The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Covalently circularized nanodiscs for studying membrane proteins and viral entry
Open accessAbstract
We engineered covalently circularized nanodiscs (cNDs) which, compared with standard nanodiscs, exhibit enhanced stability, defined diameter sizes and tunable shapes. Reconstitution into cNDs enhanced the quality of nuclear magnetic resonance spectra for both VDAC-1, a β-barrel membrane protein, and the G-protein-coupled receptor NTR1, an α-helical membrane protein. In addition, we used cNDs to visualize how simple, nonenveloped viruses translocate their genomes across membranes to initiate infection.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The authors determined cryo-EM structures of FPN reconstituted in a NW9 nanodisc and bound to Fab45D8, both in the apo state (3.2 Å) and bound to hepcidin and Co2+ (2.5 Å).
“We determined cryo-EM structures of FPN reconstituted in a NW9 nanodisc 25 and bound to Fab45D8, both in the apo state (3.2 Å, Extended Data Table 1, Extended Data Fig. 3) and bound to hepcidin and Co 2+ (2.5 Å, Extended Data Fig. 4).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [25]
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
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961
Automated electron microscope tomography using robust prediction of specimen movements
Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,136
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
EMAN2: An extensible image processing suite for electron microscopy
Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.05.009 · Cited by 2,914
Marsh, M., & Helenius, A. (2006) · Cell · doi:10.1016/j.cell.2006.02.007 · Cited by 1,209
Mendelsohn, C. L., Wimmer, E., & Racaniello, V. R. (1989) · Cell · doi:10.1016/0092-8674(89)90690-9 · Cited by 1,116
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 on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)64011-8 · Cited by 891
Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins
Bayburt, T. H., Grinkova, Y. V., & Sligar, S. G. (2002) · Nano Letters · doi:10.1021/nl025623k · Cited by 810
Negative staining and image classification — powerful tools in modern electron microscopy
Ohi, M. D., Li, Y., Cheng, Y., & Walz, T. (2004) · Biological Procedures Online · doi:10.1251/bpo70 · Cited by 685
Self-citationA general strategy for the evolution of bond-forming enzymes using yeast display
Chen, I., Dorr, B. M., & Liu, D. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101046108 · Cited by 569
Hagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310901f · Cited by 499
Self-citationHyberts, S. G., Milbradt, A. G., Wagner, A. B., Arthanari, H., & Wagner, G. (2012) · Journal of Biomolecular NMR · doi:10.1007/s10858-012-9611-z · Cited by 442
Self-citationPoliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways
Hogle, J. M. (2002) · Annual Review of Microbiology · doi:10.1146/annurev.micro.56.012302.160757 · Cited by 352
Self-citationImaging Poliovirus Entry in Live Cells
Brandenburg, B., Lee, L. Y., Lakadamyali, M., Rust, M. J., Zhuang, X., & Hogle, J. M. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050183 · Cited by 307
Self-citationEgloff, P., Hillenbrand, M., Klenk, C., Batyuk, A., Heine, P., Balada, S. B., Schlinkmann, K. M., Scott, D. J., Schütz, M., & Plückthun, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317903111 · Cited by 216
Self-citationTuthill, T. J., Groppelli, E., Hogle, J. M., & Rowlands, D. J. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_37 · Cited by 199
Self-citationGrinkova, Y. V., Denisov, I. G., & Sligar, S. G. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzq060 · Cited by 175
Raschle, T., Hiller, S., Yu, T., Rice, A. J., Walz, T., & Wagner, G. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907918r · Cited by 168
Self-citationReconstitution and Imaging of a Membrane Protein in a Nanometer-Size Phospholipid Bilayer
Bayburt, T. H., Carlson, J. W., & Sligar, S. G. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4007 · Cited by 165
A Straight Path to Circular Proteins
Antos, J. M., Popp, M. W., Ernst, R., Chew, G.-L., Spooner, E., & Ploegh, H. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901752200 · Cited by 160
Nonmicellar systems for solution NMR spectroscopy of membrane proteins
Raschle, T., Hiller, S., Etzkorn, M., & Wagner, G. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.05.006 · Cited by 118
Self-citationTuthill, T. J., Bubeck, D., Rowlands, D. J., et al. (2005) · Journal of Virology · doi:10.1128/jvi.80.1.172-180.2006 · Cited by 113
Activation of Inhibitors by Sortase Triggers Irreversible Modification of the Active Site
Maresso, A. W., Wu, R., Kern, J. W., Zhang, R., Janik, D., Missiakas, D. M., Duban, M.-E., Joachimiak, A., & Schneewind, O. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701857200 · Cited by 112
Strauss, M., Filman, D. J., Belnap, D. M., Cheng, N., Noel, R. T., & Hogle, J. M. (2015) · Journal of Virology · doi:10.1128/jvi.03101-14 · Cited by 111
Self-citationCryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex
Bubeck, D., Filman, D. J., & Hogle, J. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb955 · Cited by 92
Self-citationStrauss, M., Levy, H. C., Bostina, M., et al. (2013) · Journal of Virology · doi:10.1128/jvi.03209-12 · Cited by 83
Self-citationLi, X., Grigorieff, N., & Cheng, Y. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.06.010 · Cited by 45
Egloff, P., Deluigi, M., Heine, P., Balada, S. B., & Plückthun, A. (2014) · Protein Expression and Purification · doi:10.1016/j.pep.2014.10.006 · Cited by 18
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- Tuthill, T.J., Groppelli, E., Hogle, J.M. & Rowlands, D.J. Viruses 343, 43–89 (2010).
- Racaniello, V.R. Fields Virology 6th edn. (eds. Knipe, D.M. & Howley, P.M.) 453–489 (Lippincott, Williams & Wilkens, 2013).
Cited by
Sorted by citations
FDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation
Hu, J. J., Liu, X., Xia, S., Zhang, Z., Zhang, Y., Zhao, J., Ruan, J., Luo, X., Lou, X., Bai, Y., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0669-6 · Cited by 1,145
Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms
Billesbølle, C. B., Azumaya, C. M., Kretsch, R. C., Powers, A. S., Gonen, S., Schneider, S., Arvedson, T., Dror, R. O., Cheng, Y., & Manglik, A. (2020) · Nature · doi:10.1038/s41586-020-2668-z · Cited by 344
Metadata
- Authors
- Nasr, M. L., Baptista, D., Strauss, M., Sun, Z.-Y. J., Grigoriu, S., Huser, S., Plückthun, A., Hagn, F., Walz, T., Hogle, J. M., & Wagner, G.
- Affiliations
- Harvard University (US)
- University of Zurich (CH)
- Helmholtz Munich (DE)
- Corresponding author
- Wagner, Gerhard
- ORCID
- Venue
- Nature Methods
- Published
- 2016-11-21
- Volume
- 14
- Issue
- 1
- Pages
- 49-52
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- PMC
- PMC5199620
- OpenAlex
- W2555054553
- Cited by
- 262
- References
- 29
- Citations by year
- 2026: 20 · 2025: 18 · 2024: 15 · 2023: 32 · 2022: 21 · 2021: 33 · 2020: 37 · 2019: 26 · 2018: 32 · 2017: 27
- FWCI
- 14.73
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Methods (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R01GM075879, P01GM047467, F32GM113406)
- National Institute of Allergy and Infectious Diseases (R01AI020566, R21AI020566, R37AI020566, R01AI037581)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Keywords
- membrane protein reconstitution, membrane scaffold protein, VDAC1, neurotensin receptor 1, G protein-coupled receptors, beta-barrel membrane proteins, viral entry, non-enveloped viruses, NMR spectroscopy
- MeSH terms
- Humans, Lipid Bilayers, Models, Molecular, Poliomyelitis, Poliovirus, Receptors, Neurotensin, Nuclear Magnetic Resonance, Biomolecular, Nanostructures, Voltage-Dependent Anion Channel 1, Virus Internalization
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
