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Cited by 308

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Multiple Extracellular Elements of CCR5 and HIV-1 Entry: Dissociation from Response to Chemokines

Atchison, Robert E., Gosling, Jennifa, Monteclaro, Felipe S., Franci, Christian, Digilio, Laura, Charo, Israel F., Goldsmith, Mark A.·1996·Science

Abstract

The human β-chemokine receptor CCR5 is an important cofactor for entry of human immunodeficiency virus-type 1 (HIV-1). The murine form of CCR5, despite its 82 percent identity to the human form, was not functional as an HIV-1 coreceptor. HIV-1 entry function could be reconstituted by fusion of various individual elements derived from the extracellular region of human CCR5 onto murine CCR5. Analysis of chimeras containing elements from human CCR5 and human CCR2B suggested that a complex structure rather than single contact sites is responsible for facilitation of viral entry. Further, certain chimeras lacking the domains necessary to signal in response to their natural chemokine ligands retained vigorous HIV-1 coreceptor activity.

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Metadata

Authors
Atchison, R. E., Gosling, J., Monteclaro, F. S., Franci, C., Digilio, L., Charo, I. F., & Goldsmith, M. A.
Venue
Science
Published
1996-12-13
Volume
274
Issue
5294
Pages
1924-1926
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2026330341
Cited by
308
References
0
FWCI
17.99
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Multiple Extracellular Elements of CCR5 and HIV-1 Entry: Dissociation from Response to Chemokines. https://app.cochat.ai/papers/10.1126/science.274.5294.1924
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Atchison, R. E., Gosling, J., Monteclaro, F. S., Franci, C., Digilio, L., Charo, I. F., & Goldsmith, M. A. (1996). Multiple Extracellular Elements of CCR5 and HIV-1 Entry: Dissociation from Response to Chemokines. Science. https://doi.org/10.1126/science.274.5294.1924

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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