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Investigations into Context-Dependen...

Kornacki, James R.

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Investigations into Context-Dependent Histone Modification by SAMDI Mass Spectrometry.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Investigations into Context-Dependent Histone Modification by SAMDI Mass Spectrometry./
Author:	Kornacki, James R.
Description:	183 p.
Notes:	Source: Dissertation Abstracts International, Volume: 76-10(E), Section: B.
Contained By:	Dissertation Abstracts International76-10B(E).
Subject:	Analytical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3705294
ISBN:	9781321781984

Investigations into Context-Dependent Histone Modification by SAMDI Mass Spectrometry.
Kornacki, James R.

Investigations into Context-Dependent Histone Modification by SAMDI Mass Spectrometry. - 183 p.

Source: Dissertation Abstracts International, Volume: 76-10(E), Section: B.

Thesis (Ph.D.)--Northwestern University, 2015.

Epigenetics is directed, in part, by the regulated placement and removal of covalent histone post-translational modifications. Patterns of histone post-translational modification regulate access to the associated genome via interactions with protein complexes, which then direct transcriptional fate. This process is established and maintained by the "writing, reading, and erasing" of covalent modifications through the action of histone-modifying enzymes. In this work, I present novel mechanisms of histone modification crosstalk -- a form of enzymatic communication. I also illustrate the powerful influence of selective small molecule modulators. Both emphasize the recurrent theme that histone post-translational modification is highly context-dependent.

ISBN: 9781321781984Subjects--Topical Terms:

3168300
Analytical chemistry.

Investigations into Context-Dependent Histone Modification by SAMDI Mass Spectrometry.
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100 1 $a Kornacki, James R. $3 3192985
245 1 0 $a Investigations into Context-Dependent Histone Modification by SAMDI Mass Spectrometry.
300 $a 183 p.
500 $a Source: Dissertation Abstracts International, Volume: 76-10(E), Section: B.
500 $a Adviser: Milan Mrksich.
502 $a Thesis (Ph.D.)--Northwestern University, 2015.
520 $a Epigenetics is directed, in part, by the regulated placement and removal of covalent histone post-translational modifications. Patterns of histone post-translational modification regulate access to the associated genome via interactions with protein complexes, which then direct transcriptional fate. This process is established and maintained by the "writing, reading, and erasing" of covalent modifications through the action of histone-modifying enzymes. In this work, I present novel mechanisms of histone modification crosstalk -- a form of enzymatic communication. I also illustrate the powerful influence of selective small molecule modulators. Both emphasize the recurrent theme that histone post-translational modification is highly context-dependent.
590 $a School code: 0163.
650 4 $a Analytical chemistry. $3 3168300
650 4 $a Biochemistry. $3 518028
690 $a 0486
690 $a 0487
710 2 $a Northwestern University. $b Chemistry. $3 1030729
773 0 $t Dissertation Abstracts International $g 76-10B(E).
790 $a 0163
791 $a Ph.D.
792 $a 2015
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3705294