The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids.
Open accessAbstract
A novel yet simple method is described that facilitates the synthesis of large numbers of peptides to the extent that the synthesis process need no longer be the limiting factor in many studies involving peptides. By using the methods described, 10-20 mg of 248 different 13-residue peptides representing single amino acid variants of a segment of the hemagglutinin protein (HA1) have been prepared and characterized in less than 4 weeks. Through examination of the binding of these analogs to monoclonal antibodies raised against residues 75-110 of HA1, it was found that a single amino acid, aspartic acid at position 101, is of unique importance to the interaction. Two other residues, aspartic acid-104 and alanine-106, were found to play a lesser but significant role in the binding interaction. Other single positional residue variations appear to be of little or no importance.
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.
Integrity signals
Registry
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.
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
Geysen, H. M., Meloen, R. H., & Barteling, S. J. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.13.3998 · Cited by 1,475
The structure of an antigenic determinant in a protein
Wilson, I. A., Niman, H. L., Houghten, R. A., Cherenson, A. R., Connolly, M. L., & Lerner, R. A. (1984) · Cell · doi:10.1016/0092-8674(84)90412-4 · Cited by 828
Self-citationBittle, J. L., Houghten, R. A., Alexander, H., Shinnick, T. M., Sutcliffe, J. G., Lerner, R. A., Rowlands, D. J., & Brown, F. (1982) · Nature · doi:10.1038/298030a0 · Cited by 820
Self-citationImmunogenic structure of the influenza virus hemagglutinin
Green, N., Alexander, H., Olson, A., Alexander, S., Shinnick, T. M., Sutcliffe, J. G., & Lerner, R. A. (1982) · Cell · doi:10.1016/0092-8674(82)90202-1 · Cited by 756
Tapping the immunological repertoire to produce antibodies of predetermined specificity
Lerner, R. A. (1982) · Nature · doi:10.1038/299592a0 · Cited by 460
Niman, H. L., Houghten, R. A., Walker, L. E., Reisfeld, R. A., Wilson, I. A., Hogle, J. M., & Lerner, R. A. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.16.4949 · Cited by 377
Self-citationFreidinger, R. M., Veber, D. F., Perlow, D. S., Brooks, J. R., & Saperstein, R. (1980) · Science · doi:10.1126/science.7001627 · Cited by 315
Geysen, H. M., Barteling, S. J., & Meloen, R. H. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.1.178 · Cited by 288
JOU, W., VERHOEYEN, M., DEVOS, R., SAMAN, E., FANG, R., HUYLEBROECK, D., FIERS, W., THRELFALL, G., BARBER, C., & CAREY, N. (1980) · Cell · doi:10.1016/s0092-8674(80)80045-6 · Cited by 225
Polyamide supports for polypeptide synthesis
Atherton, E., Clive, D. L. J., & Sheppard, R. C. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00855a053 · Cited by 224
Cited by
Merrifield, B. (1986) · Science · doi:10.1126/science.3961484 · Cited by 1,005
A Molecular Basis for Insulin Resistance
Paz, K., Hemi, R., LeRoith, D., Karasik, A., Elhanany, E., Kanety, H., & Zick, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29911 · Cited by 549
Faé, K. C., da Silva, D. D., Oshiro, S. E., Tanaka, A. C., Pomerantzeff, P. M. A., Douay, C., Charron, D., Toubert, A., Cunningham, M. W., Kalil, J., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.9.5662 · Cited by 183
Metadata
- Authors
- Houghten, R. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-08
- Volume
- 82
- Issue
- 15
- Pages
- 5131-5135
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2094954825
- Cited by
- 1,643
- References
- 14
- FWCI
- 9.48
- Type
- journal article
- Language
- en
- Open access
- green
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: General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids. https://app.cochat.ai/papers/10.1073/pnas.82.15.5131
- The paper
- Houghten, R. A. (1985). General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.15.5131
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.
