Determination of histone acetylation status by chromatin immunoprecipitation
Methods in Molecular Biology, ISSN: 1064-3745, Vol: 809, Page: 255-265
2012
- 3Citations
- 19Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations3
- Citation Indexes3
- CrossRef2
- Captures19
- Readers19
- 19
Book Chapter Description
Histone acetylation is the most studied posttranslation modification of nucleosomes. Understanding the mechanisms involved in global and promoter-specific histone acetylation will shed light on the control of transcriptional regulation. Chromatin immunoprecipitation is a powerful technique to study protein-DNA interactions in vivo. Proteins and DNA are cross-linked with formaldehyde, cells are lysed, and DNA is sheared by sonication. Protein-DNA complexes are immunoprecipitated with antibodies specific for total and acetylated histones and the relative occupancy of acetylated and total histones at selected loci is assessed by real-time PCR of the purified DNA.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84555187942&origin=inward; http://dx.doi.org/10.1007/978-1-61779-376-9_17; http://www.ncbi.nlm.nih.gov/pubmed/22113281; https://link.springer.com/10.1007/978-1-61779-376-9_17; https://dx.doi.org/10.1007/978-1-61779-376-9_17; https://link.springer.com/protocol/10.1007/978-1-61779-376-9_17; http://www.springerlink.com/index/10.1007/978-1-61779-376-9_17; http://www.springerlink.com/index/pdf/10.1007/978-1-61779-376-9_17
Springer Science and Business Media LLC
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