The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks
Open accessAbstract
Interactions of LARKS protein domains: More than 1500 human proteins contain long, disordered stretches of “low complexity”—strings of just a few of the 20 common amino acids. The functions of these low-complexity domains have been unclear. Hughes et al. present atomic-resolution structures that suggest that short segments of two such domains can bind weakly to each other by forming a pair of kinked β-sheets. Because aromatic amino acid side chains stabilize these interactions, the interacting motifs are termed LARKS, for low-complexity, aromatic-rich, kinked segments. Numerous proteins associated with membraneless organelles of biological cells contain low-complexity domains housing multiple LARKS. Science , this issue p. 698
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Sheldrick, G. M. (2008) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 87,804
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,742
Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
UniProt: the Universal Protein knowledgebase
Apweiler, R. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh131 · Cited by 7,498
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,100
Towards automated crystallographic structure refinement with phenix.refine
Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511
UniProt: the universal protein knowledgebase
The UniProt Consortium (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw1099 · Cited by 4,436
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Alberti, S., Gladfelter, A., & Mittag, T. (2019) · Cell · doi:10.1016/j.cell.2018.12.035 · Cited by 2,856
Wang, J., Choi, J.-M., Holehouse, A. S., Lee, H. O., Zhang, X., Jahnel, M., Maharana, S., Lemaitre, R., Pozniakovsky, A., Drechsel, D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.006 · Cited by 2,076
Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,160
Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
Martin, E. W., Holehouse, A. S., Peran, I., Farag, M., Incicco, J. J., Bremer, A., Grace, C. R., Soranno, A., Pappu, R. V., & Mittag, T. (2020) · Science · doi:10.1126/science.aaw8653 · Cited by 1,147
α‐Synuclein aggregation nucleates through liquid‐liquid phase separation
Ray, S., Singh, N., Kumar, R., Patel, K., Pandey, S., Datta, D., Mahato, J., Panigrahi, R., Navalkar, A., Mehra, S., et al. (2020) · Nature Chemistry · doi:10.1038/s41557-020-0465-9 · Cited by 863
Metadata
- Authors
- Hughes, M. P., Sawaya, M. R., Boyer, D. R., Goldschmidt, L., Rodriguez, J. A., Cascio, D., Chong, L., Gonen, T., & Eisenberg, D. S.
- Venue
- Science
- Published
- 2018-02-09
- Volume
- 359
- Issue
- 6376
- Pages
- 698-701
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2785420592
- Cited by
- 450
- References
- 47
- FWCI
- 15.70
- Type
- journal article
- Language
- en
- Open access
- green
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