| dc.rights.license | CC-BY-NC-ND | |
| dc.contributor.advisor | Vermeulen, Michiel | |
| dc.contributor.author | Peterson, J.C. | |
| dc.date.accessioned | 2014-06-23T17:00:31Z | |
| dc.date.available | 2014-06-23T17:00:31Z | |
| dc.date.issued | 2014 | |
| dc.identifier.uri | https://studenttheses.uu.nl/handle/20.500.12932/16760 | |
| dc.description.abstract | Within eukaryotic cells chromatin plays an important role in the regulation of gene expression.
Nucleosomes form the fundamental repeating unit within chromatin. Nucleosomes consist each of the four core histones around which ~146 basepairs of DNA is wrapped. Both DNA and histone proteins carry additional information which relates to gene expression. This information is present in the form of chemical modifications known as ‘epigenetic marks’. Aberrant epigenetic regulation can result in disease. Histone post-translational modifications (PTMs) are associated with various functions within the cell and miss-regulation of histone PTM patterns have been linked to cancer. Historically many studies have analyzed histone PTMs using site-specific antibodies. However there are major drawbacks in using this approach. Mass spectrometry has been introduced as the tool of choice for studying novel epigenetic structures and understanding the role of histone PTMs. This review will cover the recent developments and applications of mass spectrometry in the field of chromatin biology. | |
| dc.description.sponsorship | Utrecht University | |
| dc.format.extent | 576063 | |
| dc.format.mimetype | application/pdf | |
| dc.language.iso | en | |
| dc.title | The histone code: what proteomics has taught us | |
| dc.type.content | Master Thesis | |
| dc.rights.accessrights | Open Access | |
| dc.subject.keywords | Proteomics, Histone modifications, histone code, histone PTMs. | |
| dc.subject.courseuu | Cancer Genomics and Developmental Biology | |
