The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
A structural overview of the PDI family of proteins
Abstract
Protein disulfide isomerases (PDIs) are enzymes that mediate oxidative protein folding in the endoplasmic reticulum. Understanding of PDIs has historically been hampered by lack of structural information. Over the last several years, partial and full‐length PDI structures have been solved at an increasing rate. Analysis of the structures reveals common features shared by several of the best known PDI family members, and also unique features related to substrate and partner binding sites. These exciting breakthroughs provide a deeper understanding of the mechanisms of oxidative protein folding in cells.
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
Wilkinson, B. M., & Gilbert, H. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.02.017 · Cited by 876
Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation
Hatahet, F., & Ruddock, L. W. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2466 · Cited by 670
Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllylä, R., Huhtala, M. L., Koivu, J., & Kivirikko, K. I. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb04803.x · Cited by 424
The protein disulfide isomerase AGR2 is essential for production of intestinal mucus
Park, S.-W., Zhen, G., Verhaeghe, C., Nakagami, Y., Nguyenvu, L. T., Barczak, A. J., Killeen, N., & Erle, D. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808722106 · Cited by 417
Tian, G., Xiang, S., Noiva, R., Lennarz, W. J., & Schindelin, H. (2006) · Cell · doi:10.1016/j.cell.2005.10.044 · Cited by 388
Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.
Wetterau, J. R., Combs, K. A., Spinner, S. N., & Joiner, B. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38742-3 · Cited by 365
Klappa, P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.4.927 · Cited by 344
Zapun, A., Darby, N. J., Tessier, D. C., Michalak, M., Bergeron, J. J. M., & Thomas, D. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6009 · Cited by 335
Self-citationDong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., & Reinisch, K. M. (2009) · Immunity · doi:10.1016/j.immuni.2008.10.018 · Cited by 293
Protein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
Self-citation
Cited by
Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 677
Chemistry and Enzymology of Disulfide Cross-Linking in Proteins
Fass, D., & Thorpe, C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00123 · Cited by 321
Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum
Soares Moretti, A. I., & Martins Laurindo, F. R. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.11.007 · Cited by 140
Glucocorticoid therapy and ocular hypertension
Dibas, A., & Yorio, T. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.06.018 · Cited by 75
Glucose-Raising Genetic Variants in MADD and ADCY5 Impair Conversion of Proinsulin to Insulin
Wagner, R., Dudziak, K., Herzberg-Schäfer, S. A., Machicao, F., Stefan, N., Staiger, H., Häring, H.-U., & Fritsche, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023639 · Cited by 50
Metadata
- Authors
- Kozlov, G., Määttänen, P., Thomas, D. Y., & Gehring, K.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2010-08-26
- Volume
- 277
- Issue
- 19
- Pages
- 3924-3936
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1528485412
- Cited by
- 269
- References
- 44
- FWCI
- 6.71
- Type
- journal article
- Language
- en
- Open access
- closed
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: A structural overview of the PDI family of proteins. https://app.cochat.ai/papers/10.1111/j.1742-4658.2010.07793.x
- The paper
- Kozlov, G., Määttänen, P., Thomas, D. Y., & Gehring, K. (2010). A structural overview of the PDI family of proteins. The FEBS Journal. https://doi.org/10.1111/j.1742-4658.2010.07793.x
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.
