The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Increase of Solubility of Foreign Proteins in Escherichia coli by Coproduction of the Bacterial Thioredoxin
Open accessAbstract
Eukaryotic proteins are frequently produced in Escherichia coli as insoluble aggregates. This is one of the barriers to studies of macromolecular structure. We have examined the effect of coproduction of the E. coli thioredoxin (Trx) or E. coli chaperones GroESL on the solubility of various foreign proteins. The solubilities of all eight vertebrate proteins examined including transcription factors and kinases were increased dramatically by coproduction of Trx. Overproduction of E. coli chaperones GroESL increased the solubilities of four out of eight proteins examined. Although the tyrosine kinase Lck that was produced as an insoluble form and solubilized by urea treatment had a very low autophosphorylating activity, Lck produced in soluble form by coproduction of Trx had an efficient activity. These results suggest that the proteins produced in soluble form by coproduction of Trx have the native protein conformation. The mechanism by which coproduction of Trx increases the solubility of the foreign proteins is discussed.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
Studier, F. W., & Moffatt, B. A. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90385-2 · Cited by 6,320
Chang, A. C., & Cohen, S. N. (1978) · Journal of Bacteriology · doi:10.1128/jb.134.3.1141-1156.1978 · Cited by 4,243
Vogelstein, B. (1992) · Cell · doi:10.1016/0092-8674(92)90421-8 · Cited by 1,862
Vectors for selective expression of cloned DNAs by T7 RNA polymerase
Rosenberg, A. H., Lade, B. N., Dao-shan, C., Lin, S.-W., Dunn, J. J., & Studier, F. W. (1987) · Gene · doi:10.1016/0378-1119(87)90165-x · Cited by 1,443
LaVallie, E. R., DiBlasio, E. A., Kovacic, S., Grant, K. L., Schendel, P. F., & McCoy, J. M. (1993) · Nature Biotechnology · doi:10.1038/nbt0293-187 · Cited by 919
Sagata, N., Watanabe, N., Vande Woude, G. F., & Ikawa, Y. (1989) · Nature · doi:10.1038/342512a0 · Cited by 642
Marth, J. D., Peet, R., Krebs, E. G., & Perlmutter, R. M. (1985) · Cell · doi:10.1016/0092-8674(85)90169-2 · Cited by 528
Ogata, K., Morikawa, S., Nakamura, H., Sekikawa, A., Inoue, T., Kanai, H., Sarai, A., Ishii, S., & Nishimura, Y. (1994) · Cell · doi:10.1016/0092-8674(94)90549-5 · Cited by 489
Self-citationAssociation of B Cell Antigen Receptor with Protein Tyrosine Kinase Lyn
Yamanashi, Y., Kakiuchi, T., Mizuguchi, J., Yamamoto, T., & Toyoshima, K. (1991) · Science · doi:10.1126/science.1702903 · Cited by 453
Self-citationLeucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain.
Maekawa, T., Sakura, H., Kanei-Ishii, C., Sudo, T., Yoshimura, T., Fujisawa, J., Yoshida, M., & Ishii, S. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03610.x · Cited by 382
Self-citation
Cited by
Recombinant protein folding and misfolding in Escherichia coli
Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,445
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
Roy, N. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.6914 · Cited by 1,301
A Single BIR Domain of XIAP Sufficient for Inhibiting Caspases
Takahashi, R., Deveraux, Q., Tamm, I., Welsh, K., Assa-Munt, N., Salvesen, G. S., & Reed, J. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.7787 · Cited by 608
Edens, W. A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J. M., Lee, T., Edens, H. A., Tang, X., Sullards, C., Flaherty, D. B., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103132 · Cited by 375
de Marco, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-26 · Cited by 367
Metadata
- Authors
- Yasukawa, T., Kanei-Ishii, C., Maekawa, T., Fujimoto, J., Yamamoto, T., & Ishii, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-10
- Volume
- 270
- Issue
- 43
- Pages
- 25328-25331
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2085881545
- Cited by
- 326
- References
- 23
- FWCI
- 5.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Increase of Solubility of Foreign Proteins in Escherichia coli by Coproduction of the Bacterial Thioredoxin. https://app.cochat.ai/papers/10.1074/jbc.270.43.25328
- The paper
- Yasukawa, T., Kanei-Ishii, C., Maekawa, T., Fujimoto, J., Yamamoto, T., & Ishii, S. (1995). Increase of Solubility of Foreign Proteins in Escherichia coli by Coproduction of the Bacterial Thioredoxin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.43.25328
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.
