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H2AFX — PARP1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: PARP1 — H2AFX (physical association, affinity chromatography technology) Heo et al., Mol Cell 2008*
• IRef Biogrid Interaction: PARP1 — H2AFX (physical association, affinity chromatography technology) Du et al., Mol Cell Proteomics 2006
• IRef Biogrid Interaction: PARP1 — H2AFX (direct interaction, pull down) Heo et al., Mol Cell 2008*
• MIPS CORUM H2AX complex I: H2AX complex I complex (CALR-DHX30-H2AFX-HIST3H2BB-HSPA5-NPM1-PARP1) Du et al., Mol Cell Proteomics 2006
• IRef Corum Interaction: Complex of 15 proteins (association, mass spectrometry studies of complexes) Du et al., Mol Cell Proteomics 2006
• IRef Dip Interaction: Complex of 15 proteins (anti tag coimmunoprecipitation) Gottschalk et al., Proc Natl Acad Sci U S A 2009
• IRef Intact Interaction: PARP1 — H2AFX (colocalization, confocal microscopy) Yang et al., J Proteome Res 2010
• IRef Intact Interaction: Complex of 103 proteins (association, anti tag coimmunoprecipitation) Yang et al., J Proteome Res 2010
• IRef Intact Interaction: Complex of H2AFX-XRCC5-TOP2A-AIRE-PARP1-PRKDC (association, anti bait coimmunoprecipitation) Abramson et al., Cell 2010
• IRef Intact Interaction: Complex of 11 proteins (association, anti tag coimmunoprecipitation) Yang et al., J Proteome Res 2010
• IRef Intact Interaction: Complex of H2AFX-YWHAZ-CALR-PARP1-CFL1-NONO-PEF1 (association, anti tag coimmunoprecipitation) Yang et al., J Proteome Res 2010

Text-mined interactions from Literome

Bryant et al., Nature 2005 (Neoplasms) : Here, we show that PARP inhibitors trigger gamma-H2AX and RAD51 foci formation
Aguilar-Quesada et al., BMC molecular biology 2007 : PARP inhibition induced gamma H2AX foci accumulation, in an ATM dependent manner
Pacurari et al., Environ Health Perspect 2008 (Neoplasms, Mesothelial) : In the present study, we exposed mesothelial cells to SWCNTs and investigated reactive oxygen species ( ROS ) generation, cell viability, DNA damage, histone H2AX phosphorylation, activation of poly(ADP-ribose) polymerase 1 ( PARP-1 ), stimulation of extracellular signal regulated kinase ( ERKs ), Jun N-terminal kinases (JNKs), protein p38, and activation of activator protein-1 (AP-1), nuclear factor kappaB (NF-kappaB), and protein serine-threonine kinase ( Akt )
Mitchell et al., Mol Pharmacol 2010 : Prior studies have demonstrated that inhibition of CHK1 can promote the activation of extracellular signal regulated kinases 1 and 2 ( ERK1/2 ) and phosphorylation of histone H2AX and that inhibition of poly(ADP-ribose) polymerase 1 ( PARP1 ) can affect growth factor induced ERK1/2 activation