The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Thioredoxin and Its Related Molecules: Update 2005
Abstract
Studies on thioredoxin (Trx) and its related molecules have expanded dramatically recently. Proteins that share the similar active-site sequence, -Cys-Xxx-Yyy-Cys-, are called the Trx family, and the number of Trx family members is increasing. Trx reductase, which reduces oxidized Trx in cooperation with NADPH, has three isoforms, and peroxiredoxin, which is Trx-dependent peroxidase, has six isoforms. In addition to a role as an antioxidant, Trx and its related molecules play crucial roles in the redox regulation of signal transduction. The classical cytosolic Trx1 and truncated Trx80 are released from cells. Plasma/serum levels of Trx1 are good markers for oxidative stress. Exogenous Trx1 shows cytoprotective and antiinflammatory effects and has a good potential for clinical application. This is an update review on Trx and its related molecules.
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
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
Neumann, C. A., Krause, D. S., Carman, C. V., Das, S., Dubey, D. P., Abraham, J. L., Bronson, R. T., Fujiwara, Y., Orkin, S. H., & Van Etten, R. A. (2003) · Nature · doi:10.1038/nature01819 · Cited by 801
Early Embryonic Lethality Caused by Targeted Disruption of the Mouse Thioredoxin Gene
Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J., & Taketo, M. M. (1996) · Developmental Biology · doi:10.1006/dbio.1996.0208 · Cited by 546
Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438
Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
Lee, T.-H. (2003) · Blood · doi:10.1182/blood-2002-08-2548 · Cited by 420
Thioredoxin‐2 (TRX‐2) is an essential gene regulating mitochondria‐dependent apoptosis
Tanaka, T., Hosoi, F., Yamaguchi‐Iwai, Y., Nakamura, H., Masutani, H., Ueda, S., Nishiyama, A., Takeda, S., Wada, H., Spyrou, G., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1695 · Cited by 322
Self-citationJohansson, C., Lillig, C. H., & Holmgren, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312719200 · Cited by 320
Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops
Kondo, N., Ishii, Y., Kwon, Y.-W., Tanito, M., Horita, H., Nishinaka, Y., Nakamura, H., & Yodoi, J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.1.442 · Cited by 116
Self-citation
Cited by
Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics
Góngora-Benítez, M., Tulla-Puche, J., & Albericio, F. (2014) · Chemical Reviews · doi:10.1021/cr400031z · Cited by 655
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633
Reitman, Z. J., & Yan, H. (2010) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djq187 · Cited by 562
Schmidt, B., Ho, L., & Hogg, P. J. (2006) · Biochemistry · doi:10.1021/bi0603064 · Cited by 332
Antioxidants, Redox Signaling, and Pathophysiology in Schizophrenia: An Integrative View
Yao, J. K., & Keshavan, M. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3603 · Cited by 285
Metadata
- Authors
- Nakamura, H.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2005-05
- Volume
- 7
- Issue
- 5-6
- Pages
- 823-828
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2060792031
- Cited by
- 191
- References
- 8
- FWCI
- 6.68
- 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: Thioredoxin and Its Related Molecules: Update 2005. https://app.cochat.ai/papers/10.1089/ars.2005.7.823
- The paper
- Nakamura, H. (2005). Thioredoxin and Its Related Molecules: Update 2005. Antioxidants & Redox Signaling. https://doi.org/10.1089/ars.2005.7.823
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.