The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Structural basis of outer membrane protein insertion by the BAM complex
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1 retracted
TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson’s Disease
Bender, A., Desplats, P., Spencer, B. J., Rockenstein, E. M., Adame, A., Elstner, M., Laub, C., Mueller, S. K., Koob, A. O., Mante, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062277 · Cited by 153
RetractedFeatures and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Polymorphic transitions in single crystals: A new molecular dynamics method
Parrinello, M., & Rahman, A. (1981) · Journal of Applied Physics · doi:10.1063/1.328693 · Cited by 19,790
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
Hess, B., Kutzner, C., van der Spoel, D., & Lindahl, E. (2008) · Journal of Chemical Theory and Computation · doi:10.1021/ct700301q · Cited by 15,908
GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit
Pronk, S., Páll, S., Schulz, R., Larsson, P., Bjelkmar, P., Apostolov, R., Shirts, M. R., Smith, J. C., Kasson, P. M., van der Spoel, D., et al. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt055 · Cited by 7,473
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
MDAnalysis: A toolkit for the analysis of molecular dynamics simulations
Michaud‐Agrawal, N., Denning, E. J., Woolf, T. B., & Beckstein, O. (2011) · Journal of Computational Chemistry · doi:10.1002/jcc.21787 · Cited by 4,486
Comparative Protein Structure Modeling Using Modeller
Eswar, N., Webb, B., Marti‐Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Sali, A. (2006) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s15 · Cited by 4,478
Cited by
Ashkenazy, H., Abadi, S., Martz, E., Chay, O., Mayrose, I., Pupko, T., & Ben-Tal, N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw408 · Cited by 3,163
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
Chorev, D. S., Baker, L. A., Wu, D., Beilsten-Edmands, V., Rouse, S. L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., et al. (2018) · Science · doi:10.1126/science.aau0976 · Cited by 191
Urner, L. H., Liko, I., Yen, H.-Y., Hoi, K.-K., Bolla, J. R., Gault, J., Almeida, F. G., Schweder, M.-P., Shutin, D., Ehrmann, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14424-8 · Cited by 107
Profiling the Escherichia coli membrane protein interactome captured in Peptidisc libraries
Carlson, M. L., Stacey, R. G., Young, J. W., Wason, I. S., Zhao, Z., Rattray, D. G., Scott, N., Kerr, C. H., Babu, M., Foster, L. J., et al. (2019) · eLife · doi:10.7554/elife.46615 · Cited by 74
Metadata
- Authors
- Gu, Y., Li, H., Dong, H., Zeng, Y., Zhang, Z., Paterson, N. G., Stansfeld, P. J., Wang, Z., Zhang, Y., Wang, W., & Dong, C.
- Venue
- Nature
- Published
- 2016-02-22
- Volume
- 531
- Issue
- 7592
- Pages
- 64-69
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2282925852
- Cited by
- 308
- References
- 59
- FWCI
- 27.64
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Structural basis of outer membrane protein insertion by the BAM complex. https://app.cochat.ai/papers/10.1038/nature17199
- The paper
- Gu, Y., Li, H., Dong, H., Zeng, Y., Zhang, Z., Paterson, N. G., Stansfeld, P. J., Wang, Z., Zhang, Y., Wang, W., & Dong, C. (2016). Structural basis of outer membrane protein insertion by the BAM complex. Nature. https://doi.org/10.1038/nature17199
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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.
