The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
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Citations
Cites
Genomic Expression Programs in the Response of Yeast Cells to Environmental Changes
Gasch, A. P., Spellman, P. T., Kao, C. M., Carmel-Harel, O., Eisen, M. B., Storz, G., Botstein, D., & Brown, P. O. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4241 · Cited by 4,815
The native 3D organization of bacterial polysomes
Brandt, F., Etchells, S. A., Ortiz, J. O., Elcock, A. H., Hartl, F. U., & Baumeister, W. (2009) · Cell · doi:10.1016/j.cell.2008.11.016 · Cited by 258
Distinct modes of signal recognition particle interaction with the ribosome.
Pool, M. R., Stumm, J., Fulga, T. A., Sinning, I., & Dobberstein, B. (2002) · Science · doi:10.1126/science.1072366 · Cited by 199
Beck, K., Wu, L., Brunner, J., & Müller, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.134 · Cited by 189
Structure of the E. coli signal recognition particle bound to a translating ribosome.
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I., & Ban, N. (2006) · Nature · doi:10.1038/nature05182 · Cited by 136
Self-citationLigand crowding at a nascent signal sequence.
Eisner, G., Koch, H.-G., Beck, K., Brunner, J., & Müller, M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200306069 · Cited by 69
Cited by
Rosenzweig, R., Nillegoda, N. B., Mayer, M. P., & Bukau, B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0133-3 · Cited by 1,285
Self-citationCysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics
Akaike, T., Ida, T., Wei, F.-Y., Nishida, M., Kumagai, Y., Alam, M. M., Ihara, H., Sawa, T., Matsunaga, T., Kasamatsu, S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01311-y · Cited by 544
Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations
Buhr, F., Jha, S., Thommen, M., Mittelstaet, J., Kutz, F., Schwalbe, H., Rodnina, M. V., & Komar, A. A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.008 · Cited by 395
Widespread Regulation of Translation by Elongation Pausing in Heat Shock
Shalgi, R., Hurt, J. A., Krykbaeva, I., Taipale, M., Lindquist, S., & Burge, C. B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.028 · Cited by 339
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Saio, T., Guan, X., Rossi, P., Economou, A., & Kalodimos, C. G. (2014) · Science · doi:10.1126/science.1250494 · Cited by 289
Metadata
- Authors
- Kramer, G., Boehringer, D., Ban, N., & Bukau, B.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-06
- Volume
- 16
- Issue
- 6
- Pages
- 589-597
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2065248572
- Cited by
- 477
- References
- 6
- FWCI
- 15.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. https://app.cochat.ai/papers/10.1038/nsmb.1614
- The paper
- Kramer, G., Boehringer, D., Ban, N., & Bukau, B. (2009). The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1614
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.
