The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Large-Scale Movement of Elongation Factor G and Extensive Conformational Change of the Ribosome during Translocation
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Citations
Cites
Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog
Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F. C., & Nyborg, J. (1995) · Science · doi:10.1126/science.270.5241.1464 · Cited by 851
Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
Van Heel, M. (1987) · Ultramicroscopy · doi:10.1016/0304-3991(87)90078-7 · Cited by 596
Self-citationX-ray Crystal Structures of 70 S Ribosome Functional Complexes
Cate, J. H., Yusupov, M. M., Yusupova, G. Z., Earnest, T. N., & Noller, H. F. (1999) · Science · doi:10.1126/science.285.5436.2095 · Cited by 583
Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
Rodnina, M. V., Savelsbergh, A., Katunin, V. I., & Wintermeyer, W. (1997) · Nature · doi:10.1038/385037a0 · Cited by 513
Self-citationInteraction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA
Moazed, D., Robertson, J. M., & Noller, H. F. (1988) · Nature · doi:10.1038/334362a0 · Cited by 483
Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes
Moazed, D., & Noller, H. F. (1986) · Cell · doi:10.1016/0092-8674(86)90813-5 · Cited by 420
Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit
Ban, N., Nissen, P., Hansen, J., Capel, M., Moore, P. B., & Steitz, T. A. (1999) · Nature · doi:10.1038/23641 · Cited by 390
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
Czworkowski, J., Wang, J., Steitz, T. A., & Moore, P. B. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06675.x · Cited by 376
AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al‐Karadaghi, S., Svensson, L. A., & Liljas, A. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06676.x · Cited by 363
Visualization of elongation factor Tu on the Escherichia coli ribosome
Stark, H., Rodnina, M. V., Rinke-Appel, J., Brimacombe, R., Wintermeyer, W., & Heel, M. V. (1997) · Nature · doi:10.1038/38770 · Cited by 347
Self-citation
Cited by
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
Carter, A. P., Clemons, W. M., Brodersen, D. E., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030019 · Cited by 1,615
Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979
Ribosome Structure and the Mechanism of Translation
Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)00619-0 · Cited by 938
Metadata
- Authors
- Stark, H., Rodnina, M. V., Wieden, H.-J., van Heel, M., & Wintermeyer, W.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 100
- Issue
- 3
- Pages
- 301-309
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2034304629
- Cited by
- 295
- References
- 46
- FWCI
- 13.63
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Large-Scale Movement of Elongation Factor G and Extensive Conformational Change of the Ribosome during Translocation. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80666-2
- The paper
- Stark, H., Rodnina, M. V., Wieden, H.-J., van Heel, M., & Wintermeyer, W. (2000). Large-Scale Movement of Elongation Factor G and Extensive Conformational Change of the Ribosome during Translocation. Cell. https://doi.org/10.1016/s0092-8674(00)80666-2
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.
