The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The Structure and Function of Proline Recognition Domains
Abstract
One particularly abundant group of modular recognition domains consists of those that bind proline-rich motifs. Such modules, including the SH3, WW, and EVH1 domains, play a critical role in the assembly and regulation of many intracellular signaling complexes. These domains use strikingly similar molecular mechanisms of proline recognition. We discuss some of the potential biological advantages conferred by proline recognition, which may explain its widespread use in signaling.
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Comparative Genomics of the Eukaryotes
Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698 · cited 1×
“The importance of proline-rich motifs in biology is highlighted by the finding that proline-rich regions (1) are the most common sequence motif in the Drosophila genome and the second most common in the Caenorhabditis elegans genome ( 2 ).”
BackgroundTsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369
Influence of proline residues on protein conformation
MacArthur, M. W., & Thornton, J. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90721-h · Cited by 1,189
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Cited by
Assembly of Cell Regulatory Systems Through Protein Interaction Domains
Pawson, T., & Nash, P. (2003) · Science · doi:10.1126/science.1083653 · Cited by 1,422
Landthaler, M., Yalcin, A., & Tuschl, T. (2004) · Current Biology · doi:10.1016/j.cub.2004.11.001 · Cited by 850
Specificity in Signal Transduction
Pawson, T. (2004) · Cell · doi:10.1016/s0092-8674(03)01077-8 · Cited by 816
Protein Sectors: Evolutionary Units of Three-Dimensional Structure
Halabi, N., Rivoire, O., Leibler, S., & Ranganathan, R. (2009) · Cell · doi:10.1016/j.cell.2009.07.038 · Cited by 707
THE ESCRT COMPLEXES: Structure and Mechanism of a Membrane-Trafficking Network
Hurley, J. H., & Emr, S. D. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102126 · Cited by 546
Metadata
- Authors
- Zarrinpar, A., Bhattacharyya, R. P., & Lim, W. A.
- Venue
- Science's STKE
- Published
- 2003-04-22
- Volume
- 2003
- Issue
- 179
- Pages
- RE8-RE8
- ISSN
- 1525-8882 (ISSN-L)
- OpenAlex
- W2158133029
- Cited by
- 365
- References
- 4
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- closed
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