The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Calcium-dependent molecular spring elements in the giant protein titin
Open accessAbstract
Titin (also known as connectin) is a giant protein with a wide range of cellular functions, including providing muscle cells with elasticity. Its physiological extension is largely derived from the PEVK segment, rich in proline (P), glutamate (E), valine (V), and lysine (K) residues. We studied recombinant PEVK molecules containing the two conserved elements: ≈28-residue PEVK repeats and E-rich motifs. Single molecule experiments revealed that calcium-induced conformational changes reduce the bending rigidity of the PEVK fragments, and site-directed mutagenesis identified four glutamate residues in the E-rich motif that was studied (exon 129), as critical for this process. Experiments with muscle fibers showed that titin-based tension is calcium responsive. We propose that the PEVK segment contains E-rich motifs that render titin a calcium-dependent molecular spring that adapts to the physiological state of the cell.
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Cites
Entropic Elasticity of λ-Phage DNA
Bustamante, C., Marko, J. F., Siggia, E. D., & Smith, S. (1994) · Science · doi:10.1126/science.8079175 · Cited by 2,154
Huxley, H. E. (1969) · Science · doi:10.1126/science.164.3886.1356 · Cited by 1,959
Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity
Labeit, S., & Kolmerer, B. (1995) · Science · doi:10.1126/science.270.5234.293 · Cited by 1,237
Self-citationFolding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers
Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L., & Bustamante, C. (1997) · Science · doi:10.1126/science.276.5315.1112 · Cited by 1,217
Self-citationMechanical unfolding intermediates in titin modules
Marszalek, P. E., Lu, H., Li, H., Carrion-Vazquez, M., Oberhauser, A. F., Schulten, K., & Fernandez, J. M. (1999) · Nature · doi:10.1038/47083 · Cited by 798
Bang, M.-L., Centner, T., Fornoff, F., Geach, A. J., Gotthardt, M., McNabb, M., Witt, C. C., Labeit, D., Gregorio, C. C., Granzier, H., et al. (2001) · Circulation Research · doi:10.1161/hh2301.100981 · Cited by 712
Self-citationGranzier, H. L., & Irving, T. C. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80278-x · Cited by 640
Self-citationReverse engineering of the giant muscle protein titin
Li, H., Linke, W. A., Oberhauser, A. F., Carrion-Vazquez, M., Kerkvliet, J. G., Lu, H., Marszalek, P. E., & Fernandez, J. M. (2002) · Nature · doi:10.1038/nature00938 · Cited by 517
Mechanical design of proteins studied by single-molecule force spectroscopy and protein engineering
Carrión‐Vázquez, M., Oberhauser, A. F., Fisher, T. E., Marszałek, P. E., Li, H., & Fernández, J. M. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00017-1 · Cited by 443
Force enhancement following stretching of skeletal muscle
Herzog, W., & Leonard, T. R. (2002) · Journal of Experimental Biology · doi:10.1242/jeb.205.9.1275 · Cited by 269
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Sommer, G., Schriefl, A. J., Andrä, M., Sacherer, M., Viertler, C., Wolinski, H., & Holzapfel, G. A. (2015) · Acta Biomaterialia · doi:10.1016/j.actbio.2015.06.031 · Cited by 290
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Nelson, C. R., Debold, E. P., & Fitts, R. H. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00206.2014 · Cited by 71
Metadata
- Authors
- Labeit, D., Watanabe, K., Witt, C., Fujita, H., Wu, Y., Lahmers, S., Funck, T., Labeit, S., & Granzier, H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-10-30
- Volume
- 100
- Issue
- 23
- Pages
- 13716-13721
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2100968871
- Cited by
- 396
- References
- 27
- FWCI
- 5.04
- Type
- journal article
- Language
- en
- Open access
- green
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- Labeit, D., Watanabe, K., Witt, C., Fujita, H., Wu, Y., Lahmers, S., Funck, T., Labeit, S., & Granzier, H. (2003). Calcium-dependent molecular spring elements in the giant protein titin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2235652100
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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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