt, T., Glass, B., Bingen, P., Engelhardt, J., Anders, M., Schneider, J., Müller, B., Hell, S. W., & Kräusslich, H.-G.
Venue
Science
Published
2012-10-26
Volume
338
Issue
6106
Pages
524-528
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1971421092
Cited by
283
References
30
FWCI
11.07
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Maturation-Dependent HIV-1 Surface Protein Redistribution Revealed by Fluorescence Nanoscopy. https://app.cochat.ai/papers/10.1126/science.1226359
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Chojnacki, J., Staudt, T., Glass, B., Bingen, P., Engelhardt, J., Anders, M., Schneider, J., Müller, B., Hell, S. W., & Kräusslich, H.-G. (2012). Maturation-Dependent HIV-1 Surface Protein Redistribution Revealed by Fluorescence Nanoscopy. Science. https://doi.org/10.1126/science.1226359

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