The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
The Site-Specific Installation of Methyl-Lysine Analogs into Recombinant Histones
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Cites
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,260
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 6×
“Furthermore, K9me2 and KC9me2 substitutions both resulted in significantly lower SUV39H1 activity as was previously observed for a K9me2 peptide (Rea et al., 2000).”
BackgroundMethodInfluentialActive Genes Are Tri-Methylated at K4 of Histone H3
Santos-Rosa, H., Schneider, R., Bannister, A. J., Sherriff, J., Bernstein, B. E., Emre, N. C. T., Schreiber, S. L., Mellor, J., & Kouzarides, T. (2002) · Nature · doi:10.1038/nature01080 · Cited by 2,138
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,057
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
Zubarev, R. A., Kelleher, N. L., & McLafferty, F. W. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973478k · Cited by 1,881
Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Shogren-Knaak, M., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J. R., & Peterson, C. L. (2006) · Science · doi:10.1126/science.1124000 · Cited by 1,873
Lowary, P. T., & Widom, J. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1494 · Cited by 1,778
Role 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
A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
Wysocka, J., Swigut, T., Xiao, H., Milne, T. A., Kwon, S. Y., Landry, J., Kauer, M., Tackett, A. J., Chait, B. T., Badenhorst, P., et al. (2006) · Nature · doi:10.1038/nature04815 · Cited by 1,185
Heterochromatin and Epigenetic Control of Gene Expression
Grewal, S. I. S., & Moazed, D. (2003) · Science · doi:10.1126/science.1086887 · Cited by 1,065
Cited by
Role of the polycomb protein EED in the propagation of repressive histone marks
Margueron, R., Justin, N., Ohno, K., Sharpe, M. L., Son, J., Drury III, W. J., Voigt, P., Martin, S. R., Taylor, W. R., De Marco, V., et al. (2009) · Nature · doi:10.1038/nature08398 · Cited by 1,196
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & David Allis, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,013
Understanding the language of Lys36 methylation at histone H3
Wagner, E. J., & Carpenter, P. B. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3274 · Cited by 936
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Fradet-Turcotte, A., Canny, M. D., Escribano-Díaz, C., Orthwein, A., Leung, C. C. Y., Huang, H., Landry, M.-C., Kitevski-LeBlanc, J., Noordermeer, S. M., Sicheri, F., et al. (2013) · Nature · doi:10.1038/nature12318 · Cited by 686
Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology
Chalker, J. M., Bernardes, G. J. L., Lin, Y. A., & Davis, B. G. (2009) · Chemistry – An Asian Journal · doi:10.1002/asia.200800427 · Cited by 649
Metadata
- Authors
- Simon, M. D., Chu, F., Racki, L. R., de la Cruz, C. C., Burlingame, A. L., Panning, B., Narlikar, G. J., & Shokat, K. M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 128
- Issue
- 5
- Pages
- 1003-1012
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W4210384175
- Cited by
- 473
- References
- 42
- FWCI
- 8.62
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Simon, M. D., Chu, F., Racki, L. R., de la Cruz, C. C., Burlingame, A. L., Panning, B., Narlikar, G. J., & Shokat, K. M. (2007). The Site-Specific Installation of Methyl-Lysine Analogs into Recombinant Histones. Cell. https://doi.org/10.1016/j.cell.2006.12.041
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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.