The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Nanodiscs for structural and functional studies of membrane proteins
Open accessAbstract
Membrane proteins have long presented a challenge to biochemical and functional studies. In the absence of a bilayer environment, individual proteins and critical macromolecular complexes may be insoluble and may display altered or absent activities. Nanodisc technology provides important advantages for the isolation, purification, structural resolution and functional characterization of membrane proteins. In addition, the ability to precisely control the nanodisc composition provides a nanoscale membrane surface for investigating molecular recognition events.
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Cites
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen, S. G. F., Choi, H.-J., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,680
Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
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Self-citationCrystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
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Self-citationMembrane protein assembly into Nanodiscs
Bayburt, T. H., & Sligar, S. G. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.10.024 · Cited by 727
Self-citationHagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310901f · Cited by 498
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Self-citationArchitecture and conformational switch mechanism of the ryanodine receptor
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Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.
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Hsu, P., Bruininks, B. M. H., Jefferies, D., Cesar Telles de Souza, P., Lee, J., Patel, D. S., Marrink, S. J., Qi, Y., Khalid, S., & Im, W. (2017) · Journal of Computational Chemistry · doi:10.1002/jcc.24895 · Cited by 202
Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine
Kishi, K. E., Kim, Y. S., Fukuda, M., Inoue, M., Kusakizako, T., Wang, P. Y., Ramakrishnan, C., Byrne, E. F. X., Thadhani, E., Paggi, J. M., et al. (2022) · Cell · doi:10.1016/j.cell.2022.01.007 · Cited by 149
Biofunctionalization of Multiplexed Silicon Photonic Biosensors
Puumala, L. S., Grist, S. M., Morales, J. M., Bickford, J. R., Chrostowski, L., Shekhar, S., & Cheung, K. C. (2022) · Biosensors · doi:10.3390/bios13010053 · Cited by 55
Metadata
- Authors
- Denisov, I. G., & Sligar, S. G.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2016-06
- Volume
- 23
- Issue
- 6
- Pages
- 481-486
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2416828046
- Cited by
- 522
- References
- 50
- FWCI
- 24.68
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Denisov, I. G., & Sligar, S. G. (2016). Nanodiscs for structural and functional studies of membrane proteins. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.3195
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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.
