The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A Proteome Analysis of the Cadmium Response in Saccharomyces cerevisiae
Open accessAbstract
Cadmium is very toxic at low concentrations, but the basis for its toxicity is not clearly understood. We analyzed the proteomic response of yeast cells to acute cadmium stress and identified 54 induced and 43 repressed proteins. A striking result is the strong induction of 9 enzymes of the sulfur amino acid biosynthetic pathway. Accordingly, we observed that glutathione synthesis is strongly increased in response to cadmium treatment. Several proteins with antioxidant properties were also induced. The induction of nine proteins is dependent upon the transactivator Yap1p, consistent with the cadmium hypersensitive phenotype of the YAP1-disrupted strain. Most of these proteins are also overexpressed in a strain overexpressing Yap1p, a result that correlates with the cadmium hyper-resistant phenotype of this strain. Two of these Yap1p-dependent proteins, thioredoxin and thioredoxin reductase, play an important role in cadmium tolerance because strains lacking the corresponding genes are hypersensitive to this metal. Altogether, our data indicate that the two cellular thiol redox systems, glutathione and thioredoxin, are essential for cellular defense against cadmium.
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
Oxidative mechanisms in the toxicity of metal ions
Stohs, S. J., & Bagchi, D. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00159-h · Cited by 4,219
Cited by
Toxic metal accumulation, responses to exposure and mechanisms of tolerance in plants
Clemens, S. (2006) · Biochimie · doi:10.1016/j.biochi.2006.07.003 · Cited by 2,021
Osmotic Stress Signaling and Osmoadaptation in Yeasts
Hohmann, S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.2.300-372.2002 · Cited by 1,767
Redox control and oxidative stress in yeast cells
Herrero, E., Ros, J., Bellí, G., & Cabiscol, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.12.004 · Cited by 484
Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation
Tamás, M., Sharma, S., Ibstedt, S., Jacobson, T., & Christen, P. (2014) · Biomolecules · doi:10.3390/biom4010252 · Cited by 468
Engineering tolerance and accumulation of lead and cadmium in transgenic plants
Song, W.-Y., Ju Sohn, E., Martinoia, E., Jik Lee, Y., Yang, Y.-Y., Jasinski, M., Forestier, C., Hwang, I., & Lee, Y. (2003) · Nature Biotechnology · doi:10.1038/nbt850 · Cited by 423
Enjalbert, B., Smith, D. A., Cornell, M. J., Alam, I., Nicholls, S., Brown, A. J. P., & Quinn, J. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0501 · Cited by 381
Sarry, J., Kuhn, L., Ducruix, C., Lafaye, A., Junot, C., Hugouvieux, V., Jourdain, A., Bastien, O., Fievet, J. B., Vailhen, D., et al. (2006) · PROTEOMICS · doi:10.1002/pmic.200500543 · Cited by 372
Fungi in freshwaters: ecology, physiology and biochemical potential
Krauss, G.-J., Solé, M., Krauss, G., Schlosser, D., Wesenberg, D., & Bärlocher, F. (2011) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2011.00266.x · Cited by 340
Extracellular and cellular mechanisms sustaining metal tolerance in ectomycorrhizal fungi
Bellion, M., Courbot, M., Jacob, C., Blaudez, D., & Chalot, M. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2005.00044.x · Cited by 311
How Saccharomyces cerevisiae copes with toxic metals and metalloids
Wysocki, R., & Tamás, M. J. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00217.x · Cited by 299
Thiol/disulfide redox states in signaling and sensing
Go, Y.-M., & Jones, D. P. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.764840 · Cited by 241
Isolation and characterization of a thioredoxin‐dependent peroxidase from Chlamydomonas reinhardtii
Goyer, A., Haslekås, C., Miginiac‐Maslow, M., Klein, U., Le Marechal, P., Jacquot, J., & Decottignies, P. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02648.x · Cited by 114
YodA from Escherichia coli is a metal-binding, lipocalin-like protein
David, G., Blondeau, K., Schiltz, M., Penel, S., & Lewit-Bentley, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304484200 · Cited by 63
Craciun, A. R. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erl062 · Cited by 51
Metadata
- Authors
- Vido, K., Spector, D., Lagniel, G., Lopez, S., Toledano, M. B., & Labarre, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 276
- Issue
- 11
- Pages
- 8469-8474
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2081663028
- Cited by
- 387
- References
- 1
- FWCI
- 6.62
- 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
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.