The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Membrane bending by protein–protein crowding
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Citations
Cites
Equation of State for Nonattracting Rigid Spheres
Carnahan, N. F., & Starling, K. E. (1969) · The Journal of Chemical Physics · doi:10.1063/1.1672048 · Cited by 5,280
BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
Peter, B. J., Kent, H. M., Mills, I. G., Vallis, Y., Butler, P. J. G., Evans, P. R., & McMahon, H. T. (2004) · Science · doi:10.1126/science.1092586 · Cited by 1,636
Angelova, M. I., & Dimitrov, D. S. (1986) · Faraday Discussions of the Chemical Society · doi:10.1039/dc9868100303 · Cited by 1,372
Curvature of clathrin-coated pits driven by epsin
Ford, M. G. J., Mills, I. G., Peter, B. J., Vallis, Y., Praefcke, G. J. K., Evans, P. R., & McMahon, H. T. (2002) · Nature · doi:10.1038/nature01020 · Cited by 1,019
Membranes are more mosaic than fluid
Engelman, D. M. (2005) · Nature · doi:10.1038/nature04394 · Cited by 924
Dynamin Undergoes a GTP-Dependent Conformational Change Causing Vesiculation
Sweitzer, S. M., & Hinshaw, J. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81207-6 · Cited by 680
Ford, M. G. J., Pearse, B. M. F., Higgins, M. K., Vallis, Y., Owen, D. J., Gibson, A., Hopkins, C. R., Evans, P. R., & McMahon, H. T. (2001) · Science · doi:10.1126/science.291.5506.1051 · Cited by 659
Amphipathic helices and membrane curvature
Drin, G., & Antonny, B. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.10.022 · Cited by 569
Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission
Rossman, J. S., Jing, X., Leser, G. P., & Lamb, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.08.029 · Cited by 513
Sar1p N-Terminal Helix Initiates Membrane Curvature and Completes the Fission of a COPII Vesicle
Lee, M. C. S., Orci, L., Hamamoto, S., Futai, E., Ravazzola, M., & Schekman, R. (2005) · Cell · doi:10.1016/j.cell.2005.07.025 · Cited by 512
Cited by
The biophysics and cell biology of lipid droplets
Thiam, A. R., Farese Jr, R. V., & Walther, T. C. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3699 · Cited by 986
Clathrin-independent pathways of endocytosis
Mayor, S., Parton, R. G., & Donaldson, J. G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016758 · Cited by 525
Membrane curvature in cell biology: An integration of molecular mechanisms
Jarsch, I. K., Daste, F., & Gallop, J. L. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201604003 · Cited by 328
MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion
Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326
Mastering Complexity: Towards Bottom-up Construction of Multifunctional Eukaryotic Synthetic Cells
Göpfrich, K., Platzman, I., & Spatz, J. P. (2018) · Trends in Biotechnology · doi:10.1016/j.tibtech.2018.03.008 · Cited by 267
Metadata
- Authors
- Stachowiak, J. C., Schmid, E. M., Ryan, C. J., Ann, H. S., Sasaki, D. Y., Sherman, M. B., Geissler, P. L., Fletcher, D. A., & Hayden, C. C.
- Venue
- Nature Cell Biology
- Published
- 2012-08-19
- Volume
- 14
- Issue
- 9
- Pages
- 944-949
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2064585995
- Cited by
- 537
- References
- 34
- FWCI
- 12.43
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Membrane bending by protein–protein crowding. https://app.cochat.ai/papers/10.1038/ncb2561
- The paper
- Stachowiak, J. C., Schmid, E. M., Ryan, C. J., Ann, H. S., Sasaki, D. Y., Sherman, M. B., Geissler, P. L., Fletcher, D. A., & Hayden, C. C. (2012). Membrane bending by protein–protein crowding. Nature Cell Biology. https://doi.org/10.1038/ncb2561
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.
