The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Deletion of Histone Deacetylase 3 Reveals Critical Roles in S Phase Progression and DNA Damage Control
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Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
Todaro, G. J., & Green, H. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.299 · Cited by 2,736
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Hayashi, S., & McMahon, A. P. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0597 · Cited by 1,342
Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,196
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Class II Histone Deacetylases Act as Signal-Responsive Repressors of Cardiac Hypertrophy
Zhang, C. L., McKinsey, T. A., Chang, S., Antos, C. L., Hill, J. A., & Olson, E. N. (2002) · Cell · doi:10.1016/s0092-8674(02)00861-9 · Cited by 973
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Cited by
Haberland, M., Montgomery, R. L., & Olson, E. N. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,526
HDAC family: What are the cancer relevant targets?
Witt, O., Deubzer, H. E., Milde, T., & Oehme, I. (2009) · Cancer Letters · doi:10.1016/j.canlet.2008.08.016 · Cited by 1,069
SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
Oberdoerffer, P., Michan, S., McVay, M., Mostoslavsky, R., Vann, J., Park, S.-K., Hartlerode, A., Stegmuller, J., Hafner, A., Loerch, P., et al. (2008) · Cell · doi:10.1016/j.cell.2008.10.025 · Cited by 852
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 804
The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance
Bouwman, P., & Jonkers, J. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3342 · Cited by 615
Metadata
- Authors
- Bhaskara, S., Chyla, B. J., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z.-W., & Hiebert, S. W.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-04
- Volume
- 30
- Issue
- 1
- Pages
- 61-72
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1997671473
- Cited by
- 372
- References
- 58
- FWCI
- 9.68
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Deletion of Histone Deacetylase 3 Reveals Critical Roles in S Phase Progression and DNA Damage Control. https://app.cochat.ai/papers/10.1016/j.molcel.2008.02.030
- The paper
- Bhaskara, S., Chyla, B. J., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z.-W., & Hiebert, S. W. (2008). Deletion of Histone Deacetylase 3 Reveals Critical Roles in S Phase Progression and DNA Damage Control. Molecular Cell. https://doi.org/10.1016/j.molcel.2008.02.030
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.
