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Cited by 576

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Dissociation of gp120 from HIV-1 Virions Induced by Soluble CD4

Moore, John P., McKeating, Jane A., Weiss, Robin A., Sattentau, Quentin J.·1990·Science

Abstract

The CD4 antigen is the high affinity cellular receptor for the human immunodeficiency virus type-1 (HIV-1). Binding of recombinant soluble CD4 (sCD4) or the purified V1 domain of sCD4 to the surface glycoprotein gp120 on virions resulted in rapid dissociation of gp120 from its complex with the transmembrane glycoprotein gp41. This may represent the initial stage in virus-cell and cell-cell fusion. Shedding of gp120 from virions induced by sCD4 may also contribute to the mechanism by which these soluble receptor molecules neutralize HIV-1.

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Crossref · 10.1126/science.2251501

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Metadata

Authors
Moore, J. P., McKeating, J. A., Weiss, R. A., & Sattentau, Q. J.
Venue
Science
Published
1990-11-23
Volume
250
Issue
4984
Pages
1139-1142
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1986865717
Cited by
576
References
5
FWCI
14.61
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Dissociation of gp120 from HIV-1 Virions Induced by Soluble CD4. https://app.cochat.ai/papers/10.1126/science.2251501
The paper
Moore, J. P., McKeating, J. A., Weiss, R. A., & Sattentau, Q. J. (1990). Dissociation of gp120 from HIV-1 Virions Induced by Soluble CD4. Science. https://doi.org/10.1126/science.2251501

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.