The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
MMS19 Assembles Iron-Sulfur Proteins Required for DNA Metabolism and Genomic Integrity
Open accessAbstract
MMS19 Joins the CIA: Iron-sulfur (Fe-S) proteins play a critical role in cell metabolism and particularly in DNA repair and replication. Mutants in eukaryotic gene MMS19 are particularly sensitive to DNA damaging agents, suggesting that it is involved in DNA repair, but the mutations can also have other wide-ranging effects on the cell (see the Perspective by Gottschling ). Now, Stehling et al. (p. 195 , published online 7 June) and Gari et al. (p. 243 , published online 7 June) show that in both yeast and humans, MMS19 functions as part of the cytosolic Fe-S protein assembly (CIA) machinery. The MMS19 is part of a specialized CIA targeting complex that plays a role late in cytosolic Fe-S protein assembly to direct Fe-S cluster transfer from the CIA scaffold complex to a subset of Fe-S proteins, including a number associated with DNA metabolism.
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
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
Washburn, M. P., Wolters, D., & Yates, J. R. (2001) · Nature Biotechnology · doi:10.1038/85686 · Cited by 4,752
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
[1] Getting started with yeast
Sherman, F. (1991) · Methods in Enzymology · doi:10.1016/0076-6879(91)94004-v · Cited by 4,067
Elias, J. E., & Gygi, S. P. (2007) · Nature Methods · doi:10.1038/nmeth1019 · Cited by 3,925
Baker Brachmann, C., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., & Boeke, J. D. (1998) · Yeast · doi:10.1002/(sici)1097-0061(19980130)14:2<115::aid-yea204>3.0.co;2-2 · Cited by 3,401
Proteome survey reveals modularity of the yeast cell machinery
Gavin, A.-C., Aloy, P., Grandi, P., Krause, R., Boesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., et al. (2006) · Nature · doi:10.1038/nature04532 · Cited by 2,575
Hoeijmakers, J. H. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804615 · Cited by 2,239
Janke, C., Magiera, M. M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno‐Borchart, A., Doenges, G., Schwob, E., Schiebel, E., et al. (2004) · Yeast · doi:10.1002/yea.1142 · Cited by 2,119
An Automated Multidimensional Protein Identification Technology for Shotgun Proteomics
Wolters, D. A., Washburn, M. P., & Yates, J. R. (2001) · Analytical Chemistry · doi:10.1021/ac010617e · Cited by 1,819
Quantitative reactivity profiling predicts functional cysteines in proteomes
Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B. D., Bachovchin, D. A., Mowen, K., Baker, D., & Cravatt, B. F. (2010) · Nature · doi:10.1038/nature09472 · Cited by 1,684
Cited by
Iron and cancer: more ore to be mined
Torti, S. V., & Torti, F. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3495 · Cited by 1,621
Aguilera, A., & García-Muse, T. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-111212-133232 · Cited by 476
Mitochondria and Iron: current questions
Paul, B. T., Manz, D. H., Torti, F. M., & Torti, S. V. (2017) · Expert Review of Hematology · doi:10.1080/17474086.2016.1268047 · Cited by 423
Mitochondrial iron–sulfur protein biogenesis and human disease
Stehling, O., Wilbrecht, C., & Lill, R. (2014) · Biochimie · doi:10.1016/j.biochi.2014.01.010 · Cited by 272
Self-citationMammalian iron-sulphur proteins: novel insights into biogenesis and function
Rouault, T. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3909 · Cited by 201
Metadata
- Authors
- Stehling, O., Vashisht, A. A., Mascarenhas, J., Jonsson, Z. O., Sharma, T., Netz, D. J. A., Pierik, A. J., Wohlschlegel, J. A., & Lill, R.
- Venue
- Science
- Published
- 2012-07-13
- Volume
- 337
- Issue
- 6091
- Pages
- 195-199
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2052916872
- Cited by
- 288
- References
- 58
- FWCI
- 11.18
- 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: MMS19 Assembles Iron-Sulfur Proteins Required for DNA Metabolism and Genomic Integrity. https://app.cochat.ai/papers/10.1126/science.1219723
- The paper
- Stehling, O., Vashisht, A. A., Mascarenhas, J., Jonsson, Z. O., Sharma, T., Netz, D. J. A., Pierik, A. J., Wohlschlegel, J. A., & Lill, R. (2012). MMS19 Assembles Iron-Sulfur Proteins Required for DNA Metabolism and Genomic Integrity. Science. https://doi.org/10.1126/science.1219723
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.