Journal article

Publication year: 2007

Pages: 40-45

Journal: International Journal of Mass Spectrometry

Volume number: 259

Issue number: 1-3

ISSN: 1387-3806

DOI Link: https://doi.org/10.1016/j.ijms.2006.07.009

Publisher: Elsevier

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. (c) 2006 Elsevier B.V. All rights reserved.

Harvard Citation style: Taverna, S., Allis, C. and Hake, S. (2007) "Hunt"-ing for post-translational modifications that underlie the histone code, International journal of mass spectrometry, 259(1-3), pp. 40-45. https://doi.org/10.1016/j.ijms.2006.07.009

APA Citation style: Taverna, S., Allis, C., & Hake, S. (2007). "Hunt"-ing for post-translational modifications that underlie the histone code. International journal of mass spectrometry. 259(1-3), 40-45. https://doi.org/10.1016/j.ijms.2006.07.009