The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Phase Separation: Linking Cellular Compartmentalization to Disease
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Cites
A census of human RNA-binding proteins
Gerstberger, S., Hafner, M., & Tuschl, T. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3813 · Cited by 2,032
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Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · cited 1×
“Given that many of the IDPs involved in dynamic phase transitions, including the FET protein family and several hnRNPs, as well as the machineries involved in stress granule clearance, are frequently mutated in proteinopathies and form pathological aggregates (Figure 2 and Table 1), we may think of protein amyloids as…”
BackgroundSelf-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504822112 · Cited by 1,278
The changing scene of amyotrophic lateral sclerosis
Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957
Parkinson’s disease: genetics and pathogenesis
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Prion-like transmission of protein aggregates in neurodegenerative diseases
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Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Walther, D. M., Kasturi, P., Zheng, M., Pinkert, S., Vecchi, G., Ciryam, P., Morimoto, R. I., Dobson, C. M., Vendruscolo, M., Mann, M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.032 · Cited by 569
Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
Jaunmuktane, Z., Mead, S., Ellis, M., Wadsworth, J. D. F., Nicoll, A. J., Kenny, J., Launchbury, F., Linehan, J., Richard-Loendt, A., Walker, A. S., et al. (2015) · Nature · doi:10.1038/nature15369 · Cited by 518
Cited by
Tau protein liquid–liquid phase separation can initiate tau aggregation
Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102
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
Cancer-Specific Retargeting of BAF Complexes by a Prion-like Domain
Boulay, G., Sandoval, G. J., Riggi, N., Iyer, S., Buisson, R., Naigles, B., Awad, M. E., Rengarajan, S., Volorio, A., McBride, M. J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.036 · Cited by 470
Physical principles of intracellular organization via active and passive phase transitions
Berry, J., Brangwynne, C. P., & Haataja, M. (2018) · Reports on Progress in Physics · doi:10.1088/1361-6633/aaa61e · Cited by 452
The role of liquid–liquid phase separation in aggregation of the TDP-43 low-complexity domain
Babinchak, W. M., Haider, R., Dumm, B. K., Sarkar, P., Surewicz, K., Choi, J.-K., & Surewicz, W. K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007222 · Cited by 396
Metadata
- Authors
- Aguzzi, A., & Altmeyer, M.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2016-07
- Volume
- 26
- Issue
- 7
- Pages
- 547-558
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W2313094648
- Cited by
- 338
- References
- 12
- FWCI
- 2.79
- Type
- journal article
- Language
- en
- Open access
- green
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- Aguzzi, A., & Altmeyer, M. (2016). Phase Separation: Linking Cellular Compartmentalization to Disease. Trends in Cell Biology. https://doi.org/10.1016/j.tcb.2016.03.004
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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.
