Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 1,203

The DOI matches its Crossref record.

The antigenic structure of the HIV gp120 envelope glycoprotein

Open access
Wyatt, Richard, Kwong, Peter D., Desjardins, Elizabeth, Sweet, Raymond W., Robinson, James, Hendrickson, Wayne A., Sodroski, Joseph G.·1998·Nature

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/31514

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 30

  1. Allen, J. et al. Identification of the major envelope glycoprotein product of HTLV-III. Science 228, 1091–1094 (1983). · DOI · Paper page
  2. Dalgleish, A. G. et al. The CD4 (T4) antigen is essential component of the receptor for the AIDS retrovirus. Nature 312, 763–767 (1984). · DOI · Paper page
  3. Klatzmann, D. et al. T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature 312, 767–768 (1984). · DOI · Paper page
  4. Feng, Y., Broder, C. C., Kennedy, P. E. & Berger, E. HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272, 872–877 (1996). · DOI · Paper page
  5. Moore, J. P. & Sodroski, J. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol. 70, 1863–1872 (1996). · DOI · Paper page
  6. Wyatt, R. et al. Analysis of the interaction of the human immunodeficiency virus type 1 (HIV-1) gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J. Virol. 71, 9722–9731 (1997). · DOI
  7. Sattentau, Q. J. & Moore, J. P. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med. 182, 185–196 (1995). · DOI · Paper page
  8. Posner, M. et al. An IgG human monoclonal antibody which reacts with HIV-1 gp120, inhibits virus binding to cells, and neutralizes infection. J. Immunol. 146, 4325–4332 (1991). · DOI · Paper page
  9. Ho, D. et al. Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody. J. Virol. 65, 489–493 (1991). · doi:10.1128/jvi.65.1.489-493.1991
  10. Wu, L. et al. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CR5. Nature 384, 179–183 (1996). · DOI · Paper page
  11. Trkola, A. et al. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature 384, 184–187 (1996). · DOI · Paper page
  12. Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648–659 (1998). · DOI · Paper page
  13. Myers, G. et al. Human Retroviruses and AIDS. A Compilation and Analysis of Nucleic Acid and Amino Acid Sequences (Los Alamos National Laboratory, (1996)).
  14. Leonard, C. et al. Assignment of interchain disulfide bonds and characterization of potential glycosylation sites of the type 1 human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265, 10373–10382 (1990). · DOI · Paper page
  15. Fung, M. S. C. et al. Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus type 1 gp120. J. Virol. 66, 848–856 (1992). · doi:10.1128/jvi.66.2.848-856.1992
  16. Putney, S. et al. HTLV-III/LAV-neutralizing antibodies to an E. coli-produced fragment of the virus envelope. Science 234, 1392–1395 (1986). · DOI · Paper page
  17. Rusche, J. R. et al. Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino-acid sequence of the viral envelope gp120. Proc. Natl Acad. Sci. USA 85, 3198–3202 (1988). · DOI · Paper page
  18. Thali, M. et al. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67, 3978–3988 (1993). · DOI · Paper page
  19. Trkola, A. et al. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 70, 1100–1108 (1996). · DOI · Paper page
  20. Binley, J. et al. Analysis of the interaction of antibodies with a conserved, enzymatically deglycosylated core of the HIV-1 gp120 envelope glycoprotein. AIDS Res. Hum. Retrovir. 14, 191–198 (1997). · DOI
  21. Wyatt, R. et al. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J. Virol. 69, 5723–5733 (1995). · DOI · Paper page
  22. Thali, M. et al. Discontinuous, conserved neutralization epitopes overlapping the CD4 binding region of the HIV-1 gp120 envelope glycoprotein. J. Virol. 66, 5635–5641 (1992). · DOI · Paper page
  23. Cao, J. et al. Replication and neutralization of human immunodeficiency virus type 1 lacking the V1/V2 variable loops of the gp120 envelope glycoprotein. J. Virol. 71, 9808–9812 (1997). · DOI
  24. Roben, P. et al. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68, 4821–4848 (1994). · DOI · Paper page
  25. Moore, J. P. et al. Exploration of antigenic variation in gp120 from clades A through F of human immunodeficiency virus type 1 by using monoclonal antibodies. J. Virol. 68, 8350–8364 (1994). · DOI
  26. Wyatt, R. et al. Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 67, 4557–4565 (1993). · DOI
  27. Watkins, B. A. et al. Immune escape by human immunodeficiency virus type 1 from neutralizing antibodies: evidence for multiple pathways. J. Virol. 67, 7493–7500 (1993). · DOI
  28. Karlsson, G. et al. Characterization of molecularly cloned simian-human immunodeficiency viruses causing rapid CD4+ lymphocyte depletion in rhesus monkeys. J. Virol. 71, 4218–4225 (1997). · doi:10.1128/jvi.71.6.4218-4225.1997
  29. Wu, H., Kwong, P. D. & Hendrickson, W. A. Dimeric association and segmental variability in the structure of human CD4. Nature 387, 527–530 (1997). · DOI · Paper page
  30. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281–296 (1991). · DOI · Paper page

Cited by

See all 1,203

Metadata

Authors
Wyatt, R., Kwong, P. D., Desjardins, E., Sweet, R. W., Robinson, J., Hendrickson, W. A., & Sodroski, J. G.
Venue
Nature
Published
1998-06
Volume
393
Issue
6686
Pages
705-711
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W1628484047
Cited by
1,203
References
0
FWCI
20.68
Type
journal article
Language
en
Open access
bronze
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: The antigenic structure of the HIV gp120 envelope glycoprotein. https://app.cochat.ai/papers/10.1038/31514
The paper
Wyatt, R., Kwong, P. D., Desjardins, E., Sweet, R. W., Robinson, J., Hendrickson, W. A., & Sodroski, J. G. (1998). The antigenic structure of the HIV gp120 envelope glycoprotein. Nature. https://doi.org/10.1038/31514

Data sources

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.