The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Comprehensive Identification of RNA-Binding Domains in Human Cells
Open accessAbstract
Mammalian cells harbor more than a thousand RNA-binding proteins (RBPs), with half of these employing unknown modes of RNA binding. We developed RBDmap to determine the RNA-binding sites of native RBPs on a proteome-wide scale. We identified 1,174 binding sites within 529 HeLa cell RBPs, discovering numerous RNA-binding domains (RBDs). Catalytic centers or protein-protein interaction domains are in close relationship with RNA-binding sites, invoking possible effector roles of RNA in the control of protein function. Nearly half of the RNA-binding sites map to intrinsically disordered regions, uncovering unstructured domains as prevalent partners in protein-RNA interactions. RNA-binding sites represent hot spots for defined posttranslational modifications such as lysine acetylation and tyrosine phosphorylation, suggesting metabolic and signal-dependent regulation of RBP function. RBDs display a high degree of evolutionary conservation and incidence of Mendelian mutations, suggestive of important functional roles. RBDmap thus yields profound insights into native protein-RNA interactions in living 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
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
Self-citationKato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012
Clemson, C. M., Hutchinson, J. N., Sara, S. A., Ensminger, A. W., Fox, A. H., Chess, A., & Lawrence, J. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.026 · Cited by 1,445
Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701
Nucleic acid recognition by the innate immune system
Barbalat, R., Ewald, S. E., Mouchess, M. L., & Barton, G. M. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101340 · Cited by 577
Nagy, E., & Rigby, W. F. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2755 · Cited by 361
Cited by
A brave new world of RNA-binding proteins
Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821
Self-citationRNA-Binding Proteins in Cancer: Old Players and New Actors
Pereira, B., Billaud, M., & Almeida, R. (2017) · Trends in Cancer · doi:10.1016/j.trecan.2017.05.003 · Cited by 773
Long Noncoding RNA in Cancer: Wiring Signaling Circuitry
Lin, C., & Yang, L. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.11.008 · Cited by 488
Properties of Stress Granule and P-Body Proteomes
Youn, J.-Y., Dyakov, B. J. A., Zhang, J., Knight, J. D. R., Vernon, R. M., Forman-Kay, J. D., & Gingras, A.-C. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.014 · Cited by 445
Queiroz, R. M. L., Smith, T., Villanueva, E., Marti-Solano, M., Monti, M., Pizzinga, M., Mirea, D.-M., Ramakrishna, M., Harvey, R. F., Dezi, V., et al. (2019) · Nature Biotechnology · doi:10.1038/s41587-018-0001-2 · Cited by 365
Metadata
- Authors
- Castello, A., Fischer, B., Frese, C. K., Horos, R., Alleaume, A.-M., Foehr, S., Curk, T., Krijgsveld, J., & Hentze, M. W.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2016-08
- Volume
- 63
- Issue
- 4
- Pages
- 696-710
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2480300184
- Cited by
- 637
- References
- 6
- FWCI
- 25.43
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Comprehensive Identification of RNA-Binding Domains in Human Cells. https://app.cochat.ai/papers/10.1016/j.molcel.2016.06.029
- The paper
- Castello, A., Fischer, B., Frese, C. K., Horos, R., Alleaume, A.-M., Foehr, S., Curk, T., Krijgsveld, J., & Hentze, M. W. (2016). Comprehensive Identification of RNA-Binding Domains in Human Cells. Molecular Cell. https://doi.org/10.1016/j.molcel.2016.06.029
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.