The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
Open accessAbstract
In vivo fluorescent labeling of an expressed protein has enabled the observation of its stability and aggregation directly in bacterial cells. Mammalian cellular retinoic acid-binding protein I (CRABP I) was mutated to incorporate in a surface-exposed omega loop the sequence Cys-Cys-Gly-Pro-Cys-Cys, which binds specifically to a biarsenical fluorescein dye (FlAsH). Unfolding of labeled tetra-Cys CRABP I is accompanied by enhancement of FlAsH fluorescence, which made it possible to determine the free energy of unfolding of this protein by urea titration in cells and to follow in real time the formation of inclusion bodies by a slow-folding, aggregationprone mutant (FlAsH-labeled P39A tetra-Cys CRABP I). Aggregation in vivo displayed a concentration-dependent apparent lag time similar to observations of protein aggregation in purified in vitro model systems.
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
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Cited by
Probing Protein Folding and Conformational Transitions with Fluorescence
Royer, C. A. (2006) · Chemical Reviews · doi:10.1021/cr0404390 · Cited by 731
Effects of Molecular Crowding on the Structures, Interactions, and Functions of Nucleic Acids
Nakano, S.-I., Miyoshi, D., & Sugimoto, N. (2014) · Chemical Reviews · doi:10.1021/cr400113m · Cited by 567
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Self-citationMacromolecular Crowding and Protein Stability
Wang, Y., Sarkar, M., Smith, A. E., Krois, A. S., & Pielak, G. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305300m · Cited by 346
Physical limits of cells and proteomes
Dill, K. A., Ghosh, K., & Schmit, J. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114477108 · Cited by 298
Metadata
- Authors
- Ignatova, Z., & Gierasch, L. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-12-30
- Volume
- 101
- Issue
- 2
- Pages
- 523-528
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2081457168
- Cited by
- 239
- References
- 1
- FWCI
- 2.79
- 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: Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. https://app.cochat.ai/papers/10.1073/pnas.0304533101
- The paper
- Ignatova, Z., & Gierasch, L. M. (2004). Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0304533101
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.
