Slow elimination of phosphorylated histone γ-H2AX from DNA of terminally differentiated mouse heart cells in situ-Reference-Cited by-同舟云学术

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Slow elimination of phosphorylated histone γ-H2AX from DNA of terminally differentiated mouse heart cells in situ

Published:2006-09 Issue:4 Volume:347 Page:1048-1052
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Gavrilov Boris,Vezhenkova Irina,Firsanov Denis,Solovjeva Liudmila,Svetlova Maria,Mikhailov Vyacheslav,Tomilin Nikolai

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference18 articles.

1. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139;Rogakou;J. Biol. Chem.,1998

2. Megabase chromatin domains involved in DNA double-strand breaks in vivo;Rogakou;J. Cell Biol.,1999

3. Dephosphorylation of histone γ-H2AX during repair of DNA double-strand breaks in mammalian cells and its inhibition by calyculin A;Nazarov;Radiat. Res.,2003

4. Radiation sensitivity, H2AX phosphorylation, and kinetics of repair of DNA strand breaks in irradiated cervical cancer cell lines;Banath;Cancer Res.,2004

5. A double-strand break repair defect in ATM-deficient cells contributes to radiosensitivity;Kuhne;Cancer Res.,2004

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