The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Chemistry for the analysis of protein–protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
Open accessAbstract
Chemical cross-linking is a potentially useful technique for probing the architecture of multiprotein complexes. However, analyses using typical bifunctional cross-linkers often suffer from poor yields, and large-scale modification of nucleophilic side chains can result in artifactual results attributable to structural destabilization. We report here the de novo design and development of a type of protein cross-linking reaction that uses a photogenerated oxidant to mediate rapid and efficient cross-linking of associated proteins. The process involves brief photolysis of tris-bipyridylruthenium(II) dication with visible light in the presence of the electron acceptor ammonium persulfate and the proteins of interest. Very high yields of cross-linked products can be obtained with irradiation times of <1 second. This chemistry obviates many of the problems associated with standard cross-linking reagents.
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
Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.
Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354
Cited by
Prier, C. K., Rankic, D. A., & MacMillan, D. W. C. (2013) · Chemical Reviews · doi:10.1021/cr300503r · Cited by 9,590
Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,287
Targeting proteins with metal complexes
Meggers, E. (2009) · Chemical Communications · doi:10.1039/b813568a · Cited by 450
Copper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42
Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327
Potential applications of silk sericin, a natural protein from textile industry by-products
Aramwit, P., Siritientong, T., & Srichana, T. (2012) · Waste Management & Research: The Journal for a Sustainable Circular Economy · doi:10.1177/0734242x11404733 · Cited by 320
Metadata
- Authors
- Fancy, D. A., & Kodadek, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-05-25
- Volume
- 96
- Issue
- 11
- Pages
- 6020-6024
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2099014270
- Cited by
- 576
- References
- 1
- FWCI
- 3.63
- 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: Chemistry for the analysis of protein–protein interactions: Rapid and efficient cross-linking triggered by long wavelength light. https://app.cochat.ai/papers/10.1073/pnas.96.11.6020
- The paper
- Fancy, D. A., & Kodadek, T. (1999). Chemistry for the analysis of protein–protein interactions: Rapid and efficient cross-linking triggered by long wavelength light. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.11.6020
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.