"Hunt"-ing for post-translational modifications that underlie the histone code

Sean Dixon Taverna, C. David Allis, Sandra B. Hake

Research output: Contribution to journalArticle

Abstract

Eukaryotic cells package their DNA with histone proteins to form chromatin that can be regulated to enable transcription, DNA repair and replication in response to cellular needs and external stimuli. A wealth of recent studies of post-translational histone modifications and histone variants have led to an explosion of insights into and more questions about how these processes might be regulated. Work from Donald Hunt and colleagues contributed greatly to our understanding of the "histone code" by developing novel methods to study and identify histone modifications in both generic and specialized variant histone proteins. Without his expertise, the field of chromatin biology would not be where it is today. In recognition, we are pleased to contribute to a special issue of the International Journal of Mass Spectrometry dedicated to the many advances pioneered by the Hunt laboratory, which have enhanced the science of many fields and the careers of many scientists.

Original languageEnglish (US)
Pages (from-to)40-45
Number of pages6
JournalInternational Journal of Mass Spectrometry
Volume259
Issue number1-3
DOIs
StatePublished - Jan 1 2007
Externally publishedYes

Fingerprint

chromatin
Histones
DNA
deoxyribonucleic acid
proteins
Proteins
Transcription
biology
stimuli
Explosions
Mass spectrometry
explosions
Repair
mass spectroscopy
Chromatin
cells

Keywords

  • Donald Hunt
  • Histone code
  • Mass spectrometry
  • Post-translational modifications

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Spectroscopy

Cite this

"Hunt"-ing for post-translational modifications that underlie the histone code. / Taverna, Sean Dixon; David Allis, C.; Hake, Sandra B.

In: International Journal of Mass Spectrometry, Vol. 259, No. 1-3, 01.01.2007, p. 40-45.

Research output: Contribution to journalArticle

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