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The Nucleation and Maintenance of Heterochromatin by a Histone Deacetylase in Fission Yeast
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Citations
Cites
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845 · cited 1×
“Clr4, an H3K9-specific methyltransferase and member of the highly conserved Suv39h protein family, has been implicated in silencing and heterochromatin formation in several different organisms (Ivanova et al., 1998; Rea et al., 2000; Nakayama et al., 2001).”
BackgroundSelf-citationRegulation of Heterochromatic Silencing and Histone H3 Lysine-9 Methylation by RNAi
Volpe, T. A., Kidner, C., Hall, I. M., Teng, G., Grewal, S. I. S., & Martienssen, R. A. (2002) · Science · doi:10.1126/science.1074973 · Cited by 2,055
Self-citationRole of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
Nakayama, J.-I., Rice, J. C., Strahl, B. D., Allis, C. D., & Grewal, S. I. S. (2001) · Science · doi:10.1126/science.1060118 · Cited by 1,739
Self-citationSchultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313
RNAi-Mediated Targeting of Heterochromatin by the RITS Complex
Verdel, A., Jia, S., Gerber, S., Sugiyama, T., Gygi, S., Grewal, S. I. S., & Moazed, D. (2004) · Science · doi:10.1126/science.1093686 · Cited by 1,221
Self-citationPartitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin
Peters, A. H. F. M., Kubicek, S., Mechtler, K., O'Sullivan, R. J., Derijck, A. A. H. A., Perez-Burgos, L., Kohlmaier, A., Opravil, S., Tachibana, M., Shinkai, Y., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00477-5 · Cited by 1,152
Rb targets histone H3 methylation and HP1 to promoters
Nielsen, S. J., Schneider, R., Bauer, U.-M., Bannister, A. J., Morrison, A., O'Carroll, D., Firestein, R., Cleary, M., Jenuwein, T., Herrera, R. E., et al. (2001) · Nature · doi:10.1038/35087620 · Cited by 904
Establishment and Maintenance of a Heterochromatin Domain
Hall, I. M., Shankaranarayana, G. D., Noma, K.-I., Ayoub, N., Cohen, A., & Grewal, S. I. S. (2002) · Science · doi:10.1126/science.1076466 · Cited by 895
Self-citationRNAi-mediated pathways in the nucleus
Matzke, M. A., & Birchler, J. A. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1500 · Cited by 844
Research works printed but not linked: 1
- Morishita, 2001, Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair, Genes Cells, 6, 743, 10.1046/j.1365-2443.2001.00459.x · doi:10.1046/j.1365-2443.2001.00459.x
Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Writing, erasing and reading histone lysine methylations
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250
Grewal, S. I. S., & Jia, S. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2008 · Cited by 1,263
Self-citationYang, X.-J., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210599 · Cited by 940
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
Metadata
- Authors
- Yamada, T., Fischle, W., Sugiyama, T., Allis, C. D., & Grewal, S. I. S.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2005-10
- Volume
- 20
- Issue
- 2
- Pages
- 173-185
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2055223560
- Cited by
- 313
- References
- 50
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2882 d)
- Funders
- Damon Runyon Cancer Research Foundation
- Japan Society for the Promotion of Science
- National Institutes of Health
- National Cancer Institute
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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.
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- CoChat. (2026). Citation check: The Nucleation and Maintenance of Heterochromatin by a Histone Deacetylase in Fission Yeast. https://app.cochat.ai/papers/10.1016/j.molcel.2005.10.002
- The paper
- Yamada, T., Fischle, W., Sugiyama, T., Allis, C. D., & Grewal, S. I. S. (2005). The Nucleation and Maintenance of Heterochromatin by a Histone Deacetylase in Fission Yeast. Molecular Cell. https://doi.org/10.1016/j.molcel.2005.10.002
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.
