The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Forced Unfolding of Proteins Within Cells
Open accessAbstract
To identify cytoskeletal proteins that change conformation or assembly within stressed cells, in situ labeling of sterically shielded cysteines with fluorophores was analyzed by fluorescence imaging, quantitative mass spectrometry, and sequential two-dye labeling. Within red blood cells, shotgun labeling showed that shielded cysteines in the two isoforms of the cytoskeletal protein spectrin were increasingly labeled as a function of shear stress and time, indicative of forced unfolding of specific domains. Within mesenchymal stem cells—as a prototypical adherent cell—nonmuscle myosin IIA and vimentin are just two of the cytoskeletal proteins identified that show differential labeling in tensed versus drug-relaxed cells. Cysteine labeling of proteins within live cells can thus be used to fluorescently map out sites of molecular-scale deformation, and the results also suggest means to colocalize signaling events such as phosphorylation with forced unfolding.
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Cites
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Self-citationEnvironmental sensing through focal adhesions
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Physical approaches to biomaterial design
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Red cell membrane: past, present, and future
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Mechanical Integration of Actin and Adhesion Dynamics in Cell Migration
Gardel, M. L., Schneider, I. C., Aratyn-Schaus, & Waterman, C. M. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.011209.122036 · Cited by 981
Metadata
- Authors
- Johnson, C. P., Tang, H.-Y., Carag, C., Speicher, D. W., & Discher, D. E.
- Venue
- Science
- Published
- 2007-08-03
- Volume
- 317
- Issue
- 5838
- Pages
- 663-666
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2137825287
- Cited by
- 377
- References
- 38
- FWCI
- 14.75
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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