The Occurrence of iε-N-Methyl Lysine in Histones
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe Occurrence of iε-N-Methyl Lysine in HistonesK. MurrayCite this: Biochemistry 1964, 3, 1, 10–15Publication Date (Print):January 1, 1964Publication History Published online1 May 2002Published inissue 1 January 1964https://pubs.acs.org/doi/10.1021/bi00889a003https://doi.org/10.1021/bi00889a003research-articleACS PublicationsRequest reuse permissionsArticle Views987Altmetric-Citations400LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Histone methylation involves transfer of methyl groups to amino acids in histone proteins, adding one, two, or three methyl groups to lysine or arginine residues.
“Histone methylation involves the transfer of methyl groups to amino acids in histone proteins,162 occurring at various locations along the histone tails, resulting in the addition of one, two, or three methyl groups to the lysine or arginine residues.”
From Epigenetic regulation in major depression and other stress-related disorders: molecular mechanisms, clinical relevance and therapeutic potential (2023) · cites this paper as [162]
Cited by
Sorted by citations
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241 · see citing works
Epigenetic mechanisms in memory formation
Levenson, J. M., & Sweatt, J. D. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1604 · Cited by 767 · see citing works
Roles and regulation of histone methylation in animal development
Jambhekar, A., Dhall, A., & Shi, Y. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0151-1 · Cited by 556 · see citing works
Non-histone protein methylation as a regulator of cellular signalling and function
Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479 · see citing works
The epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381 · see citing works
Critical roles of non-histone protein lysine methylation in human tumorigenesis
Hamamoto, R., Saloura, V., & Nakamura, Y. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3884 · Cited by 376 · see citing works
Histones: At the Crossroads of Peptide and Protein Chemistry
Müller, M. M., & Muir, T. W. (2015) · Chemical Reviews · doi:10.1021/cr5003529 · Cited by 247 · see citing works
Yuan, M., Yang, B., Rothschild, G., Mann, J. J., Sanford, L. D., Tang, X., Huang, C., Wang, C., & Zhang, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01519-z · Cited by 246 · see citing works
- Authors
- Murray, K.
- Corresponding author
- Murray, K.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1964-01-01
- Volume
- 3
- Issue
- 1
- Pages
- 10-15
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1963736084
- Cited by
- 521
- References
- 0
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 11 · 2023: 20 · 2022: 23 · 2021: 19 · 2020: 15 · 2019: 28 · 2018: 21 · 2017: 19 · 2016: 22 · 2015: 18 · 2014: 29 · 2013: 16 · 2012: 20
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histones, lysine methylation, histone modifications, post-translational modification, histone methylation
- MeSH terms
- Amino Acids, Animals, Carbon Isotopes, Cattle, Chromatography, Electrophoresis, Histones, Kidney, Liver, Lysine, Methionine, Rabbits, Research, Spectrum Analysis, Spleen, Thymus Gland
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