The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Histone H3-K56 Acetylation Is Catalyzed by Histone Chaperone-Dependent Complexes
Open accessOverview
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
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A. P., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,952
Lowary, P. T., & Widom, J. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1494 · Cited by 1,778
Histones and histone modifications
Peterson, C. L., & Laniel, M.-A. (2004) · Current Biology · doi:10.1016/j.cub.2004.07.007 · Cited by 1,313
A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Masumoto, H., Hawke, D., Kobayashi, R., & Verreault, A. (2005) · Nature · doi:10.1038/nature03714 · Cited by 544
Expression and Purification of Recombinant Histones and Nucleosome Reconstitution
Luger, K., Rechsteiner, T. J., & Richmond, T. J. (2003) · Chromatin Protocols · doi:10.1385/1-59259-681-9:1 · Cited by 467
Structural Basis for the Histone Chaperone Activity of Asf1
English, C. M., Adkins, M. W., Carson, J. J., Churchill, M. E. A., & Tyler, J. K. (2006) · Cell · doi:10.1016/j.cell.2006.08.047 · Cited by 449
Neuwald, A. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01034-7 · Cited by 447
Yeast Rtt109 Promotes Genome Stability by Acetylating Histone H3 on Lysine 56
Driscoll, R., Hudson, A., & Jackson, S. P. (2007) · Science · doi:10.1126/science.1135862 · Cited by 439
Rtt109 Acetylates Histone H3 Lysine 56 and Functions in DNA Replication
Han, J., Zhou, H., Horazdovsky, B., Zhang, K., Xu, R.-M., & Zhang, Z. (2007) · Science · doi:10.1126/science.1133234 · Cited by 421
Cited by
Yang, X.-J., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210599 · Cited by 940
CBP/p300-mediated acetylation of histone H3 on lysine 56
Das, C., Lucia, M. S., Hansen, K. C., & Tyler, J. K. (2009) · Nature · doi:10.1038/nature07861 · Cited by 697
Signals and Combinatorial Functions of Histone Modifications
Suganuma, T., & Workman, J. L. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-175347 · Cited by 499
Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z. (2008) · Cell · doi:10.1016/j.cell.2008.06.018 · Cited by 447
Chen, C.-C., Carson, J. J., Feser, J., Tamburini, B., Zabaronick, S., Linger, J., & Tyler, J. K. (2008) · Cell · doi:10.1016/j.cell.2008.06.035 · Cited by 425
Metadata
- Authors
- Tsubota, T., Berndsen, C. E., Erkmann, J. A., Smith, C. L., Yang, L., Freitas, M. A., Denu, J. M., & Kaufman, P. D.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 25
- Issue
- 5
- Pages
- 703-712
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2053289821
- Cited by
- 278
- References
- 43
- FWCI
- 10.30
- Type
- journal article
- Language
- en
- Open access
- bronze
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: Histone H3-K56 Acetylation Is Catalyzed by Histone Chaperone-Dependent Complexes. https://app.cochat.ai/papers/10.1016/j.molcel.2007.02.006
- The paper
- Tsubota, T., Berndsen, C. E., Erkmann, J. A., Smith, C. L., Yang, L., Freitas, M. A., Denu, J. M., & Kaufman, P. D. (2007). Histone H3-K56 Acetylation Is Catalyzed by Histone Chaperone-Dependent Complexes. Molecular Cell. https://doi.org/10.1016/j.molcel.2007.02.006
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.