The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
Abstract
Using a recently described self-assembly process (Bayburt, T. H.; Grinkova, Y. V.; Sligar, S. G. Nano Letters 2002, 2, 853-856), we prepared soluble monodisperse discoidal lipid/protein particles with controlled size and composition, termed Nanodiscs, in which the fragment of dipalmitoylphosphatidylcholine (DPPC) bilayer is surrounded by a helical protein belt. We have customized the size of these particles by changing the length of the amphipathic helical part of this belt, termed membrane scaffold protein (MSP). Herein we describe the design of extended and truncated MSPs, the optimization of self-assembly for each of these proteins, and the structure and composition of the resulting Nanodiscs. We show that the length of the protein helix surrounding the lipid part of a Nanodisc determines the particle diameter, as measured by HPLC and small-angle X-ray scattering (SAXS). Using different scaffold proteins, we obtained Nanodiscs with the average size from 9.5 to 12.8 nm with a very narrow size distribution (+/-3%). Functionalization of the N-terminus of the scaffold protein does not perturb their ability to form homogeneous discoidal structures. Detailed analysis of the solution scattering confirms the presence of a lipid bilayer of 5.5 nm thickness in Nanodiscs of different sizes. The results of this study provide an important structural characterization of self-assembled phospholipid bilayers and establish a framework for the design of soluble amphiphilic nanoparticles of controlled size.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Whitesides, G. M., & Grzybowski, B. (2002) · Science · doi:10.1126/science.1070821 · Cited by 7,439
Svergun, D. I. (1992) · Journal of Applied Crystallography · doi:10.1107/s0021889892001663 · Cited by 3,759
Molecular Self-Assembly and Nanochemistry: a Chemical Strategy for the Synthesis of Nanostructures
Whitesides, G. M., Mathias, J. P., & Seto, C. T. (1991) · Science · doi:10.1126/science.1962191 · Cited by 3,632
Svergun, D., Barberato, C., & Koch, M. H. J. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,434
Nagle, J. F., & Tristram-Nagle, S. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(00)00016-2 · Cited by 2,669
Structure Analysis by Small-Angle X-Ray and Neutron Scattering
Feigin, L. A., & Svergun, D. I. (1987) · Springer eBooks · doi:10.1007/978-1-4757-6624-0 · Cited by 2,473
Pedersen, J. S. (1997) · Advances in Colloid and Interface Science · doi:10.1016/s0001-8686(97)00312-6 · Cited by 1,653
Atomic and Molecular Manipulation with the Scanning Tunneling Microscope
Stroscio, J. A., & Eigler, D. M. (1991) · Science · doi:10.1126/science.254.5036.1319 · Cited by 1,131
Functional Materials Based on Self-Assembly of Polymeric Supramolecules
Ikkala, O., & ten Brinke, G. (2002) · Science · doi:10.1126/science.1067794 · Cited by 1,046
Protein hydration in solution: Experimental observation by x-ray and neutron scattering
Svergun, D. I., Richard, S., Koch, M. H. J., Sayers, Z., Kuprin, S., & Zaccai, G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2267 · Cited by 912
Cited by
Functional Liquid‐Crystalline Assemblies: Self‐Organized Soft Materials
Kato, T., Mizoshita, N., & Kishimoto, K. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200501384 · Cited by 1,545
Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184
Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000
Reconstitution of Membrane Proteins in Phospholipid Bilayer Nanodiscs
Ritchie, T. K., Grinkova, Y. V., Bayburt, T. H., Denisov, I. G., Zolnerciks, J. K., Atkins, W. M., & Sligar, S. G. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(09)64011-8 · Cited by 872
Self-citationNanodiscs for structural and functional studies of membrane proteins
Denisov, I. G., & Sligar, S. G. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3195 · Cited by 522
Self-citationHagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310901f · Cited by 498
Regulation of Integrin Activation
Kim, C., Ye, F., & Ginsberg, M. H. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104104 · Cited by 437
Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update
Parkinson, J. S., Hazelbauer, G. L., & Falke, J. J. (2015) · Trends in Microbiology · doi:10.1016/j.tim.2015.03.003 · Cited by 428
A Molecular Description of Cellulose Biosynthesis
McNamara, J. T., Morgan, J. L. W., & Zimmer, J. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033930 · Cited by 382
LILRB4 signalling in leukaemia cells mediates T cell suppression and tumour infiltration
Deng, M., Gui, X., Kim, J., Xie, L., Chen, W., Li, Z., He, L., Chen, Y., Chen, H., Luo, W., et al. (2018) · Nature · doi:10.1038/s41586-018-0615-z · Cited by 305
Small-Angle X-Ray Scattering from RNA, Proteins, and Protein Complexes
Lipfert, J., & Doniach, S. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132655 · Cited by 300
Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.
Frauenfeld, J., Gumbart, J., Sluis, E. O. V. D., Funes, S., Gartmann, M., Beatrix, B., Mielke, T., Berninghausen, O., Becker, T., Schulten, K., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2026 · Cited by 298
Popot, J.-L. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052208.114057 · Cited by 288
Ca2+ regulates T-cell receptor activation by modulating the charge property of lipids
Shi, X., Bi, Y., Yang, W., Guo, X., Jiang, Y., Wan, C., Li, L., Bai, Y., Guo, J., Wang, Y., et al. (2013) · Nature · doi:10.1038/nature11699 · Cited by 275
Omadjela, O., Narahari, A., Strumillo, J., Mélida, H., Mazur, O., Bulone, V., & Zimmer, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314063110 · Cited by 273
Coarse grained protein- lipid model with application to lipoprotein particles
Shih, A. Y., Arkhipov, A., Freddolino, L., & Schulten, K. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp0550816 · Cited by 267
A statistical framework for analyzing deep mutational scanning data
Rubin, A. F., Gelman, H., Lucas, N., Bajjalieh, S. M., Papenfuss, A. T., Speed, T. P., & Fowler, D. M. (2017) · Genome Biology · doi:10.1186/s13059-017-1272-5 · Cited by 262
Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2
Nguyen, L., McCord, K. A., Bui, D. T., Bouwman, K. M., Kitova, E. N., Elaish, M., Kumawat, D., Daskhan, G. C., Tomris, I., Han, L., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-021-00924-1 · Cited by 259
Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view
Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188
Structural insights into integrin α 5 β 1 opening by fibronectin ligand
Schumacher, S., Dedden, D., Nunez, R. V., Matoba, K., Takagi, J., Biertümpfel, C., & Mizuno, N. (2021) · Science Advances · doi:10.1126/sciadv.abe9716 · Cited by 150
Native Mass Spectrometry of Membrane Proteins
Keener, J. E., Zhang, G., & Marty, M. T. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04342 · Cited by 126
Fang, Z., Marshall, C. B., Nishikawa, T., Gossert, A. D., Jansen, J. M., Jahnke, W., & Ikura, M. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.07.009 · Cited by 86
Peter, M. F., Depping, P., Schneberger, N., Severi, E., Gatterdam, K., Tindall, S., Durand, A., Heinz, V., Koenig, P.-A., Geyer, M., et al. (2021) · doi:10.1101/2021.12.03.471092 · Cited by 38
Bradberry, M. M., Bao, H., Lou, X., & Chapman, E. R. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007929 · Cited by 38
Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter
Peter, M. F., Ruland, J. A., Depping, P., Schneberger, N., Severi, E., Moecking, J., Gatterdam, K., Tindall, S., Durand, A., Heinz, V., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31907-y · Cited by 38
The bacterial SRP receptor, FtsY, is activated on binding to the translocon.
Draycheva, A., Bornemann, T., Ryazanov, S., Lakomek, N., & Wintermeyer, W. (2016) · Molecular Microbiology · doi:10.1111/mmi.13452 · Cited by 34
Role of the cytosolic loop C2 and the C terminus of YidC in ribosome binding and insertion activity.
Geng, Y., Kedrov, A., Caumanns, J. J., Crevenna, A. H., Lamb, D. C., Beckmann, R., & Driessen, A. J. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.650309 · Cited by 30
CRISPR antiphage defence mediated by the cyclic nucleotide-binding membrane protein Csx23
Grüschow, S., McQuarrie, S., Ackermann, K., McMahon, S., Bode, B. E., Gloster, T. M., & White, M. F. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae167 · Cited by 25
Marcink, T. C., Simoncic, J. A., An, B., Knapinska, A. M., Fulcher, Y. G., Akkaladevi, N., Fields, G. B., & Van Doren, S. R. (2019) · Structure · doi:10.1016/j.str.2018.10.008 · Cited by 24
Peripheral membrane associations of matrix metalloproteinases.
Van Doren, S. R., Marcink, T. C., Koppisetti, R. K., Jurkevich, A., & Fulcher, Y. G. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.04.013 · Cited by 22
Odorčić, I., Hamed, M. B., Lismont, S., Chávez-Gutiérrez, L., & Efremov, R. G. (2024) · Nature Communications · doi:10.1038/s41467-024-48776-2 · Cited by 15
Insights from aquaporin structures into drug-resistant sleeping sickness
Matusevicius, M., Corey, R. A., Gragera, M., Yamashita, K., Sprenger, T., Ungogo, M. A., Blaza, J. N., Castro-Hartmann, P., Chirgadze, D. Y., Chaitanya Vedithi, S., et al. (2025) · doi:10.1101/2025.05.15.654314 · Cited by 1
Insights from aquaporin structures into drug-resistant sleeping sickness
Matusevicius, M., Corey, R. A., Gragera, M., Yamashita, K., Sprenger, T., Ungogo, M., Blaza, J. N., Castro-Hartmann, P., Chirgadze, D. Y., Chaitanya Vedithi, S., et al. (2026) · eLife · doi:10.7554/elife.107460.3 · Cited by 1
Insights from aquaporin structures into drug-resistant sleeping sickness
Matusevicius, M., Corey, R. A., Gragera, M., Yamashita, K., Sprenger, T., Ungogo, M., Blaza, J. N., Castro-Hartmann, P., Chirgadze, D. Y., Chaitanya Vedithi, S., et al. (2026) · eLife · doi:10.7554/elife.107460 · Cited by 1
Metadata
- Authors
- Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., & Sligar, S. G.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-03-01
- Volume
- 126
- Issue
- 11
- Pages
- 3477-3487
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2005574282
- Cited by
- 1,064
- References
- 43
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.