The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP
Open accessAbstract
Adenosine triphosphate (ATP) plays fundamental roles in cellular biochemistry and was recently discovered to function as a biological hydrotrope. Here, we use mass spectrometry to interrogate ATP-mediated regulation of protein thermal stability and protein solubility on a proteome-wide scale. Thermal proteome profiling reveals high affinity interactions of ATP as a substrate and as an allosteric modulator that has widespread influence on protein complexes and their stability. Further, we develop a strategy for proteome-wide solubility profiling, and discover ATP-dependent solubilization of at least 25% of the insoluble proteome. ATP increases the solubility of positively charged, intrinsically disordered proteins, and their susceptibility for solubilization varies depending on their localization to different membrane-less organelles. Moreover, a few proteins, exhibit an ATP-dependent decrease in solubility, likely reflecting polymer formation. Our data provides a proteome-wide, quantitative insight into how ATP influences protein structure and solubility across the spectrum of physiologically relevant concentrations.
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
clusterProfiler: an R Package for Comparing Biological Themes Among Gene Clusters
Yu, G., Wang, L.-G., Han, Y., & He, Q.-Y. (2012) · OMICS: A Journal of Integrative Biology · doi:10.1089/omi.2011.0118 · Cited by 36,259
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Perez-Riverol, Y., Csordas, A., Bai, J., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1106 · Cited by 6,693
Dose-Response Analysis Using R
Ritz, C., Baty, F., Streibig, J. C., & Gerhard, D. (2015) · PLOS ONE · doi:10.1371/journal.pone.0146021 · Cited by 3,658
Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation
Brangwynne, C. P., Eckmann, C. R., Courson, D. S., Rybarska, A., Hoege, C., Gharakhani, J., Jülicher, F., & Hyman, A. A. (2009) · Science · doi:10.1126/science.1172046 · Cited by 3,202
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155
Huber, W., von Heydebreck, A., Sültmann, H., Poustka, A., & Vingron, M. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.suppl_1.s96 · Cited by 2,440
Self-citationMonitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay
Molina, D. M., Jafari, R., Ignatushchenko, M., Seki, T., Larsson, E. A., Dan, C., Sreekumar, L., Cao, Y., & Nordlund, P. (2013) · Science · doi:10.1126/science.1233606 · Cited by 2,261
InterPro: the integrative protein signature database
Hunter, S., Apweiler, R., Attwood, T. K., Bairoch, A., Bateman, A., Binns, D., Bork, P., Das, U., Daugherty, L., Duquenne, L., et al. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn785 · Cited by 2,107
Wang, J., Choi, J.-M., Holehouse, A. S., Lee, H. O., Zhang, X., Jahnel, M., Maharana, S., Lemaitre, R., Pozniakovsky, A., Drechsel, D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.006 · Cited by 2,076
Cited by
A new antibiotic selectively kills Gram-negative pathogens
Imai, Y., Meyer, K. J., Iinishi, A., Favre-Godal, Q., Green, R., Manuse, S., Caboni, M., Mori, M., Niles, S., Ghiglieri, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1791-1 · Cited by 743
Self-citationThermal proteome profiling for interrogating protein interactions
Mateus, A., Kurzawa, N., Becher, I., Sridharan, S., Helm, D., Stein, F., Typas, A., & Savitski, M. M. (2020) · Molecular Systems Biology · doi:10.15252/msb.20199232 · Cited by 258
Self-citationKurzawa, N., Becher, I., Sridharan, S., Franken, H., Mateus, A., Anders, S., Bantscheff, M., Huber, W., & Savitski, M. M. (2020) · Nature Communications · doi:10.1038/s41467-020-19529-8 · Cited by 53
Self-citationImproved Proteomics-Based Drug Mechanism-of-Action Studies Using 16-Plex Isobaric Mass Tags
Zinn, N., Werner, T., Doce, C., Mathieson, T., Boecker, C., Sweetman, G., Fufezan, C., & Bantscheff, M. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00900 · Cited by 49
Self-citationAggregation and disaggregation features of the human proteome
Määttä, T. A., Rettel, M., Sridharan, S., Helm, D., Kurzawa, N., Stein, F., & Savitski, M. M. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209500 · Cited by 34
Self-citation
Metadata
- Authors
- Sridharan, S., Kurzawa, N., Werner, T., Günthner, I., Helm, D., Huber, W., Bantscheff, M., & Savitski, M. M.
- Venue
- Nature Communications
- Published
- 2019-03-11
- Volume
- 10
- Issue
- 1
- Pages
- 1155-1155
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2903493617
- Cited by
- 267
- References
- 60
- FWCI
- 12.17
- Type
- journal article
- Language
- en
- Open access
- gold
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: Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP. https://app.cochat.ai/papers/10.1038/s41467-019-09107-y
- The paper
- Sridharan, S., Kurzawa, N., Werner, T., Günthner, I., Helm, D., Huber, W., Bantscheff, M., & Savitski, M. M. (2019). Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP. Nature Communications. https://doi.org/10.1038/s41467-019-09107-y
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.
