Fragile epitopes—Antibody’s guess is as good as yours
Open accessAbstract
Critical research antibodies need systematic validation (Frohner et al . and Schüchner et al ., in 28 January 2020 issue).
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
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Antibodies have limitations including batch-to-batch variation, high production cost, poor chemical stability, and lack of proteoform-specific epitope recognition, which contribute to reproducibility issues.
“However, antibodies possess many inherent limitations: batch-to-batch variation, high cost of production, poor chemical stability, and lack of proteoform-specific epitope recognition that collectively contribute to reproducibility issues [62–64].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [62]
The intrinsic challenge of designing and evaluating epitope-specific antibodies for PTMs makes it difficult to develop robust antibodies suitable for proteoform analysis.
“Moreover, the intrinsic challenge of designing and evaluating epitope-specific antibodies for PTMs makes it difficult to develop robust antibodies suitable for proteoform analysis16.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [16]
These NPs can serve as replacements to conventional immuno-based techniques to overcome antibody-related limitations in cTnI immunoassays and potentially address the current reproducibility crisis caused by antibodies in general.
“Thus, these NPs can serve as replacements to conventional immuno-based techniques to overcome the antibody-related limitations in cTnI immunoassays and potentially address the current reproducibility crisis caused by antibodies in general14–16,51,53.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [16]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product.
Evan, G. I., Lewis, G. K., Ramsay, G. M., & Bishop, J. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3610 · Cited by 2,412 · see citing works
Isolation of Monoclonal Antibodies Specific for Human c-myc Proto-Oncogene Product
Evan, G. I., Lewis, G. K., Ramsay, G. M., & Bishop, J. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3610-3616.1985 · Cited by 795 · see citing works
Reproducibility: Standardize antibodies used in research
Bradbury, A., & Plückthun, A. (2015) · Nature · doi:10.1038/518027a · Cited by 647 · see citing works
Three-dimensional structure of an antibody-antigen complex.
Sheriff, S., Silverton, E. W., PADLAN, E. A., Cohen, G. H., Smith‐Gill, S. J., Finzel, B. C., & Davies, D. R. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8075 · Cited by 607 · see citing works
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459 · see citing works
An analysis of critical factors for quantitative immunoblotting
Janes, K. A. (2015) · Science Signaling · doi:10.1126/scisignal.2005966 · Cited by 206 · see citing works
Self-citationYu, X. X., Du, X., Moreno, C. S., Green, R. E., Ogris, E., Feng, Q., Chou, L., McQuoid, M. J., & Pallas, D. C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.185 · Cited by 160 · see citing works
Krauß, N., Wessner, H., Welfle, K., Welfle, H., Scholz, C., Seifert, M., Zubow, K., Aÿ, J., Hahn, M. G., Scheerer, P., et al. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22080 · Cited by 34 · see citing works
Frohner, I. E., Mudrak, I., Kronlachner, S., Schüchner, S., & Ogris, E. (2020) · Science Signaling · doi:10.1126/scisignal.aax6490 · Cited by 34 · see citing works
Schüchner, S., Behm, C., Mudrak, I., & Ogris, E. (2020) · Science Signaling · doi:10.1126/scisignal.aax9730 · Cited by 28 · see citing works
Profiling Subcellular Protein Phosphatase Responses to Coxsackievirus B3 Infection of Cardiomyocytes
Shah, M., Smolko, C. M., Kinicki, S., Chapman, Z. D., Brautigan, D. L., & Janes, K. A. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o116.063487 · Cited by 14 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Top-down proteomics: challenges, innovations, and applications in basic and clinical research
Brown, K. A., Melby, J. A., Roberts, D. S., & Ge, Y. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1855982 · Cited by 152 · see citing works
Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum
Tiambeng, T. N., Roberts, D. S., Brown, K. A., Zhu, Y., Chen, B., Wu, Z., Mitchell, S. D., Guardado-Alvarez, T. M., Jin, S., & Ge, Y. (2020) · Nature Communications · doi:10.1038/s41467-020-17643-1 · Cited by 76 · see citing works
- Authors
- Janes, K. A.
- Affiliations
- University of Virginia (US)
- Corresponding author
- Janes, Kevin A.
- ORCID
- Janes, Kevin A.
- Venue
- Science Signaling
- Published
- 2020-01-28
- Volume
- 13
- Issue
- 616
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC7231929
- OpenAlex
- W3003157002
- Cited by
- 16
- References
- 11
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2022: 3 · 2021: 2 · 2020: 4
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (U01CA215794, R01CA194470, R01CA214718)
- National Institute of General Medical Sciences (T32GM145443)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- monoclonal antibodies, antibody-antigen binding, post-translational modification, epitope mapping
- MeSH terms
- Animals, Antibodies, Monoclonal, Antibody Affinity, Antibody Specificity, Epitopes, Humans
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
