The DOI matches its Crossref record.
Cross-Linking of Lens Crystallins in a Photodynamic System: A Process Mediated by Singlet Oxygen
Abstract
In a dye-sensitized photooxidation system, lens crystallin polypeptides become cross-linked, and a blue fluorescence that is associated with the proteins is produced. These changes are similar to those seen in vivo in the aging human lens. Evidence implicating singlet oxygen as the causative agent of the effects in vitro is presented, and the possibility that this species may play a role in aging and cataractogenesis in vivo is discussed.
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
Cited by
Singlet oxygen-mediated damage to proteins and its consequences
Davies, M. J. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00817-9 · Cited by 992
Singlet Molecular Oxygen Reactions with Nucleic Acids, Lipids, and Proteins
Di Mascio, P., Martinez, G. R., Miyamoto, S., Ronsein, G. E., Medeiros, M. H. G., & Cadet, J. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00554 · Cited by 659
Pattison, D. I., Rahmanto, A. S., & Davies, M. J. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05164d · Cited by 573
Hydrogen peroxide and human cataract
Spector, A., & Garner, W. H. (1981) · Experimental Eye Research · doi:10.1016/s0014-4835(81)80107-8 · Cited by 502
Photo-oxidation of proteins and its role in cataractogenesis
Davies, M. J., & Truscott, R. J. W. (2001) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/s1011-1344(01)00208-1 · Cited by 448
Metadata
- Authors
- Goosey, J. D., Zigler, J. S., & Kinoshita, J. H.
- Venue
- Science
- Published
- 1980-06-13
- Volume
- 208
- Issue
- 4449
- Pages
- 1278-1280
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1988871512
- Cited by
- 205
- References
- 0
- FWCI
- 4.88
- Type
- journal article
- Language
- en
- Open access
- closed
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: Cross-Linking of Lens Crystallins in a Photodynamic System: A Process Mediated by Singlet Oxygen. https://app.cochat.ai/papers/10.1126/science.7375939
- The paper
- Goosey, J. D., Zigler, J. S., & Kinoshita, J. H. (1980). Cross-Linking of Lens Crystallins in a Photodynamic System: A Process Mediated by Singlet Oxygen. Science. https://doi.org/10.1126/science.7375939
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.
