Assaying pharmacodynamic endpoints with targeted therapy: Flavopiridol and 17AAG induced dephosphorylation of histone H1.5 in acute myeloid leukemia-Reference-Cited by-同舟云学术

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Assaying pharmacodynamic endpoints with targeted therapy: Flavopiridol and 17AAG induced dephosphorylation of histone H1.5 in acute myeloid leukemia

Published:2010-11-26 Issue:23 Volume:10 Page:4281-4292
ISSN:1615-9853
Container-title:PROTEOMICS
language:en
Short-container-title:Proteomics

Author:

Wang Liwen,Harshman Sean W.,Liu Shujun,Ren Chen,Xu Hua,Sallans Larry,Grever Michael,Byrd John C.,Marcucci Guido,Freitas Michael A.

Funder

Ohio State University

National Institutes of Health

V Foundation

Leukemia & Lymphoma Society

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pmic.201000080/fullpdf

Reference98 articles.

1. Influence of histone H1 on chromatin structure;Thoma;Cell,1977

2. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin;Thoma;J. Cell Biol.,1979

3. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue;Wisniewski;Mol. Cell Proteomics,2007

4. Chromatin condensation: does histone H1 dephosphorylation play a role?;Roth;Trends Biochem. Sci.,1992

5. Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts;Herrera;Proc. Natl. Acad. Sci. USA,1996

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