The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.
Protein quality in bacterial inclusion bodies
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Citations
Cites
Recombinant protein folding and misfolding in Escherichia coli
Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,445
Protein aggregation: folding aggregates, inclusion bodies and amyloid
Fink, A. L. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00002-9 · Cited by 1,157
Amyloid fibrillogenesis: themes and variations
Rochet, J.-C., & Lansbury, P. T. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00049-4 · Cited by 1,095
Rationalization of the effects of mutations on peptide andprotein aggregation rates
Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
Advanced genetic strategies for recombinant protein expression in Escherichia coli
Sørensen, H. P., & Mortensen, K. K. (2005) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2004.08.004 · Cited by 963
Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
Sørensen, H. P., & Mortensen, K. K. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-1 · Cited by 841
The power of two: protein dimerization in biology
Marianayagam, N. J., Sunde, M., & Matthews, J. M. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.09.006 · Cited by 599
Mogk, A. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.6934 · Cited by 595
Goloubinoff, P., Mogk, A., Zvi, A. P. B., Tomoyasu, T., & Bukau, B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13732 · Cited by 582
Protein refolding for industrial processes
Clark, E. D. B. (2001) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00200-7 · Cited by 507
Cited by
The CamSol method of rational design of protein mutants with enhanced solubility
Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.09.026 · Cited by 494
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., & Panda, A. K. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0222-8 · Cited by 444
Niwa, T., Ying, B.-W., Saito, K., Jin, W., Takada, S., Ueda, T., & Taguchi, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811922106 · Cited by 321
Upadhyay, A. K., Murmu, A., Singh, A., & Panda, A. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033951 · Cited by 118
A relationship between mRNA expression levels and protein solubility in E. coli
Tartaglia, G. G., Pechmann, S., Dobson, C. M., & Vendruscolo, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.03.002 · Cited by 63
Metadata
- Authors
- Ventura, S., & Villaverde, A.
- Venue
- Trends in Biotechnology
- Publisher
- Elsevier BV
- Published
- 2006-04
- Volume
- 24
- Issue
- 4
- Pages
- 179-185
- ISSN
- 0167-7799 (ISSN-L)
- OpenAlex
- W2009845005
- Cited by
- 381
- References
- 77
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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- CoChat. (2026). Citation check: Protein quality in bacterial inclusion bodies. https://app.cochat.ai/papers/10.1016/j.tibtech.2006.02.007
- The paper
- Ventura, S., & Villaverde, A. (2006). Protein quality in bacterial inclusion bodies. Trends in Biotechnology. https://doi.org/10.1016/j.tibtech.2006.02.007
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.