The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
SurA assists the folding of Escherichia coli outer membrane proteins
Open accessAbstract
Many proteins require enzymatic assistance in order to achieve a functional conformation. One rate-limiting step in protein folding is the cis-trans isomerization of prolyl residues, a reaction catalyzed by prolyl isomerases. SurA, a periplasmic protein of Escherichia coli, has sequence similarity with the prolyl isomerase parvulin. We tested whether SurA was involved in folding periplasmic and outer membrane proteins by using trypsin sensitivity as an assay for protein conformation. We determined that the efficient folding of three outer membrane proteins (OmpA, OmpF, and LamB) requires SurA in vivo, while the folding of four periplasmic proteins was independent of SurA. We conclude that SurA assists in the folding of certain secreted proteins.
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
Specific incorporation of cyclophilin A into HIV-1 virions
Franke, E. K., Yuan, H. E. H., & Luban, J. (1994) · Nature · doi:10.1038/372359a0 · Cited by 745
Cited by
Secretory and extracellular production of recombinant proteins using Escherichia coli
Choi, J. H., & Lee, S. Y. (2004) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-004-1559-9 · Cited by 614
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
Sklar, J. G., Wu, T., Kahne, D., & Silhavy, T. J. (2007) · Genes & Development · doi:10.1101/gad.1581007 · Cited by 459
Advances in understanding bacterial outer-membrane biogenesis
Ruiz, N., Kahne, D., & Silhavy, T. J. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1322 · Cited by 458
Robert, V., Volokhina, E. B., Senf, F., Bos, M. P., Gelder, P. V., & Tommassen, J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040377 · Cited by 326
Danese, P. N., & Silhavy, T. J. (1997) · Genes & Development · doi:10.1101/gad.11.9.1183 · Cited by 273
Metadata
- Authors
- Lazar, S. W., & Kolter, R.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1996-03
- Volume
- 178
- Issue
- 6
- Pages
- 1770-1773
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W1754378627
- Cited by
- 326
- References
- 1
- FWCI
- 7.82
- Type
- journal article
- Language
- en
- Open access
- green
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: SurA assists the folding of Escherichia coli outer membrane proteins. https://app.cochat.ai/papers/10.1128/jb.178.6.1770-1773.1996
- The paper
- Lazar, S. W., & Kolter, R. (1996). SurA assists the folding of Escherichia coli outer membrane proteins. Journal of Bacteriology. https://doi.org/10.1128/jb.178.6.1770-1773.1996
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.
