PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
33868466-6	2021	Both cell types exhibited a slight decrease in viability following increasing doses of IR; the chondrosarcoma cells demonstrated a significant dose-dependent increase in the expression levels of the DNA damage marker histone H2AX phosphorylation at serine 139 (gammaH2AX).	Serine	249-255	H2A.X variant histone	Homo sapiens	217-229
33868466-6	2021	Both cell types exhibited a slight decrease in viability following increasing doses of IR; the chondrosarcoma cells demonstrated a significant dose-dependent increase in the expression levels of the DNA damage marker histone H2AX phosphorylation at serine 139 (gammaH2AX).	gammah2ax	261-270	H2A.X variant histone	Homo sapiens	217-229
33272936-7	2021	p21-deficient sg12 clones demonstrated less repair of DNA-platinum adducts and increased -H2AX foci after cisplatin exposure, suggesting there was persistent DNA damage after p21 loss.	Cisplatin	106-115	H2A.X variant histone	Homo sapiens	90-94
33631200-3	2021	Portimine induced phosphorylation of H2AX, which could possibly be consistent with the previously published induction of apoptosis with this toxin.	Portimine	0-9	H2A.X variant histone	Homo sapiens	37-41
33323683-7	2021	The MGMT inhibitor O-benzylguanine (O6BG) enhanced TMZ+SN38 in-vitro cytotoxicity, H2AX phosphorylation, caspase-3 cleavage, and apoptosis by terminal deoxynucleotidyl transferase dUTP nick end labeling.	o-benzylguanine	19-34	H2A.X variant histone	Homo sapiens	83-87
33323683-7	2021	The MGMT inhibitor O-benzylguanine (O6BG) enhanced TMZ+SN38 in-vitro cytotoxicity, H2AX phosphorylation, caspase-3 cleavage, and apoptosis by terminal deoxynucleotidyl transferase dUTP nick end labeling.	o6bg	36-40	H2A.X variant histone	Homo sapiens	83-87
32737244-1	2021	Background: DNA double-strand breaks (DSBs) in cells of radionuclide-treated patients are quantifiable by immunofluorescence microscopy, using phosphorylation of histone variant H2AX (gamma-H2AX) to mark radiation-induced foci (RIF).	Radioisotopes	56-68	H2A.X variant histone	Homo sapiens	178-182
32737244-1	2021	Background: DNA double-strand breaks (DSBs) in cells of radionuclide-treated patients are quantifiable by immunofluorescence microscopy, using phosphorylation of histone variant H2AX (gamma-H2AX) to mark radiation-induced foci (RIF).	Radioisotopes	56-68	H2A.X variant histone	Homo sapiens	184-194
33546433-7	2021	Immunoblot analysis revealed rapid onset of D2O-induced stress response phospho-protein activation (p-ERK, p-JNK, p-eIF2alpha, or p-H2AX) or attenuation (p-AKT).	Deuterium Oxide	44-47	H2A.X variant histone	Homo sapiens	132-136
33574926-3	2021	The present study found that the activity of the serine/threonine kinase Akt was negatively associated with H2A.X phosphorylated at the Ser16 site (H2A.X S16ph), but the mechanism of the inverse relationship remains elusive.	Serine	49-55	H2A.X variant histone	Homo sapiens	108-113
33574926-3	2021	The present study found that the activity of the serine/threonine kinase Akt was negatively associated with H2A.X phosphorylated at the Ser16 site (H2A.X S16ph), but the mechanism of the inverse relationship remains elusive.	Serine	49-55	H2A.X variant histone	Homo sapiens	148-153
33574926-6	2021	The changes of cellular proliferation and migration induced by the interaction of Akt, RSK2 and H2A.X was determined by MTT, soft agar colony formation and cell migration experiments.	monooxyethylene trimethylolpropane tristearate	120-123	H2A.X variant histone	Homo sapiens	96-101
33574926-8	2021	The current study indicated that the serine/threonine kinase ribosomal S6 kinase 2 (RSK2) as a kinase of H2A.X could be phosphorylated by Akt at Ser19 site.	Serine	37-43	H2A.X variant histone	Homo sapiens	105-110
33597753-6	2021	We propose a model in which H2AX-containing nucleosomes are rapidly phosphorylated as they actively pass by DSB-anchored cohesin.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	108-111	H2A.X variant histone	Homo sapiens	28-32
33496997-7	2021	PIO also significantly induced the formation of phosphorylated H2AX and p53 binding protein 1 foci.	Pioglitazone	0-3	H2A.X variant histone	Homo sapiens	63-67
33264433-0	2021	ADP-ribosylation of histone variant H2AX promotes base excision repair.	Adenosine Diphosphate	0-3	H2A.X variant histone	Homo sapiens	36-40
33356180-6	2021	The 0.05% DFS-treated HCEP cells presented cell cycle arrest at S phase, reactive oxygen species (ROS) overproduction, and positive staining of phosphorylated H2AX, suggesting that DFS caused ROS-mediated DNA damage.	Diclofenac	10-13	H2A.X variant histone	Homo sapiens	159-163
33356180-6	2021	The 0.05% DFS-treated HCEP cells presented cell cycle arrest at S phase, reactive oxygen species (ROS) overproduction, and positive staining of phosphorylated H2AX, suggesting that DFS caused ROS-mediated DNA damage.	Diclofenac	181-184	H2A.X variant histone	Homo sapiens	159-163
33356180-6	2021	The 0.05% DFS-treated HCEP cells presented cell cycle arrest at S phase, reactive oxygen species (ROS) overproduction, and positive staining of phosphorylated H2AX, suggesting that DFS caused ROS-mediated DNA damage.	Reactive Oxygen Species	192-195	H2A.X variant histone	Homo sapiens	159-163
33039867-8	2021	Histone H2AX phosphorylation on Ser139, an indicator for DNA double-strand break, was upregulated in NaAsO2-exposed DU145 and PC-3 cells.	sodium arsenite	101-107	H2A.X variant histone	Homo sapiens	0-12
33264433-3	2021	Herein, using unbiased mass spectrometry, we identify that glutamate residue 141 (E141) of variant histone H2AX is ADP-ribosylated following oxidative DNA damage.	Glutamic Acid	59-68	H2A.X variant histone	Homo sapiens	99-111
33264433-4	2021	In-depth studies performed with wild-type H2AX and the ADP-ribosylation-deficient E141A mutant suggest that H2AX ADP-ribosylation plays a critical role in base excision repair (BER).	Adenosine Diphosphate	55-58	H2A.X variant histone	Homo sapiens	108-112
33264433-4	2021	In-depth studies performed with wild-type H2AX and the ADP-ribosylation-deficient E141A mutant suggest that H2AX ADP-ribosylation plays a critical role in base excision repair (BER).	Adenosine Diphosphate	113-116	H2A.X variant histone	Homo sapiens	108-112
33264433-6	2021	Moreover, loss of this ADP-ribosylation enhances serine-139 phosphorylation of H2AX (gammaH2AX) upon oxidative DNA damage and erroneously causes the accumulation of DNA double-strand break (DSB) response factors.	Adenosine Diphosphate	23-26	H2A.X variant histone	Homo sapiens	79-83
33264433-6	2021	Moreover, loss of this ADP-ribosylation enhances serine-139 phosphorylation of H2AX (gammaH2AX) upon oxidative DNA damage and erroneously causes the accumulation of DNA double-strand break (DSB) response factors.	Serine	49-55	H2A.X variant histone	Homo sapiens	79-83
33264433-7	2021	Taken together, these results reveal that H2AX ADP-ribosylation not only facilitates BER repair, but also suppresses the gammaH2AX-mediated DSB response.	Adenosine Diphosphate	47-50	H2A.X variant histone	Homo sapiens	42-46
33101488-3	2020	The results demonstrated that 2,3-DCPE upregulated phosphorylated (p-)H2A histone family member X, a biomarker of DNA damage, in the DLD-1 colon cancer cell line.	2-((3-(2,3-dichlorophenoxy)propyl)amino)ethanol	30-38	H2A.X variant histone	Homo sapiens	70-97
33441412-4	2021	We show that in P. falciparum that lacks the H2A.X variant, the canonical P. falciparum H2A (PfH2A) is phosphorylated on serine 121 upon exposure to sources of DNA damage.	Serine	121-127	H2A.X variant histone	Homo sapiens	45-50
33441544-8	2021	In contrast, cells making predominantly poly(A)+ mRNA require this isoform for de novo H2A.X synthesis, required for efficient DDR.	Poly A	40-48	H2A.X variant histone	Homo sapiens	87-92
33505956-5	2020	Findings: Cocaine exposure reduced human microglial cell (HMC3) viability, decreased expression of CD63 and dectin-1 in HMC3-derived EVs, and increased expression of the apoptotic marker histone H2A.x in HMC3-derived EVs.	Cocaine	10-17	H2A.X variant histone	Homo sapiens	187-200
33246341-11	2021	DNA damage was assessed by immunohistochemical localization of gamma-H2AFX (a phosphorylated variant of histone H2AX) and 8-OHdG (8-hydroxy-2"-deoxyguanosine).	gamma-h2afx	63-74	H2A.X variant histone	Homo sapiens	104-116
33389482-10	2021	SCR7 and NU7441 also significantly increased VP-16; CDDP induced DNA double-stand breaks level and delayed drug-induced DSB repair, as seen on the comet assay and measured using H2AX foci.	Cisplatin	52-56	H2A.X variant histone	Homo sapiens	178-182
32814079-8	2020	Further studies indicate that prodigiosin induced apoptosis and DNA damage, as detected by increased caspase-3 cleavage and histone H2AX phosphorylation, further arguing for the downregulation of survivin.	Prodigiosin	30-41	H2A.X variant histone	Homo sapiens	124-136
33065487-5	2020	In the AGS cells expressing APE1, isolated or combined treatment with H2O2 and HPE promoted a slight increase in the cell proliferation and increased the levels of intracellular ROS and DNA double strand breaks (DSBs) indicated by  H2AX foci, a reduction in the proportion of cells in the G0/G1 phase and an increase in the initial apoptosis rate.	Hydrogen Peroxide	70-74	H2A.X variant histone	Homo sapiens	232-236
33297235-4	2021	DEL + THIA significantly induced the foci formation of phosphorylated H2AX protein and p53 binding protein 1 at the highest concentration (44 muM DEL+666 muM THIA) for 120 h. Because gH2AX foci number was still higher in the recovery group given an additional 24 h after 120 h, the recovery period was not sufficient for DNA double-strand breaks repair.	thiacloprid	6-10	H2A.X variant histone	Homo sapiens	70-74
33297235-4	2021	DEL + THIA significantly induced the foci formation of phosphorylated H2AX protein and p53 binding protein 1 at the highest concentration (44 muM DEL+666 muM THIA) for 120 h. Because gH2AX foci number was still higher in the recovery group given an additional 24 h after 120 h, the recovery period was not sufficient for DNA double-strand breaks repair.	thiacloprid	158-162	H2A.X variant histone	Homo sapiens	70-74
33290798-0	2021	Cytosine arabinoside induces phosphorylation of histone H2AX in hippocampal neurons via a noncanonical pathway.	Cytarabine	0-20	H2A.X variant histone	Homo sapiens	48-60
33290798-3	2021	To identify the mechanism by which Ara-C kills neurons, we assessed the levels of phosphorylated histone H2AX (gamma-H2AX), a marker for DNA double-strand breaks (DSBs), in hippocampal neurons cultured for 48 h with Ara-C.	Cytarabine	35-40	H2A.X variant histone	Homo sapiens	97-109
33424554-8	2020	We observed in vitro and in vivo that sevoflurane exposure resulted in DNA damage, given that 8-hydroxydeoxyguanosine (8-OHdG) and phosphorylation of histone variant H2AX (gammaH2AX) were improved.	Sevoflurane	38-49	H2A.X variant histone	Homo sapiens	166-170
33380653-1	2020	Objective: The objective of this study is to observe the effect of 100-mg melatonin in reducing the levels of double-strand breaks (DSB) induced by 10 mGy and 100 mGy X-ray in peripheral lymphocyte applying H2AX immunofluorescence microscopy and comparing the different efficacies of melatonin ingestion 1 and 2 h before irradiation.	Melatonin	74-83	H2A.X variant histone	Homo sapiens	207-211
33380653-1	2020	Objective: The objective of this study is to observe the effect of 100-mg melatonin in reducing the levels of double-strand breaks (DSB) induced by 10 mGy and 100 mGy X-ray in peripheral lymphocyte applying H2AX immunofluorescence microscopy and comparing the different efficacies of melatonin ingestion 1 and 2 h before irradiation.	Melatonin	284-293	H2A.X variant histone	Homo sapiens	207-211
33292101-8	2020	Likewise, fibroblast immunostaining showed that autophagy deficiency established by ammonium chloride (NH4Cl) has significantly increased P38 signalling, DNA damage marker (H2A.X), and oxidative stress marker (dityrosine).	Ammonium Chloride	84-101	H2A.X variant histone	Homo sapiens	173-178
33292101-8	2020	Likewise, fibroblast immunostaining showed that autophagy deficiency established by ammonium chloride (NH4Cl) has significantly increased P38 signalling, DNA damage marker (H2A.X), and oxidative stress marker (dityrosine).	Ammonium Chloride	103-108	H2A.X variant histone	Homo sapiens	173-178
33256213-6	2020	We found an increase in phosphorylation of histone H2A.X at serine 139 (H2A.XpS139), a marker of DSB, in the Npas4, but not c-fos, promoter region 5 min after retrieval, which correlated with increased H3K4me3 levels, suggesting that the two epigenetic marks may work in concert during the reconsolidation process.	Serine	60-66	H2A.X variant histone	Homo sapiens	43-56
32839491-2	2020	It also activates DNA-dependent protein kinase and poly (adenosine diphosphate [ADP]-ribose) polymerase enzymes that induce phosphorylation of H2AX and protein PARylation.	Adenosine	57-66	H2A.X variant histone	Homo sapiens	143-147
33207735-7	2020	In this altered context, beta-HCH can also induce DNA damage through H2AX phosphorylation, demonstrating its multifaceted mechanisms of action.	beta-hexachlorocyclohexane	25-33	H2A.X variant histone	Homo sapiens	69-73
33183998-11	2021	The HBV/HCV/alcohol-associated tumor tissues studied had reduced H2AX but higher gammaH2AX protein levels compared to peritumor and control tissues providing evidence of increased DNA damage during liver disease progression.	Alcohols	12-19	H2A.X variant histone	Homo sapiens	65-69
33077594-8	2020	POLD1 and POLD2 each colocalize with phosphorylated H2AX at ionizing radiation-induced DSBs but not with 53BP1.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	87-91	H2A.X variant histone	Homo sapiens	52-56
32801161-0	2020	Platinum-Induced Ubiquitination of Phosphorylated H2AX by RING1A is Mediated by Replication Protein A in Ovarian Cancer.	Platinum	0-8	H2A.X variant histone	Homo sapiens	50-54
32801161-6	2020	We demonstrate that the PRC1 complex member RING1A mediates monoubiquitination of lysine 119 of phosphorylated H2AX (gammaH2AXub1) at sites of platinum DNA damage in OC cells.	Lysine	82-88	H2A.X variant histone	Homo sapiens	111-115
32801161-6	2020	We demonstrate that the PRC1 complex member RING1A mediates monoubiquitination of lysine 119 of phosphorylated H2AX (gammaH2AXub1) at sites of platinum DNA damage in OC cells.	Platinum	143-151	H2A.X variant histone	Homo sapiens	111-115
32934735-8	2020	Furthermore, treatment with AMF increased the expression levels of phospho-Histone H2AX (gamma-H2AX; a variant of histone 2A, that belongs to the histone 2A family member X) and the DNA repair protein RAD51 homolog 1 (Rad51), indicating the occurrence of DNA damage since gamma-H2AX and Rad51 are both key markers of DNA damage.	amentoflavone	28-31	H2A.X variant histone	Homo sapiens	75-87
33118542-6	2020	Nutritional parameters, DNA damage [histone-variant H2AX phosphorylated on the 139-serine residue (gamma-H2AX) foci/cell], oxidative status, subclinical inflammation were measured.	Serine	83-89	H2A.X variant histone	Homo sapiens	52-56
33195208-3	2020	In the current study, treatment of 5"-Aza or MS-275/enzalutamide induced poly (ADP-ribose) polymerase (PARP) cleavage and p-H2A.X in CaP cells with an increase of maspin expression but a decrease of AR.	Azacitidine	35-41	H2A.X variant histone	Homo sapiens	124-129
33195208-3	2020	In the current study, treatment of 5"-Aza or MS-275/enzalutamide induced poly (ADP-ribose) polymerase (PARP) cleavage and p-H2A.X in CaP cells with an increase of maspin expression but a decrease of AR.	entinostat	45-51	H2A.X variant histone	Homo sapiens	124-129
33195208-3	2020	In the current study, treatment of 5"-Aza or MS-275/enzalutamide induced poly (ADP-ribose) polymerase (PARP) cleavage and p-H2A.X in CaP cells with an increase of maspin expression but a decrease of AR.	enzalutamide	52-64	H2A.X variant histone	Homo sapiens	124-129
31802375-5	2020	GEM induced apoptosis by increasing DNA damage (phosphorylated core histone protein H2AX (gamma-H2AX)), MBRI-001 activated mitochondrial-apoptotic pathway (cleaved poly-ADP ribose polymerase (PARP)).	gemcitabine	0-3	H2A.X variant histone	Homo sapiens	84-88
31983282-7	2020	Taken together, our data suggest that PRKDC-mediated phosphorylation of PRKAG1 primes AMPK complex to the lysosomal activation by STK11 in cancer cells thereby linking DNA damage response to autophagy and cellular metabolism.Abbreviations: AXIN1: axin 1; 3-MA: 3-methyladenine; 5-FU: 5-fluorouracil; AA mutant: double alanine mutant (S192A, T284A) of PRKAG1; ACACA: acetyl-CoA carboxylase alpha; AICAR: 5-Aminoimidazole-4-carboxamide ribonucleotide; AMPK: AMP-activated protein kinase; ATG: autophagy-related; ATM: ataxia telangiectasia mutated; ATR: ATM serine/threonine kinase; AV: autophagic vacuole; AVd: degradative autophagic vacuole; AVi: initial autophagic vacuole; BECN1: beclin 1; BSA: bovine serum albumin; CBS: cystathionine beta-synthase; CDK7: cyclin dependent kinase 7; CDKN1A: cyclin dependent kinase inhibitor 1A; EGFP: enhanced green fluorescent protein; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GST: glutathione S transferase; H2AX/H2AFX: H2A.X variant histone; HBSS: Hanks balanced salt solution; IP: immunopurification; IR: ionizing radiation; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MAP3K9: mitogen-activated protein kinase kinase kinase 9; mRFP: monomeric red fluorescent protein; mCh: mCherry; MCM7: minichromosome maintenance complex component 7; MTORC1: mechanistic target of rapamycin kinase complex 1; NHEJ: non-homologous end joining; NRBP2: nuclear receptor binding protein 2; NTC: non-targeting control; NUAK1: NUAK family kinase 1; PBS: phosphate-buffered saline; PIK3AP1: phosphoinositide-3-kinase adaptor protein 1; PIK3CA: phosphatidylinositol-4,5-biphosphate 3-kinase catalytic subunit alpha; PIKK: phosphatidylinositol 3-kinase-related kinase; PRKAA: protein kinase AMP-activated catalytic subunit alpha; PRKAB: protein kinase AMP-activated non-catalytic subunit beta; PRKAG: protein kinase AMP-activated non-catalytic subunit gamma; PRKDC: protein kinase, DNA-activated, catalytic subunit; RLuc: Renilla luciferase; RPS6KB1: ribosomal protein S6 kinase B1; SQSTM1: sequestosome 1; STK11/LKB1: serine/threonine kinase 11; TP53: tumor protein p53; TSKS: testis specific serine kinase substrate; ULK1: unc-51 like autophagy activating kinase 1; WIPI2: WD repeat domain, phosphoinositide interacting 2; WT: wild type.	Adenosine Monophosphate	86-89	H2A.X variant histone	Homo sapiens	954-958
31983282-7	2020	Taken together, our data suggest that PRKDC-mediated phosphorylation of PRKAG1 primes AMPK complex to the lysosomal activation by STK11 in cancer cells thereby linking DNA damage response to autophagy and cellular metabolism.Abbreviations: AXIN1: axin 1; 3-MA: 3-methyladenine; 5-FU: 5-fluorouracil; AA mutant: double alanine mutant (S192A, T284A) of PRKAG1; ACACA: acetyl-CoA carboxylase alpha; AICAR: 5-Aminoimidazole-4-carboxamide ribonucleotide; AMPK: AMP-activated protein kinase; ATG: autophagy-related; ATM: ataxia telangiectasia mutated; ATR: ATM serine/threonine kinase; AV: autophagic vacuole; AVd: degradative autophagic vacuole; AVi: initial autophagic vacuole; BECN1: beclin 1; BSA: bovine serum albumin; CBS: cystathionine beta-synthase; CDK7: cyclin dependent kinase 7; CDKN1A: cyclin dependent kinase inhibitor 1A; EGFP: enhanced green fluorescent protein; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GST: glutathione S transferase; H2AX/H2AFX: H2A.X variant histone; HBSS: Hanks balanced salt solution; IP: immunopurification; IR: ionizing radiation; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MAP3K9: mitogen-activated protein kinase kinase kinase 9; mRFP: monomeric red fluorescent protein; mCh: mCherry; MCM7: minichromosome maintenance complex component 7; MTORC1: mechanistic target of rapamycin kinase complex 1; NHEJ: non-homologous end joining; NRBP2: nuclear receptor binding protein 2; NTC: non-targeting control; NUAK1: NUAK family kinase 1; PBS: phosphate-buffered saline; PIK3AP1: phosphoinositide-3-kinase adaptor protein 1; PIK3CA: phosphatidylinositol-4,5-biphosphate 3-kinase catalytic subunit alpha; PIKK: phosphatidylinositol 3-kinase-related kinase; PRKAA: protein kinase AMP-activated catalytic subunit alpha; PRKAB: protein kinase AMP-activated non-catalytic subunit beta; PRKAG: protein kinase AMP-activated non-catalytic subunit gamma; PRKDC: protein kinase, DNA-activated, catalytic subunit; RLuc: Renilla luciferase; RPS6KB1: ribosomal protein S6 kinase B1; SQSTM1: sequestosome 1; STK11/LKB1: serine/threonine kinase 11; TP53: tumor protein p53; TSKS: testis specific serine kinase substrate; ULK1: unc-51 like autophagy activating kinase 1; WIPI2: WD repeat domain, phosphoinositide interacting 2; WT: wild type.	Adenosine Monophosphate	86-89	H2A.X variant histone	Homo sapiens	959-964
31983282-7	2020	Taken together, our data suggest that PRKDC-mediated phosphorylation of PRKAG1 primes AMPK complex to the lysosomal activation by STK11 in cancer cells thereby linking DNA damage response to autophagy and cellular metabolism.Abbreviations: AXIN1: axin 1; 3-MA: 3-methyladenine; 5-FU: 5-fluorouracil; AA mutant: double alanine mutant (S192A, T284A) of PRKAG1; ACACA: acetyl-CoA carboxylase alpha; AICAR: 5-Aminoimidazole-4-carboxamide ribonucleotide; AMPK: AMP-activated protein kinase; ATG: autophagy-related; ATM: ataxia telangiectasia mutated; ATR: ATM serine/threonine kinase; AV: autophagic vacuole; AVd: degradative autophagic vacuole; AVi: initial autophagic vacuole; BECN1: beclin 1; BSA: bovine serum albumin; CBS: cystathionine beta-synthase; CDK7: cyclin dependent kinase 7; CDKN1A: cyclin dependent kinase inhibitor 1A; EGFP: enhanced green fluorescent protein; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GST: glutathione S transferase; H2AX/H2AFX: H2A.X variant histone; HBSS: Hanks balanced salt solution; IP: immunopurification; IR: ionizing radiation; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MAP3K9: mitogen-activated protein kinase kinase kinase 9; mRFP: monomeric red fluorescent protein; mCh: mCherry; MCM7: minichromosome maintenance complex component 7; MTORC1: mechanistic target of rapamycin kinase complex 1; NHEJ: non-homologous end joining; NRBP2: nuclear receptor binding protein 2; NTC: non-targeting control; NUAK1: NUAK family kinase 1; PBS: phosphate-buffered saline; PIK3AP1: phosphoinositide-3-kinase adaptor protein 1; PIK3CA: phosphatidylinositol-4,5-biphosphate 3-kinase catalytic subunit alpha; PIKK: phosphatidylinositol 3-kinase-related kinase; PRKAA: protein kinase AMP-activated catalytic subunit alpha; PRKAB: protein kinase AMP-activated non-catalytic subunit beta; PRKAG: protein kinase AMP-activated non-catalytic subunit gamma; PRKDC: protein kinase, DNA-activated, catalytic subunit; RLuc: Renilla luciferase; RPS6KB1: ribosomal protein S6 kinase B1; SQSTM1: sequestosome 1; STK11/LKB1: serine/threonine kinase 11; TP53: tumor protein p53; TSKS: testis specific serine kinase substrate; ULK1: unc-51 like autophagy activating kinase 1; WIPI2: WD repeat domain, phosphoinositide interacting 2; WT: wild type.	Adenosine Monophosphate	86-89	H2A.X variant histone	Homo sapiens	966-971
33020527-6	2020	Application of CAP in conjunction TMZ increased DNA damage measured by the phosphorylation of H2AX and induced G2/M cell cycle arrest.	Temozolomide	34-37	H2A.X variant histone	Homo sapiens	94-98
31802375-5	2020	GEM induced apoptosis by increasing DNA damage (phosphorylated core histone protein H2AX (gamma-H2AX)), MBRI-001 activated mitochondrial-apoptotic pathway (cleaved poly-ADP ribose polymerase (PARP)).	gemcitabine	0-3	H2A.X variant histone	Homo sapiens	90-100
32060401-3	2020	Distinctly, prior to apoptosis, MEDI2228 activates DDRs in MM cells via phosphorylation of ATM/ATR kinases, CHK1/2, CDK1/2, and H2AX, associated with expression of DDR-related genes.	medi2228	32-40	H2A.X variant histone	Homo sapiens	128-132
32878783-7	2020	In addition, this sclareol-induced growth arrest was associated with DNA damage as indicated by phosphorylation of H2AX, activation of ATR and Chk1.	sclareol	18-26	H2A.X variant histone	Homo sapiens	115-119
32821342-6	2020	Further investigation revealed that TQ treatment led to increased TUNEL positivity and a dramatic increase in the amount of the DNA damage marker gamma H2AX particularly in 5FU-resistant colonospheres, suggesting that the diminished sphere forming ability in TQ-treated colonospheres is due to induction of DNA damage and apoptotic cell death.	thymoquinone	36-38	H2A.X variant histone	Homo sapiens	152-156
31855905-2	2020	Earlier, we demonstrated the accumulation of phosphorylated histone H2AX (gammaH2AX), a marker for DNA damage when mGluR1-expressing melanoma cells were treated with a functional inhibitor, riluzole.	Riluzole	190-198	H2A.X variant histone	Homo sapiens	68-72
32492431-3	2020	Here, we show that the original version of catalytically dead Cas12a (dCas12a)-conjugated BEs induce a basal level of DNA breaks and minimally activate DDR proteins, including H2AX, ATM, ATR, and p53.	BES	90-93	H2A.X variant histone	Homo sapiens	176-180
32236595-0	2020	Systematic analysis of lysine acetylome and succinylome reveals the correlation between modification of H2A.X complexes and DNA damage response in breast cancer.	lysine acetylome	23-39	H2A.X variant histone	Homo sapiens	104-109
32236595-0	2020	Systematic analysis of lysine acetylome and succinylome reveals the correlation between modification of H2A.X complexes and DNA damage response in breast cancer.	succinylome	44-55	H2A.X variant histone	Homo sapiens	104-109
31855905-5	2020	Using flow cytometry and a fluorescent antibody to gamma H2AX, our results demonstrate that NHEJ is likely to be the preferred DNA repair pathway to restore DNA double-stranded breaks induced by riluzole in mGluR1-expressing melanoma cells.	Riluzole	195-203	H2A.X variant histone	Homo sapiens	57-61
32424115-2	2020	RNF168 catalyzes H2A and H2AX ubiquitination on lysine 13/15 (K13/K15) upon DNA damage and promotes the accrual of downstream repair factors at damaged chromatin.	Lysine	48-54	H2A.X variant histone	Homo sapiens	25-29
32485940-4	2020	Increased levels of the phosphorylated isoform of the H2AX histone are directly correlated with DSBs and proposed as a molecular biomarker of DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	96-100	H2A.X variant histone	Homo sapiens	54-66
32397119-8	2020	Interestingly, in human cancer cells exposure to 3-BP also induces DNA breaks that trigger H2A.X phosphorylation.	bromopyruvate	49-53	H2A.X variant histone	Homo sapiens	91-96
32198455-5	2020	Inhibiting the ubiquitin-proteasome machinery with bortezomib is effective in GIST cells through a dual mechanism of KIT transcriptional downregulation and upregulation of the pro-apoptotic histone H2AX but clinically problematic due to the drug"s adverse effects.	Bortezomib	51-61	H2A.X variant histone	Homo sapiens	190-202
32494130-7	2020	We demonstrated that CuONPs uptake induced DNA damage in HUVECs as evidenced by gammaH2AX foci formation and increased phosphorylation levels of ATR, ATM, p53 and H2AX.	cuonps	21-27	H2A.X variant histone	Homo sapiens	85-89
32213959-4	2020	Cell death induced by PGA2 was associated with phosphorylation of histone H2A variant H2AX (H2AX), activation of caspase-3 and cleavage of poly(ADP-ribose) polymerase 1 in HCT116 cells.	prostaglandin A2	22-26	H2A.X variant histone	Homo sapiens	86-90
32213959-4	2020	Cell death induced by PGA2 was associated with phosphorylation of histone H2A variant H2AX (H2AX), activation of caspase-3 and cleavage of poly(ADP-ribose) polymerase 1 in HCT116 cells.	prostaglandin A2	22-26	H2A.X variant histone	Homo sapiens	92-96
32213959-11	2020	Delayed apoptosis by PGA2 in HCT116 p53-/- cells was also associated with phosphorylation of H2AX but was not inhibited by either PFT-  or NU7441.	prostaglandin A2	21-25	H2A.X variant histone	Homo sapiens	93-97
31864052-4	2020	PBDEs (-47, -99 and -209) at the environment relevant concentrations (0.01 and 1  muM) induce oxidative stress (in term of NOX-4 expression as well as ROS and JC-1 production), activate the mechanism of DNA-damage and repair affecting Olive Tail length (comet assay) production and H2AX phosphorylation (ser139) in normal human bronchial epithelial cells.	Halogenated Diphenyl Ethers	0-5	H2A.X variant histone	Homo sapiens	282-286
31984785-6	2020	WABM caused phospho-H2AX increases that were blocked by a reactive oxygen species (ROS) scavenger.	Oxygen	67-73	H2A.X variant histone	Homo sapiens	20-24
31861721-9	2019	Additionally, downregulation of Prx5 augmented rotenone-induced DNA damage manifested as induction of phosphorylated histone H2AX (gamma-H2AX) and activation of ataxia telangiectasia mutated (ATM) kinase.	Rotenone	47-55	H2A.X variant histone	Homo sapiens	117-129
31622995-7	2020	Eglerisine induced cell cycle arrest after 72 h of treatment by phosphorylation of H2AX histone, reducing the S phase and increasing the G2 phase of the cell cycle.	eglerisine	0-10	H2A.X variant histone	Homo sapiens	83-95
31952105-8	2020	Furthermore, casticin increased p-ATM at 6 h and increased p-ATR and BRCA1 at 6-24 h treatment but decreased p-ATM at 24-48 h, as well as decreased p-ATR and BRCA1 at 48 h. Furthermore, casticin decreased p-p53 at 6-24 h but increased at 48 h. Casticin increased p-H2A.X and MDC1 at 6-48 h treatment.	casticin	13-21	H2A.X variant histone	Homo sapiens	265-270
31952105-10	2020	Casticin induced the expressions and nuclear translocation of p-H2AX in A549 cells by confocal laser microscopy.	casticin	0-8	H2A.X variant histone	Homo sapiens	64-68
31948066-9	2020	Moreover, Rad51 and -H2AX foci were mislocalized in FGFR-inhibited GIST and the amount of Rad51 was substantially decreased in -H2AX-immunoprecipitated complexes, thereby illustrating the defect of Rad51 recombinase loading to the Dox-induced DSBs.	Doxorubicin	231-234	H2A.X variant histone	Homo sapiens	128-132
31855962-0	2019	Isobaric tags for relative and absolute quantitation-based quantitative proteomic analysis of X-linked inhibitor of apoptosis and H2AX in etoposide-induced renal cell carcinoma apoptosis.	Etoposide	138-147	H2A.X variant histone	Homo sapiens	130-134
31410901-5	2019	A C-terminal dual serine target motif unique to H2AX in the plant lineage showed 171-fold phosphorylation that was absent in atm mutant lines.	Serine	18-24	H2A.X variant histone	Homo sapiens	48-52
31736361-0	2019	KRas-ERK signalling promotes the onset and maintenance of uveal melanoma through regulating JMJD6-mediated H2A.X phosphorylation at tyrosine 39.	Tyrosine	132-140	H2A.X variant histone	Homo sapiens	107-112
31736361-1	2019	Since DNA damage is a first incident occurred during a tumour attack, it is rational that histone H2A.X phosphorylation on tyrosine 39 (H2A.XY39ph) may act as a tumour-relevant factor.	Tyrosine	123-131	H2A.X variant histone	Homo sapiens	98-103
31848352-3	2019	We characterize the kinetics of PARP1 binding to a variety of nucleosomes harbouring DNA double-strand breaks, which reveal that PARP1 associates faster with (gamma)H2A.X- versus H2A-nucleosomes, resulting in a higher affinity for the former, which is maximal for gammaH2A.X-nucleosome that is also the activator eliciting the greatest poly-ADP-ribosylation catalytic efficiency.	Adenosine Diphosphate	336-344	H2A.X variant histone	Homo sapiens	159-170
31848352-4	2019	The enhanced activities with gammaH2A.X-nucleosome coincide with increased accessibility of the DNA termini resulting from the H2A.X-Ser139 phosphorylation.	seryl-seryl-seryl-arginine	133-136	H2A.X variant histone	Homo sapiens	34-39
31818017-6	2019	Coronarin D potently suppressed cell viability in glioblastoma U-251 cell line, and also induced G1 arrest by reducing p21 protein and histone H2AX phosphorylation, leading to DNA damage and apoptosis.	coronarin D	0-11	H2A.X variant histone	Homo sapiens	135-147
31614172-0	2019	Formaldehyde inhibits UV-induced phosphorylation of histone H2AX.	Formaldehyde	0-12	H2A.X variant histone	Homo sapiens	52-64
31750234-0	2019	Actinomycin D-Activated RNase L Promotes H2A.X/H2B-Mediated DNA Damage and Apoptosis in Lung Cancer Cells.	Dactinomycin	0-13	H2A.X variant histone	Homo sapiens	41-46
31799193-6	2019	Results: Co-immunoprecipitation studies confirmed that Livin interacted with H2A.X and that it was phosphorylation dependent.	12-(4'-azido-2'-nitrophenoxy)dodecanoyl-coenzyme A	9-11	H2A.X variant histone	Homo sapiens	77-82
31617531-6	2019	The phosphorylation of H2A.X, which is a DNA damage marker, was induced by DATS both in a dose- and time-dependent manner.	diallyl trisulfide	75-79	H2A.X variant histone	Homo sapiens	23-28
31750234-7	2019	The present study highlighted the crucial role of RNase L in triggering apoptosis mechanism through the Caspase-3/ROCK-1/PARP/H2A.X+H2B/p21 axis during Act D treatment.	Dactinomycin	152-157	H2A.X variant histone	Homo sapiens	126-131
31519582-7	2019	Western blotting showed that Ro 90-7501 suppressed the phosphorylation of ATM and its downstream proteins, such as H2AX, Chk1, and Chk2, after irradiation.	ro 90	29-34	H2A.X variant histone	Homo sapiens	115-119
31777420-7	2019	In addition, NC profoundly increased phosphorylation of the histone variant H2AX at Ser139, a typical marker of DNA damage.	nitidine	13-15	H2A.X variant histone	Homo sapiens	76-80
31777420-7	2019	In addition, NC profoundly increased phosphorylation of the histone variant H2AX at Ser139, a typical marker of DNA damage.	seryl-seryl-seryl-arginine	84-87	H2A.X variant histone	Homo sapiens	76-80
31445935-5	2019	We demonstrated that Livin induced a colon cancer phenotype, including proliferation and migration, by regulating H2A.XY39ph (histone family 2A variant (H2AX) phosphorylated on the 39th serine site).	Serine	186-192	H2A.X variant histone	Homo sapiens	153-157
31438980-8	2019	CONCLUSIONS: The results indicate that the IFC-based gamma-H2AX protocol may provide a practical and high-throughput platform for measurements of individual global DNA DSB repair capacity which can facilitate precision medicine by predicting individual radiosensitivity and risk of developing adverse effects related to radiotherapy treatment.	propham	43-46	H2A.X variant histone	Homo sapiens	59-63
31391500-6	2019	In addition, both metal complexes induced phosphorylation of histone H2AX (S139), JNK2 (T183/Y185) and p38alpha (T180/Y182), and cotreatment with JNK/SAPK and p38 MAPK inhibitors reduced complexes-induced apoptosis, indicating DNA double-strand break and activation of caspase-mediated apoptosis through JNK/p38 pathways.	Metals	18-23	H2A.X variant histone	Homo sapiens	61-73
31146257-7	2019	In addition, tungsten-exposed thyrospheres had abnormal expression of genes commonly altered also in thyroid cancer and increased activation of the DNA-repair proteins H2AX and 53BP1.	Tungsten	13-21	H2A.X variant histone	Homo sapiens	168-172
31289893-1	2019	The H2AX histone protein is rapidly phosphorylated at the serine-139 position (gammaH2AX) in response to a broad range of DNA lesions.	Serine	58-64	H2A.X variant histone	Homo sapiens	4-16
30624777-10	2019	Further, we found that arecoline-induced H2AX expression was regulated by FMO3.	Arecoline	23-32	H2A.X variant histone	Homo sapiens	41-45
30155717-10	2019	Importantly, the hexane partition derived from the crude extract presented cytotoxic effect both in vitro and in vivo, and initiates cell responses, such as DNA damage (H2AX activity), apoptosis via intrinsic pathway (cleavage of caspase-9, caspase-3, poly (ADP-ribose) polymerase (PARP) and mitochondrial membrane depolarization) and decreased p21 expression by ubiquitin proteasome pathway.	Hexanes	17-23	H2A.X variant histone	Homo sapiens	169-173
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	ptyr142	53-60	H2A.X variant histone	Homo sapiens	8-12
31384396-5	2019	We found that, in colon cancer cells, HG attenuated ADR-induced ROS production that consequently diminished ADR-induced H2AX phosphorylation and micronuclei (MN) formation.	Reactive Oxygen Species	64-67	H2A.X variant histone	Homo sapiens	120-124
31839711-8	2019	As expected, ATR inhibition with VE-822 reversed cisplatin-induced DDR and enhanced cisplatin-induced activation of H2AX, which is an important marker of DNA damage.	Cisplatin	84-93	H2A.X variant histone	Homo sapiens	116-120
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	ptyr142	53-60	H2A.X variant histone	Homo sapiens	62-66
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	ptyr142	53-60	H2A.X variant histone	Homo sapiens	62-66
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	py142	67-72	H2A.X variant histone	Homo sapiens	8-12
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	py142	67-72	H2A.X variant histone	Homo sapiens	62-66
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	py142	67-72	H2A.X variant histone	Homo sapiens	62-66
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	pser139	77-84	H2A.X variant histone	Homo sapiens	8-12
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	gammah2ax	86-95	H2A.X variant histone	Homo sapiens	8-12
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	py142	168-173	H2A.X variant histone	Homo sapiens	8-12
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	py142	168-173	H2A.X variant histone	Homo sapiens	62-66
31045206-1	2019	Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (gammaH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive.	py142	168-173	H2A.X variant histone	Homo sapiens	62-66
31141305-4	2019	DSBs also trigger the activation of the DNA damage response pathway, in which protein kinase ataxia-telangiectasia mutated (ATM) phosphorylates multiple substrates, including histone H2AX.	dsbs	0-4	H2A.X variant histone	Homo sapiens	175-187
30825294-0	2019	Synergetic Effect of Silver Nanoparticles and UVC Irradiation on H2AX Gene Expression in TK6 Cells.	Silver	21-27	H2A.X variant histone	Homo sapiens	65-69
30797556-8	2019	In addition, DNA double strand breaks (DSBs), measured by phosphorylation of the core histone H2A variant (H2AX) on serine 139 (gammaH2AX), markedly increased in Atg5KO MEFs compared to wild-type MEFs.	dsbs	39-43	H2A.X variant histone	Homo sapiens	107-111
31059083-8	2019	Expression of cleaved caspase-3, cleaved poly(ADP-ribose) polymerase and p-H2AX was enhanced by tranilast in combination with cisplatin.	Phosphorus	2-3	H2A.X variant histone	Homo sapiens	75-79
31059083-8	2019	Expression of cleaved caspase-3, cleaved poly(ADP-ribose) polymerase and p-H2AX was enhanced by tranilast in combination with cisplatin.	Cisplatin	126-135	H2A.X variant histone	Homo sapiens	75-79
31275862-6	2019	Using a RPPA approach, we showed that Phospho-H2AX/H2AX and Phospho-NBS1/NBS1 were predictive of Dbait efficacy in xenograft models.	dbait	97-102	H2A.X variant histone	Homo sapiens	46-50
31275862-6	2019	Using a RPPA approach, we showed that Phospho-H2AX/H2AX and Phospho-NBS1/NBS1 were predictive of Dbait efficacy in xenograft models.	dbait	97-102	H2A.X variant histone	Homo sapiens	51-55
30900384-7	2019	In addition, we observed that KLF5 knockdown could decrease DNA repair potential by inhibiting H2AX S139 phosphorylation in response to cisplatin.	Cisplatin	136-145	H2A.X variant histone	Homo sapiens	95-99
31212679-6	2019	The expression levels of p-H2.AX and AMPK alpha2 induced by high glucose were also significantly decreased in response to treatment with the C. turczaninowii extract.	Glucose	65-72	H2A.X variant histone	Homo sapiens	27-32
31174565-10	2019	Moreover, H. cordata and 2-undecanone effectively decreased B[a]P-induced intracellular reactive oxygen species (ROS) overproduction and further notably protected BEAS.2B cells from B[a]P-induced DNA damage and inflammation by significantly inhibiting phosphorylated H2A.X overexpression and interleukin-1beta secretion.	undecan-2-one	25-37	H2A.X variant histone	Homo sapiens	267-272
31174565-10	2019	Moreover, H. cordata and 2-undecanone effectively decreased B[a]P-induced intracellular reactive oxygen species (ROS) overproduction and further notably protected BEAS.2B cells from B[a]P-induced DNA damage and inflammation by significantly inhibiting phosphorylated H2A.X overexpression and interleukin-1beta secretion.	Phosphorus	64-65	H2A.X variant histone	Homo sapiens	267-272
31237414-0	2019	Detection of Histone H2AX Phosphorylation on Ser-139 as an Indicator of DNA Damage.	Serine	45-48	H2A.X variant histone	Homo sapiens	13-25
31237414-1	2019	This unit describes immunocytochemical detection of histone H2AX phosphorylated on Ser-139 (gammaH2AX) to reveal DNA damage, particularly when the damage involves the presence of DNA double-strand breaks (DSBs).	Serine	83-86	H2A.X variant histone	Homo sapiens	52-64
31151422-1	2019	BACKGROUND: Histone H2AX phosphorylation at the site of Tyr-142 can participates in multiple biological progressions, which is including DNA repair.	Tyrosine	56-59	H2A.X variant histone	Homo sapiens	20-24
30797556-8	2019	In addition, DNA double strand breaks (DSBs), measured by phosphorylation of the core histone H2A variant (H2AX) on serine 139 (gammaH2AX), markedly increased in Atg5KO MEFs compared to wild-type MEFs.	Serine	116-122	H2A.X variant histone	Homo sapiens	107-111
30696938-6	2019	We also observed low phosphorylation of H2AX, which activates DSBs repair signaling, in emphysema.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	62-66	H2A.X variant histone	Homo sapiens	40-44
29872938-6	2019	Immunofluorescence staining assay was performed to detect the expression of the DNA injury marker tsadi-H2AX after treatment with rucaparib and radiotherapy.	rucaparib	130-139	H2A.X variant histone	Homo sapiens	104-108
30464209-7	2018	Phosphorylation of H2AX as indicator for DNA damage, was detected for Rf-1 in a strictly light-dependent fashion while in case of free cisplatin also in the dark.	Cisplatin	135-144	H2A.X variant histone	Homo sapiens	19-23
30678426-6	2019	The top ten hub genes (CDC20, H2AFX, ENO1, ACTB, ISG15,KAT2B, HNRNPD, YWHAE, GJA1 and CAV1) were identified, which play important roles in critical signalingpathways that regulate the process of oxidation-reduction reaction and carboxylic acid metabolism.	Carboxylic Acids	228-243	H2A.X variant histone	Homo sapiens	30-35
30827262-12	2019	Ex vivo results showed Gossypetin inhibited solar UV-induced phosphorylation of PBK/TOPK, p38 MAPK, ERK1/2 and H2AX by suppressing PBK/TOPK activity.	gossypetin	23-33	H2A.X variant histone	Homo sapiens	111-115
30168750-4	2019	The H2AX and MRE11 proteins generated following DSBs formation and pro-inflammatory cytokines (CKs) secreted after irradiation are relevant candidates to monitor the cellular responses induced by CBCT.	dsbs	48-52	H2A.X variant histone	Homo sapiens	4-8
31168028-7	2019	PHMG-p promoted ROS generation and consequently increased the expression of DNA damage markers such as ATM and H2AX phosphorylation.	polyhexamethyleneguanidine	0-6	H2A.X variant histone	Homo sapiens	111-115
31168028-8	2019	The antioxidant N-acetylcysteine reduced the expression of phosphorylated ATM and H2AX, and the ATM inhibitor, caffeine, inhibited p53 activation.	Acetylcysteine	16-32	H2A.X variant histone	Homo sapiens	82-86
30547460-2	2019	In response to DNA damage, histone H2AX molecules are rapidly phosphorylated at serine 139 near the site of DNA DSBs and form gamma-H2AX foci.	Serine	80-86	H2A.X variant histone	Homo sapiens	27-39
30346110-6	2018	By utilizing the multifunctionality of MPAA, we carried out a one-pot five-segment ligation to afford histone H2AX (142 amino acids), which was isolated in 59 % yield.	mpaa	39-43	H2A.X variant histone	Homo sapiens	102-114
30031728-4	2018	Markers of generic and oxidative DNA damage [phosphorylated histone H2AX (gammaH2AX) and 8-hydroxy-2"-deoxyguanosine (8-OHdG)] were significantly higher in liver metastases compared with their corresponding primary tumors.	gammah2ax	74-83	H2A.X variant histone	Homo sapiens	60-72
30295471-4	2018	Furthermore, we showed PBDEQ exposure result in increased DNA migration, micronucleus frequency, and the promotion of 8-OHdG and phosphorylation of histone H2AX (gamma-H2AX) levels.	pbdeq	23-28	H2A.X variant histone	Homo sapiens	148-160
30279363-5	2018	We also observed that the cisplatin-mediated bystander effect was elicited as DNA Double Strand Breaks (DSBs) with positive H2AX Ser139 phosphorylation (gammaH2AX) formation, an indicator of DNA DSBs.	Cisplatin	26-35	H2A.X variant histone	Homo sapiens	124-128
30103844-7	2018	Phosphorylated H2AX (gammaH2AX) foci assay demonstrate that both resveratrol and cisplatin treatment result in a significant increase of gammaH2AX foci in hepatoma cells, and the resveratrol and cisplatin combined treatment results in much more gammaH2AX foci formation than either resveratrol or cisplatin treatment alone.	gammah2ax	21-30	H2A.X variant histone	Homo sapiens	15-19
30132044-8	2018	In addition, CYP2E1 inhibitors and the antioxidant, N-acetylcysteine, also attenuated gamma-H2AX generation following exposure to 2,4-DMA.	Acetylcysteine	52-68	H2A.X variant histone	Homo sapiens	86-96
30132044-8	2018	In addition, CYP2E1 inhibitors and the antioxidant, N-acetylcysteine, also attenuated gamma-H2AX generation following exposure to 2,4-DMA.	2,4-xylidine	130-137	H2A.X variant histone	Homo sapiens	86-96
30132044-9	2018	Collectively, these results suggest that gamma-H2AX is formed following exposure to 2,4-DMA via reactive oxygen species produced by CYP2E1-mediated metabolism.	2,4-xylidine	84-91	H2A.X variant histone	Homo sapiens	41-51
30132044-9	2018	Collectively, these results suggest that gamma-H2AX is formed following exposure to 2,4-DMA via reactive oxygen species produced by CYP2E1-mediated metabolism.	Reactive Oxygen Species	96-119	H2A.X variant histone	Homo sapiens	41-51
30006243-2	2018	Involvement of DSBs in many pathologies has led to frequent measurements of these lesions, primarily via biodosimetry of S139-phosphorylated histone H2AX (gamma-H2AX).	dsbs	15-19	H2A.X variant histone	Homo sapiens	141-153
30132044-0	2018	2,4-Dimethylaniline generates phosphorylated histone H2AX in human urothelial and hepatic cells through reactive oxygen species produced by cytochrome P450 2E1.	2,4-xylidine	0-19	H2A.X variant histone	Homo sapiens	45-57
30132044-0	2018	2,4-Dimethylaniline generates phosphorylated histone H2AX in human urothelial and hepatic cells through reactive oxygen species produced by cytochrome P450 2E1.	Reactive Oxygen Species	104-127	H2A.X variant histone	Homo sapiens	45-57
30132044-5	2018	We examined genotoxic properties of 2,4-DMA using phosphorylated histone H2AX (gamma-H2AX), a sensitive and reliable marker of DNA damage, in cultured human urothelial and hepatic cells.	2,4-xylidine	36-43	H2A.X variant histone	Homo sapiens	73-77
30132044-5	2018	We examined genotoxic properties of 2,4-DMA using phosphorylated histone H2AX (gamma-H2AX), a sensitive and reliable marker of DNA damage, in cultured human urothelial and hepatic cells.	2,4-xylidine	36-43	H2A.X variant histone	Homo sapiens	79-89
30132044-6	2018	Our results clearly showed that 2,4-DMA at a concentration range of 1-10 mM generates gamma-H2AX in both cell lines, indicating that 2,4-DMA is genotoxic.	2,4-xylidine	32-39	H2A.X variant histone	Homo sapiens	86-96
30132044-6	2018	Our results clearly showed that 2,4-DMA at a concentration range of 1-10 mM generates gamma-H2AX in both cell lines, indicating that 2,4-DMA is genotoxic.	2,4-xylidine	133-140	H2A.X variant histone	Homo sapiens	86-96
30103844-7	2018	Phosphorylated H2AX (gammaH2AX) foci assay demonstrate that both resveratrol and cisplatin treatment result in a significant increase of gammaH2AX foci in hepatoma cells, and the resveratrol and cisplatin combined treatment results in much more gammaH2AX foci formation than either resveratrol or cisplatin treatment alone.	Resveratrol	65-76	H2A.X variant histone	Homo sapiens	15-19
30103844-7	2018	Phosphorylated H2AX (gammaH2AX) foci assay demonstrate that both resveratrol and cisplatin treatment result in a significant increase of gammaH2AX foci in hepatoma cells, and the resveratrol and cisplatin combined treatment results in much more gammaH2AX foci formation than either resveratrol or cisplatin treatment alone.	Cisplatin	81-90	H2A.X variant histone	Homo sapiens	15-19
29702145-5	2018	Moreover, analysis of the expression of phosphorylated histone H2AX (gamma-H2AX) indicated that the treatment with N-8-Iper produced a decreased cell survival by induction of DNA damage.	n-8-iper	115-123	H2A.X variant histone	Homo sapiens	55-67
29722447-0	2018	Trichloroethylene exposure results in the phosphorylation of histone H2AX in a human hepatic cell line through cytochrome P450 2E1-mediated oxidative stress.	Trichloroethylene	0-17	H2A.X variant histone	Homo sapiens	61-73
29722447-5	2018	In the present study, we examined the genotoxicity of TCE by assessing phosphorylated histone H2AX (gamma-H2AX), a new sensitive and reliable marker of DNA damage, in WRL-68 cells, cultured human hepatocytes and mouse livers.	Trichloroethylene	54-57	H2A.X variant histone	Homo sapiens	86-98
29993186-7	2018	The cellular data confirmed that TB-triggered DNA damage and induced apoptosis of U2OS cells by regulation of Mki67, PARP, caspase 3 and H2AX, and Western blot assay showed an activation of p53 signalling pathway.	Terbium	33-35	H2A.X variant histone	Homo sapiens	137-141
30109442-5	2018	Exposure to the nephrotoxicant cisplatin caused a dose-dependent disruption of the epithelial barrier, a decrease in viability, an increase in effluent LDH activity, and changes in expression of tight-junction marker zona-occludence 1, actin, and DNA-damage marker H2A.X, as detected by immunostaining.	Cisplatin	31-40	H2A.X variant histone	Homo sapiens	265-270
29802120-3	2018	The Eyes Absent (EYA) proteins dephosphorylate the terminal tyrosine residue of H2AX, thus permitting assembly of a productive DNA repair complex.	Tyrosine	60-68	H2A.X variant histone	Homo sapiens	80-84
30104472-7	2018	In vivo, the combination of oridonin and radiation effectively inhibited H460 xenograft tumor growth, with higher caspase-3 activation and H2A histone family member X (H2AX) phosphorylation compared with that of radiation alone.	oridonin	28-36	H2A.X variant histone	Homo sapiens	139-166
30104472-7	2018	In vivo, the combination of oridonin and radiation effectively inhibited H460 xenograft tumor growth, with higher caspase-3 activation and H2A histone family member X (H2AX) phosphorylation compared with that of radiation alone.	oridonin	28-36	H2A.X variant histone	Homo sapiens	168-172
29383524-1	2018	OBJECTIVES: To investigate DNA double-strand breaks (DSBs) in blood lymphocytes induced by two-day 99mTc-MIBI myocardial perfusion scintigraphy (MPS) using y-H2AX immunofluorescence microscopy and to correlate the results with 99mTc activity in blood samples.	dsbs	53-57	H2A.X variant histone	Homo sapiens	158-162
29970961-3	2018	Patients and methods: The levels of phosphorylated H2AX (gammaH2AX), a molecule that promotes DNA repair, were assessed in vastus lateralis biopsies from 10 COPD patients with low fat-free mass index (FFMI; COPDL), 10 with preserved FFMI and 10 age- and gender-matched healthy controls.	gammah2ax	57-66	H2A.X variant histone	Homo sapiens	51-55
29529298-4	2018	Chromatin immunoprecipitation following a single DSB shows that the reduced levels of gammaH2AX accumulation at DSBs in CHD1-KO cells are due to both a global reduction in H2AX incorporation and poor retention of H2AX at the DSBs.	gammah2ax	86-95	H2A.X variant histone	Homo sapiens	172-176
29620223-10	2018	RES also maintained serine 139 phosphorylation of histone H2AX, suggesting that RES prevents the repair of DSBs.	Serine	20-26	H2A.X variant histone	Homo sapiens	58-62
29785231-1	2018	gammaH2AX, the phosphorylated form of a histone variant H2AX at Ser 139, is already widely used as a biomarker to research the fundamental biology of DNA damage and repair and to assess the risk of environmental chemicals, pollutants, radiation, and so on.	Serine	64-67	H2A.X variant histone	Homo sapiens	5-9
29529298-4	2018	Chromatin immunoprecipitation following a single DSB shows that the reduced levels of gammaH2AX accumulation at DSBs in CHD1-KO cells are due to both a global reduction in H2AX incorporation and poor retention of H2AX at the DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	112-116	H2A.X variant histone	Homo sapiens	91-95
29529298-4	2018	Chromatin immunoprecipitation following a single DSB shows that the reduced levels of gammaH2AX accumulation at DSBs in CHD1-KO cells are due to both a global reduction in H2AX incorporation and poor retention of H2AX at the DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	225-229	H2A.X variant histone	Homo sapiens	91-95
28690315-5	2018	Silencing nucleolin and challenging DLBCL cells with doxorubicin enhanced the phosphorylation of H2AX (gammaH2AX-marker of DNA damage) and allowed DNA fragmentation.	Doxorubicin	53-64	H2A.X variant histone	Homo sapiens	97-101
29780501-3	2018	One key signal integrator is the histone variant H2A.X, which is phosphorylated at a C-terminal serine (S139ph), and ubiquitylated within its N-terminal tail at lysines 13 and 15 (K13/15ub).	Serine	96-102	H2A.X variant histone	Homo sapiens	49-54
29780501-3	2018	One key signal integrator is the histone variant H2A.X, which is phosphorylated at a C-terminal serine (S139ph), and ubiquitylated within its N-terminal tail at lysines 13 and 15 (K13/15ub).	Lysine	161-168	H2A.X variant histone	Homo sapiens	49-54
29780501-8	2018	Applied to H2A.X, expression of a central protein fragment, containing a protected N-terminal cysteine and a C-terminal thioester masked as a split intein, enables sequential C- and N-terminal protein modification and results in the convergent production of H2A.X carrying K15ub and S139ph.	Cysteine	94-102	H2A.X variant histone	Homo sapiens	11-16
29780501-8	2018	Applied to H2A.X, expression of a central protein fragment, containing a protected N-terminal cysteine and a C-terminal thioester masked as a split intein, enables sequential C- and N-terminal protein modification and results in the convergent production of H2A.X carrying K15ub and S139ph.	Cysteine	94-102	H2A.X variant histone	Homo sapiens	258-263
29228353-8	2018	The increase in cleaved caspase-3 and cleaved mammalian sterile-20-like-1 kinase levels induced by hydroxyurea was also P53-dependent; in contrast, the increase in phosphorylated H2AX, a marker of DNA double-strand breaks, in response to hydroxyurea treatment was only partially P53-dependent.	Hydroxyurea	99-110	H2A.X variant histone	Homo sapiens	179-183
29228353-8	2018	The increase in cleaved caspase-3 and cleaved mammalian sterile-20-like-1 kinase levels induced by hydroxyurea was also P53-dependent; in contrast, the increase in phosphorylated H2AX, a marker of DNA double-strand breaks, in response to hydroxyurea treatment was only partially P53-dependent.	Hydroxyurea	238-249	H2A.X variant histone	Homo sapiens	179-183
29437857-7	2018	Moreover, we show that H2afx and Mdc1 cooperate in promoting the activation of the recombination-dependent checkpoint, a mechanism that restrains the differentiation of cells with unrepaired DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	191-195	H2A.X variant histone	Homo sapiens	23-28
29117515-0	2018	Metformin and epothilone A treatment up regulate pro-apoptotic PARP-1, Casp-3 and H2AX genes and decrease of AKT kinase level to control cell death of human hepatocellular carcinoma and ovary adenocarcinoma cells.	Metformin	0-9	H2A.X variant histone	Homo sapiens	82-86
28676400-4	2017	The overexpression of B7-H3 increased oxaliplatin resistance reducing the formation of phosphorylated histone H2AX (gammaH2AX) loci.	Oxaliplatin	38-49	H2A.X variant histone	Homo sapiens	102-114
29117515-0	2018	Metformin and epothilone A treatment up regulate pro-apoptotic PARP-1, Casp-3 and H2AX genes and decrease of AKT kinase level to control cell death of human hepatocellular carcinoma and ovary adenocarcinoma cells.	epothilone A	14-26	H2A.X variant histone	Homo sapiens	82-86
29117515-6	2018	Compared to either drug alone, combination of epothilone A and metformin was more potent; decreased Akt level; and elevated percentage of apoptotic cells, induced cell cycle arrest at G1 phase and elevated the sub-G1 cell population by increasing the mRNA level of caspase-3, poly (ADP-ribose) polymerase-1 and H2AX.	epothilone A	46-58	H2A.X variant histone	Homo sapiens	311-315
29117515-6	2018	Compared to either drug alone, combination of epothilone A and metformin was more potent; decreased Akt level; and elevated percentage of apoptotic cells, induced cell cycle arrest at G1 phase and elevated the sub-G1 cell population by increasing the mRNA level of caspase-3, poly (ADP-ribose) polymerase-1 and H2AX.	Metformin	63-72	H2A.X variant histone	Homo sapiens	311-315
29115375-5	2018	Elevated levels of reactive oxygen species (ROS) and DNA double-strand breaks were identified in K562/G cells using flow cytometric and phosphorylated H2AX (gamma-H2AX) foci immunofluorescence assays, respectively, compared with the imatinib-sensitive K562 cells.	Reactive Oxygen Species	19-42	H2A.X variant histone	Homo sapiens	151-155
29115375-5	2018	Elevated levels of reactive oxygen species (ROS) and DNA double-strand breaks were identified in K562/G cells using flow cytometric and phosphorylated H2AX (gamma-H2AX) foci immunofluorescence assays, respectively, compared with the imatinib-sensitive K562 cells.	Reactive Oxygen Species	44-47	H2A.X variant histone	Homo sapiens	151-155
29115375-6	2018	The levels of intracellular ROS and gamma-H2AX were decreased by the ROS scavenger (N-acetylcysteine), and ROS levels were also markedly reduced by STAT5 inhibitor (SH-4-54).	Reactive Oxygen Species	69-72	H2A.X variant histone	Homo sapiens	36-46
29115375-6	2018	The levels of intracellular ROS and gamma-H2AX were decreased by the ROS scavenger (N-acetylcysteine), and ROS levels were also markedly reduced by STAT5 inhibitor (SH-4-54).	Acetylcysteine	84-100	H2A.X variant histone	Homo sapiens	36-46
29115375-6	2018	The levels of intracellular ROS and gamma-H2AX were decreased by the ROS scavenger (N-acetylcysteine), and ROS levels were also markedly reduced by STAT5 inhibitor (SH-4-54).	Reactive Oxygen Species	69-72	H2A.X variant histone	Homo sapiens	36-46
28838761-7	2017	Glutathione depletion with the glutathione synthetase inhibitor buthionine sulfoximine increased the cytotoxic effect of the photochemical treatment (PDT) most strongly in the SK-LMS-1 cells, and reduced PCIBLM-induced H2AX activation in the MES-SA cells, but not in the SK-LMS-1 cells.	Glutathione	0-11	H2A.X variant histone	Homo sapiens	219-223
28838761-7	2017	Glutathione depletion with the glutathione synthetase inhibitor buthionine sulfoximine increased the cytotoxic effect of the photochemical treatment (PDT) most strongly in the SK-LMS-1 cells, and reduced PCIBLM-induced H2AX activation in the MES-SA cells, but not in the SK-LMS-1 cells.	Buthionine Sulfoximine	64-86	H2A.X variant histone	Homo sapiens	219-223
29312595-5	2017	Depletion of PKM2 decreased the level of serine 139-phosphorylated H2AX (gamma-H2AX) in response to DNA damage.	Serine	41-47	H2A.X variant histone	Homo sapiens	67-71
29312595-5	2017	Depletion of PKM2 decreased the level of serine 139-phosphorylated H2AX (gamma-H2AX) in response to DNA damage.	Serine	41-47	H2A.X variant histone	Homo sapiens	73-83
29312595-6	2017	The in vitro kinase assay reveals that PKM2 directly phosphorylates H2AX at serine 139, which is abolished by the deletion of FBP-binding pocket of PKM2 (PKM2-Del515-520).	Serine	76-82	H2A.X variant histone	Homo sapiens	68-72
28936177-7	2017	Flow cytometry analysis shows that WFA-treated Ca9-22 oral cancer cells induced G2/M cell cycle arrest, ROS production, mitochondrial membrane depolarization, and phosphorylated histone H2A.X (gammaH2AX)-based DNA damage.	withaferin A	35-38	H2A.X variant histone	Homo sapiens	178-191
29969371-7	2018	Apoptotic ELISA and western blot analyses revealed that the combinations of cladribine and entinostat exerted a much more profound activity to induce apoptosis and DNA damage response, evidenced by enhanced phosphorylation of histone H2A.X and the DNA repair enzymes Chk1 and Chk2.	Cladribine	76-86	H2A.X variant histone	Homo sapiens	226-239
29969371-7	2018	Apoptotic ELISA and western blot analyses revealed that the combinations of cladribine and entinostat exerted a much more profound activity to induce apoptosis and DNA damage response, evidenced by enhanced phosphorylation of histone H2A.X and the DNA repair enzymes Chk1 and Chk2.	entinostat	91-101	H2A.X variant histone	Homo sapiens	226-239
29128613-5	2018	Notably, histone H2AX was activated following exposure to BPA, which is a sensitive marker of DNA damage.	bisphenol A	58-61	H2A.X variant histone	Homo sapiens	9-21
29340025-8	2017	Treatment with irinotecan significantly elevated the ATM pathway evident by an increase in the activation of H2AX and RAD50.	Irinotecan	15-25	H2A.X variant histone	Homo sapiens	109-113
29340025-9	2017	Combinational therapy reduced the activation of H2AX and RAD50 when compared to irinotecan alone in the combination sensitive CRC098.	Irinotecan	80-90	H2A.X variant histone	Homo sapiens	48-52
29187454-8	2017	Moreover, G2 phase arrest and apoptosis of cells co-treated with vincristine and XL019 resulted from the up-regulation of phosphorylated retinoblastoma protein (pRb), p21, and the DNA-damage protein, phosphorylated H2A histone family, member X (pH2AX).	Vincristine	65-76	H2A.X variant histone	Homo sapiens	215-243
28882572-6	2017	In addition to the top candidate p53, we identified several other interesting TFs that modulated gamma-H2AX after BaP and AFB1 treatment.	Benzo(a)pyrene	114-117	H2A.X variant histone	Homo sapiens	97-107
28882572-6	2017	In addition to the top candidate p53, we identified several other interesting TFs that modulated gamma-H2AX after BaP and AFB1 treatment.	Aflatoxin B1	122-126	H2A.X variant histone	Homo sapiens	97-107
28882572-11	2017	Finally, knock-down of ARNT reduced gamma-H2AX in response to BaP, which was associated with reduced CYP1A1 expression.	Benzo(a)pyrene	62-65	H2A.X variant histone	Homo sapiens	36-46
28567015-5	2017	USP22 enhances DNA damage repair and induce cisplatin resistance by promoting the phosphorylation of histone H2AX via deubiquitinating histone H2A.	Cisplatin	44-53	H2A.X variant histone	Homo sapiens	101-113
29221122-6	2017	The main characteristic of this effect was the sustained accumulation of teriflunomide-induced DNA damage as cells displayed increased phospho serine 139 H2AX (gammaH2AX) levels and concentration-dependent phosphorylation of Chk1 on serine 345 upon exposure to the combination as compared with either inhibitor alone.	teriflunomide	73-86	H2A.X variant histone	Homo sapiens	154-158
29221122-6	2017	The main characteristic of this effect was the sustained accumulation of teriflunomide-induced DNA damage as cells displayed increased phospho serine 139 H2AX (gammaH2AX) levels and concentration-dependent phosphorylation of Chk1 on serine 345 upon exposure to the combination as compared with either inhibitor alone.	Serine	143-149	H2A.X variant histone	Homo sapiens	154-158
28604675-8	2017	Co-staining of phospho-H2AX with phospho-Ku70 and TUNEL reveals that clusters rather than nano-foci represent single DSBs.	dsbs	117-121	H2A.X variant histone	Homo sapiens	23-27
28786938-9	2017	After 13 weeks in low folate, an increase in the phosphorylation of the histone H2AX was noted, indicative of an accumulation of DNA double strand breaks.	Folic Acid	22-28	H2A.X variant histone	Homo sapiens	72-84
28714549-1	2017	In a recent study, we showed that lymphocytes of obese Italian children/adolescents displayed levels of double strand breaks (DSB), assayed as serine 139-phosphorylated histone H2AX (gamma-H2AX), about eightfold higher than normal weight controls, and that 30% of this damage-generated micronuclei.	Serine	143-149	H2A.X variant histone	Homo sapiens	169-181
28461497-7	2017	Phosphorylated histone H2AX (gammaH2AX), a marker of DNA double-strand breaks, was increased in vitamin B12 depletion, and this effect was exacerbated by folate depletion.	Vitamin B 12	96-107	H2A.X variant histone	Homo sapiens	15-27
28340407-2	2017	After the initial breaks and chromatin destabilization, a set of post-translational modifications of histones occurs, including phosphorylation of serine 139 of histone H2AX (gammaH2AX), which leads to the formation of ionizing radiation-induced foci (IRIF).	Serine	147-153	H2A.X variant histone	Homo sapiens	161-173
28156042-5	2017	The compounds presented herein are potent metal-based cytostatics displaying LD50 values from 3.5-38 mum in different tumor cell lines and induce double-strand DNA breaks (DSB) as shown by H2AX phosphorylation (gammaH2AX) at foci of DSBs.	Metals	42-47	H2A.X variant histone	Homo sapiens	189-193
27633574-6	2017	The results illustrated that differences in the levels of phosphorylated H2AX, a double-strand break marker, exist after therapeutic proton and carbon ion irradiations.	Carbon	144-150	H2A.X variant histone	Homo sapiens	73-77
28395470-6	2017	Results: After treatment with TCE for 24 h in L-02 cells, the 36 TCE related histone methylation sites in 28 peptide segments were identified by MS. After treatment with TCE in concentrations of 0 and 8.0 mmol/L in L-02 cells for 24 h, the relative expression level of histone H3K79 me3 were 1.00+-0.06, 0.70+-0.09 (t=15.01, P=0.015); the relative expression level of histone H3K79 me2 were 1.00+-0.05, 0.74+-0.07 (t=16.69, P=0.018); the Olive Tail Moment about DNA damage were 1.46+-0.28, 3.12+- 0.68 (t=15.22, P=0.018); the relative expression levels of p53 were 1.00+-0.04, 1.24+-0.04 (t=18.71, P= 0.012); and the relative expression levels of  H2AX were 1.00 +- 0.03, 1.56 +- 0.11 (t=8.32, P=0 045).	Trichloroethylene	30-33	H2A.X variant histone	Homo sapiens	648-652
28369097-5	2017	In our study, we measured alcohol-mediated oxidative DNA damage in MCF-7 cells using 8-OHdG and p-H2AX foci formation assays.	Alcohols	26-33	H2A.X variant histone	Homo sapiens	98-102
28369097-8	2017	Alcohol treatment resulted in significant DNA damage in MCF-7 cells, as indicated by increased levels of 8-OHdG and p-H2AX foci number.	Alcohols	0-7	H2A.X variant histone	Homo sapiens	118-122
27655665-11	2017	Bendamustine-elicited H2AX phosphorylation was not dose-dependent, but markedly increased after fludarabine.	Bendamustine Hydrochloride	0-12	H2A.X variant histone	Homo sapiens	22-26
27655665-11	2017	Bendamustine-elicited H2AX phosphorylation was not dose-dependent, but markedly increased after fludarabine.	fludarabine	96-107	H2A.X variant histone	Homo sapiens	22-26
28300663-0	2017	1,2-Dichloropropane generates phosphorylated histone H2AX via cytochrome P450 2E1-mediated metabolism.	propylene dichloride	0-19	H2A.X variant histone	Homo sapiens	53-57
28300663-7	2017	During an in vitro mechanistic investigation, we found that gamma-H2AX generation by 1,2-DCP was clearly attenuated in the presence of disulfiram and 4-methylpyrazole, a specific cytochrome P450 2E1 (CYP2E1) inhibitor.	Disulfiram	135-145	H2A.X variant histone	Homo sapiens	60-70
28300663-7	2017	During an in vitro mechanistic investigation, we found that gamma-H2AX generation by 1,2-DCP was clearly attenuated in the presence of disulfiram and 4-methylpyrazole, a specific cytochrome P450 2E1 (CYP2E1) inhibitor.	Fomepizole	150-166	H2A.X variant histone	Homo sapiens	60-70
28300663-9	2017	These results suggested that ROS produced via the cytochrome P450 2E1 metabolic process of 1,2-DCP was a major causal factor for gamma-H2AX generation by treatment with 1,2-DCP.	Reactive Oxygen Species	29-32	H2A.X variant histone	Homo sapiens	129-139
28351323-2	2017	The histone variant H2AX undergoes phosphorylation at serine 139 due to double-strand breaks, and the gamma-H2AX is formatted as a result of genomic instability.	Serine	54-60	H2A.X variant histone	Homo sapiens	20-24
28187758-7	2017	Genotoxicity and mutagenicity were accessed via flow cytometry with anti-gama-H2AX and micronuclei assay, respectively.	gama	73-77	H2A.X variant histone	Homo sapiens	78-82
28185200-3	2017	It has been found that DSBs are always followed by phosphorylation of histone protein H2AX, a member of the H2A family, and immunocytochemical detection of phosphorylated H2AX (referred to as gamma-H2AX) is one of the frequently used techniques for assessing DNA damage.	dsbs	23-27	H2A.X variant histone	Homo sapiens	192-202
28572698-1	2017	Phosphorylation of H2A.X (serine 139) in the histone H2A family located in the downstream of the DNA damage kinase signaling cascade is an important indicator of DNA damage.	Serine	26-32	H2A.X variant histone	Homo sapiens	19-24
28572698-7	2017	Phosphorylation of H2A.X in PBMCs (percentages and mean fluorescence intensity) was significantly higher in the MetS-risk group than in the super healthy group after adjusting for age, sex, cigarette smoking, and alcohol consumption.	Alcohols	213-220	H2A.X variant histone	Homo sapiens	19-24
28572698-8	2017	Phosphorylated H2A.X was positively correlated with the number of MetS-RF as well as waist circumference, blood pressures, triglyceride, HbA1C, oxidized LDL, high sensitivity C-reactive protein, tumor necrosis factor-alpha, and alanine aminotransferase after the adjustment.	Triglycerides	123-135	H2A.X variant histone	Homo sapiens	15-20
28477120-1	2017	Activation of Ataxia Telangiectasia Mediated protein kinase (ATM) by its phosphorylation on serine 1981 and phosphorylation of histone H2AX on serine 139 (gammaH2AX) are the key events reporting DNA damage, primarily formation of DNA double strand breaks.	Serine	143-149	H2A.X variant histone	Homo sapiens	135-139
28477120-6	2017	Examples of ATM activation and H2AX phosphorylation in response to DNA damage in leukemic HL-60 cells by DNA topoisomerase I inhibitor topotecan, and in lung carcinoma A549 cells by hydrogen peroxide, are presented.	Topotecan	135-144	H2A.X variant histone	Homo sapiens	31-35
28477120-6	2017	Examples of ATM activation and H2AX phosphorylation in response to DNA damage in leukemic HL-60 cells by DNA topoisomerase I inhibitor topotecan, and in lung carcinoma A549 cells by hydrogen peroxide, are presented.	Hydrogen Peroxide	182-199	H2A.X variant histone	Homo sapiens	31-35
27503200-11	2017	A veliparib-induced increase in H2AX phosphorylation in CD34+ cells was observed in responders.	veliparib	2-11	H2A.X variant histone	Homo sapiens	32-36
28436335-3	2017	H2AX plays a part in the rapid, sensitive, cellular response to the ionizing radiation or DNA-damaging chemotherapeutic agents that cause DSBs.	dsbs	138-142	H2A.X variant histone	Homo sapiens	0-4
28710758-3	2017	Typically, DSBs are followed by phosphorylation of histone protein H2AX, a member of the H2A family.	dsbs	11-15	H2A.X variant histone	Homo sapiens	67-71
27720638-0	2016	Genetic modification of H2AX renders mesenchymal stromal cell-derived dopamine neurons more resistant to DNA damage and subsequent apoptosis.	Dopamine	70-78	H2A.X variant histone	Homo sapiens	24-28
28710765-2	2017	The sites of DSBs can be visualized as focal sites of gamma-H2AX using antibodies and immunofluorescence microscopy.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	13-17	H2A.X variant histone	Homo sapiens	60-64
27154731-4	2016	For this purpose, the amount of DNA damage occurred with irinotecan (CPT-11), etoposide (ETP), doxorubicin (Doxo), and H2O2 was determined by immunofluorescence through phosphorylation of H2AX(Ser139) and pATM(Ser1981) in the absence and presence of BA.	Hydrogen Peroxide	119-123	H2A.X variant histone	Homo sapiens	188-192
27154731-6	2016	Our results demonstrated that H2AX(Ser139) foci numbers were significantly decreased in the presence of BA while wound healing was accelerated by BA compared to that in the control and only drug-treated cells.	boric acid	104-106	H2A.X variant histone	Homo sapiens	30-34
27815899-2	2017	When cultured in the presence of such inhibitors as hydroxyurea, aphidicolin or excess of thymidine the cells that become arrested at the entrance to S-phase upon release from the block initiate progression through S then G2 and M. However, exposure to these inhibitors at concentrations commonly used to synchronize cells leads to activation of ATR and ATM protein kinases as well as phosphorylation of Ser139 of histone H2AX.	Hydroxyurea	52-63	H2A.X variant histone	Homo sapiens	422-426
27815899-2	2017	When cultured in the presence of such inhibitors as hydroxyurea, aphidicolin or excess of thymidine the cells that become arrested at the entrance to S-phase upon release from the block initiate progression through S then G2 and M. However, exposure to these inhibitors at concentrations commonly used to synchronize cells leads to activation of ATR and ATM protein kinases as well as phosphorylation of Ser139 of histone H2AX.	Aphidicolin	65-76	H2A.X variant histone	Homo sapiens	422-426
27815899-2	2017	When cultured in the presence of such inhibitors as hydroxyurea, aphidicolin or excess of thymidine the cells that become arrested at the entrance to S-phase upon release from the block initiate progression through S then G2 and M. However, exposure to these inhibitors at concentrations commonly used to synchronize cells leads to activation of ATR and ATM protein kinases as well as phosphorylation of Ser139 of histone H2AX.	Thymidine	90-99	H2A.X variant histone	Homo sapiens	422-426
27815899-6	2017	It also presents the protocol describing an assessment of phosphorylation of Ser139 on H2AX and activation of ATM in cells treated with aphidicolin, as a demonstrative of one of several DNA replication inhibitors that are being used for cell synchronization.	Aphidicolin	136-147	H2A.X variant histone	Homo sapiens	87-91
27941214-6	2016	Particularly, loading with BAPTA attenuated phosphorylation of the main DNA damage response members, including ATM, 53BP1 and H2A.X and reduced activation of the p53/p21/Rb pathway in H2O2-stimulated cells.	1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid	27-32	H2A.X variant histone	Homo sapiens	126-131
27720638-5	2016	We introduced a mutant form Y142F of H2AX into dopamine (DA) neuron-like cells differentiated from bone marrow-derived mesenchymal stromal cells (BMSCs).	Dopamine	47-55	H2A.X variant histone	Homo sapiens	37-41
27720638-5	2016	We introduced a mutant form Y142F of H2AX into dopamine (DA) neuron-like cells differentiated from bone marrow-derived mesenchymal stromal cells (BMSCs).	Dopamine	57-59	H2A.X variant histone	Homo sapiens	37-41
27720638-6	2016	RESULTS: Expression of H2AX(Y142F) renders DA neuron-like cells more resistant to DNA damage and subsequent cell death induced by ultraviolet irradiation and 1-methyl-4-phenylpyridinium (MPP+) treatment.	Dopamine	43-45	H2A.X variant histone	Homo sapiens	23-27
27720638-6	2016	RESULTS: Expression of H2AX(Y142F) renders DA neuron-like cells more resistant to DNA damage and subsequent cell death induced by ultraviolet irradiation and 1-methyl-4-phenylpyridinium (MPP+) treatment.	1-Methyl-4-phenylpyridinium	158-185	H2A.X variant histone	Homo sapiens	23-27
27720638-6	2016	RESULTS: Expression of H2AX(Y142F) renders DA neuron-like cells more resistant to DNA damage and subsequent cell death induced by ultraviolet irradiation and 1-methyl-4-phenylpyridinium (MPP+) treatment.	mangion-purified polysaccharide (Candida albicans)	187-191	H2A.X variant histone	Homo sapiens	23-27
27748797-6	2016	Furthermore, we detected that oxymatrine induced a significant increase in DNA damage and the expression of PARP and phosphorylated H2AX, and a significant decrease in that of nuclear APE1 and AP endonuclease activity in A549 cells.	oxymatrine	30-40	H2A.X variant histone	Homo sapiens	132-136
27773672-5	2016	Upon genotoxic stress in G2, high levels of H2A.X lead to persistent gammaH2A.X signaling, high levels of H2A.X phosphorylated on Tyr142, high levels of p53, and induction of apoptosis.	gammah2a	69-77	H2A.X variant histone	Homo sapiens	44-49
27813335-1	2016	Double-stranded DNA breaks induce serine phosphorylation of histone H2A.X, producing gamma-H2A.X foci that are then recognized by DNA damage response pathway proteins.	Serine	34-40	H2A.X variant histone	Homo sapiens	68-73
27813335-1	2016	Double-stranded DNA breaks induce serine phosphorylation of histone H2A.X, producing gamma-H2A.X foci that are then recognized by DNA damage response pathway proteins.	Serine	34-40	H2A.X variant histone	Homo sapiens	91-96
27907109-4	2016	When cells are exposed to a DNA-damaging agent Doxorubicin (Dox), double strand breaks (DSBs) are generated that result in the phosphorylation of histone H2A variant H2AX (gammaH2AX) within an hour.	Doxorubicin	47-58	H2A.X variant histone	Homo sapiens	166-170
27907109-4	2016	When cells are exposed to a DNA-damaging agent Doxorubicin (Dox), double strand breaks (DSBs) are generated that result in the phosphorylation of histone H2A variant H2AX (gammaH2AX) within an hour.	Doxorubicin	47-50	H2A.X variant histone	Homo sapiens	166-170
27710854-7	2016	Oxidative biomarkers (TBARS and protein carbonyl levels) and activity of antioxidant enzymes (CAT, SOD and GR) increased, and reduced glutathione (GSH) was depleted in animals treated with ABZ, indicating an oxidative stress condition, leading to a DNA damage causing phosphorylation of histone H2A variant, H2AX, and triggering apoptosis signaling, which was confirmed by increasing Bax/Bcl-xL rate, p53 and Bax expression.	Albendazole	189-192	H2A.X variant histone	Homo sapiens	308-312
27383448-0	2016	Coexposure to silver nanoparticles and ultraviolet A synergistically enhances the phosphorylation of histone H2AX.	Silver	14-20	H2A.X variant histone	Homo sapiens	109-113
27383448-9	2016	8-Hydroxy-2"-deoxyguanosine was formed in the cells treated with AgNPs, which was augmented by UVA irradiation, suggesting that intracellular oxidation caused oxidative DNA damage, leading to the enhanced formation of DSBs and gamma-H2AX.	8-ohdg	0-27	H2A.X variant histone	Homo sapiens	227-237
27383448-9	2016	8-Hydroxy-2"-deoxyguanosine was formed in the cells treated with AgNPs, which was augmented by UVA irradiation, suggesting that intracellular oxidation caused oxidative DNA damage, leading to the enhanced formation of DSBs and gamma-H2AX.	dsbs	218-222	H2A.X variant histone	Homo sapiens	227-237
27511066-2	2016	In this study we found that bile acid taurodeoxycholic acid (TDCA) significantly increased the tail moment (TM) and histone H2AX phosphorylation in FLO-1 EA cells, an increase which was significantly decreased by knockdown of TGR5.	Bile Acids and Salts	28-37	H2A.X variant histone	Homo sapiens	124-128
27342972-3	2016	We found that INPP4B-mediated resistance to genotoxic drug, cytarabine, was accompanied by lower p-H2AX accumulation in KG-1 cells, and INPP4B knockdown evidently sensitized KG-1 cells to cytarabine, meanwhile, p-H2AX expression was increased dramatically.	Cytarabine	60-70	H2A.X variant histone	Homo sapiens	99-103
27342972-3	2016	We found that INPP4B-mediated resistance to genotoxic drug, cytarabine, was accompanied by lower p-H2AX accumulation in KG-1 cells, and INPP4B knockdown evidently sensitized KG-1 cells to cytarabine, meanwhile, p-H2AX expression was increased dramatically.	Cytarabine	60-70	H2A.X variant histone	Homo sapiens	213-217
27342972-4	2016	Then, we observed that INPP4B knockdown inhibited the loss of p-H2AX expression after cytarabine removal in INPP4B-silenced KG-1 cells, whereas, in control KG-1 cells, the expression of p-H2AX was reduced in a time-dependent manner.	Cytarabine	86-96	H2A.X variant histone	Homo sapiens	64-68
27511066-2	2016	In this study we found that bile acid taurodeoxycholic acid (TDCA) significantly increased the tail moment (TM) and histone H2AX phosphorylation in FLO-1 EA cells, an increase which was significantly decreased by knockdown of TGR5.	Taurodeoxycholic Acid	38-59	H2A.X variant histone	Homo sapiens	124-128
27391338-0	2016	Low level phosphorylation of histone H2AX on serine 139 (gammaH2AX) is not associated with DNA double-strand breaks.	Serine	45-51	H2A.X variant histone	Homo sapiens	37-41
27511066-4	2016	In addition, NADPH oxidase inhibitor diphenylene iodonium significantly inhibited the TDCA-induced increase in TM and H2AX phosphorylation.	diphenyleneiodonium	37-57	H2A.X variant histone	Homo sapiens	118-122
27391338-1	2016	Phosphorylation of histone H2AX on serine 139 (gammaH2AX) is an early step in cellular response to a DNA double-strand break (DSB).	Serine	35-41	H2A.X variant histone	Homo sapiens	27-31
27389782-3	2016	We demonstrate here that Aurora B-mediated phosphorylation of histone H2AX at serine 121 (H2AX-pS121) promotes Aurora B autophosphorylation and is essential for proper chromosome segregation.	Serine	78-84	H2A.X variant histone	Homo sapiens	70-74
27468685-4	2016	Primary leukemia blasts isolated from APL patients showed high phosphorylation levels of H2AX (gamma-H2AX), an initial DSBs sensor.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	119-123	H2A.X variant histone	Homo sapiens	89-93
27468685-4	2016	Primary leukemia blasts isolated from APL patients showed high phosphorylation levels of H2AX (gamma-H2AX), an initial DSBs sensor.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	119-123	H2A.X variant histone	Homo sapiens	95-105
27389782-3	2016	We demonstrate here that Aurora B-mediated phosphorylation of histone H2AX at serine 121 (H2AX-pS121) promotes Aurora B autophosphorylation and is essential for proper chromosome segregation.	Serine	78-84	H2A.X variant histone	Homo sapiens	90-94
27174706-3	2016	Thus, we investigated DSBs repair efficiency in a group of obese adolescents assessing the kinetic of H2AX phosphorylation in mitomycin C (MMC)-treated lymphocytes harvested 2 h- or 4 h-post mutagen treatment.	Mitomycin	126-137	H2A.X variant histone	Homo sapiens	102-106
27174706-3	2016	Thus, we investigated DSBs repair efficiency in a group of obese adolescents assessing the kinetic of H2AX phosphorylation in mitomycin C (MMC)-treated lymphocytes harvested 2 h- or 4 h-post mutagen treatment.	Mitomycin	139-142	H2A.X variant histone	Homo sapiens	102-106
27177470-1	2016	The H3K9 protein lysine methyltransferase SUV39H2 was reported to methylate K134 of H2AX and stimulate H2AX phosphorylation during DNA damage response [Sone K et al.	K-134	76-80	H2A.X variant histone	Homo sapiens	84-88
27177470-3	2016	However, the sequence context of H2AX-K134 differs from the specificity of SUV39H2.	K-134	38-42	H2A.X variant histone	Homo sapiens	33-37
26976643-6	2016	We also show that the acetylation of histone H2AX at Lys5 by TIP60, but not the phosphorylation of H2AX, is required for the ADP-ribosylation activity of PARP-1 and its dynamic binding to damaged chromatin.	Adenosine Diphosphate	125-128	H2A.X variant histone	Homo sapiens	45-49
26928355-4	2016	We demonstrated that the inhibition of CPT-induced MDC1 foci formation by PG was caused by the direct suppression of histone H2AX phosphorylation at Ser139 (gammaH2AX), which is required for MDC1 foci formation, by quantifying gammaH2AX in cells and in vitro 9-AA also directly suppressed H2AX Ser139-phosphorylation in vitro but the concentration was much higher than that required to suppress CPT-induced MDC1 foci formation in cells.	Propyl Gallate	74-76	H2A.X variant histone	Homo sapiens	125-129
26928355-4	2016	We demonstrated that the inhibition of CPT-induced MDC1 foci formation by PG was caused by the direct suppression of histone H2AX phosphorylation at Ser139 (gammaH2AX), which is required for MDC1 foci formation, by quantifying gammaH2AX in cells and in vitro 9-AA also directly suppressed H2AX Ser139-phosphorylation in vitro but the concentration was much higher than that required to suppress CPT-induced MDC1 foci formation in cells.	Propyl Gallate	74-76	H2A.X variant histone	Homo sapiens	162-166
26928355-4	2016	We demonstrated that the inhibition of CPT-induced MDC1 foci formation by PG was caused by the direct suppression of histone H2AX phosphorylation at Ser139 (gammaH2AX), which is required for MDC1 foci formation, by quantifying gammaH2AX in cells and in vitro 9-AA also directly suppressed H2AX Ser139-phosphorylation in vitro but the concentration was much higher than that required to suppress CPT-induced MDC1 foci formation in cells.	gammah2ax	157-166	H2A.X variant histone	Homo sapiens	125-129
26928355-4	2016	We demonstrated that the inhibition of CPT-induced MDC1 foci formation by PG was caused by the direct suppression of histone H2AX phosphorylation at Ser139 (gammaH2AX), which is required for MDC1 foci formation, by quantifying gammaH2AX in cells and in vitro 9-AA also directly suppressed H2AX Ser139-phosphorylation in vitro but the concentration was much higher than that required to suppress CPT-induced MDC1 foci formation in cells.	Camptothecin	39-42	H2A.X variant histone	Homo sapiens	125-129
26928355-4	2016	We demonstrated that the inhibition of CPT-induced MDC1 foci formation by PG was caused by the direct suppression of histone H2AX phosphorylation at Ser139 (gammaH2AX), which is required for MDC1 foci formation, by quantifying gammaH2AX in cells and in vitro 9-AA also directly suppressed H2AX Ser139-phosphorylation in vitro but the concentration was much higher than that required to suppress CPT-induced MDC1 foci formation in cells.	Camptothecin	39-42	H2A.X variant histone	Homo sapiens	162-166
27006338-3	2016	We observe that persistent accumulation of ROS, due to a deficient JunD-/Nrf2-antioxidant response, reduces H2AX protein levels.	Reactive Oxygen Species	43-46	H2A.X variant histone	Homo sapiens	108-112
27006338-5	2016	ROS-mediated H2AX decrease plays a crucial role in chemosensitivity.	Reactive Oxygen Species	0-3	H2A.X variant histone	Homo sapiens	13-17
27006338-6	2016	Indeed, cycles of chemotherapy that sustainably increase ROS reduce H2AX protein levels in Triple-Negative breast cancer (TNBC) patients.	Reactive Oxygen Species	57-60	H2A.X variant histone	Homo sapiens	68-72
27006338-8	2016	Thus, our data describe a novel ROS-mediated regulation of H2AX turnover, which provides new insights into genetic instability and treatment efficacy in TNBC patients.	Reactive Oxygen Species	32-35	H2A.X variant histone	Homo sapiens	59-63
26986084-5	2016	Cantharidin treatment in the HCSCs for 48 h increased expression of histone H2AX, Myt1, cyclin A2, cyclin B1, p53 and cdc2 (Tyr15) phosphorylation significantly compared to the parental cells.	Cantharidin	0-11	H2A.X variant histone	Homo sapiens	68-80
26986476-8	2016	The results showed that knockdown of PTEN strongly antagonized ATM activation in response to etoposide treatment, and thereby reduced the phosphorylation level of ATM substrates, including H2AX, P53 and Chk2.	Etoposide	93-102	H2A.X variant histone	Homo sapiens	189-193
27077006-14	2016	However, it should be noticed that PARP inhibitor ABT-888 further enhanced the phosphorylation of H2AX (S139) after SM exposure, which indicated that we should be very careful in the application of PARP inhibitors in SM injury treatment because of the enhancement of DNA damage.	veliparib	50-57	H2A.X variant histone	Homo sapiens	98-102
27137793-16	2016	8-OHdG and gamma-H2AX increased more in oscillating glucose than in constant high glucose.	Glucose	52-59	H2A.X variant histone	Homo sapiens	11-21
27137793-16	2016	8-OHdG and gamma-H2AX increased more in oscillating glucose than in constant high glucose.	Glucose	82-89	H2A.X variant histone	Homo sapiens	11-21
27016423-9	2016	Ex vivo studies further showed cefradine inhibited SUV-induced the phosphorylation level of p38, JNKs and H2AX through inhibiting TOPK activity in a dose and time dependent manner, and cefradine inhibited the secretion of IL6 and TNF-alpha in HaCat and JB6 cells.	Cephradine	31-40	H2A.X variant histone	Homo sapiens	106-110
27077811-6	2016	We have found that a treatment with a low dose (75 nM) of MK-1775, a recently described specific chemical inhibitor of Wee1, decreases CDDP-induced H2AX phosphorylation in p53-negative cells and enhances the Wip1-sensitization of p53-negative tumors.	adavosertib	58-65	H2A.X variant histone	Homo sapiens	148-152
27077811-6	2016	We have found that a treatment with a low dose (75 nM) of MK-1775, a recently described specific chemical inhibitor of Wee1, decreases CDDP-induced H2AX phosphorylation in p53-negative cells and enhances the Wip1-sensitization of p53-negative tumors.	Cisplatin	135-139	H2A.X variant histone	Homo sapiens	148-152
27169377-4	2016	In the present study, we evaluated radiation-related changes in the frequency of phosphorylated (Ser-139) H2AX (gammaH2AX) foci formation in circulating CD34-positive/lineage marker-negative (CD34+Lin-) hematopoietic stem and progenitor cells (HSPCs) among 226Hiroshima A-bomb survivors.	Serine	97-100	H2A.X variant histone	Homo sapiens	106-110
27158526-4	2016	METHODS: DSBs were quantified in peripheral blood mononuclear cell subsets from patients with SLE, healthy controls, and patients with rheumatoid arthritis (RA) by measuring phosphorylated H2AX (phospho-H2AX) levels with flow cytometry.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	9-13	H2A.X variant histone	Homo sapiens	189-193
27158526-4	2016	METHODS: DSBs were quantified in peripheral blood mononuclear cell subsets from patients with SLE, healthy controls, and patients with rheumatoid arthritis (RA) by measuring phosphorylated H2AX (phospho-H2AX) levels with flow cytometry.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	9-13	H2A.X variant histone	Homo sapiens	203-207
26967561-3	2016	Here we show that miR-24, which has been demonstrated to target genes involved in the DNA repair process, targets p38, p53, PML and H2AX simultaneously.	mir-24	18-24	H2A.X variant histone	Homo sapiens	132-136
26972001-3	2016	Moreover, RBBP4 silencing enhanced TMZ-induced H2AX phosphorylation and apoptosis in GBM cells.	Temozolomide	35-38	H2A.X variant histone	Homo sapiens	47-51
26752212-8	2016	Analysis of cell cycle redistribution, apoptosis and expression of histone H2AX phosphorylation (lambda-H2AX) was used to evaluate the mechanism by which HCPT loaded micelles led to radiosensitization.	hydroxycamptothecinum	154-158	H2A.X variant histone	Homo sapiens	67-79
26752212-8	2016	Analysis of cell cycle redistribution, apoptosis and expression of histone H2AX phosphorylation (lambda-H2AX) was used to evaluate the mechanism by which HCPT loaded micelles led to radiosensitization.	hydroxycamptothecinum	154-158	H2A.X variant histone	Homo sapiens	75-79
26752212-9	2016	Taken together, the results showed that HCPT-loaded FA decorated micelles efficiently sensitized xenografts in mice to RT, and induced G2/M phase arrest, apoptosis and expression of lambda-H2AX.	hydroxycamptothecinum	40-44	H2A.X variant histone	Homo sapiens	189-193
26782830-8	2016	Phosphorylation of H2AX, a marker of DNA DSBs, was revealed to be upregulated in myricetin-treated cells.	myricetin	81-90	H2A.X variant histone	Homo sapiens	19-23
27001483-1	2016	2-Ethylphenyl 4-(3-ethylureido)benzenesulfonate (SFOM-0046) is a novel anticancer agent that arrests cell cycle in S-phase and causes DNA replication stress leading to the phosphorylation of H2AX into gamma-H2AX.	2-ethylphenyl 4-(3-ethylureido)benzenesulfonate	0-47	H2A.X variant histone	Homo sapiens	191-195
27001483-1	2016	2-Ethylphenyl 4-(3-ethylureido)benzenesulfonate (SFOM-0046) is a novel anticancer agent that arrests cell cycle in S-phase and causes DNA replication stress leading to the phosphorylation of H2AX into gamma-H2AX.	2-ethylphenyl 4-(3-ethylureido)benzenesulfonate	0-47	H2A.X variant histone	Homo sapiens	207-211
27001483-1	2016	2-Ethylphenyl 4-(3-ethylureido)benzenesulfonate (SFOM-0046) is a novel anticancer agent that arrests cell cycle in S-phase and causes DNA replication stress leading to the phosphorylation of H2AX into gamma-H2AX.	sfom-0046	49-58	H2A.X variant histone	Homo sapiens	191-195
27001483-1	2016	2-Ethylphenyl 4-(3-ethylureido)benzenesulfonate (SFOM-0046) is a novel anticancer agent that arrests cell cycle in S-phase and causes DNA replication stress leading to the phosphorylation of H2AX into gamma-H2AX.	sfom-0046	49-58	H2A.X variant histone	Homo sapiens	207-211
26893544-6	2016	Curcumin synergistically potentiated the cytotoxic effect of etoposide, and it intensified apoptosis and phosphorylation of the histone H2AX induced by this cytostatic drug in leukemic HL-60 cells.	Curcumin	0-8	H2A.X variant histone	Homo sapiens	136-140
26904506-4	2016	Interestingly, using phosphorylated H2AX as a DSB marker, our data in human fibroblasts revealed that after therapy-relevant spread-out Bragg peak irradiation with carbon ions DSBs are very efficiently rejoined, despite an increased RBE for cell survival.	Carbon	164-170	H2A.X variant histone	Homo sapiens	36-40
26667983-2	2016	H2AX is a histone protein directly associated with DNA that is phosphorylated to produce gammaH2AX that accumulates in foci in an early response to DNA double-strand breaks, the most deleterious lesion caused by anticancer therapy.	gammah2ax	89-98	H2A.X variant histone	Homo sapiens	0-4
26683224-3	2016	GL did not induce double strand DNA break but activated the ATR and ATM-mediated DNA damage response (DDR) inducing CHK1, H2AX phosphorylation (fH2AX) and CDC25C downregulation.	galiellalactone	0-2	H2A.X variant histone	Homo sapiens	122-126
26612134-6	2016	Co-administration of LY2603618 with gemcitabine showed a clear inhibition of CHK1 autophosphorylation for at least 24 h. Combining LY2603618 with gemcitabine resulted in an increase in H2AX serine 139 phosphorylation, indicating a corresponding increase in damaged DNA in the tumors.	LY2603618	21-30	H2A.X variant histone	Homo sapiens	185-189
26612134-6	2016	Co-administration of LY2603618 with gemcitabine showed a clear inhibition of CHK1 autophosphorylation for at least 24 h. Combining LY2603618 with gemcitabine resulted in an increase in H2AX serine 139 phosphorylation, indicating a corresponding increase in damaged DNA in the tumors.	gemcitabine	36-47	H2A.X variant histone	Homo sapiens	185-189
26612134-6	2016	Co-administration of LY2603618 with gemcitabine showed a clear inhibition of CHK1 autophosphorylation for at least 24 h. Combining LY2603618 with gemcitabine resulted in an increase in H2AX serine 139 phosphorylation, indicating a corresponding increase in damaged DNA in the tumors.	LY2603618	131-140	H2A.X variant histone	Homo sapiens	185-189
26612134-6	2016	Co-administration of LY2603618 with gemcitabine showed a clear inhibition of CHK1 autophosphorylation for at least 24 h. Combining LY2603618 with gemcitabine resulted in an increase in H2AX serine 139 phosphorylation, indicating a corresponding increase in damaged DNA in the tumors.	gemcitabine	146-157	H2A.X variant histone	Homo sapiens	185-189
26820970-1	2016	BACKGROUND: In response to DNA double-strand breaks, the histone protein H2AX becomes phosphorylated at its C-terminal serine 139 residue, referred to as gamma-H2AX.	Serine	119-125	H2A.X variant histone	Homo sapiens	73-77
26820970-1	2016	BACKGROUND: In response to DNA double-strand breaks, the histone protein H2AX becomes phosphorylated at its C-terminal serine 139 residue, referred to as gamma-H2AX.	Serine	119-125	H2A.X variant histone	Homo sapiens	160-164
27325258-3	2016	Here, we provide a protocol to perform immunostaining for phospho-H2AX on cells, cryosections and formalin-fixed, paraffin-embedded tissues.	Paraffin	114-122	H2A.X variant histone	Homo sapiens	66-70
26442630-3	2016	In this study, we have reported that curcumin induces significant DNA damage in human papillary thyroid carcinoma BCPAP cells in a dose-dependent manner as evidenced by the upregulated phosphorylation of H2A.X at Ser139, which was further confirmed by the long tails in the comet assay and the increase in the number of TUNEL-positive cells.	Curcumin	37-45	H2A.X variant histone	Homo sapiens	204-209
27076919-9	2016	Consistent with these cytotoxic profiles, cisplatin/mitomycin C, triapine, and paclitaxel differed in the capacity to induce phosphorylation of H2AX, and produced unique inhibitory patterns of DNA/RNA syntheses in HL-60 human leukemia cells.	Cisplatin	42-51	H2A.X variant histone	Homo sapiens	144-148
26819332-2	2016	One of the earliest molecular responses following DSB formation is the phosphorylation of the histone H2AX, giving rise to gammaH2AX.	gammah2ax	123-132	H2A.X variant histone	Homo sapiens	102-106
26442630-8	2016	In addition, the ATM-specific inhibitor KU-55933 reversed curcumin-induced phosphorylation of H2A.X.	2-morpholin-4-yl-6-thianthren-1-yl-pyran-4-one	40-48	H2A.X variant histone	Homo sapiens	94-99
26442630-8	2016	In addition, the ATM-specific inhibitor KU-55933 reversed curcumin-induced phosphorylation of H2A.X.	Curcumin	58-66	H2A.X variant histone	Homo sapiens	94-99
27076919-9	2016	Consistent with these cytotoxic profiles, cisplatin/mitomycin C, triapine, and paclitaxel differed in the capacity to induce phosphorylation of H2AX, and produced unique inhibitory patterns of DNA/RNA syntheses in HL-60 human leukemia cells.	Mitomycin	52-63	H2A.X variant histone	Homo sapiens	144-148
27076919-9	2016	Consistent with these cytotoxic profiles, cisplatin/mitomycin C, triapine, and paclitaxel differed in the capacity to induce phosphorylation of H2AX, and produced unique inhibitory patterns of DNA/RNA syntheses in HL-60 human leukemia cells.	3-aminopyridine-2-carboxaldehyde thiosemicarbazone	65-73	H2A.X variant histone	Homo sapiens	144-148
27076919-9	2016	Consistent with these cytotoxic profiles, cisplatin/mitomycin C, triapine, and paclitaxel differed in the capacity to induce phosphorylation of H2AX, and produced unique inhibitory patterns of DNA/RNA syntheses in HL-60 human leukemia cells.	Paclitaxel	79-89	H2A.X variant histone	Homo sapiens	144-148
26645158-7	2015	The mechanisms underlying MK-1775 radiosensitization were studied by observing H2AX phosphorylation and mitotic catastrophe.	adavosertib	26-33	H2A.X variant histone	Homo sapiens	79-83
26884865-0	2015	Anacardic acid sensitizes prostate cancer cells to radiation therapy by regulating H2AX expression.	anacardic acid	0-14	H2A.X variant histone	Homo sapiens	83-87
26711340-2	2015	Here we show that H2AX is rapidly stabilized in response to DSBs to efficiently generate gammaH2AX foci.	dsbs	60-64	H2A.X variant histone	Homo sapiens	18-22
26711340-5	2015	Synthesized H2AX ordinarily underwent degradation through poly-ubiquitination mediated by the E3 ligase HUWE1; however, H2AX ubiquitination was transiently halted upon DSB formation.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	168-171	H2A.X variant histone	Homo sapiens	12-16
26711340-5	2015	Synthesized H2AX ordinarily underwent degradation through poly-ubiquitination mediated by the E3 ligase HUWE1; however, H2AX ubiquitination was transiently halted upon DSB formation.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	168-171	H2A.X variant histone	Homo sapiens	120-124
26711340-6	2015	Such rapid H2AX stabilization by DSBs was associated with chromatin incorporation of H2AX and halting of its poly-ubiquitination mediated by the ATM kinase, the sirtuin protein SIRT6, and the chromatin remodeler SNF2H.	dsbs	33-37	H2A.X variant histone	Homo sapiens	11-15
26711340-6	2015	Such rapid H2AX stabilization by DSBs was associated with chromatin incorporation of H2AX and halting of its poly-ubiquitination mediated by the ATM kinase, the sirtuin protein SIRT6, and the chromatin remodeler SNF2H.	dsbs	33-37	H2A.X variant histone	Homo sapiens	85-89
26416514-5	2015	We found that treatment of 1 mM cyclo(phenylalanine-proline) induces phosphorylation of H2AX (S139) through ATM-CHK2 activation as well as DNA double strand breaks.	emodepside	32-37	H2A.X variant histone	Homo sapiens	88-92
26416514-5	2015	We found that treatment of 1 mM cyclo(phenylalanine-proline) induces phosphorylation of H2AX (S139) through ATM-CHK2 activation as well as DNA double strand breaks.	phenylalanine-proline	38-59	H2A.X variant histone	Homo sapiens	88-92
25940934-0	2015	The Histone Deacetylase Inhibitor Valproic Acid Sensitizes Gemcitabine-Induced Cytotoxicity in Gemcitabine-Resistant Pancreatic Cancer Cells Possibly Through Inhibition of the DNA Repair Protein Gamma-H2AX.	Valproic Acid	34-47	H2A.X variant histone	Homo sapiens	201-205
26645158-13	2015	MK-1775 also significantly increased H2AX phosphorylation and mitotic catastrophe in irradiated cells.	adavosertib	0-7	H2A.X variant histone	Homo sapiens	37-41
25940934-0	2015	The Histone Deacetylase Inhibitor Valproic Acid Sensitizes Gemcitabine-Induced Cytotoxicity in Gemcitabine-Resistant Pancreatic Cancer Cells Possibly Through Inhibition of the DNA Repair Protein Gamma-H2AX.	gemcitabine	59-70	H2A.X variant histone	Homo sapiens	201-205
25940934-5	2015	Moreover, GEM induces activation of the DNA repair protein H2AX proportional to the dosage.	gemcitabine	10-13	H2A.X variant histone	Homo sapiens	59-63
25964244-3	2015	We conducted a phase I study of single-agent AZD1775 in adult patients with refractory solid tumors to determine its maximum-tolerated dose (MTD), pharmacokinetics, and modulation of phosphorylated Tyr15-Cdk (pY15-Cdk) and phosphorylated histone H2AX (gammaH2AX) levels in paired tumor biopsies.	adavosertib	45-52	H2A.X variant histone	Homo sapiens	238-250
26520369-5	2015	We demonstrated that APE1 knockdown associated with TMZ treatment efficiently reduced cell proliferation and clonogenic survival of resistant cells (T98G), which appears to be a consequence of increased DNA damage, S-phase arrest, and H2AX phosphorylation, resulting in apoptosis induction.	Temozolomide	52-55	H2A.X variant histone	Homo sapiens	235-239
26509888-4	2015	We show that asynapsed chromosomes trigger oocyte elimination at diplonema, which is linked to the presence of phosphorylated H2AFX (gammaH2AFX).	gammah2afx	133-143	H2A.X variant histone	Homo sapiens	126-131
26615020-7	2016	In comparing DNA damage signaling after dosing with veliparib/TMZ or TMZ alone, increased phosphorylation of damage-responsive proteins (KAP1, Chk1, Chk2, and H2AX) was observed only in MGMT promoter-hypermethylated lines.	veliparib	52-61	H2A.X variant histone	Homo sapiens	159-163
26615020-7	2016	In comparing DNA damage signaling after dosing with veliparib/TMZ or TMZ alone, increased phosphorylation of damage-responsive proteins (KAP1, Chk1, Chk2, and H2AX) was observed only in MGMT promoter-hypermethylated lines.	Temozolomide	62-65	H2A.X variant histone	Homo sapiens	159-163
26615020-7	2016	In comparing DNA damage signaling after dosing with veliparib/TMZ or TMZ alone, increased phosphorylation of damage-responsive proteins (KAP1, Chk1, Chk2, and H2AX) was observed only in MGMT promoter-hypermethylated lines.	Temozolomide	69-72	H2A.X variant histone	Homo sapiens	159-163
26553138-8	2015	The addition of NU7026 significantly increased H2AX phosphorylation after C ion and x-ray irradiations in H1299 cells, but not B02.	2-(morpholin-4-yl)benzo(h)chromen-4-one	16-22	H2A.X variant histone	Homo sapiens	47-51
26194899-4	2015	In further experiments, p53 protein expression was increased, and H2AX phosphorylation and p21 protein expression were induced after treatment with 3EZ, 20Ac-ingenol.	3EZ	148-151	H2A.X variant histone	Homo sapiens	66-70
26334102-6	2015	In addition to increased phosphorylation of H2AX at serine 139 (gammaH2AX), AZD1775 led to increased phosphorylation of H2AX at tyrosine 142, a signaling event associated with promotion of apoptosis over DNA repair.	Serine	52-58	H2A.X variant histone	Homo sapiens	44-48
26194899-4	2015	In further experiments, p53 protein expression was increased, and H2AX phosphorylation and p21 protein expression were induced after treatment with 3EZ, 20Ac-ingenol.	20ac-ingenol	153-165	H2A.X variant histone	Homo sapiens	66-70
26013168-7	2015	Gemcitabine induced phosphorylation of H2AX (gamma-H2AX) and ataxia-telangiectasia mutated kinase (pATM), specific markers for DNA double-strand breaks.	gemcitabine	0-11	H2A.X variant histone	Homo sapiens	39-43
26141948-9	2015	Changes in the ratio of RPA2 to phosphorylated H2AX following LY2606368 treatment further support replication catastrophe as the mechanism of DNA damage.	prexasertib	62-71	H2A.X variant histone	Homo sapiens	47-51
26013168-7	2015	Gemcitabine induced phosphorylation of H2AX (gamma-H2AX) and ataxia-telangiectasia mutated kinase (pATM), specific markers for DNA double-strand breaks.	gemcitabine	0-11	H2A.X variant histone	Homo sapiens	45-55
26013168-8	2015	Both gemcitabine-induced phosphorylation of H2AX and ATM were reduced by PTK6 knockdown and increased by PTK6 overexpression.	gemcitabine	5-16	H2A.X variant histone	Homo sapiens	44-48
26183311-7	2015	In vitro the triple medication efavirenz, tenofovir and emtricitabine leads to a reduced survival fraction and an increased activation of the DNA repair proteins H2AX, Nbs, Atm and 53BP1 in combination with ionizing radiation.	efavirenz	31-40	H2A.X variant histone	Homo sapiens	162-166
26183311-7	2015	In vitro the triple medication efavirenz, tenofovir and emtricitabine leads to a reduced survival fraction and an increased activation of the DNA repair proteins H2AX, Nbs, Atm and 53BP1 in combination with ionizing radiation.	Tenofovir	42-51	H2A.X variant histone	Homo sapiens	162-166
26183311-7	2015	In vitro the triple medication efavirenz, tenofovir and emtricitabine leads to a reduced survival fraction and an increased activation of the DNA repair proteins H2AX, Nbs, Atm and 53BP1 in combination with ionizing radiation.	Emtricitabine	56-69	H2A.X variant histone	Homo sapiens	162-166
26119999-0	2015	Non-canonical Bromodomain within DNA-PKcs Promotes DNA Damage Response and Radioresistance through Recognizing an IR-Induced Acetyl-Lysine on H2AX.	N(alpha)-acetyllysine	125-138	H2A.X variant histone	Homo sapiens	142-146
25895498-11	2015	YM155 activates the DNA damage pathway leading to phosphorylation of Chk2 and H2AX.	YM 155	0-5	H2A.X variant histone	Homo sapiens	78-82
26119999-2	2015	Here, we discover a bromodomain (BRD)-like module in DNA-PKcs (DNA-PKcs-BRD) that specifically recognizes H2AX acetyl-lysine 5 (K5ac) for sequential induction of gammaH2AX and concurrent cell fate decision(s).	k5ac	128-132	H2A.X variant histone	Homo sapiens	106-110
26119999-2	2015	Here, we discover a bromodomain (BRD)-like module in DNA-PKcs (DNA-PKcs-BRD) that specifically recognizes H2AX acetyl-lysine 5 (K5ac) for sequential induction of gammaH2AX and concurrent cell fate decision(s).	gammah2ax	162-171	H2A.X variant histone	Homo sapiens	106-110
26119999-3	2015	First, top-down mass spectrometry of radiation-phenotypic, full-length H2AX revealed a radiation-inducible, K5ac-dependent induction of gammaH2AX.	k5ac	108-112	H2A.X variant histone	Homo sapiens	71-75
26119999-3	2015	First, top-down mass spectrometry of radiation-phenotypic, full-length H2AX revealed a radiation-inducible, K5ac-dependent induction of gammaH2AX.	gammah2ax	136-145	H2A.X variant histone	Homo sapiens	71-75
25818601-6	2015	The observed phosphorylated histone H2AX (gamma-H2AX) foci and the elevation of 8-hydroxy-2"-deoxyguanosine (8-OHdG) indicated that DDR was stimulated by PCB29-pQ treatment.	ddr	132-135	H2A.X variant histone	Homo sapiens	36-40
25818601-6	2015	The observed phosphorylated histone H2AX (gamma-H2AX) foci and the elevation of 8-hydroxy-2"-deoxyguanosine (8-OHdG) indicated that DDR was stimulated by PCB29-pQ treatment.	ddr	132-135	H2A.X variant histone	Homo sapiens	42-52
25818601-6	2015	The observed phosphorylated histone H2AX (gamma-H2AX) foci and the elevation of 8-hydroxy-2"-deoxyguanosine (8-OHdG) indicated that DDR was stimulated by PCB29-pQ treatment.	2,3,5-trichloro-6-phenyl-(1,4)benzoquinone	154-162	H2A.X variant histone	Homo sapiens	42-52
25697484-4	2015	Both alkaloids increased the protein level of S139-phosphorylated H2AX (gammaH2AX), which however was independent of the induction of DNA damage.	Alkaloids	5-14	H2A.X variant histone	Homo sapiens	66-70
25935680-5	2015	The estimated number of molecules of gammaH2AX (ATQA(pS)QEY) per vehicle-treated HeLa S3 cell was 9.4 x 10(4) and increased to 6.2 x 10(5) molecules/cell after exposure to the DNA-damaging agent camptothecin (10 muM) for 1 h. The estimated total amount of H2AX (ATQA(pS)QEY + ATQASQEY) was 3.3-3.6 x 10(6) molecules/cell.	Camptothecin	195-207	H2A.X variant histone	Homo sapiens	42-46
26124332-7	2015	Curcumin also increased phosphorylation of p53 and Histone H2A.X (S140) in the nuclei of NCI-H460 cells.	Curcumin	0-8	H2A.X variant histone	Homo sapiens	51-64
26114388-5	2015	Atrazine treatment increased H2AX phosphorylation (gammaH2AX) and the formation of gammaH2AX foci in the nuclei of MCF-10A cells.	Atrazine	0-8	H2A.X variant histone	Homo sapiens	29-33
25699650-8	2015	Moreover, we were able to show that miR-138 potently inhibits H2AX expression, which suggests that H2AX may serve as a downstream executor for miR-138.	mir-138	36-43	H2A.X variant histone	Homo sapiens	62-66
25875766-4	2015	Treatment of HuH7 cells with etoposide (25 muM, 30 min) or gamma irradiation (4 Gy) increased the phosphorylation of H2AX by 1.94 +- 0.13 and 2.0 +- 0.02 fold, respectively.	Etoposide	29-38	H2A.X variant histone	Homo sapiens	117-121
25699650-4	2015	Also, there is a recent report showing the role of miR-138 in mediating DNA damage response by targeting H2AX.	mir-138	51-58	H2A.X variant histone	Homo sapiens	105-109
25699650-8	2015	Moreover, we were able to show that miR-138 potently inhibits H2AX expression, which suggests that H2AX may serve as a downstream executor for miR-138.	mir-138	36-43	H2A.X variant histone	Homo sapiens	99-103
25699650-5	2015	In light of these data, we sought to characterize the role of miR-138 for SCLC cell growth and cell-cycle progression by regulating H2AX expression.	mir-138	62-69	H2A.X variant histone	Homo sapiens	132-136
25699650-8	2015	Moreover, we were able to show that miR-138 potently inhibits H2AX expression, which suggests that H2AX may serve as a downstream executor for miR-138.	mir-138	143-150	H2A.X variant histone	Homo sapiens	62-66
25699650-8	2015	Moreover, we were able to show that miR-138 potently inhibits H2AX expression, which suggests that H2AX may serve as a downstream executor for miR-138.	mir-138	143-150	H2A.X variant histone	Homo sapiens	99-103
25699650-10	2015	We also showed that H2AX overexpression largely abolished miR-138-mediated SCLC cancer cell growth and cell-cycle progression inhibition, which strongly suggests, at least in vitro, that miR-138 potently regulates SCLC development by targeting H2AX.	mir-138	58-65	H2A.X variant histone	Homo sapiens	20-24
25699650-10	2015	We also showed that H2AX overexpression largely abolished miR-138-mediated SCLC cancer cell growth and cell-cycle progression inhibition, which strongly suggests, at least in vitro, that miR-138 potently regulates SCLC development by targeting H2AX.	mir-138	58-65	H2A.X variant histone	Homo sapiens	244-248
25699650-10	2015	We also showed that H2AX overexpression largely abolished miR-138-mediated SCLC cancer cell growth and cell-cycle progression inhibition, which strongly suggests, at least in vitro, that miR-138 potently regulates SCLC development by targeting H2AX.	mir-138	187-194	H2A.X variant histone	Homo sapiens	20-24
25699650-10	2015	We also showed that H2AX overexpression largely abolished miR-138-mediated SCLC cancer cell growth and cell-cycle progression inhibition, which strongly suggests, at least in vitro, that miR-138 potently regulates SCLC development by targeting H2AX.	mir-138	187-194	H2A.X variant histone	Homo sapiens	244-248
25722453-11	2015	CONCLUSION: gamma-H2AX can be exploited in the LuTate PRRT as a biomarker of PBL cytotoxicity.	177Lu-DOTA-octreotate	47-53	H2A.X variant histone	Homo sapiens	12-22
25581256-7	2015	We report, for the first time, that VPA activates a previously unrecognized calpain-dependent necroptosis cascade that initiates with JNK1 activation and involves AIF cleavage/nuclear translocation and H2AX phosphorylation as well as an altered Smac/DIABLO to XIAP balance.	Valproic Acid	36-39	H2A.X variant histone	Homo sapiens	202-206
25515035-8	2015	Pretreatment with Gps (1, 10 and 100 microg/ml) effectively attenuated cholesterol-induced DNA damage in HUVECs by inhibiting phosphorylation of H2AX, a member of the histone family.	Cholesterol	71-82	H2A.X variant histone	Homo sapiens	145-149
25619392-9	2015	Overexpression of H2AX in K562 cells markedly increased resveratrol-induced apoptosis, whereas overexpression of H2AX-139m (Ser139 was mutated to block phosphorylation) inhibited resveratrol-induced apoptosis.	Resveratrol	56-67	H2A.X variant histone	Homo sapiens	18-22
25733871-2	2015	BRIT1 (breast cancer susceptibility gene C terminus-repeat inhibitor of human telomerase repeat transcriptase expression), a tumor suppressor and early DDR factor, is recruited to DNA double-strand breaks (DSBs) by phosphorylated H2A histone family, member X (gamma-H2AX), where it promotes chromatin relaxation by recruiting the switch/sucrose nonfermentable (SWI-SNF) chromatin remodeler to facilitate DDR.	Sucrose	337-344	H2A.X variant histone	Homo sapiens	230-258
25712102-1	2015	In the last decade, many papers highlighted that the histone variant H2AX and its phosphorylation on Ser 139 (gammaH2AX) cannot be simply considered a specific DNA double-strand-break (DSB) marker with a role restricted to the DNA damage response, but rather as a "protagonist" in different scenarios.	Serine	101-104	H2A.X variant histone	Homo sapiens	69-73
25619392-0	2015	Resveratrol induces apoptosis of human chronic myelogenous leukemia cells in vitro through p38 and JNK-regulated H2AX phosphorylation.	Resveratrol	0-11	H2A.X variant histone	Homo sapiens	113-117
25619392-9	2015	Overexpression of H2AX in K562 cells markedly increased resveratrol-induced apoptosis, whereas overexpression of H2AX-139m (Ser139 was mutated to block phosphorylation) inhibited resveratrol-induced apoptosis.	Resveratrol	179-190	H2A.X variant histone	Homo sapiens	113-117
25619392-2	2015	The aim of this study was to examine whether H2AX phosphorylation was required for resveratrol-induced apoptosis of human chronic myelogenous leukemia (CML) cells in vitro.	Resveratrol	83-94	H2A.X variant histone	Homo sapiens	45-49
25619392-10	2015	K562 cells transfected with H2AX-specific siRNAs were resistant to resveratrol-induced apoptosis.	Resveratrol	67-78	H2A.X variant histone	Homo sapiens	28-32
25619392-6	2015	RESULTS: Treatment of K562 cells with resveratrol (20-100 mumol/L) induced apoptosis and phosphorylation of H2AX at Ser139 in time- and dose-dependent manners, but reduced phosphorylation of histone H3 at Ser10.	Resveratrol	38-49	H2A.X variant histone	Homo sapiens	108-112
25619392-8	2015	Pretreatment with the p38 inhibitor SB202190 or the JNK inhibitor SP600125 dose-dependently reduced resveratrol-induced phosphorylation of H2AX, which were also observed when the cells were transfected with p38- or JNK-specific siRNAs.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	36-44	H2A.X variant histone	Homo sapiens	139-143
25619392-11	2015	CONCLUSION: H2AX phosphorylation at Ser139 in human CML cells, which is regulated by p38 and JNK, is essential for resveratrol-induced apoptosis.	Resveratrol	115-126	H2A.X variant histone	Homo sapiens	12-16
25705129-4	2015	Oxidative stress-induced DNA damage resulted in increased H2AX((S139)) phosphorylation (a hallmark of DNA damage), along with the degradation of the androgen receptor (AR), p53 and NKX3.1, upon treatment with conditioned medium (CM) obtained from activated macrophages or H2O2.	Hydrogen Peroxide	272-276	H2A.X variant histone	Homo sapiens	58-62
25619392-8	2015	Pretreatment with the p38 inhibitor SB202190 or the JNK inhibitor SP600125 dose-dependently reduced resveratrol-induced phosphorylation of H2AX, which were also observed when the cells were transfected with p38- or JNK-specific siRNAs.	pyrazolanthrone	66-74	H2A.X variant histone	Homo sapiens	139-143
25619392-8	2015	Pretreatment with the p38 inhibitor SB202190 or the JNK inhibitor SP600125 dose-dependently reduced resveratrol-induced phosphorylation of H2AX, which were also observed when the cells were transfected with p38- or JNK-specific siRNAs.	Resveratrol	100-111	H2A.X variant histone	Homo sapiens	139-143
25480829-2	2015	The phosphorylation of histone H2AX at Ser 139, termed gamma-H2AX, was originally identified as an early event after the direct formation of DNA double-strand breaks (DSBs) by ionizing radiation.	Serine	39-42	H2A.X variant histone	Homo sapiens	23-35
25595187-8	2015	Cyclopamine increased Shh plus IR-induced H2AX, a marker of DNA double-strand breaks, in these cells.	cyclopamine	0-11	H2A.X variant histone	Homo sapiens	42-46
25609707-5	2015	Furthermore, RUNX2, INTS3 and BAZ1B form UV-responsive complexes with the serine-139-phosphorylated isoform of H2AX (gammaH2AX).	Serine	74-80	H2A.X variant histone	Homo sapiens	111-115
25459351-5	2015	RESULTS: Hydroxyurea, UV and 4NQO induced Chk1 and H2AX phosphorylation in MCF7 and K562 cells.	Hydroxyurea	9-20	H2A.X variant histone	Homo sapiens	51-55
25459351-5	2015	RESULTS: Hydroxyurea, UV and 4NQO induced Chk1 and H2AX phosphorylation in MCF7 and K562 cells.	4-Nitroquinoline-1-oxide	29-33	H2A.X variant histone	Homo sapiens	51-55
26697837-4	2015	Moreover, Erk5-depleted leukemic Jurkat cells presented a marked sensitivity to thymidine-induced S phase stalling, as evidenced by increased H2AX phosphorylation and apoptosis.	Thymidine	80-89	H2A.X variant histone	Homo sapiens	142-146
25450480-4	2015	Jaridonin also resulted in enhanced phosphorylation of Cdc25C via the activation of checkpoint kinases Chk1 and Chk2, as well as in increased phospho-H2A.X (Ser139), which is known to be phosphorylated by ATM in response to DNA damage.	jaridonin	0-9	H2A.X variant histone	Homo sapiens	150-155
25458954-5	2015	We demonstrate that MK-1775 treatment results in increased H2AX phosphorylation, indicating increased DNA double-strand breaks, and activation of CHK1, which are both dependent on CDK activity.	adavosertib	20-27	H2A.X variant histone	Homo sapiens	59-63
25726170-6	2015	Results show that the clastogen etoposide produced a dose related increase in gammaH2AX and mono-ubiquitinated H2AX and a dose related decrease in p-H3 positive mitotic cells.	clastogen etoposide	22-41	H2A.X variant histone	Homo sapiens	83-87
26189260-2	2015	OBJECTIVE: This study aimed to determine whether phosphorylation of histone H2AX (gammaH2AX) is a predictive marker for neoadjuvant chemotherapy patients of cervical cancer.	gammah2ax	82-91	H2A.X variant histone	Homo sapiens	68-80
25262359-12	2015	Curcumin induced DNA double strand breaks, which were indicated by phosphorylated H2AX.	Curcumin	0-8	H2A.X variant histone	Homo sapiens	82-86
25351918-7	2015	Consistent with this biologic response, DP68 induces a strong DNA damage response, including phosphorylation of ATM, Chk1 and Chk2 kinases, KAP1, and histone variant H2AX.	dp68	40-44	H2A.X variant histone	Homo sapiens	166-170
25793019-11	2015	Naphthoquinones, combined with ascorbate, caused phosphorylation of H2AX and inhibited pAkt.	Naphthoquinones	0-15	H2A.X variant histone	Homo sapiens	68-72
25793019-11	2015	Naphthoquinones, combined with ascorbate, caused phosphorylation of H2AX and inhibited pAkt.	Ascorbic Acid	31-40	H2A.X variant histone	Homo sapiens	68-72
25365214-2	2014	Recently, we found that TPX2 regulates the levels of serine 139-phosphoryated H2AX (gamma-H2AX) at chromosomal breaks induced by ionizing radiation.	Serine	53-59	H2A.X variant histone	Homo sapiens	84-94
25487737-0	2014	Critical role of lysine 134 methylation on histone H2AX for gamma-H2AX production and DNA repair.	Lysine	17-23	H2A.X variant histone	Homo sapiens	51-55
25487737-0	2014	Critical role of lysine 134 methylation on histone H2AX for gamma-H2AX production and DNA repair.	Lysine	17-23	H2A.X variant histone	Homo sapiens	60-70
25487737-3	2014	Here we find that the histone methyltransferase SUV39H2 methylates histone H2AX on lysine 134.	Lysine	83-89	H2A.X variant histone	Homo sapiens	75-79
25487737-4	2014	When H2AX was mutated to abolish K134 methylation, the level of gamma-H2AX became significantly reduced.	K-134	33-37	H2A.X variant histone	Homo sapiens	5-9
25487737-4	2014	When H2AX was mutated to abolish K134 methylation, the level of gamma-H2AX became significantly reduced.	K-134	33-37	H2A.X variant histone	Homo sapiens	64-74
25487737-7	2014	Furthermore, introduction of K134-substituted histone H2AX enhanced radio- and chemosensitivity of cancer cells.	K-134	29-33	H2A.X variant histone	Homo sapiens	54-58
25468822-9	2014	Furthermore, G226 (0.125-2 mumol/L) dose-dependently elevated the intracellular levels of H2O2 and in the cancer cells, and pretreatment with GSH, NAC or DTT not only blocked G226-induced intracellular accumulation of ROS, but also abrogated G226-mediated phosphorylation of H2AX, apoptosis and cytotoxicity.	Lovastatin	13-17	H2A.X variant histone	Homo sapiens	275-279
25468822-9	2014	Furthermore, G226 (0.125-2 mumol/L) dose-dependently elevated the intracellular levels of H2O2 and in the cancer cells, and pretreatment with GSH, NAC or DTT not only blocked G226-induced intracellular accumulation of ROS, but also abrogated G226-mediated phosphorylation of H2AX, apoptosis and cytotoxicity.	Glutathione	142-145	H2A.X variant histone	Homo sapiens	275-279
25468822-9	2014	Furthermore, G226 (0.125-2 mumol/L) dose-dependently elevated the intracellular levels of H2O2 and in the cancer cells, and pretreatment with GSH, NAC or DTT not only blocked G226-induced intracellular accumulation of ROS, but also abrogated G226-mediated phosphorylation of H2AX, apoptosis and cytotoxicity.	Dithiothreitol	154-157	H2A.X variant histone	Homo sapiens	275-279
25365214-2	2014	Recently, we found that TPX2 regulates the levels of serine 139-phosphoryated H2AX (gamma-H2AX) at chromosomal breaks induced by ionizing radiation.	Serine	53-59	H2A.X variant histone	Homo sapiens	78-82
25202016-4	2014	Phosphorylation of H2AX at serine 139 was catalyzed by hyperosmotic stress-induced activation of Plk3.	Serine	27-33	H2A.X variant histone	Homo sapiens	19-23
24938898-4	2014	5-ATAN induced apoptosis via both caspase-independent and -dependent pathways, in which 5-ATAN induced the translocation of apoptosis inducing factor and phosphorylation of H2AX as well as poly (ADP-ribose) polymerase cleavage, caspase-3 activation.	5-acetyl-6,7,8,4'-tetramethylnortangeretin	0-6	H2A.X variant histone	Homo sapiens	173-177
24938898-4	2014	5-ATAN induced apoptosis via both caspase-independent and -dependent pathways, in which 5-ATAN induced the translocation of apoptosis inducing factor and phosphorylation of H2AX as well as poly (ADP-ribose) polymerase cleavage, caspase-3 activation.	5-acetyl-6,7,8,4'-tetramethylnortangeretin	88-94	H2A.X variant histone	Homo sapiens	173-177
25164823-1	2014	Histone H2A variant H2AX is phosphorylated at Ser(139) in response to DNA double-strand break (DSB) and single-stranded DNA (ssDNA) formation.	Serine	46-49	H2A.X variant histone	Homo sapiens	20-24
24830786-0	2014	H2AX phosphorylation regulated by p38 is involved in Bim expression and apoptosis in chronic myelogenous leukemia cells induced by imatinib.	Imatinib Mesylate	131-139	H2A.X variant histone	Homo sapiens	0-4
25130544-8	2014	Cell death after 16 h exposure to triapine paralleled the appearance of phospho-(gamma)H2AX, a marker of DNA double-strand breaks induced by collapse of DNA replication forks after prolonged replication arrest.	3-aminopyridine-2-carboxaldehyde thiosemicarbazone	34-42	H2A.X variant histone	Homo sapiens	87-91
25123929-2	2014	Chemotherapeutic drug doxorubicin has been reported to elicit additional H2AX phosphorylation in polyploidy.	Doxorubicin	22-33	H2A.X variant histone	Homo sapiens	73-77
24928205-5	2014	A marked induction of DDR, including the phosphorylation of ATM, Chk2, p53 and histone H2AX, was observed after LY2603618 treatment.	LY2603618	112-121	H2A.X variant histone	Homo sapiens	79-91
24607809-4	2014	Here, we found that treatment with 4-OHE2 (3 muM) and NA (3 nM) significantly induced the phosphorylation of histone H2AX (gamma-H2AX), one of the earliest indicators of DNA damage, and apurinic (AP) sites via the alpha2-adrenergic receptor (alpha2-AR) in human mammary epithelial MCF-10A cells.	4-hydroxyestradiol	35-41	H2A.X variant histone	Homo sapiens	109-121
24962331-5	2014	The mechanism by which MK-1775 enhanced AraC cytotoxicity was investigated in the cell lines using Western blots to probe CDK1 and H2AX phosphorylation and flow cytometry to determine apoptosis, cell cycle arrest, DNA damage, and aberrant mitotic entry.	adavosertib	23-30	H2A.X variant histone	Homo sapiens	131-135
25123929-9	2014	Since increased chromosomal damage resulted in extensive H2AX phosphorylation during polyploidy, we propose that the additional gamma-H2AX during polyploidy incurred by carbon-ion radiation provides a final opportunity for these dangerous and chromosomally unstable cells to be eliminated.	Carbon	169-175	H2A.X variant histone	Homo sapiens	57-61
25123929-9	2014	Since increased chromosomal damage resulted in extensive H2AX phosphorylation during polyploidy, we propose that the additional gamma-H2AX during polyploidy incurred by carbon-ion radiation provides a final opportunity for these dangerous and chromosomally unstable cells to be eliminated.	Carbon	169-175	H2A.X variant histone	Homo sapiens	134-138
24830786-5	2014	Overexpression of H2AX increased apoptotic sensitivity of CML cells (K562) induced by imatinib.	Imatinib Mesylate	86-94	H2A.X variant histone	Homo sapiens	18-22
24830786-15	2014	Taken together, these data demonstrated that H2AX phosphorylation regulated by p38 is involved in Bim expression and apoptosis in CML cells induced by imatinib.	Imatinib Mesylate	151-159	H2A.X variant histone	Homo sapiens	45-49
24793486-9	2014	Blocking autophagy using chloroquine magnified CCT128930-induced apoptotic cell death and the phosphorylation of H2AX.	Chloroquine	25-36	H2A.X variant histone	Homo sapiens	113-117
25847270-3	2014	H2AFX has at least two alternate transcripts that encode the same reading frame; a short 0.6kb transcript that lacks an intron or poly-A tail and is predicted to be highly expressed during the replication stage of the cell cycle, and a long 1.6kb poly-A tailed transcript that is expressed in a replication-independent manner.	Poly A	130-136	H2A.X variant histone	Homo sapiens	0-5
24965603-7	2014	Treatment with the PARPi AZD2281 +/- temozolomide induced DNA damage in CyclinA2+ cells in both primary AML cells and cell lines and distngiushed cell lines deficient (BRCA2-/-) or impaired (BRCA1+/-) in HRR activity from BRCA1+/+ cell lines based on p-H2AX induction.	olaparib	25-32	H2A.X variant histone	Homo sapiens	253-257
24597763-0	2014	Phosphorylation of histone H2AX generated by linear alkylbenzene sulfonates and its suppression by UVB exposure.	alkylbenzene sulfonates	52-75	H2A.X variant histone	Homo sapiens	19-31
24597763-1	2014	We previously demonstrated that the nonionic surfactants, nonylphenol polyethoxylates (NPEOs) induced the phosphorylation of histone H2AX (gamma-H2AX), accompanied by DNA double-strand breaks (DSBs), and that exposure to ultraviolet (UV) degraded NPEOs, which sometimes enhanced their DNA-damaging ability.	nonylphenol polyethoxylates	58-85	H2A.X variant histone	Homo sapiens	125-137
24597763-1	2014	We previously demonstrated that the nonionic surfactants, nonylphenol polyethoxylates (NPEOs) induced the phosphorylation of histone H2AX (gamma-H2AX), accompanied by DNA double-strand breaks (DSBs), and that exposure to ultraviolet (UV) degraded NPEOs, which sometimes enhanced their DNA-damaging ability.	npeos	87-92	H2A.X variant histone	Homo sapiens	125-137
24965603-7	2014	Treatment with the PARPi AZD2281 +/- temozolomide induced DNA damage in CyclinA2+ cells in both primary AML cells and cell lines and distngiushed cell lines deficient (BRCA2-/-) or impaired (BRCA1+/-) in HRR activity from BRCA1+/+ cell lines based on p-H2AX induction.	Temozolomide	37-49	H2A.X variant histone	Homo sapiens	253-257
24934860-2	2014	Here, we showed that exogenous H2O2 induces a rapid phosphorylation and co-localization of ATM, H2A.X, 53BP1 leading to DNA damage response (DDR) activation.	Hydrogen Peroxide	31-35	H2A.X variant histone	Homo sapiens	96-101
24440659-12	2014	Compared with day 1 (cyclophosphamide alone), H2AX phosphorylation was increased on day 2 when clofarabine and cyclophosphamide were administered as a couplet (n = 8).	Clofarabine	95-106	H2A.X variant histone	Homo sapiens	46-50
24440659-12	2014	Compared with day 1 (cyclophosphamide alone), H2AX phosphorylation was increased on day 2 when clofarabine and cyclophosphamide were administered as a couplet (n = 8).	Cyclophosphamide	111-127	H2A.X variant histone	Homo sapiens	46-50
24064905-4	2014	We further gained to determine a marker of DNA double strand breaks, phosphorylated histone H2A.X (Ser139) (gammaH2A.X), in HMJ-38-treated HUVECs by flow cytometry and Western blotting assay.	gammah2a	108-116	H2A.X variant histone	Homo sapiens	92-97
24064905-4	2014	We further gained to determine a marker of DNA double strand breaks, phosphorylated histone H2A.X (Ser139) (gammaH2A.X), in HMJ-38-treated HUVECs by flow cytometry and Western blotting assay.	2-(3'-methoxyphenyl)-6-pyrrolidinyl-4-quinazolinone	124-130	H2A.X variant histone	Homo sapiens	92-97
24064905-6	2014	Importantly, the effect of above DNA damage response was prevented by N-acetyl-l-cysteine (a reactive oxygen species scavenger), and NU7026 (a DNA-PK inhibitor) could attenuate DNA-PK catalytic subunit and phosphorylation of H2A.X on Ser139 expression in comparison with HMJ-38 alone treated HUVECs.	Acetylcysteine	70-89	H2A.X variant histone	Homo sapiens	225-230
24064905-6	2014	Importantly, the effect of above DNA damage response was prevented by N-acetyl-l-cysteine (a reactive oxygen species scavenger), and NU7026 (a DNA-PK inhibitor) could attenuate DNA-PK catalytic subunit and phosphorylation of H2A.X on Ser139 expression in comparison with HMJ-38 alone treated HUVECs.	Reactive Oxygen Species	93-116	H2A.X variant histone	Homo sapiens	225-230
24462707-11	2014	miR-383 impairs the phosphorylation of H2AX by targeting PNUTS and inducing cell cycle arrest independently, as well as sensitizing NT-2 cells to cisplatin.	Cisplatin	146-155	H2A.X variant histone	Homo sapiens	39-43
24064905-6	2014	Importantly, the effect of above DNA damage response was prevented by N-acetyl-l-cysteine (a reactive oxygen species scavenger), and NU7026 (a DNA-PK inhibitor) could attenuate DNA-PK catalytic subunit and phosphorylation of H2A.X on Ser139 expression in comparison with HMJ-38 alone treated HUVECs.	2-(morpholin-4-yl)benzo(h)chromen-4-one	133-139	H2A.X variant histone	Homo sapiens	225-230
24064905-6	2014	Importantly, the effect of above DNA damage response was prevented by N-acetyl-l-cysteine (a reactive oxygen species scavenger), and NU7026 (a DNA-PK inhibitor) could attenuate DNA-PK catalytic subunit and phosphorylation of H2A.X on Ser139 expression in comparison with HMJ-38 alone treated HUVECs.	2-(3'-methoxyphenyl)-6-pyrrolidinyl-4-quinazolinone	271-277	H2A.X variant histone	Homo sapiens	225-230
24804719-5	2014	Furthermore, this growth arrest by piperine treatment was associated with DNA damage as indicated by phosphorylation of H2AX at Ser139, activation of ataxia telangiectasia and rad3-related protein (ATR) and checkpoint kinase 1 (Chk1).	piperine	35-43	H2A.X variant histone	Homo sapiens	120-124
24015987-3	2013	OkA-induced apoptosis was also due to the suppression of expression of Bcl-2, Bcl-x(L) and XIAP, and the activation of caspases-3, -8 and -9, and caspase-3 downstream mammalian STE20-like kinase 1 and H2AX.	Okadaic Acid	0-3	H2A.X variant histone	Homo sapiens	201-205
24352470-4	2014	Phosphorylated H2AX (gammaH2AX) colocalized at 30 min (0.5 h) with the KSHV genome entering the nuclei.	gammah2ax	21-30	H2A.X variant histone	Homo sapiens	15-19
24418705-1	2014	We previously showed that nucleotide P2 receptor agonists such as ATP and UTP amplify gamma-ray-induced focus formation of phosphorylated histone H2A variant H2AX (gammaH2AX), which is considered to be an indicator of DNA damage so far, by activating purine P2Y6 and P2Y12 receptors.	Adenosine Triphosphate	66-69	H2A.X variant histone	Homo sapiens	158-162
24418705-1	2014	We previously showed that nucleotide P2 receptor agonists such as ATP and UTP amplify gamma-ray-induced focus formation of phosphorylated histone H2A variant H2AX (gammaH2AX), which is considered to be an indicator of DNA damage so far, by activating purine P2Y6 and P2Y12 receptors.	Uridine Triphosphate	74-77	H2A.X variant histone	Homo sapiens	158-162
24418705-1	2014	We previously showed that nucleotide P2 receptor agonists such as ATP and UTP amplify gamma-ray-induced focus formation of phosphorylated histone H2A variant H2AX (gammaH2AX), which is considered to be an indicator of DNA damage so far, by activating purine P2Y6 and P2Y12 receptors.	purine	251-257	H2A.X variant histone	Homo sapiens	158-162
24196443-8	2014	We further identified that the USP3 removes Ub at lysine 13 and 15 of H2A and gammaH2AX, as well as lysine 118 and 119 of H2AX in response to DNA damage.	Lysine	50-56	H2A.X variant histone	Homo sapiens	83-87
24556918-10	2014	Importantly, in BxPC-3 and MIA PaCa-2 cells, inhibition of MK2 also rescued increased H2AX phosphorylation caused by inhibition of the checkpoint kinase Chk1 in the presence of gemcitabine.	gemcitabine	177-188	H2A.X variant histone	Homo sapiens	86-90
24036252-3	2013	The ensuing Slug-dependent serine 139 phosphorylation of the DNA damage sensor H2AX in breast cancer stem cells induces tumor necrosis factor-alpha and IL-8 mRNAs, whose stability is enhanced by cytoplasmic beta-catenin.	Serine	27-33	H2A.X variant histone	Homo sapiens	79-83
23846844-4	2013	Whereas an increased level of H2AX histone phosphorylation is seen in S-phase of cells subjected to H2O2, only a minor proportion of gammaH2AX foci coincide with DNA replication sites.	Hydrogen Peroxide	100-104	H2A.X variant histone	Homo sapiens	30-42
23846844-5	2013	Thus, the increased level of H2AX phosphorylation induced by H2O2 is not a direct consequence of formation of DNA lesions at the sites of moving DNA replication forks.	Hydrogen Peroxide	61-65	H2A.X variant histone	Homo sapiens	29-33
24464582-6	2014	In this study, we show that Pu-27 induces profound DNA damage, resulting in striking chromosomal abnormalities in the form of chromatid or chromosomal breaks, radial formation, and telomeric DNA loss, which induces gamma-H2AX in U937 cells.	Plutonium	28-30	H2A.X variant histone	Homo sapiens	221-225
24464582-11	2014	Telomere dysfunction-induced foci assay revealed co-association of TRF1with gamma-H2AX in ATM deficient cells, which are differentially sensitive to Pu-27 than ATM proficient cells.	Plutonium	149-151	H2A.X variant histone	Homo sapiens	82-86
24603765-2	2014	In particular, RNF168 and RING1B/BMI1 function in the DDR by ubiquitinating H2A/H2AX on Lys-13/15 and Lys-118/119, respectively.	ddr	54-57	H2A.X variant histone	Homo sapiens	80-84
24603765-2	2014	In particular, RNF168 and RING1B/BMI1 function in the DDR by ubiquitinating H2A/H2AX on Lys-13/15 and Lys-118/119, respectively.	Lysine	88-91	H2A.X variant histone	Homo sapiens	80-84
24603765-2	2014	In particular, RNF168 and RING1B/BMI1 function in the DDR by ubiquitinating H2A/H2AX on Lys-13/15 and Lys-118/119, respectively.	Lysine	102-105	H2A.X variant histone	Homo sapiens	80-84
24603765-4	2014	Here we identify the nucleosome acid patch as a critical chromatin mediator of H2A/H2AX ubiquitination (ub).	nucleosome acid	21-36	H2A.X variant histone	Homo sapiens	83-87
25486192-8	2014	Resection of complex DSBs is driven by meiotic recombination 11 homolog A (MRE11), CTBP-interacting protein (CtIP), and exonuclease 1 (EXO1) but seems not controlled by the Ku heterodimer or by phosphorylation of H2AX.	dsbs	21-25	H2A.X variant histone	Homo sapiens	213-217
24362713-8	2014	AZD7762 effectively suppressed the Chk signaling pathways activated by cisplatin, dramatically enhanced expression of phosphorylated H2A.X, cleaved caspase 9 and PARP, decreased the proportion of cells in the gap 0/ gap 1 phase and the synthesis-phase fraction, and increased apoptotic cells.	3-(carbamoylamino)-5-(3-fluorophenyl)-N-(3-piperidyl)thiophene-2-carboxamide	0-7	H2A.X variant histone	Homo sapiens	133-138
24163101-2	2014	Here we demonstrate that H2AX is dynamically reorganized to preoccupy gammaH2AX hotspots on increased replication stress by activated cell proliferation and that H2AX is enriched in aphidicolin-induced replisome stalling sites in cycling cells.	gammah2ax	70-79	H2A.X variant histone	Homo sapiens	25-29
24163101-2	2014	Here we demonstrate that H2AX is dynamically reorganized to preoccupy gammaH2AX hotspots on increased replication stress by activated cell proliferation and that H2AX is enriched in aphidicolin-induced replisome stalling sites in cycling cells.	Aphidicolin	182-193	H2A.X variant histone	Homo sapiens	25-29
24163101-2	2014	Here we demonstrate that H2AX is dynamically reorganized to preoccupy gammaH2AX hotspots on increased replication stress by activated cell proliferation and that H2AX is enriched in aphidicolin-induced replisome stalling sites in cycling cells.	Aphidicolin	182-193	H2A.X variant histone	Homo sapiens	75-79
23222712-4	2013	This DNA entered nuclei of BM or other cells and induced H2A.X phosphorylation at serine 139, similar to double-strand break-inducing agents.	Serine	82-88	H2A.X variant histone	Homo sapiens	57-62
24015987-9	2013	The results showed that PP2A inhibition caused reactive oxygen species generation and affected distinct signaling pathways, resulting in the activation of H2AX and subsequent apoptotic cell death.	Reactive Oxygen Species	47-70	H2A.X variant histone	Homo sapiens	155-159
23916969-1	2013	Chromosomal double strand breaks provoke an extensive reaction in neighboring chromatin, characterized by phosphorylation of histone H2AX on serine 139 of its C-terminal tail (to form "gammaH2AX").	Serine	141-147	H2A.X variant histone	Homo sapiens	125-137
23916969-1	2013	Chromosomal double strand breaks provoke an extensive reaction in neighboring chromatin, characterized by phosphorylation of histone H2AX on serine 139 of its C-terminal tail (to form "gammaH2AX").	gammah2ax	185-194	H2A.X variant histone	Homo sapiens	125-137
23903906-8	2013	Flow cytometry revealed that cyclopamine treatment enhanced gamma-H2AX foci in Colo-357 and SW-1990 cells exposed to irradiation.	cyclopamine	29-40	H2A.X variant histone	Homo sapiens	66-70
23896517-5	2013	TA induced rapid generation of intracellular ROS and led to an increase of phosphorylation of H2AX, a tail moment of comet and distribution of fragmented genomic DNA traces.	tolfenamic acid	0-2	H2A.X variant histone	Homo sapiens	94-98
23903906-10	2013	EGF also rescued pancreatic cancer cells from cyclopamine-induced H2AX phosphorylation following irradiation.	cyclopamine	46-57	H2A.X variant histone	Homo sapiens	66-70
23783842-9	2013	Particularly, we found that NH4Cl treatment increased cisplatin-induced phosphorylation of H2AX.	Ammonium Chloride	28-33	H2A.X variant histone	Homo sapiens	91-95
23783842-9	2013	Particularly, we found that NH4Cl treatment increased cisplatin-induced phosphorylation of H2AX.	Cisplatin	54-63	H2A.X variant histone	Homo sapiens	91-95
23580445-6	2013	In particular, the compound labeled NSC 130813 [4-[(6-chloro-2-methoxy-9-acridinyl)amino]-2-[(4-methyl-1-piperazinyl)methyl]] was shown to act synergistically with cisplatin and mitomycin C; to increase UVC-mediated cytotoxicity; to modify DNA repair as indicated by the staining of phosphorylated H2AX; and to disrupt interaction between ERCC1 and XPF in cells.	6-chloro-2-methoxy-9-acridinyl)amino]-2-[(4-methyl-1-piperazinyl	52-116	H2A.X variant histone	Homo sapiens	298-302
23903043-1	2013	Phosphorylation of the H2AX protein is an early step in the double strand break (DSB) repair pathway; therefore, phosphorylated histone (gammaH2AX) foci scoring is widely used as a measure for DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	193-197	H2A.X variant histone	Homo sapiens	23-27
23585020-8	2013	DNA replicative stress was identified by associated H2A.X phosphorylation in AICAr-treated cells, which was also prevented by uridine add-back.	Uridine	126-133	H2A.X variant histone	Homo sapiens	52-57
23580445-6	2013	In particular, the compound labeled NSC 130813 [4-[(6-chloro-2-methoxy-9-acridinyl)amino]-2-[(4-methyl-1-piperazinyl)methyl]] was shown to act synergistically with cisplatin and mitomycin C; to increase UVC-mediated cytotoxicity; to modify DNA repair as indicated by the staining of phosphorylated H2AX; and to disrupt interaction between ERCC1 and XPF in cells.	methyl radical	96-102	H2A.X variant histone	Homo sapiens	298-302
23580445-6	2013	In particular, the compound labeled NSC 130813 [4-[(6-chloro-2-methoxy-9-acridinyl)amino]-2-[(4-methyl-1-piperazinyl)methyl]] was shown to act synergistically with cisplatin and mitomycin C; to increase UVC-mediated cytotoxicity; to modify DNA repair as indicated by the staining of phosphorylated H2AX; and to disrupt interaction between ERCC1 and XPF in cells.	Cisplatin	164-173	H2A.X variant histone	Homo sapiens	298-302
23580445-6	2013	In particular, the compound labeled NSC 130813 [4-[(6-chloro-2-methoxy-9-acridinyl)amino]-2-[(4-methyl-1-piperazinyl)methyl]] was shown to act synergistically with cisplatin and mitomycin C; to increase UVC-mediated cytotoxicity; to modify DNA repair as indicated by the staining of phosphorylated H2AX; and to disrupt interaction between ERCC1 and XPF in cells.	Mitomycin	178-189	H2A.X variant histone	Homo sapiens	298-302
23536184-8	2013	Treatment with camptothecin, a topoisomerase I inhibitor, caused normal cells to down-regulate H2AX and become quiescent, a process mediated by both Arf and p53.	Camptothecin	15-27	H2A.X variant histone	Homo sapiens	95-99
23696313-0	2013	Kinetics of nuclear phosphorylation (gamma-H2AX) in human lymphocytes treated in vitro with UVB, bleomycin and mitomycin C.	Bleomycin	97-106	H2A.X variant histone	Homo sapiens	43-47
23696313-0	2013	Kinetics of nuclear phosphorylation (gamma-H2AX) in human lymphocytes treated in vitro with UVB, bleomycin and mitomycin C.	Mitomycin	111-122	H2A.X variant histone	Homo sapiens	43-47
23696313-1	2013	After double-strand break induction, formation of gamma-H2AX foci due to phosphorylation at Ser-139 of histone H2AX represents an early event of the DNA damage response (DDR).	Serine	92-95	H2A.X variant histone	Homo sapiens	56-60
23696313-1	2013	After double-strand break induction, formation of gamma-H2AX foci due to phosphorylation at Ser-139 of histone H2AX represents an early event of the DNA damage response (DDR).	Serine	92-95	H2A.X variant histone	Homo sapiens	111-115
23696313-4	2013	Here, we investigated the time-course of gamma-H2AX in unstimulated or cultured peripheral lymphocytes in vitro treated with UVB, bleomycin and mitomycin C (MMC).	Mitomycin	144-155	H2A.X variant histone	Homo sapiens	47-51
23696313-4	2013	Here, we investigated the time-course of gamma-H2AX in unstimulated or cultured peripheral lymphocytes in vitro treated with UVB, bleomycin and mitomycin C (MMC).	Mitomycin	157-160	H2A.X variant histone	Homo sapiens	47-51
23620287-3	2013	As the locally restricted phosphorylation of H2AX to form gammaH2AX is a key step in facilitating efficient DSB repair, we investigated this process after localized induction of clustered damage by ionizing radiation.	gammah2ax	58-67	H2A.X variant histone	Homo sapiens	45-49
23518201-0	2013	The effects of selenium and the GPx-1 selenoprotein on the phosphorylation of H2AX.	Selenium	15-23	H2A.X variant histone	Homo sapiens	78-82
23518201-3	2013	Selenium"s ability to alter the phosphorylation of the H2AX, a histone protein that functions in the reduction of DNA damage by recruiting repair proteins to the damage site, following exposure to ionizing radiation and bleomycin was investigated.	Selenium	0-8	H2A.X variant histone	Homo sapiens	55-59
23518201-3	2013	Selenium"s ability to alter the phosphorylation of the H2AX, a histone protein that functions in the reduction of DNA damage by recruiting repair proteins to the damage site, following exposure to ionizing radiation and bleomycin was investigated.	Bleomycin	220-229	H2A.X variant histone	Homo sapiens	55-59
23518201-7	2013	RESULTS: In colon-derived cells, selenium increases GPx-1 and attenuated H2AX phosphorylation following genotoxic exposures while the viability of these cells was unaffected.	Selenium	33-41	H2A.X variant histone	Homo sapiens	73-77
23536184-11	2013	Thus, the expression of H2AX and gammaH2AX (phosphorylated form of H2AX at Ser-139) is a critical factor that determines drug sensitivity and should be considered when administering chemotherapy.	Serine	75-78	H2A.X variant histone	Homo sapiens	24-28
23536184-11	2013	Thus, the expression of H2AX and gammaH2AX (phosphorylated form of H2AX at Ser-139) is a critical factor that determines drug sensitivity and should be considered when administering chemotherapy.	Serine	75-78	H2A.X variant histone	Homo sapiens	38-42
23577291-0	2013	Intense THz pulses cause H2AX phosphorylation and activate DNA damage response in human skin tissue.	thz	8-11	H2A.X variant histone	Homo sapiens	25-29
23449797-5	2013	We now also observed phosphorylation of H2AX at serine 139 during KSHV infection.	Serine	48-54	H2A.X variant histone	Homo sapiens	40-44
23403624-7	2013	BEZ235 treatment induced apoptotic tumor regressions in vivo that correlated with suppression of mTORC1-regulated substrates and reduced H2AX phosphorylation and also with feedback phosphorylation of AKT.	dactolisib	0-6	H2A.X variant histone	Homo sapiens	137-141
23264066-1	2013	PURPOSE: The purpose of our study was to evaluate the degree of radiotoxicity to lymphocytes in thyroid cancer after iodine-131(I-131) therapy using gamma-H2AX foci immunodetection.	Iodine-131	128-133	H2A.X variant histone	Homo sapiens	155-159
23264066-8	2013	CONCLUSION: gamma-H2AX foci immunodetection in lymphocytes may detect radiation-induced DNA damage associated with I-131 therapy for thyroid cancer, and may facilitate estimation of the radiation doses absorbed with this therapy.	Iodine-131	115-120	H2A.X variant histone	Homo sapiens	18-22
23577291-5	2013	We observe that exposure to intense THz pulses for ten minutes leads to a significant induction of H2AX phosphorylation, indicating that THz pulse irradiation may cause DNA damage in exposed skin tissue.	thz	36-39	H2A.X variant histone	Homo sapiens	99-103
23577291-5	2013	We observe that exposure to intense THz pulses for ten minutes leads to a significant induction of H2AX phosphorylation, indicating that THz pulse irradiation may cause DNA damage in exposed skin tissue.	thz	137-140	H2A.X variant histone	Homo sapiens	99-103
23333390-6	2013	The steady and etoposide-induced phosphorylated H2AX (gamma-H2AX) were higher in PES1-silenced cells than in control cells.	Etoposide	15-24	H2A.X variant histone	Homo sapiens	48-52
23333498-11	2013	Furthermore, phosphorylated H2AX is up-regulated after 6 days of treatment with SFN alone, and EGCG can potentiate this effect, suggesting that DNA damage is a potential cellular mechanism contributing to the inhibiting effect of EGCG and SFN combination treatment.	sulforaphane	80-83	H2A.X variant histone	Homo sapiens	28-32
23333498-11	2013	Furthermore, phosphorylated H2AX is up-regulated after 6 days of treatment with SFN alone, and EGCG can potentiate this effect, suggesting that DNA damage is a potential cellular mechanism contributing to the inhibiting effect of EGCG and SFN combination treatment.	epigallocatechin gallate	230-234	H2A.X variant histone	Homo sapiens	28-32
23333498-11	2013	Furthermore, phosphorylated H2AX is up-regulated after 6 days of treatment with SFN alone, and EGCG can potentiate this effect, suggesting that DNA damage is a potential cellular mechanism contributing to the inhibiting effect of EGCG and SFN combination treatment.	sulforaphane	239-242	H2A.X variant histone	Homo sapiens	28-32
23333390-6	2013	The steady and etoposide-induced phosphorylated H2AX (gamma-H2AX) were higher in PES1-silenced cells than in control cells.	Etoposide	15-24	H2A.X variant histone	Homo sapiens	54-64
23333390-7	2013	Besides, etoposide-induced gamma-H2AX persisted longer in PES1-silenced cells after removing the etoposide.	Etoposide	9-18	H2A.X variant histone	Homo sapiens	27-37
23333390-7	2013	Besides, etoposide-induced gamma-H2AX persisted longer in PES1-silenced cells after removing the etoposide.	Etoposide	97-106	H2A.X variant histone	Homo sapiens	27-37
23390564-11	2013	Either cladribine or bendamustine led to a remarkable increase of the phosphorylated H2A.X, CHK1 and CHK2 in both MM1.S and MM1.R cells, suggesting an induction of DNA damage response.	Cladribine	7-17	H2A.X variant histone	Homo sapiens	85-90
23144294-5	2013	In triple-negative cell lines, RNAi-mediated PLK1 depletion or inhibition of PLK1 activity with a small molecule (BI-2536) induced an increase in phosphorylated H2AX, G(2)-M arrest, and apoptosis.	BI 2536	114-121	H2A.X variant histone	Homo sapiens	161-165
23111755-8	2013	CAFs were also less sensitive to doxorubicin as evidenced by less H2AX phosphorylation and reduced apoptosis on flow cytometric analysis of Annexin V compared with NBFs.	Doxorubicin	33-44	H2A.X variant histone	Homo sapiens	66-70
23390564-11	2013	Either cladribine or bendamustine led to a remarkable increase of the phosphorylated H2A.X, CHK1 and CHK2 in both MM1.S and MM1.R cells, suggesting an induction of DNA damage response.	Bendamustine Hydrochloride	21-33	H2A.X variant histone	Homo sapiens	85-90
22946062-6	2012	Furthermore, we demonstrate that the ability of LSH to hydrolyse ATP is necessary for efficient phosphorylation of H2AX at DNA double-strand breaks and successful repair of DNA damage.	Adenosine Triphosphate	65-68	H2A.X variant histone	Homo sapiens	115-119
23041231-9	2012	Dovitinib was also found to be a cellular topoisomerase II poison in human leukemia K562 cells and induced double-strand DNA breaks in K562 cells as evidenced by increased phosphorylation of H2AX.	4-amino-5-fluoro-3-(5-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl)quinolin-2(1H)-one	0-9	H2A.X variant histone	Homo sapiens	191-195
23715267-4	2013	The histone variant H2AX, which is a key component of the DNA damage response, is also evicted by anthracyclines, and H2AX eviction is associated with attenuated DNA repair.	Anthracyclines	98-112	H2A.X variant histone	Homo sapiens	20-24
22752636-10	2012	After prednisolone withdrawal, there was overexpression of H2AX, CC3, and p53 in the latter group.	Prednisolone	6-18	H2A.X variant histone	Homo sapiens	59-63
22908299-0	2012	Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1.	Phosphoserine	20-33	H2A.X variant histone	Homo sapiens	73-78
23058634-3	2012	Indeed, we showed that etoposide could influence transcription and was able to activate DDR in resting human T cells by inducing phosphorylation of ATM and its substrates, H2AX and p53.	Etoposide	23-32	H2A.X variant histone	Homo sapiens	172-176
23058634-7	2012	Pretreatment of resting T cells with KU 55933 blocked phosphorylation of ATM, H2AX and p53, which, in turn, prevented PUMA expression, caspase activation and apoptosis.	2-morpholin-4-yl-6-thianthren-1-yl-pyran-4-one	37-45	H2A.X variant histone	Homo sapiens	78-82
23076878-4	2012	Phosphorylation of H2AX, Chk1, and RPA2 was more strongly activated in K562 cells than in hMSCs, at equivalent doses of doxorubicin.	Doxorubicin	120-131	H2A.X variant histone	Homo sapiens	19-23
22627294-8	2012	Clioquinol in fact induced phosphorylation of ATM and histone H2AX, a marker of DNA double-strand breaks (DSBs).	Clioquinol	0-10	H2A.X variant histone	Homo sapiens	54-66
22972498-2	2012	In this study, the interaction between TOPORS (topoisomerase I-binding protein) and H2AX was verified using mammalian cell extracts exposed to diverse DNA damaging stresses such as ionizing radiation, doxorubicin, camptothecin, and hydrogen peroxide.	Doxorubicin	201-212	H2A.X variant histone	Homo sapiens	84-88
22972498-2	2012	In this study, the interaction between TOPORS (topoisomerase I-binding protein) and H2AX was verified using mammalian cell extracts exposed to diverse DNA damaging stresses such as ionizing radiation, doxorubicin, camptothecin, and hydrogen peroxide.	Camptothecin	214-226	H2A.X variant histone	Homo sapiens	84-88
22972498-2	2012	In this study, the interaction between TOPORS (topoisomerase I-binding protein) and H2AX was verified using mammalian cell extracts exposed to diverse DNA damaging stresses such as ionizing radiation, doxorubicin, camptothecin, and hydrogen peroxide.	Hydrogen Peroxide	232-249	H2A.X variant histone	Homo sapiens	84-88
22972498-5	2012	The protein stability of H2AX was decreased when TOPORS was ectopically expressed in cells, and oxidative stresses such as hydrogen peroxide and ionizing radiation induced recovery of the H2AX protein level.	Hydrogen Peroxide	123-140	H2A.X variant histone	Homo sapiens	25-29
22972498-5	2012	The protein stability of H2AX was decreased when TOPORS was ectopically expressed in cells, and oxidative stresses such as hydrogen peroxide and ionizing radiation induced recovery of the H2AX protein level.	Hydrogen Peroxide	123-140	H2A.X variant histone	Homo sapiens	188-192
22796259-4	2012	The present results show that MED induces DNA damage through the production of reactive oxygen species (ROS), which resulted in the phosphorylation of H2AX and the activation of the Ataxia telangiectasia mutated kinase (ATM) and p53 signaling pathways.	Reactive Oxygen Species	79-102	H2A.X variant histone	Homo sapiens	151-155
22796259-4	2012	The present results show that MED induces DNA damage through the production of reactive oxygen species (ROS), which resulted in the phosphorylation of H2AX and the activation of the Ataxia telangiectasia mutated kinase (ATM) and p53 signaling pathways.	Reactive Oxygen Species	104-107	H2A.X variant histone	Homo sapiens	151-155
23772364-1	2012	Under normal conditions histone H2AX is constitutively phosphorylated on tyrosine (Y) 142 by Williams-Beuren syndrome transcription factor kinase (WSTF).	Tyrosine	73-81	H2A.X variant histone	Homo sapiens	32-36
22290195-6	2012	RESULTS: H(2) O(2) induced apoptosis and phosphorylation of ATM, Chk2, and H2AX in LNCaP cells.	Hydrogen Peroxide	9-18	H2A.X variant histone	Homo sapiens	75-79
22908299-0	2012	Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1.	Phosphotyrosine	38-53	H2A.X variant histone	Homo sapiens	73-78
22908299-2	2012	In response to DNA double-strand breaks (DSBs), H2A.X is instantaneously phosphorylated at Ser139 by the kinases ATM and ATR and is progressively dephosphorylated at Tyr142 by the Eya1 and Eya3 tyrosine phosphatases, resulting in a temporal switch from a postulated diphosphorylated (pSer139, pTyr142) to monophosphorylated (pSer139) H2A.X state.	ptyr142	293-300	H2A.X variant histone	Homo sapiens	48-53
22435726-4	2012	The increased expression of miR-24 in CD8(+) CD28(-)  T cells is associated with decreased expression of the histone variant H2AX, a protein that plays a key role in the DNA damage response (DDR).	mir-24	28-34	H2A.X variant histone	Homo sapiens	125-129
22753480-1	2012	The "apoptotic ring" is characterized by the phosphorylation of histone H2AX at serine 139 (gamma-H2AX) by DNA-dependent protein kinase (DNA-PK).	Serine	80-86	H2A.X variant histone	Homo sapiens	72-76
22753480-1	2012	The "apoptotic ring" is characterized by the phosphorylation of histone H2AX at serine 139 (gamma-H2AX) by DNA-dependent protein kinase (DNA-PK).	Serine	80-86	H2A.X variant histone	Homo sapiens	98-102
22753480-7	2012	In contrast, HSP90 inhibition by geldanamycin markedly enhances TRAIL-induced DNA-PK and H2AX activation.	geldanamycin	33-45	H2A.X variant histone	Homo sapiens	89-93
22828439-3	2012	Increased phosphorylation levels of Chk2 and H2AX were observed and were reversed by the DNA damage inhibitor caffeine in calactin-treated cells.	Caffeine	110-118	H2A.X variant histone	Homo sapiens	45-49
22828439-3	2012	Increased phosphorylation levels of Chk2 and H2AX were observed and were reversed by the DNA damage inhibitor caffeine in calactin-treated cells.	Calactin	122-130	H2A.X variant histone	Homo sapiens	45-49
22739265-6	2012	In addition, etoposide induced p53 phosphorylation and H2AX foci formation in proliferating SH-SY5Y cells but failed to do so in differentiated SH-SY5Y cells.	Etoposide	13-22	H2A.X variant histone	Homo sapiens	55-59
21713384-3	2012	Phosphorylation of the DNA repair enzyme H2AX by emtricitabine/tenofovir indicated that it interfered with the integrity of the DNA and replication machinery in human cancer cells.	Emtricitabine	49-62	H2A.X variant histone	Homo sapiens	41-45
21713384-3	2012	Phosphorylation of the DNA repair enzyme H2AX by emtricitabine/tenofovir indicated that it interfered with the integrity of the DNA and replication machinery in human cancer cells.	Tenofovir	63-72	H2A.X variant histone	Homo sapiens	41-45
22694057-3	2012	In addition, PUB-SOs induced histone H2AX (gammaH2AX) phosphorylation, indicating that these molecules induce DNA double-strand breaks.	pub-sos	13-20	H2A.X variant histone	Homo sapiens	29-41
22833098-2	2012	H2AX senses DSBs through rapid serine 139 phosphorylation, concurrently leading to the formation of phospho-(gamma)H2AX foci with various proteins.	dsbs	12-16	H2A.X variant histone	Homo sapiens	0-4
22833098-2	2012	H2AX senses DSBs through rapid serine 139 phosphorylation, concurrently leading to the formation of phospho-(gamma)H2AX foci with various proteins.	dsbs	12-16	H2A.X variant histone	Homo sapiens	115-119
22833098-2	2012	H2AX senses DSBs through rapid serine 139 phosphorylation, concurrently leading to the formation of phospho-(gamma)H2AX foci with various proteins.	Serine	31-37	H2A.X variant histone	Homo sapiens	0-4
22833098-2	2012	H2AX senses DSBs through rapid serine 139 phosphorylation, concurrently leading to the formation of phospho-(gamma)H2AX foci with various proteins.	Serine	31-37	H2A.X variant histone	Homo sapiens	115-119
22467212-3	2012	Genome-wide locations of possible endogenous and exogenous DSBs were identified based on gamma-H2AX distribution in dividing cancer cells without irradiation and that in resting cells upon irradiation, respectively.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	59-63	H2A.X variant histone	Homo sapiens	95-99
22430255-4	2012	The efficient repair of DSBs relies in part on the rapid formation of foci of phosphorylated histone H2AX (gamma-H2AX) at each break site, and the subsequent recruitment of repair factors.	dsbs	24-28	H2A.X variant histone	Homo sapiens	93-105
22430255-4	2012	The efficient repair of DSBs relies in part on the rapid formation of foci of phosphorylated histone H2AX (gamma-H2AX) at each break site, and the subsequent recruitment of repair factors.	gamma-h2ax	107-117	H2A.X variant histone	Homo sapiens	93-105
22622028-9	2012	Nutlin-3, an HDM2 inhibitor, mimicked the effects of alpha-MSH resulting in reduced phosphorylation of H2AX (gamma-H2AX), a marker of DNA damage.	nutlin 3	0-8	H2A.X variant histone	Homo sapiens	103-107
22523229-2	2012	We now report that TGHQ induces severe DNA damage, as evidenced by DNA ladder formation and H2AX phosphorylation.	2,3,5-(triglutathion-S-yl)hydroquinone	19-23	H2A.X variant histone	Homo sapiens	92-96
22622028-9	2012	Nutlin-3, an HDM2 inhibitor, mimicked the effects of alpha-MSH resulting in reduced phosphorylation of H2AX (gamma-H2AX), a marker of DNA damage.	nutlin 3	0-8	H2A.X variant histone	Homo sapiens	109-119
22222994-0	2012	Titanium dioxide particles phosphorylate histone H2AX independent of ROS production.	titanium dioxide	0-16	H2A.X variant histone	Homo sapiens	49-53
22431734-2	2012	We found that intercellular contact stabilizes histone H2AX and gammaH2AX (H2AX phosphorylated on Ser-139) by up-regulating N/E-cadherin and gamma-catenin.	Serine	98-101	H2A.X variant histone	Homo sapiens	69-73
22388075-0	2012	Imatinib induces H2AX phosphorylation and apoptosis in chronic myelogenous leukemia cells in vitro via caspase-3/Mst1 pathway.	Imatinib Mesylate	0-8	H2A.X variant histone	Homo sapiens	17-21
22388075-2	2012	The aim of the present study was to elucidate the mechanisms underlying imatinib-induced C-terminal phosphorylation of H2AX in chronic myelogenous leukemia cells in vitro.	Imatinib Mesylate	72-80	H2A.X variant histone	Homo sapiens	119-123
22388075-4	2012	Microscopy, Western blotting and flow cytometry were used to study the signaling pathways that regulate imatinib-induced H2AX phosphorylation and the apoptotic mechanisms.	Imatinib Mesylate	104-112	H2A.X variant histone	Homo sapiens	121-125
22388075-5	2012	RESULTS: Treatment of K562 cells with imatinib (1-8 mumol/L) induced phosphorylation of H2AX at Ser139 and Tyr142 in time- and dose-dependent manners.	Imatinib Mesylate	38-46	H2A.X variant histone	Homo sapiens	88-92
22388075-8	2012	The caspase-3 inhibitor Z-VAD (40 mumol/L) reduced imatinib-induced H2AX phosphorylation at Ser139 and Tyr142 and blocked imatinib-induced apoptosis of K562 cells.	z-vad	24-29	H2A.X variant histone	Homo sapiens	68-72
22388075-8	2012	The caspase-3 inhibitor Z-VAD (40 mumol/L) reduced imatinib-induced H2AX phosphorylation at Ser139 and Tyr142 and blocked imatinib-induced apoptosis of K562 cells.	Imatinib Mesylate	51-59	H2A.X variant histone	Homo sapiens	68-72
22388075-10	2012	CONCLUSION: The caspase-3/Mst1 pathway is required for H2AX C-terminal phosphorylation at Ser139 and Tyr142 and subsequent apoptosis in Bcr-Abl-positive K562 cells induced by imatinib.	Imatinib Mesylate	175-183	H2A.X variant histone	Homo sapiens	55-59
22370485-6	2012	KU-60019 inhibited the phosphorylation of the major DNA damage effectors p53, H2AX and KAP1 as well as AKT.	2-(2,6-dimethylmorpholin-4-yl)-N-(5-(6-morpholin-4-yl-4-oxo-4H-pyran-2-yl)-9H-thioxanthen-2-yl)acetamide	0-8	H2A.X variant histone	Homo sapiens	78-82
21678400-10	2012	Western blot results show enhanced activation of DNA laddering marker H2.aX by resveratrol at acidic pH that was reversed by neocuproine and not by orthophenanthroline.	Resveratrol	79-90	H2A.X variant histone	Homo sapiens	70-75
21678400-10	2012	Western blot results show enhanced activation of DNA laddering marker H2.aX by resveratrol at acidic pH that was reversed by neocuproine and not by orthophenanthroline.	neocuproine	125-136	H2A.X variant histone	Homo sapiens	70-75
22121209-8	2012	Oocytes from ovaries cultured and treated with BPA show changes in the expression of Spo11, H2ax and Blm genes, with a significant increase from 3- to 5-fold (P<= 0.05).	bisphenol A	47-50	H2A.X variant histone	Homo sapiens	92-96
22042585-11	2012	Detection of histone gamma-H2AX (phosphorylated H2AX) reveals activation of DNA-dependent protein kinase (DNA-PK) by Dbait, which has been shown to be the key step for sensitization to genotoxic therapy.	dbait	117-122	H2A.X variant histone	Homo sapiens	27-31
22042585-11	2012	Detection of histone gamma-H2AX (phosphorylated H2AX) reveals activation of DNA-dependent protein kinase (DNA-PK) by Dbait, which has been shown to be the key step for sensitization to genotoxic therapy.	dbait	117-122	H2A.X variant histone	Homo sapiens	48-52
22222994-2	2012	In this study, we examined the genotoxicity of two different sized TiO(2) particles in the lung adenocarcinoma epithelial cell line A549 based on the phosphorylation of histone H2AX (gamma-H2AX), recently regarded as a sensitive marker for DNA damage.	titanium dioxide	67-73	H2A.X variant histone	Homo sapiens	169-181
22222994-2	2012	In this study, we examined the genotoxicity of two different sized TiO(2) particles in the lung adenocarcinoma epithelial cell line A549 based on the phosphorylation of histone H2AX (gamma-H2AX), recently regarded as a sensitive marker for DNA damage.	titanium dioxide	67-73	H2A.X variant histone	Homo sapiens	183-193
22222994-3	2012	TiO(2) particles generated gamma-H2AX, which was more remarkable with the smaller particles.	titanium dioxide	0-6	H2A.X variant histone	Homo sapiens	27-37
22222994-4	2012	Flow cytometric analysis showed that the generation was independent of cell cycle phases and cells which incorporated larger amounts of TiO(2) particles had more significant gamma-H2AX.	titanium dioxide	136-142	H2A.X variant histone	Homo sapiens	174-184
22222994-6	2012	In addition, the generation of gamma-H2AX by TiO(2) particles was more significant than that after treatment with hydrogen peroxide.	titanium dioxide	45-51	H2A.X variant histone	Homo sapiens	31-41
22222994-6	2012	In addition, the generation of gamma-H2AX by TiO(2) particles was more significant than that after treatment with hydrogen peroxide.	Hydrogen Peroxide	114-131	H2A.X variant histone	Homo sapiens	31-41
22222994-7	2012	On the other hand, the generation of gamma-H2AX was attenuated by coating the surface of TiO(2) particles with bovine serum albumin.	titanium dioxide	89-95	H2A.X variant histone	Homo sapiens	37-47
22222994-8	2012	These results suggested that smaller TiO(2) particles were easy to incorporate into cells and generated cell cycle phase-independent gamma-H2AX, which was dependent on the condition of the TiO(2) surface but not on the formation of ROS.	titanium dioxide	37-43	H2A.X variant histone	Homo sapiens	133-143
22222994-8	2012	These results suggested that smaller TiO(2) particles were easy to incorporate into cells and generated cell cycle phase-independent gamma-H2AX, which was dependent on the condition of the TiO(2) surface but not on the formation of ROS.	titanium dioxide	189-195	H2A.X variant histone	Homo sapiens	133-143
21993423-7	2012	Further, differential expression levels of cleaved (ADP) ribose polymerase 1 (PARP-1) and phosphorylated histone H2AX (gamma-H2AX) were observed after curcumin treatment.	Curcumin	151-159	H2A.X variant histone	Homo sapiens	105-117
21993423-7	2012	Further, differential expression levels of cleaved (ADP) ribose polymerase 1 (PARP-1) and phosphorylated histone H2AX (gamma-H2AX) were observed after curcumin treatment.	Curcumin	151-159	H2A.X variant histone	Homo sapiens	119-129
21993423-8	2012	It seems that PARP-1 similar to H2AX, confers cellular protection against radiation and estrogen-induced DNA damage mediated by curcumin.	Curcumin	128-136	H2A.X variant histone	Homo sapiens	32-36
22249335-11	2012	The increased H2AX phosphorylation status of the SAHA-treated tumor cells post irradiation likely reflects its delayed dephosphorylation within the DNA damage signal decay rather than chromatin acetylation-dependent differences in the overall efficacy of DSB induction and rejoining.	Vorinostat	49-53	H2A.X variant histone	Homo sapiens	14-18
22941631-4	2012	Because phosphorylation of H2AX at Ser 139 (gamma-H2AX) is abundant, fast, and correlates well with each DSB, it is the most sensitive marker that can be used to examine the DNA damage produced and the subsequent repair of the DNA lesion.	Serine	35-38	H2A.X variant histone	Homo sapiens	27-31
22051700-0	2012	Nonylphenol polyethoxylates induce phosphorylation of histone H2AX.	nonylphenol polyethoxylates	0-27	H2A.X variant histone	Homo sapiens	54-66
22237206-0	2012	DNA damage induces reactive oxygen species generation through the H2AX-Nox1/Rac1 pathway.	Reactive Oxygen Species	19-42	H2A.X variant histone	Homo sapiens	66-70
22237206-2	2012	This study demonstrates that ROS induction after treatment of cells with neocarzinostatin (NCS), an ionizing radiation mimetic, is at least partly mediated by increasing histone H2AX.	Reactive Oxygen Species	29-32	H2A.X variant histone	Homo sapiens	178-182
22237206-2	2012	This study demonstrates that ROS induction after treatment of cells with neocarzinostatin (NCS), an ionizing radiation mimetic, is at least partly mediated by increasing histone H2AX.	Zinostatin	73-89	H2A.X variant histone	Homo sapiens	178-182
22237206-2	2012	This study demonstrates that ROS induction after treatment of cells with neocarzinostatin (NCS), an ionizing radiation mimetic, is at least partly mediated by increasing histone H2AX.	Zinostatin	91-94	H2A.X variant histone	Homo sapiens	178-182
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	Reactive Oxygen Species	20-23	H2A.X variant histone	Homo sapiens	50-54
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	Reactive Oxygen Species	20-23	H2A.X variant histone	Homo sapiens	101-105
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	Reactive Oxygen Species	20-23	H2A.X variant histone	Homo sapiens	101-105
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	3-aminodiphenyleneiodium	233-236	H2A.X variant histone	Homo sapiens	50-54
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	3-aminodiphenyleneiodium	233-236	H2A.X variant histone	Homo sapiens	101-105
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	3-aminodiphenyleneiodium	233-236	H2A.X variant histone	Homo sapiens	101-105
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	Reactive Oxygen Species	327-330	H2A.X variant histone	Homo sapiens	50-54
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	Reactive Oxygen Species	327-330	H2A.X variant histone	Homo sapiens	101-105
22237206-3	2012	Increased levels of ROS and cell death induced by H2AX overexpression alone or DNA damage leading to H2AX accumulation are reduced by treating cells with the antioxidant N-Acetyl-L-Cysteine (NAC), the NADP(H) oxidase (Nox) inhibitor DPI, expression of Rac1N17, and knockdown of Nox1, but not Nox4, indicating that induction of ROS by H2AX is mediated through Nox1 and Rac1 GTPase.	Reactive Oxygen Species	327-330	H2A.X variant histone	Homo sapiens	101-105
22237206-5	2012	These results point to a novel role of histone H2AX that regulates Nox1-mediated ROS generation after DNA damage.	Reactive Oxygen Species	81-84	H2A.X variant histone	Homo sapiens	47-51
22941631-4	2012	Because phosphorylation of H2AX at Ser 139 (gamma-H2AX) is abundant, fast, and correlates well with each DSB, it is the most sensitive marker that can be used to examine the DNA damage produced and the subsequent repair of the DNA lesion.	Serine	35-38	H2A.X variant histone	Homo sapiens	50-54
21854619-7	2011	A2780s cells subjected to combination platinum and M344 treatment, demonstrated increased DNA damage as assessed by the presence of phosphorylated H2A.X foci in comparison to either treatment alone.	Platinum	38-46	H2A.X variant histone	Homo sapiens	147-152
22642109-11	2012	The 24-hour treatment of MOLT-4 leukemia cells with 2 mM VA results in radiosensitizing, increases apoptosis induction, H2AX phosphorylation, and also p53 and p21 activation.	Valproic Acid	57-59	H2A.X variant histone	Homo sapiens	120-124
22094106-7	2011	RESULTS: ABZ induces DNA damage as measured by increased H2AX phosphorylation.	Albendazole	9-12	H2A.X variant histone	Homo sapiens	57-61
21824484-1	2011	The measurement of serine139-phosphorylated histone H2AX (gammaH2AX) provides a biomarker of DNA double-strand breaks (DSBs) and may identify potential genotoxic activity.	serine139	19-28	H2A.X variant histone	Homo sapiens	44-56
21690091-2	2011	Histone variant H2AX is a critical sensor that undergoes phosphorylation at serine 139 upon genotoxic stress, which provides a docking site to recruit the mediator of DNA damage checkpoint protein 1 (MDC1) and DNA repair protein complex to sites of DNA breaks for DNA repair.	Serine	76-82	H2A.X variant histone	Homo sapiens	16-20
21690091-3	2011	Here, we show that monoubiquitination of H2AX is induced upon DNA double strand breaks and plays a critical role in H2AX Ser-139 phosphorylation (gamma-H2AX), in turn facilitating the recruitment of MDC1 to DNA damage foci.	Serine	121-124	H2A.X variant histone	Homo sapiens	41-45
21690091-3	2011	Here, we show that monoubiquitination of H2AX is induced upon DNA double strand breaks and plays a critical role in H2AX Ser-139 phosphorylation (gamma-H2AX), in turn facilitating the recruitment of MDC1 to DNA damage foci.	Serine	121-124	H2A.X variant histone	Homo sapiens	116-120
21690091-3	2011	Here, we show that monoubiquitination of H2AX is induced upon DNA double strand breaks and plays a critical role in H2AX Ser-139 phosphorylation (gamma-H2AX), in turn facilitating the recruitment of MDC1 to DNA damage foci.	Serine	121-124	H2A.X variant histone	Homo sapiens	116-120
21882403-0	2004	(111)In-Labeled DTPA-conjugated Tat-linked anti-phosphorylated histone protein H2AX antibody Chemotherapy and radiotherapy, or a combination of the two, are often used to treat cancer and are known to either damage cellular DNA itself or to interfere with the DNA metabolic pathways and generate DNA double-strand breaks (dsb) that are fatal for the neoplastic cells (1).	Pentetic Acid	16-20	H2A.X variant histone	Homo sapiens	79-83
23227178-9	2012	In M059K cells, BPA inhibited the phosphorylation of DNA-PKcs at Ser2056 and H2AX at Ser139 in response to ionizing radiation (IR)-irradiation.	bisphenol A	16-19	H2A.X variant histone	Homo sapiens	77-81
23028696-5	2012	Decreases in doxorubicin fluorescence lifetimes were found to be concurrent with increases in phosphorylation of H2AX (an immediate signal of DNA double-strand breakage), but preceded activation of caspase-3 (a late signature of apoptosis) by more than 150 minutes.	Doxorubicin	13-24	H2A.X variant histone	Homo sapiens	113-117
20697895-2	2012	In the apoptosis assay, resveratrol increased TUNEL-positive cells and stimulated H2A.X phosphorylation.	Resveratrol	24-35	H2A.X variant histone	Homo sapiens	82-87
21917453-4	2011	Amentoflavone, a well known biflavonoid, inhibited the increase of Lamin A or phospho-H2AX protein in dose dependent manner which was induced by UVB irradiation, and also protected nuclear aberration dramatically.	amentoflavone	0-13	H2A.X variant histone	Homo sapiens	86-90
21917453-4	2011	Amentoflavone, a well known biflavonoid, inhibited the increase of Lamin A or phospho-H2AX protein in dose dependent manner which was induced by UVB irradiation, and also protected nuclear aberration dramatically.	Biflavonoids	28-39	H2A.X variant histone	Homo sapiens	86-90
22037398-4	2011	Cisplatin and gamma-irradiation activated the DNA damage response in hMSCs, including induction of p53 and p21, and activation of PI3 kinase-related protein kinase (PIKK)-dependent phosphorylation of histone H2AX on serine 139, and replication protein A2 on serine4/serine8.	Cisplatin	0-9	H2A.X variant histone	Homo sapiens	208-212
22037398-4	2011	Cisplatin and gamma-irradiation activated the DNA damage response in hMSCs, including induction of p53 and p21, and activation of PI3 kinase-related protein kinase (PIKK)-dependent phosphorylation of histone H2AX on serine 139, and replication protein A2 on serine4/serine8.	Serine	216-222	H2A.X variant histone	Homo sapiens	208-212
22037398-4	2011	Cisplatin and gamma-irradiation activated the DNA damage response in hMSCs, including induction of p53 and p21, and activation of PI3 kinase-related protein kinase (PIKK)-dependent phosphorylation of histone H2AX on serine 139, and replication protein A2 on serine4/serine8.	serine4	258-265	H2A.X variant histone	Homo sapiens	208-212
22037398-4	2011	Cisplatin and gamma-irradiation activated the DNA damage response in hMSCs, including induction of p53 and p21, and activation of PI3 kinase-related protein kinase (PIKK)-dependent phosphorylation of histone H2AX on serine 139, and replication protein A2 on serine4/serine8.	serine8	266-273	H2A.X variant histone	Homo sapiens	208-212
21674128-3	2011	The pattern of DNA damage checkpoint activation in bolus 5-FU-treated HT29 (TP53-deficient/MMR-proficient) cultures suggested SSB formation (CHEK1 activation) followed by DSB formation (CHEK2 activation and increased phospho-H2AX levels), but no cell death suggested that DNA repair capacity was not overwhelmed.	Fluorouracil	57-61	H2A.X variant histone	Homo sapiens	225-229
21674128-8	2011	Overall, activation of ATM, CHEK1 and/or CHEK2 and phospho-H2AX levels reflected the nature of 5-FU-induced DNA damage and indi-cated when DNA damage was significant (5-FU-dose-dependent).	Fluorouracil	95-99	H2A.X variant histone	Homo sapiens	59-63
21674128-8	2011	Overall, activation of ATM, CHEK1 and/or CHEK2 and phospho-H2AX levels reflected the nature of 5-FU-induced DNA damage and indi-cated when DNA damage was significant (5-FU-dose-dependent).	Fluorouracil	167-171	H2A.X variant histone	Homo sapiens	59-63
21676867-3	2011	In mammalian cells, a key component in this network is H2AX, which becomes rapidly phosphorylated at Ser(139) (gamma-H2AX) at DSBs.	Serine	101-104	H2A.X variant histone	Homo sapiens	55-59
21676867-3	2011	In mammalian cells, a key component in this network is H2AX, which becomes rapidly phosphorylated at Ser(139) (gamma-H2AX) at DSBs.	Serine	101-104	H2A.X variant histone	Homo sapiens	117-121
21676867-5	2011	RNF2-BMI1 interacts with H2AX in a DNA damage-dependent manner and is required for monoubiquitination of H2AX at Lys(119)/Lys(120).	Lysine	113-116	H2A.X variant histone	Homo sapiens	25-29
21676867-5	2011	RNF2-BMI1 interacts with H2AX in a DNA damage-dependent manner and is required for monoubiquitination of H2AX at Lys(119)/Lys(120).	Lysine	113-116	H2A.X variant histone	Homo sapiens	105-109
21676867-5	2011	RNF2-BMI1 interacts with H2AX in a DNA damage-dependent manner and is required for monoubiquitination of H2AX at Lys(119)/Lys(120).	Lysine	122-125	H2A.X variant histone	Homo sapiens	25-29
21676867-5	2011	RNF2-BMI1 interacts with H2AX in a DNA damage-dependent manner and is required for monoubiquitination of H2AX at Lys(119)/Lys(120).	Lysine	122-125	H2A.X variant histone	Homo sapiens	105-109
21676867-6	2011	As a functional consequence, we show that the H2AX K120R mutant abolishes H2AX monoubiquitination, impairs the recruitment of p-ATM (Ser(1981)) to DSBs, and thereby reduces the formation of gamma-H2AX and the recruitment of MDC1 to DNA damage sites.	Serine	133-136	H2A.X variant histone	Homo sapiens	46-50
21676867-6	2011	As a functional consequence, we show that the H2AX K120R mutant abolishes H2AX monoubiquitination, impairs the recruitment of p-ATM (Ser(1981)) to DSBs, and thereby reduces the formation of gamma-H2AX and the recruitment of MDC1 to DNA damage sites.	Serine	133-136	H2A.X variant histone	Homo sapiens	74-78
21676867-6	2011	As a functional consequence, we show that the H2AX K120R mutant abolishes H2AX monoubiquitination, impairs the recruitment of p-ATM (Ser(1981)) to DSBs, and thereby reduces the formation of gamma-H2AX and the recruitment of MDC1 to DNA damage sites.	Serine	133-136	H2A.X variant histone	Homo sapiens	74-78
21676867-6	2011	As a functional consequence, we show that the H2AX K120R mutant abolishes H2AX monoubiquitination, impairs the recruitment of p-ATM (Ser(1981)) to DSBs, and thereby reduces the formation of gamma-H2AX and the recruitment of MDC1 to DNA damage sites.	dsbs	147-151	H2A.X variant histone	Homo sapiens	46-50
21566653-7	2011	Treatment with wortmannin decreased phosphorylation of H2AX and suggests phosphoinositide (PI) 3-kinases and/or PI3-kinase-like family members underlie the presence of gammaH2AX foci in MM cells.	Wortmannin	15-25	H2A.X variant histone	Homo sapiens	55-59
21566653-7	2011	Treatment with wortmannin decreased phosphorylation of H2AX and suggests phosphoinositide (PI) 3-kinases and/or PI3-kinase-like family members underlie the presence of gammaH2AX foci in MM cells.	gammah2ax	168-177	H2A.X variant histone	Homo sapiens	55-59
21624350-6	2011	Moreover, when the free radical (ROS) generating capacity of the compounds was studied by 2",7"-dichlorofluorescein-diacetate assay using flow cytometry, we found that a known antioxidant N-acetyl-cysteine almost completely abrogated the H2AX((S139)) phosphorylations and the caspase 3 cleavage and activation.	Free Radicals	19-31	H2A.X variant histone	Homo sapiens	238-242
21546556-4	2011	The consequence of this is the formation of DNA DSBs, as demonstrated by pulsed-field gel electrophoresis and H2AX phosphorylation.	dsbs	48-52	H2A.X variant histone	Homo sapiens	110-114
21693595-9	2011	Reintroduction of histone H2AX in miR-138 overexpressing cells attenuated miR-138-mediated sensitization to cisplatin and camptothecin.	mir-138	34-41	H2A.X variant histone	Homo sapiens	18-30
21693595-9	2011	Reintroduction of histone H2AX in miR-138 overexpressing cells attenuated miR-138-mediated sensitization to cisplatin and camptothecin.	mir-138	74-81	H2A.X variant histone	Homo sapiens	18-30
21693595-9	2011	Reintroduction of histone H2AX in miR-138 overexpressing cells attenuated miR-138-mediated sensitization to cisplatin and camptothecin.	Cisplatin	108-117	H2A.X variant histone	Homo sapiens	18-30
21693595-9	2011	Reintroduction of histone H2AX in miR-138 overexpressing cells attenuated miR-138-mediated sensitization to cisplatin and camptothecin.	Camptothecin	122-134	H2A.X variant histone	Homo sapiens	18-30
21624350-6	2011	Moreover, when the free radical (ROS) generating capacity of the compounds was studied by 2",7"-dichlorofluorescein-diacetate assay using flow cytometry, we found that a known antioxidant N-acetyl-cysteine almost completely abrogated the H2AX((S139)) phosphorylations and the caspase 3 cleavage and activation.	ros	33-36	H2A.X variant histone	Homo sapiens	238-242
21624350-6	2011	Moreover, when the free radical (ROS) generating capacity of the compounds was studied by 2",7"-dichlorofluorescein-diacetate assay using flow cytometry, we found that a known antioxidant N-acetyl-cysteine almost completely abrogated the H2AX((S139)) phosphorylations and the caspase 3 cleavage and activation.	Acetylcysteine	188-205	H2A.X variant histone	Homo sapiens	238-242
21680038-9	2011	We propose a model whereby DSBs induce chromatin modification at sites of DNA damage which are tracked by the ATM substrates gamma H2AX and 53BP1(Ser25) in a mechanism distinct from p53-mediated cell cycle arrest.	dsbs	27-31	H2A.X variant histone	Homo sapiens	131-135
21371266-3	2011	It was shown that, like cDDP, Pd(2) -Spm triggers phosphorylation of H2AX, indicating that this compound damages DNA.	Cisplatin	24-28	H2A.X variant histone	Homo sapiens	69-73
21371266-3	2011	It was shown that, like cDDP, Pd(2) -Spm triggers phosphorylation of H2AX, indicating that this compound damages DNA.	pd(2)	30-35	H2A.X variant histone	Homo sapiens	69-73
21367753-6	2011	The expression level of survivin was decreased in rapamycin pre-treatment glioblastoma cells followed by radiation; meanwhile, the phosphorylation of H2A histone family member X (H2AX) at serine-139 (gamma-H2AX) was increased.	Serine	188-194	H2A.X variant histone	Homo sapiens	150-177
21549309-7	2011	These data elucidate the molecular events that are required for 53BP1 to maintain genomic stability and point to a model wherein 53BP1 and H2AX cooperate to repress resection of DSBs.	dsbs	178-182	H2A.X variant histone	Homo sapiens	139-143
21367753-6	2011	The expression level of survivin was decreased in rapamycin pre-treatment glioblastoma cells followed by radiation; meanwhile, the phosphorylation of H2A histone family member X (H2AX) at serine-139 (gamma-H2AX) was increased.	Serine	188-194	H2A.X variant histone	Homo sapiens	179-183
21505975-0	2011	Expression of histone H2AX phosphorylation and its potential to modulate adriamycin resistance in K562/A02 cell line.	Doxorubicin	73-83	H2A.X variant histone	Homo sapiens	14-26
20888899-0	2011	Benzo[a]pyrene induces complex H2AX phosphorylation patterns by multiple kinases including ATM, ATR, and DNA-PK.	Benzo(a)pyrene	0-14	H2A.X variant histone	Homo sapiens	31-35
21372041-5	2011	Prior to the induction of apoptosis, CDDO-Im induced DNA damage and the phosphorylation of H2AX followed by activation of the DNA damage response.	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	37-44	H2A.X variant histone	Homo sapiens	91-95
21216934-7	2011	Moreover, under the conditions of nonstress and adriamycin-induced genotoxic stress, attenuation of p53R2 in KB cells significantly increased phosphorylated H2AX, which indicates that attenuation of p53R2 may enhance DNA damage induced by adriamycin.	Doxorubicin	48-58	H2A.X variant histone	Homo sapiens	157-161
21216934-7	2011	Moreover, under the conditions of nonstress and adriamycin-induced genotoxic stress, attenuation of p53R2 in KB cells significantly increased phosphorylated H2AX, which indicates that attenuation of p53R2 may enhance DNA damage induced by adriamycin.	Doxorubicin	239-249	H2A.X variant histone	Homo sapiens	157-161
21347609-0	2011	Premature chromosome condensation induced by caffeine, 2-aminopurine, staurosporine and sodium metavanadate in S-phase arrested HeLa cells is associated with a decrease in Chk1 phosphorylation, formation of phospho-H2AX and minor cytoskeletal rearrangements.	2-Aminopurine	55-68	H2A.X variant histone	Homo sapiens	215-219
21347609-0	2011	Premature chromosome condensation induced by caffeine, 2-aminopurine, staurosporine and sodium metavanadate in S-phase arrested HeLa cells is associated with a decrease in Chk1 phosphorylation, formation of phospho-H2AX and minor cytoskeletal rearrangements.	Staurosporine	70-83	H2A.X variant histone	Homo sapiens	215-219
21347609-0	2011	Premature chromosome condensation induced by caffeine, 2-aminopurine, staurosporine and sodium metavanadate in S-phase arrested HeLa cells is associated with a decrease in Chk1 phosphorylation, formation of phospho-H2AX and minor cytoskeletal rearrangements.	Vanadates	88-107	H2A.X variant histone	Homo sapiens	215-219
21134073-6	2011	Combined treatment of isoflavones and curcumin additively suppressed cellular proliferation and induced phosphorylation of ATM, histone H2AX, Chk2 and p53.	Isoflavones	22-33	H2A.X variant histone	Homo sapiens	136-140
21134073-6	2011	Combined treatment of isoflavones and curcumin additively suppressed cellular proliferation and induced phosphorylation of ATM, histone H2AX, Chk2 and p53.	Curcumin	38-46	H2A.X variant histone	Homo sapiens	136-140
21263216-4	2011	BrdU photolysis resulted in well-controlled, dose- dependent generation of DSBs equivalent to radiation doses between 0.2 - 20 Gy, as determined by pulsed-field gel electrophoresis, and accompanied by dose-dependent ATM (ser-1981), H2AX (ser-139), Chk2 (thr-68), and p53 (ser-15) phosphorylation.	dsbs	75-79	H2A.X variant histone	Homo sapiens	232-236
21263216-4	2011	BrdU photolysis resulted in well-controlled, dose- dependent generation of DSBs equivalent to radiation doses between 0.2 - 20 Gy, as determined by pulsed-field gel electrophoresis, and accompanied by dose-dependent ATM (ser-1981), H2AX (ser-139), Chk2 (thr-68), and p53 (ser-15) phosphorylation.	Serine	221-224	H2A.X variant histone	Homo sapiens	232-236
21183548-1	2011	Upon DNA double-strand break (DSB) formation, hundreds of H2AX molecules in the chromatin flanking the break site are phosphorylated on serine residue 139, termed gamma-H2AX, so that virtually every DSB site in a nucleus can be visualised within 10 min of its formation using an antibody to gamma-H2AX.	Serine	136-142	H2A.X variant histone	Homo sapiens	58-62
21183548-1	2011	Upon DNA double-strand break (DSB) formation, hundreds of H2AX molecules in the chromatin flanking the break site are phosphorylated on serine residue 139, termed gamma-H2AX, so that virtually every DSB site in a nucleus can be visualised within 10 min of its formation using an antibody to gamma-H2AX.	Serine	136-142	H2A.X variant histone	Homo sapiens	169-173
21183548-1	2011	Upon DNA double-strand break (DSB) formation, hundreds of H2AX molecules in the chromatin flanking the break site are phosphorylated on serine residue 139, termed gamma-H2AX, so that virtually every DSB site in a nucleus can be visualised within 10 min of its formation using an antibody to gamma-H2AX.	Serine	136-142	H2A.X variant histone	Homo sapiens	169-173
20888899-9	2011	Taken together, these data suggest that BaP alone can induce H2AX phosphorylation in certain cell systems, and that members of the PI3K family, including ATM, ATR, and DNA-PK can participate in the phosphorylation of H2AX in the various cell types.	Benzo(a)pyrene	40-43	H2A.X variant histone	Homo sapiens	61-65
21074544-4	2011	Furthermore, we find that DRB-induced transcriptional stress is associated with formation of the nuclear foci of the phosphorylated form of H2AX (gammaH2AX).	Dichlororibofuranosylbenzimidazole	26-29	H2A.X variant histone	Homo sapiens	140-144
21184737-0	2011	Ectopic expression of H2AX protein promotes TrkA-induced cell death via modulation of TrkA tyrosine-490 phosphorylation and JNK activity upon DNA damage.	Tyrosine	91-99	H2A.X variant histone	Homo sapiens	22-26
21184737-3	2011	We found that TrkA co-localizes with ectopically expressed GFP-H2AX proteins in the cytoplasm, especially at the juxta-nuclear membranes, which supports our previous results about a functional connection between TrkA and gammaH2AX in TrkA-induced cell death.	gammah2ax	221-230	H2A.X variant histone	Homo sapiens	63-67
21184737-5	2011	Moreover, ectopic expression of H2AX activated TrkA-mediated signal pathways via up-regulation of TrkA tyrosine-490 phosphorylation.	Tyrosine	103-111	H2A.X variant histone	Homo sapiens	32-36
21184737-6	2011	In addition, suppression of TrkA tyrosine-490 phosphorylation under a certain condition was removed by ectopic expression of H2AX, indicating a functional role of H2AX in the maintenance of TrkA activity.	Tyrosine	33-41	H2A.X variant histone	Homo sapiens	125-129
21184737-6	2011	In addition, suppression of TrkA tyrosine-490 phosphorylation under a certain condition was removed by ectopic expression of H2AX, indicating a functional role of H2AX in the maintenance of TrkA activity.	Tyrosine	33-41	H2A.X variant histone	Homo sapiens	163-167
21261999-4	2011	Radiation exposure often results in the formation of DNA double-strand breaks, which are marked by the induction of H2AX phosphorylation to generate gammaH2AX.	gammah2ax	149-158	H2A.X variant histone	Homo sapiens	116-120
21283714-5	2011	We have utilized gamma-H2AX to detect DNA damage induced by non-thermal plasma and found that it is initiated by production of active neutral species that most likely induce formation of organic peroxides in cell medium.	Peroxides	195-204	H2A.X variant histone	Homo sapiens	23-27
21283714-6	2011	Phosphorylation of H2AX following non-thermal plasma treatment is ATR dependent and ATM independent, suggesting that plasma treatment may lead to replication arrest or formation of single-stranded DNA breaks; however, plasma does not lead to formation of bulky adducts/thymine dimers.	Thymine	269-276	H2A.X variant histone	Homo sapiens	19-23
21057933-2	2011	DSBs can be detected in the nuclei of cultured cells and tissues with an antibody to H2AX phosphorylated on serine residue 139 (gamma-H2AX).	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	0-4	H2A.X variant histone	Homo sapiens	85-89
20840867-3	2011	This resulted in reduction of HU-induced phosphorylation of CHK1 S345 (serine 345), p53 S15, and H2AX S139.	Hydroxyurea	30-32	H2A.X variant histone	Homo sapiens	97-101
21057933-2	2011	DSBs can be detected in the nuclei of cultured cells and tissues with an antibody to H2AX phosphorylated on serine residue 139 (gamma-H2AX).	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	0-4	H2A.X variant histone	Homo sapiens	134-138
21057933-2	2011	DSBs can be detected in the nuclei of cultured cells and tissues with an antibody to H2AX phosphorylated on serine residue 139 (gamma-H2AX).	Serine	108-114	H2A.X variant histone	Homo sapiens	85-89
21057933-2	2011	DSBs can be detected in the nuclei of cultured cells and tissues with an antibody to H2AX phosphorylated on serine residue 139 (gamma-H2AX).	Serine	108-114	H2A.X variant histone	Homo sapiens	134-138
20921231-3	2010	Here we show that MST1 induces apoptotic chromatin condensation through its phosphorylation of histone H2AX at Ser-139.	Serine	111-114	H2A.X variant histone	Homo sapiens	103-107
21938931-2	2011	One of the earliest response of cells to DSBs formation is phosphorylation by 139 serine of core variant histone H2AX in megabase chromatin domains around DSB (gamma-H2AX), which amplify signal and makes it possible to identify even one DSB in genome.	dsbs	41-45	H2A.X variant histone	Homo sapiens	105-117
21938931-2	2011	One of the earliest response of cells to DSBs formation is phosphorylation by 139 serine of core variant histone H2AX in megabase chromatin domains around DSB (gamma-H2AX), which amplify signal and makes it possible to identify even one DSB in genome.	Serine	82-88	H2A.X variant histone	Homo sapiens	105-117
20921231-4	2010	During etoposide-induced apoptosis in Jurkat cells, the cleavage of MST1 directly corresponded with strong H2AX phosphorylation.	Etoposide	7-16	H2A.X variant histone	Homo sapiens	107-111
20921231-6	2010	Western blot and kinase assay results with a mutant S139A H2AX confirmed that MST1 phosphorylates H2AX at Ser-139.	Serine	106-109	H2A.X variant histone	Homo sapiens	58-62
20921231-6	2010	Western blot and kinase assay results with a mutant S139A H2AX confirmed that MST1 phosphorylates H2AX at Ser-139.	Serine	106-109	H2A.X variant histone	Homo sapiens	98-102
21035408-2	2010	One of the most discernible hallmarks of the cellular response to DSBs is the accumulation and local concentration of a plethora of DNA damage signaling and repair proteins in the vicinity of the lesion, initiated by ATM-mediated phosphorylation of H2AX (gamma-H2AX) and culminating in the generation of distinct nuclear compartments, so-called Ionizing Radiation-Induced Foci (IRIF).	dsbs	66-70	H2A.X variant histone	Homo sapiens	249-253
20921231-9	2010	The caspase-3 inhibitor benzyloxycarbonyl-DEVD-fluoromethyl ketone (Z-DEVD-fmk) attenuates phosphorylation of H2AX by MST1 but cannot inhibit MST1-NT-induced histone H2AX phosphorylation, indicating that cleaved MST1 is responsible for H2AX phosphorylation during apoptosis.	benzyloxycarbonyl-devd-fluoromethyl ketone	24-66	H2A.X variant histone	Homo sapiens	110-114
21035408-2	2010	One of the most discernible hallmarks of the cellular response to DSBs is the accumulation and local concentration of a plethora of DNA damage signaling and repair proteins in the vicinity of the lesion, initiated by ATM-mediated phosphorylation of H2AX (gamma-H2AX) and culminating in the generation of distinct nuclear compartments, so-called Ionizing Radiation-Induced Foci (IRIF).	dsbs	66-70	H2A.X variant histone	Homo sapiens	255-265
20921231-9	2010	The caspase-3 inhibitor benzyloxycarbonyl-DEVD-fluoromethyl ketone (Z-DEVD-fmk) attenuates phosphorylation of H2AX by MST1 but cannot inhibit MST1-NT-induced histone H2AX phosphorylation, indicating that cleaved MST1 is responsible for H2AX phosphorylation during apoptosis.	benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone	68-78	H2A.X variant histone	Homo sapiens	110-114
20921231-9	2010	The caspase-3 inhibitor benzyloxycarbonyl-DEVD-fluoromethyl ketone (Z-DEVD-fmk) attenuates phosphorylation of H2AX by MST1 but cannot inhibit MST1-NT-induced histone H2AX phosphorylation, indicating that cleaved MST1 is responsible for H2AX phosphorylation during apoptosis.	benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone	68-78	H2A.X variant histone	Homo sapiens	166-170
20921231-9	2010	The caspase-3 inhibitor benzyloxycarbonyl-DEVD-fluoromethyl ketone (Z-DEVD-fmk) attenuates phosphorylation of H2AX by MST1 but cannot inhibit MST1-NT-induced histone H2AX phosphorylation, indicating that cleaved MST1 is responsible for H2AX phosphorylation during apoptosis.	benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone	68-78	H2A.X variant histone	Homo sapiens	166-170
20921231-10	2010	Histone H2AX phosphorylation and DNA fragmentation were suppressed in MST1 knockdown Jurkat cells after etoposide treatment.	Etoposide	104-113	H2A.X variant histone	Homo sapiens	8-12
21077998-9	2010	Treatment with OA and (-)-sesamin induced p53-independent DNA damage responses in NSCLC cells, including G(1) /S checkpoint activation and apoptosis, as evidenced by phosphorylation of checkpoint proteins (H2AX, Nbs1, and Chk2), caspase-3 cleavage, and sub-G(1) accumulation.	sesamin	22-33	H2A.X variant histone	Homo sapiens	206-210
20832459-7	2010	Concomitantly the genotoxicity of these PAHs was investigated in different cell lines, using a new genotoxic assay (H2AX) in 96-well plates.	Polycyclic Aromatic Hydrocarbons	40-44	H2A.X variant histone	Homo sapiens	116-120
20564478-9	2010	This might be a DNA damage response as indicated by Ser-139 phosphorylation of histine H2A.X.	Serine	52-55	H2A.X variant histone	Homo sapiens	87-92
20978201-4	2010	IR, doxorubicin, and etoposide induced the phosphorylation of H2A.X on Ser(139) (gammaH2AX) and DNA damage foci formation.	Doxorubicin	4-15	H2A.X variant histone	Homo sapiens	62-67
20978201-4	2010	IR, doxorubicin, and etoposide induced the phosphorylation of H2A.X on Ser(139) (gammaH2AX) and DNA damage foci formation.	Etoposide	21-30	H2A.X variant histone	Homo sapiens	62-67
20978201-4	2010	IR, doxorubicin, and etoposide induced the phosphorylation of H2A.X on Ser(139) (gammaH2AX) and DNA damage foci formation.	Serine	71-74	H2A.X variant histone	Homo sapiens	62-67
20978201-6	2010	The attenuated gammaH2AX response seems to result from low levels of total H2A.X in the luminal cells.	gammah2ax	15-24	H2A.X variant histone	Homo sapiens	75-80
20655390-2	2010	Our previous paper showed that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL) induced phosphorylation of histone H2AX (gamma-H2AX) [T. Toyooka, G. Ohnuki, Y. Ibuki, Solar-simulated light-exposed benzo[a]pyrene induces phosphorylation of histone H2AX, Mutat.	Benzo(a)pyrene	31-45	H2A.X variant histone	Homo sapiens	118-130
20506293-3	2010	In the present study, we investigate the possible roles of securin and gamma-H2AX in baicalein-induced cancer cell death.	baicalein	85-94	H2A.X variant histone	Homo sapiens	77-81
20506293-10	2010	Additionally, blockade of the AKT pathway by treatment with wortmannin or AKT shRNA lowered the levels of gamma-H2AX and enhanced cytotoxicity in baicalein-treated cells.	Wortmannin	60-70	H2A.X variant histone	Homo sapiens	112-116
20667493-6	2010	A significant increase in the phosphorylation of DNA damage response proteins (ATM, ATR, H2AX and p53) in OHBI in comparison to controls suggested that OHBI induces DNA damage in peripheral blood lymphocytes and elicit a PI3 kinase mediated cellular response.	ohbi	106-110	H2A.X variant histone	Homo sapiens	89-93
20667493-6	2010	A significant increase in the phosphorylation of DNA damage response proteins (ATM, ATR, H2AX and p53) in OHBI in comparison to controls suggested that OHBI induces DNA damage in peripheral blood lymphocytes and elicit a PI3 kinase mediated cellular response.	ohbi	152-156	H2A.X variant histone	Homo sapiens	89-93
20637859-8	2010	Knockdown of either kinases significantly reduced ATM activation in response to etoposide treatment, and thereby attenuated phosphorylation of the ATM substrates, including the S139 of H2AX (gammaH2AX), p53 S15, and CHK2 T68.	Etoposide	80-89	H2A.X variant histone	Homo sapiens	185-189
20732333-4	2010	MATERIALS AND METHODS: We used immunocytochemical methods to measure the accumulation of phosphorylated H2AX (gammaH2AX) foci following ionizing radiation (IR) in patient-derived lymphoblastoid cells exposed to methylproamine.	methylproamine	211-225	H2A.X variant histone	Homo sapiens	104-108
20655390-0	2010	UVB in solar-simulated light causes formation of BaP-photoproducts capable of generating phosphorylated histone H2AX.	Benzo(a)pyrene	49-52	H2A.X variant histone	Homo sapiens	104-116
20655390-2	2010	Our previous paper showed that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL) induced phosphorylation of histone H2AX (gamma-H2AX) [T. Toyooka, G. Ohnuki, Y. Ibuki, Solar-simulated light-exposed benzo[a]pyrene induces phosphorylation of histone H2AX, Mutat.	Benzo(a)pyrene	31-45	H2A.X variant histone	Homo sapiens	250-262
20655390-2	2010	Our previous paper showed that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL) induced phosphorylation of histone H2AX (gamma-H2AX) [T. Toyooka, G. Ohnuki, Y. Ibuki, Solar-simulated light-exposed benzo[a]pyrene induces phosphorylation of histone H2AX, Mutat.	Benzo(a)pyrene	47-50	H2A.X variant histone	Homo sapiens	118-130
20655390-2	2010	Our previous paper showed that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL) induced phosphorylation of histone H2AX (gamma-H2AX) [T. Toyooka, G. Ohnuki, Y. Ibuki, Solar-simulated light-exposed benzo[a]pyrene induces phosphorylation of histone H2AX, Mutat.	Benzo(a)pyrene	47-50	H2A.X variant histone	Homo sapiens	250-262
20655390-2	2010	Our previous paper showed that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL) induced phosphorylation of histone H2AX (gamma-H2AX) [T. Toyooka, G. Ohnuki, Y. Ibuki, Solar-simulated light-exposed benzo[a]pyrene induces phosphorylation of histone H2AX, Mutat.	Benzo(a)pyrene	208-222	H2A.X variant histone	Homo sapiens	118-130
20643785-5	2010	Acute exposure to trichostatin A resulted in marked inhibition of cell proliferation, an increase in the proportion of G(2)-M cells, activation of H2A.X, and subsequent induction of apoptosis in the majority of cell lines.	trichostatin A	18-32	H2A.X variant histone	Homo sapiens	147-152
20823146-2	2010	Because DSBs induce the phosphorylation of histone H2AX (gammaH2AX) in the chromatin flanking the break site, an antibody directed against gammaH2AX can be employed to measure DNA damage levels before and after patient treatment.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	8-12	H2A.X variant histone	Homo sapiens	43-55
20703100-1	2010	Histone H2AX phosphorylation on a C-terminal serine residue to form "gamma-H2AX" is a critical early event in the chromatin response to chromosomal DNA double strand breaks in eukaryotes.	Serine	45-51	H2A.X variant histone	Homo sapiens	0-12
20703100-1	2010	Histone H2AX phosphorylation on a C-terminal serine residue to form "gamma-H2AX" is a critical early event in the chromatin response to chromosomal DNA double strand breaks in eukaryotes.	Serine	45-51	H2A.X variant histone	Homo sapiens	8-12
20703100-2	2010	In mammalian cells, gamma-H2AX is formed when H2AX is phosphorylated on serine 139 by ATM or by other DNA damage response kinases.	Serine	72-78	H2A.X variant histone	Homo sapiens	26-30
20703100-2	2010	In mammalian cells, gamma-H2AX is formed when H2AX is phosphorylated on serine 139 by ATM or by other DNA damage response kinases.	Serine	72-78	H2A.X variant histone	Homo sapiens	46-50
20936109-1	2010	Following genotoxic stress, the histone H2AX becomes phosphorylated at serine 139 by the ATM/ATR family of kinases.	Serine	71-77	H2A.X variant histone	Homo sapiens	40-44
20936109-7	2010	We found that H2AX is ubiquitinated at lysines 119 and 119 in vivo and that blockage of 26S proteasome function stabilizes gamma-H2AX levels within cells.	Lysine	39-46	H2A.X variant histone	Homo sapiens	14-18
20493860-1	2010	Phosphorylation of histone variant H2AX at serine 139, named gammaH2AX, has been widely used as a sensitive marker for DNA double-strand breaks (DSBs).	Serine	43-49	H2A.X variant histone	Homo sapiens	35-39
20660387-0	2010	In vivo formation of gamma-H2AX and 53BP1 DNA repair foci in blood cells after radioiodine therapy of differentiated thyroid cancer.	Iodine-131	79-90	H2A.X variant histone	Homo sapiens	21-31
20472715-8	2010	While in GBM cells treated with the chemotherapeutic agent 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU), HDMX appears to stabilize p53 and promote phosphorylation of the DNA double-stranded break repair protein H2AX, up-regulate the DNA repair gene VPX, stimulate DNA repair, and confer resistance to BCNU.	Carmustine	59-95	H2A.X variant histone	Homo sapiens	210-214
20736911-1	2010	An early molecular response to DNA double-strand breaks (DSBs) is phosphorylation of the Ser-139 residue within the terminal SQEY motif of the histone H2AX.	Serine	89-92	H2A.X variant histone	Homo sapiens	151-155
20736911-3	2010	The phosphorylated form of H2AX, referred to as gammaH2AX, spreads to adjacent regions of chromatin from the site of the DSB, forming discrete foci, which are easily visualized by immunofluorescence microscopy.	gammah2ax	48-57	H2A.X variant histone	Homo sapiens	27-31
19783790-3	2010	One of the earliest responses to DNA DSBs is the phosphorylation of a histone, H2AX, at serine 139 (gamma-H2AX), which can be detected by a fluorescent antibody.	dsbs	37-41	H2A.X variant histone	Homo sapiens	79-83
19783790-3	2010	One of the earliest responses to DNA DSBs is the phosphorylation of a histone, H2AX, at serine 139 (gamma-H2AX), which can be detected by a fluorescent antibody.	dsbs	37-41	H2A.X variant histone	Homo sapiens	106-110
19783790-3	2010	One of the earliest responses to DNA DSBs is the phosphorylation of a histone, H2AX, at serine 139 (gamma-H2AX), which can be detected by a fluorescent antibody.	Serine	88-94	H2A.X variant histone	Homo sapiens	79-83
19783790-3	2010	One of the earliest responses to DNA DSBs is the phosphorylation of a histone, H2AX, at serine 139 (gamma-H2AX), which can be detected by a fluorescent antibody.	Serine	88-94	H2A.X variant histone	Homo sapiens	106-110
20679231-6	2010	In transformed cells, phosphorylated H2AX (gammaH2AX), a marker of DNA DSBs, levels increased with continued culture with vorinostat, whereas in normal cells, this marker decreased with time.	Vorinostat	122-132	H2A.X variant histone	Homo sapiens	37-41
20811597-4	2010	The formation of DSBs triggers activation of many factors, including phosphorylation of the histone variant H2AX, producing gammaH2AX.	dsbs	17-21	H2A.X variant histone	Homo sapiens	108-112
20492564-4	2010	Acute UVB irradiation of human keratinocytes increased the phosphorylation of H2AX in a dose-dependent manner; two types of gammaH2AX response were observed either in vitro or in vivo.	gammah2ax	124-133	H2A.X variant histone	Homo sapiens	78-82
20488183-0	2010	Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway.	Lysine	23-29	H2A.X variant histone	Homo sapiens	15-19
20488183-2	2010	Here, we report that H2AX is constitutively acetylated on lysine 36 (H2AXK36Ac) by the CBP/p300 acetyltransferases.	Lysine	58-64	H2A.X variant histone	Homo sapiens	21-25
20488183-2	2010	Here, we report that H2AX is constitutively acetylated on lysine 36 (H2AXK36Ac) by the CBP/p300 acetyltransferases.	h2axk36ac	69-78	H2A.X variant histone	Homo sapiens	21-25
20360685-4	2010	We show here that, through its C-terminal proline-rich binding domain (PBD, residues 543-559), AIF associates in the nucleus with histone H2AX.	Proline	42-49	H2A.X variant histone	Homo sapiens	138-142
20495376-2	2010	A key early event in the DNA damage response (DDR) is ATM phosphorylation of the histone variant H2AX at serine 139 at the site of the DNA break.	Serine	105-111	H2A.X variant histone	Homo sapiens	97-101
20585393-6	2010	Here we report that Cr(VI) exposure of human fibroblasts induced telomeric damage as indicated by phosphorylated H2AX (gammaH2AX) at telomeric foci.	chromium hexavalent ion	20-26	H2A.X variant histone	Homo sapiens	113-117
20460517-5	2010	On repair completion, gamma-H2AX must then be reverted to H2AX by dephosphorylation for attenuation of the DDR.	ddr	107-110	H2A.X variant histone	Homo sapiens	22-32
20460517-5	2010	On repair completion, gamma-H2AX must then be reverted to H2AX by dephosphorylation for attenuation of the DDR.	ddr	107-110	H2A.X variant histone	Homo sapiens	28-32
20224553-2	2010	Here, we show that the SWI/SNF chromatin remodelling complex, earlier known to facilitate the phosphorylation of histone H2AX at Ser-139 (S139ph) after DNA damage, binds to gamma-H2AX (the phosphorylated form of H2AX)-containing nucleosomes in S139ph-dependent manner.	Serine	129-132	H2A.X variant histone	Homo sapiens	121-125
20372780-5	2010	Treatment with CDDP and 5-FU led to phosphorylation of H2AX preferentially in S-phase cells, consistent with the induction of replication stress.	cddp	15-19	H2A.X variant histone	Homo sapiens	55-59
20372780-5	2010	Treatment with CDDP and 5-FU led to phosphorylation of H2AX preferentially in S-phase cells, consistent with the induction of replication stress.	Fluorouracil	24-28	H2A.X variant histone	Homo sapiens	55-59
20118229-1	2010	In response to DNA double strand breaks, the histone variant H2AX at the break site is phosphorylated at serine 139 by DNA damage sensor kinases such as ataxia telangiectasia-mutated, forming gamma-H2AX.	Serine	105-111	H2A.X variant histone	Homo sapiens	61-65
20118229-1	2010	In response to DNA double strand breaks, the histone variant H2AX at the break site is phosphorylated at serine 139 by DNA damage sensor kinases such as ataxia telangiectasia-mutated, forming gamma-H2AX.	Serine	105-111	H2A.X variant histone	Homo sapiens	198-202
20118229-5	2010	Here, we demonstrate that the wild-type p53-induced phosphatase 1 (WIP1) also dephosphorylates gamma-H2AX at serine 139 in vitro and in vivo.	Serine	109-115	H2A.X variant histone	Homo sapiens	101-105
20224553-2	2010	Here, we show that the SWI/SNF chromatin remodelling complex, earlier known to facilitate the phosphorylation of histone H2AX at Ser-139 (S139ph) after DNA damage, binds to gamma-H2AX (the phosphorylated form of H2AX)-containing nucleosomes in S139ph-dependent manner.	Serine	129-132	H2A.X variant histone	Homo sapiens	179-183
20224553-2	2010	Here, we show that the SWI/SNF chromatin remodelling complex, earlier known to facilitate the phosphorylation of histone H2AX at Ser-139 (S139ph) after DNA damage, binds to gamma-H2AX (the phosphorylated form of H2AX)-containing nucleosomes in S139ph-dependent manner.	Serine	129-132	H2A.X variant histone	Homo sapiens	179-183
20351298-1	2010	UV irradiation induces histone variant H2AX phosphorylated on serine 139 (gammaH2AX) foci and high levels of pan-nuclear gammaH2AX staining without foci, but the significance of this finding is still uncertain.	Serine	62-68	H2A.X variant histone	Homo sapiens	39-43
20372103-2	2010	An early response to the induction of DSBs is phosphorylation of the H2A histone variant, H2AX, at the serine-139 residue, in the highly conserved C-terminal SQEY motif, forming gammaH2AX(1).	dsbs	38-42	H2A.X variant histone	Homo sapiens	90-94
20227390-5	2010	Pretreatment with rosiglitazone also suppressed radiation-induced H2AX phosphorylation in response to DNA damage and AKT activation for cell survival; on the contrary, rosiglitazone pretreatment enhanced radiation-induced caspase-8, -9, and -3 activation and PARP cleavage in HT-29 cells.	Rosiglitazone	18-31	H2A.X variant histone	Homo sapiens	66-70
20372103-2	2010	An early response to the induction of DSBs is phosphorylation of the H2A histone variant, H2AX, at the serine-139 residue, in the highly conserved C-terminal SQEY motif, forming gammaH2AX(1).	Serine	103-109	H2A.X variant histone	Homo sapiens	90-94
20372103-2	2010	An early response to the induction of DSBs is phosphorylation of the H2A histone variant, H2AX, at the serine-139 residue, in the highly conserved C-terminal SQEY motif, forming gammaH2AX(1).	gammah2ax	178-187	H2A.X variant histone	Homo sapiens	90-94
20372103-3	2010	Following induction of DSBs, H2AX is rapidly phosphorylated by the phosphatidyl-inosito 3-kinase (PIKK) family of proteins, ataxia telangiectasia mutated (ATM), DNA-protein kinase catalytic subunit and ATM and RAD3-related (ATR)(2).	dsbs	23-27	H2A.X variant histone	Homo sapiens	29-33
20198334-6	2010	Moreover, BaF3-MIGR1 and BaF3-BCR/ABL cells were exposed to 50 microM H2O2 in the absence or presence of Apg-2 overexpression and induction of H2AX phosphorylation, the reporters of DNA damage were assessed by Western blot and immunofluorescence.	Hydrogen Peroxide	70-74	H2A.X variant histone	Homo sapiens	143-147
20198334-7	2010	Results showed that exposure to H2O2 induced H2AX phosphorylation in BaF3-MIGR1 cells, but no increase was observed in BaF3-BCR/ABL cells.	Hydrogen Peroxide	32-36	H2A.X variant histone	Homo sapiens	45-49
20004467-4	2010	BisGMA at the EC50 concentration of 0.09 mm evoked the highest rate of gamma-H2AX foci-formation that was 11-fold higher DNA DSBs as compared to the negative controls that ranged between 0.25 and 0.5gamma-H2AX foci/HGF cell.	Bisphenol A-Glycidyl Methacrylate	0-6	H2A.X variant histone	Homo sapiens	77-81
20000738-8	2010	Treatment with the DSB-inducing agent bleomycin enhanced binding of these proteins to H2AX, suggesting an active role of H2AX in coordinating the functional pathways of each protein in DNA damage recognition and repair.	Bleomycin	38-47	H2A.X variant histone	Homo sapiens	86-90
20000738-8	2010	Treatment with the DSB-inducing agent bleomycin enhanced binding of these proteins to H2AX, suggesting an active role of H2AX in coordinating the functional pathways of each protein in DNA damage recognition and repair.	Bleomycin	38-47	H2A.X variant histone	Homo sapiens	121-125
20356374-7	2010	Euchromatins respond rapidly to DSBs induced by irradiation with the phosphorylation of H2AX, gamma-H2AX, and these initiate the DSB repair process.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	32-36	H2A.X variant histone	Homo sapiens	88-92
20356374-7	2010	Euchromatins respond rapidly to DSBs induced by irradiation with the phosphorylation of H2AX, gamma-H2AX, and these initiate the DSB repair process.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	32-36	H2A.X variant histone	Homo sapiens	100-104
20356374-11	2010	RESULTS: We observed a significant number of methylated RIND-EDSBs that are retained within deacetylated chromatin and free from an immediate cellular response to DSBs, the gamma-H2AX.	rind-edsbs	56-66	H2A.X variant histone	Homo sapiens	179-183
20356374-11	2010	RESULTS: We observed a significant number of methylated RIND-EDSBs that are retained within deacetylated chromatin and free from an immediate cellular response to DSBs, the gamma-H2AX.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	62-66	H2A.X variant histone	Homo sapiens	179-183
20356374-12	2010	When cells were treated with tricostatin A (TSA) and the histones became hyperacetylated, the amount of gamma-H2AX-bound DNA increased and the retained RIND-EDSBs were rapidly repaired.	trichostatin A	29-42	H2A.X variant histone	Homo sapiens	110-114
20356374-12	2010	When cells were treated with tricostatin A (TSA) and the histones became hyperacetylated, the amount of gamma-H2AX-bound DNA increased and the retained RIND-EDSBs were rapidly repaired.	trichostatin A	44-47	H2A.X variant histone	Homo sapiens	110-114
20205745-5	2010	An increased gamma H2AX was also induced in the ATM deficient cell line AT5BIVA at 0.5 - 1.0 h after 4 Gy gamma rays, and this IR-increased gamma H2AX in ATM deficient cells was dramatically abolished by the PIKK inhibitor wortmannin and the DNA-PKcs specific inhibitor NU7026.	Wortmannin	223-233	H2A.X variant histone	Homo sapiens	19-23
20205745-5	2010	An increased gamma H2AX was also induced in the ATM deficient cell line AT5BIVA at 0.5 - 1.0 h after 4 Gy gamma rays, and this IR-increased gamma H2AX in ATM deficient cells was dramatically abolished by the PIKK inhibitor wortmannin and the DNA-PKcs specific inhibitor NU7026.	Wortmannin	223-233	H2A.X variant histone	Homo sapiens	146-150
20205745-5	2010	An increased gamma H2AX was also induced in the ATM deficient cell line AT5BIVA at 0.5 - 1.0 h after 4 Gy gamma rays, and this IR-increased gamma H2AX in ATM deficient cells was dramatically abolished by the PIKK inhibitor wortmannin and the DNA-PKcs specific inhibitor NU7026.	2-(morpholin-4-yl)benzo(h)chromen-4-one	270-276	H2A.X variant histone	Homo sapiens	19-23
20205745-5	2010	An increased gamma H2AX was also induced in the ATM deficient cell line AT5BIVA at 0.5 - 1.0 h after 4 Gy gamma rays, and this IR-increased gamma H2AX in ATM deficient cells was dramatically abolished by the PIKK inhibitor wortmannin and the DNA-PKcs specific inhibitor NU7026.	2-(morpholin-4-yl)benzo(h)chromen-4-one	270-276	H2A.X variant histone	Homo sapiens	146-150
20205745-13	2010	However, this gamma H2AX alteration associated with cell cycle progressing was remarkably suppressed in the DNA-PKcs depleted HeLa-H1 cells, while wortmannin and NU7026 could also suppress this cell cycle related phosphorylation of H2AX.	Wortmannin	147-157	H2A.X variant histone	Homo sapiens	232-236
20205745-13	2010	However, this gamma H2AX alteration associated with cell cycle progressing was remarkably suppressed in the DNA-PKcs depleted HeLa-H1 cells, while wortmannin and NU7026 could also suppress this cell cycle related phosphorylation of H2AX.	2-(morpholin-4-yl)benzo(h)chromen-4-one	162-168	H2A.X variant histone	Homo sapiens	20-24
20205745-13	2010	However, this gamma H2AX alteration associated with cell cycle progressing was remarkably suppressed in the DNA-PKcs depleted HeLa-H1 cells, while wortmannin and NU7026 could also suppress this cell cycle related phosphorylation of H2AX.	2-(morpholin-4-yl)benzo(h)chromen-4-one	162-168	H2A.X variant histone	Homo sapiens	232-236
20004467-4	2010	BisGMA at the EC50 concentration of 0.09 mm evoked the highest rate of gamma-H2AX foci-formation that was 11-fold higher DNA DSBs as compared to the negative controls that ranged between 0.25 and 0.5gamma-H2AX foci/HGF cell.	Bisphenol A-Glycidyl Methacrylate	0-6	H2A.X variant histone	Homo sapiens	205-209
20028860-3	2010	Upregulation of soluble, non-chromatin-bound histone H2AX has an important role in imatinib-induced apoptosis of GIST cells.	Imatinib Mesylate	83-91	H2A.X variant histone	Homo sapiens	45-57
20053681-1	2010	H2AX phosphorylation at serine 139 (gammaH2AX) is a sensitive indicator of both DNA damage and DNA replication stress.	Serine	24-30	H2A.X variant histone	Homo sapiens	0-4
19946169-6	2010	When applied on fibroblasts, amide functionalized SWCNTs also induce gamma H2AX foci, 3.18-fold higher than the control.	Amides	29-34	H2A.X variant histone	Homo sapiens	75-79
19903865-8	2010	HUVECs in 25 mmol/l glucose showed increased p300 production accompanied by increased binding of p300 to ET-1 and FN promoters, augmented histone acetylation, H2AX phosphorylation, activation of multiple transcription factors, and increased mRNA expression of vasoactive factors and ECM proteins.	Glucose	20-27	H2A.X variant histone	Homo sapiens	159-163
19682466-2	2010	Formation of double-strand breaks (DSBs) in DNA is followed by the rapid local phosphorylation of the C-terminal serine in the replacement histone H2AX in megabase chromatin domains around DSBs and formation of discrete nuclear foci called gammaH2AX foci.	Serine	113-119	H2A.X variant histone	Homo sapiens	139-151
20150765-2	2010	Rapid phosphorylation of the histone variant H2AX at Ser-139 to form gammaH2AX is an early cellular response to DNA double-strand breaks.	Serine	53-56	H2A.X variant histone	Homo sapiens	45-49
20150765-2	2010	Rapid phosphorylation of the histone variant H2AX at Ser-139 to form gammaH2AX is an early cellular response to DNA double-strand breaks.	gammah2ax	69-78	H2A.X variant histone	Homo sapiens	45-49
20051375-10	2010	Frondanol A5 showed growth inhibition at S and G(2)-M phase with a decrease in Cdc25c and an increase in p21(WAF1/CIP) with significant apoptosis associated with H2AX phosphorylation and caspase-2 cleavage in HCT116 cells.	frondanol a5	0-12	H2A.X variant histone	Homo sapiens	162-166
20028860-5	2010	In this study, we asked whether bortezomib-mediated inhibition of the ubiquitin-proteasome machinery could lead to upregulation of histone H2AX and GIST cell death.	Bortezomib	32-42	H2A.X variant histone	Homo sapiens	139-143
20028860-6	2010	We show that bortezomib rapidly triggers apoptosis in GIST cells through a combination of mechanisms involving H2AX upregulation and loss of KIT protein expression.	Bortezomib	13-23	H2A.X variant histone	Homo sapiens	111-115
20551639-6	2010	The accumulation of ROS correlated with increased DNA damage as evidenced by increased H2AX.	Reactive Oxygen Species	20-23	H2A.X variant histone	Homo sapiens	87-91
20448412-1	2010	Heating induces histone H2AX phosphorylation at serine 139 (gammaH2AX).	Serine	48-54	H2A.X variant histone	Homo sapiens	24-28
19913408-0	2010	Enzastaurin induces H2AX phosphorylation to regulate apoptosis via MAPK signalling in malignant glioma cells.	enzastaurin	0-11	H2A.X variant histone	Homo sapiens	20-24
19913408-5	2010	Enzastaurin treatment activated H2AX and Chk2 phosphorylation, and enhanced phosphorylation of mitogen-activated protein kinase (MAPK) family kinases.	enzastaurin	0-11	H2A.X variant histone	Homo sapiens	32-36
20448412-5	2010	To elucidate mechanisms of induction of phosphorylation of H2AX after heating, ATM/ATR inhibitor (CGK733) and DNA-PK inhibitor (NU7026) were used.	2-(morpholin-4-yl)benzo(h)chromen-4-one	128-134	H2A.X variant histone	Homo sapiens	59-63
21116096-2	2010	Because of the close association with DNA double strand break (DSB) repair, phosphorylation of the histone H2AX protein (gammaH2AX), quantified by immunodetection, has recently been used as a method to study DSB induction and repair at low and clinically relevant radiation doses.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	63-66	H2A.X variant histone	Homo sapiens	107-111
20448412-9	2010	Phosphorylation of H2AX after heating was suppressed by a combination of CGK733 and NU7026 in the culture medium in DNA-PKcs-/- cells, ATM-/- cells and in their parental cells.	2-(morpholin-4-yl)benzo(h)chromen-4-one	84-90	H2A.X variant histone	Homo sapiens	19-23
20814172-5	2010	Recently, several reports have suggested that DSBs can be induced after hyperthermia because heat-induced phosphorylated histone H2AX (gamma-H2AX) foci formation can be observed in several mammalian cell lines.	dsbs	46-50	H2A.X variant histone	Homo sapiens	121-133
19658174-3	2009	We recently reported that exposure of normal human bronchial epithelial cells (NHBEs) or A549 pulmonary carcinoma cells to CS induces the activation of ATM through its phosphorylation on Ser1981 and phosphorylation of histone H2AX on Ser139 (gammaH2AX) most likely in response to the formation of potentially carcinogenic DNA double-strand breaks (DSBs).	Cesium	123-125	H2A.X variant histone	Homo sapiens	226-230
19707781-1	2009	Upon DNA double-strand break (DSB) induction in mammals, the histone H2A variant, H2AX, becomes rapidly phosphorylated at serine 139.	Serine	122-128	H2A.X variant histone	Homo sapiens	82-86
19616017-4	2009	Human FANCC cells also showed a reduced phosphorylation of H2AX and SAPK/JNK at early time point after cisplatin treatment.	Cisplatin	103-112	H2A.X variant histone	Homo sapiens	59-63
20012577-4	2010	The most well known of these is a specific serine at the extreme C-terminus of H2AX which is phosphorylated by Phosphoinositide-3-Kinase-related protein Kinases (PIKKs) to generate the gammaH2AX mark.	Serine	43-49	H2A.X variant histone	Homo sapiens	79-83
19735649-0	2009	Oxaliplatin-induced gamma-H2AX activation via both p53-dependent and -independent pathways but is not associated with cell cycle arrest in human colorectal cancer cells.	Oxaliplatin	0-11	H2A.X variant histone	Homo sapiens	26-30
19735649-5	2009	Both phosphorylated-p53 (Ser-15) and gamma-H2AX were up-regulated and accumulated in the nuclei of p53-wild type human colorectal cancer HCT116 cells after exposure to oxaliplatin.	Oxaliplatin	168-179	H2A.X variant histone	Homo sapiens	43-47
19735649-8	2009	Furthermore, inhibition of p53 phosphorylation by pifithrin-alpha was sufficient to reduce the oxaliplatin-induced up-regulation of gamma-H2AX and apoptosis.	Oxaliplatin	95-106	H2A.X variant histone	Homo sapiens	138-142
19735649-9	2009	Oxaliplatin-induced gamma-H2AX via a p53-independent pathway but did not cause caspase-3 activation in p53-null HCT116 cells.	Oxaliplatin	0-11	H2A.X variant histone	Homo sapiens	26-30
19735649-11	2009	Taken together, these data indicate that a molecular pathway involving p53, gamma-H2AX and cell cycle arrest plays a pivotal role in the cellular response to oxaliplatin.	Oxaliplatin	158-169	H2A.X variant histone	Homo sapiens	82-86
19920191-5	2009	DSBs were detected by Western blotting and immunofluorescence for histone H2AX phosphorylation and by CometAssay.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	0-4	H2A.X variant histone	Homo sapiens	74-78
19920191-7	2009	In BAR-T cells, acid exposure resulted in ROS production and caused a time-dependent increase in levels of phospho-H2AX that continued for at least 48 h. Pretreatment with disodium 4,4"-diisothiocyanatostilbene-2,2"-disulfonate or N-acety-l-cysteine prevented the acid-induced increase in phospho-H2AX levels.	disodium 4,4"-diisothiocyanatostilbene-2,2"-disulfonate	172-227	H2A.X variant histone	Homo sapiens	115-119
19616017-3	2009	CL-V5B cells are characterized by attenuated cisplatin-induced early (2-6 h) stress response, such as phosphorylation of stress-activated protein kinases (SAPK/JNK), ATM and Rad3-related (ATR) protein kinase, histone H2AX and checkpoint kinase-1 (Chk-1).	Cisplatin	45-54	H2A.X variant histone	Homo sapiens	217-221
19787270-4	2009	TBB and DMAT treatment together with cisplatin lead to an inhibition of cisplatin-induced stress signaling (as detected by phosphorylation of JNK and H2AX).	2-ethylhexyl 2,3,4,5-tetrabromobenzoate	0-3	H2A.X variant histone	Homo sapiens	150-154
19787270-4	2009	TBB and DMAT treatment together with cisplatin lead to an inhibition of cisplatin-induced stress signaling (as detected by phosphorylation of JNK and H2AX).	Cisplatin	37-46	H2A.X variant histone	Homo sapiens	150-154
19787270-4	2009	TBB and DMAT treatment together with cisplatin lead to an inhibition of cisplatin-induced stress signaling (as detected by phosphorylation of JNK and H2AX).	Cisplatin	72-81	H2A.X variant histone	Homo sapiens	150-154
19405149-5	2009	Here I analyze H2AX phosphorylation in immunostained testis sections comparing PAS/cresyl violet counterstained, noncounterstained, and immuno-fluorescence preparations and show several waves of H2AX phosphorylation/dephosphorylation coupled to various developmental phases of spermatogonia and spermatocytes as well as to spermatid differentiation.	Protactinium	79-82	H2A.X variant histone	Homo sapiens	15-19
19405149-5	2009	Here I analyze H2AX phosphorylation in immunostained testis sections comparing PAS/cresyl violet counterstained, noncounterstained, and immuno-fluorescence preparations and show several waves of H2AX phosphorylation/dephosphorylation coupled to various developmental phases of spermatogonia and spermatocytes as well as to spermatid differentiation.	cresyl violet	83-96	H2A.X variant histone	Homo sapiens	15-19
19770593-2	2009	Phosphorylation of H2AX to form gamma-H2AX in chromatin around DNA double strand breaks (DSBs) is an early event following induction of these hazardous lesions.	dsbs	89-93	H2A.X variant histone	Homo sapiens	19-23
19770593-2	2009	Phosphorylation of H2AX to form gamma-H2AX in chromatin around DNA double strand breaks (DSBs) is an early event following induction of these hazardous lesions.	dsbs	89-93	H2A.X variant histone	Homo sapiens	38-42
19658174-6	2009	The CS-dose-dependent induction and increase in the extent of phosphorylation of ATM, Chk2, H2AX, and p53 were seen in both cell types.	Cesium	4-6	H2A.X variant histone	Homo sapiens	92-96
19658174-8	2009	The dephosphorylation of ATM, Chk2, and H2AX was seen after 2 h following CS exposure.	Cesium	74-76	H2A.X variant histone	Homo sapiens	40-44
19825992-8	2009	HCT116R cells exhibit decreased H2AX phosphorylation in response to treatment with TMZ and ABT-888 relative to parental HCT116 cells.	Temozolomide	83-86	H2A.X variant histone	Homo sapiens	32-36
19530246-6	2009	HKH40A-induced apoptosis was probably mediated by JNK-H2A.X interaction, since phospho-c-Jun and phospho-H2A.X were able to co-localize in the nucleus and to co-immuno-precipitate.	RTA 502	0-6	H2A.X variant histone	Homo sapiens	54-59
19530246-6	2009	HKH40A-induced apoptosis was probably mediated by JNK-H2A.X interaction, since phospho-c-Jun and phospho-H2A.X were able to co-localize in the nucleus and to co-immuno-precipitate.	RTA 502	0-6	H2A.X variant histone	Homo sapiens	105-110
19530246-7	2009	Furthermore, inhibition of JNK kinase activity by JNK inhibitor SP600125 abolished both HKH40A-induced H2A.X phosphorylation and apoptosis.	pyrazolanthrone	64-72	H2A.X variant histone	Homo sapiens	103-108
19530246-7	2009	Furthermore, inhibition of JNK kinase activity by JNK inhibitor SP600125 abolished both HKH40A-induced H2A.X phosphorylation and apoptosis.	RTA 502	88-94	H2A.X variant histone	Homo sapiens	103-108
19825992-8	2009	HCT116R cells exhibit decreased H2AX phosphorylation in response to treatment with TMZ and ABT-888 relative to parental HCT116 cells.	2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid	91-94	H2A.X variant histone	Homo sapiens	32-36
19351884-0	2009	Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent.	cyclo(tyrosyl-tyrosyl)	36-43	H2A.X variant histone	Homo sapiens	86-91
19713747-4	2009	We show that both cisplatin and carboplatin induce strong S-phase arrest in poleta-deficient XP30RO cells, associated with reduced expression of cyclin E and cyclin B. PIK kinase-mediated phosphorylation of Chk1, H2AX and RPA2 was strongly activated by both cisplatin and carboplatin, but phosphorylation of these proteins was induced earlier by cisplatin than by an equitoxic dose of carboplatin.	Cisplatin	18-27	H2A.X variant histone	Homo sapiens	213-217
19713747-4	2009	We show that both cisplatin and carboplatin induce strong S-phase arrest in poleta-deficient XP30RO cells, associated with reduced expression of cyclin E and cyclin B. PIK kinase-mediated phosphorylation of Chk1, H2AX and RPA2 was strongly activated by both cisplatin and carboplatin, but phosphorylation of these proteins was induced earlier by cisplatin than by an equitoxic dose of carboplatin.	Carboplatin	32-43	H2A.X variant histone	Homo sapiens	213-217
19455703-3	2009	H2AX is immediately activated by ATM in response to DNA damage and its phosphorylated form, gammaH2AX, flanks the DSB through several megabases.	gammah2ax	92-101	H2A.X variant histone	Homo sapiens	0-4
19448405-1	2009	We recently showed that histone H2AX phosphorylated on serine 139 (gamma-H2AX), a hallmark of DNA damage response (DDR), also forms early during apoptosis induced by death receptor activation.	Serine	55-61	H2A.X variant histone	Homo sapiens	24-36
19448405-1	2009	We recently showed that histone H2AX phosphorylated on serine 139 (gamma-H2AX), a hallmark of DNA damage response (DDR), also forms early during apoptosis induced by death receptor activation.	Serine	55-61	H2A.X variant histone	Homo sapiens	32-36
19448405-3	2009	During apoptosis induced by death receptors agonists (TRAIL and FasL) and staurosporine, gamma-H2AX is initiated in the nuclear periphery immediately inside the nuclear envelope while total H2AX remains distributed throughout the nucleus.	Staurosporine	74-87	H2A.X variant histone	Homo sapiens	95-99
19448405-3	2009	During apoptosis induced by death receptors agonists (TRAIL and FasL) and staurosporine, gamma-H2AX is initiated in the nuclear periphery immediately inside the nuclear envelope while total H2AX remains distributed throughout the nucleus.	Staurosporine	74-87	H2A.X variant histone	Homo sapiens	190-194
19448405-7	2009	Notably, we show here that the gamma-H2AX ring coincides with phosphorylated H2B on serine 14 (P(S14)-H2B), another histone modification associated with apoptosis.	Serine	84-90	H2A.X variant histone	Homo sapiens	37-41
19597473-4	2009	Knockdown of RB induced gamma-H2AX foci formation in non-small cell lung cancer (NSCLC) cells with wild-type RB, in association with growth inhibition and reactive oxygen species (ROS) generation, which was canceled by overexpression of miR-17-92.	Reactive Oxygen Species	155-178	H2A.X variant histone	Homo sapiens	24-34
19597473-4	2009	Knockdown of RB induced gamma-H2AX foci formation in non-small cell lung cancer (NSCLC) cells with wild-type RB, in association with growth inhibition and reactive oxygen species (ROS) generation, which was canceled by overexpression of miR-17-92.	Reactive Oxygen Species	180-183	H2A.X variant histone	Homo sapiens	24-34
19597473-5	2009	Conversely, induction of gamma-H2AX was observed in a miR-17-92-overexpressing SCLC cell line with miR-20a antisense oligonucleotides.	Oligonucleotides	117-133	H2A.X variant histone	Homo sapiens	25-35
19461054-7	2009	DHMEQ-treated cells exhibited DNA damage, as evaluated by accumulation in nuclear foci of phospho-H2AX, which was completely reversed by NAC.	dehydroxymethylepoxyquinomicin	0-5	H2A.X variant histone	Homo sapiens	98-102
19815954-0	2009	Fluoroquinolones lower constitutive H2AX and ATM phosphorylation in TK6 lymphoblastoid cells via modulation of the intracellular redox status.	Fluoroquinolones	0-16	H2A.X variant histone	Homo sapiens	36-40
19815954-3	2009	Recently, a biomarker of DNA double-strand breaks (DSBs), serine 139-phosphorylated histone H2AX (gammaH2AX), and its upstream mediator, activated PI-3-related kinase, ATM (ATM(P1981)), were shown to be constitutively expressed in cells and modulated by antioxidant treatment.	Serine	58-64	H2A.X variant histone	Homo sapiens	84-96
19815954-4	2009	Thus, both constitutive histone H2AX phosphorylation (CHP) and constitutive ATM activation (CAA) are thought to reflect a cell"s response to endogenous ROS-induced DSBs.	Reactive Oxygen Species	152-155	H2A.X variant histone	Homo sapiens	32-36
19516899-6	2009	By comparing the level of DSBs, H2AX phosphorylation and toxicity induced by etoposide and calicheamicin, we found that only 10% of etoposide-induced DSBs resulted in histone H2AX phosphorylation and toxicity.	Etoposide	132-141	H2A.X variant histone	Homo sapiens	32-36
19516899-6	2009	By comparing the level of DSBs, H2AX phosphorylation and toxicity induced by etoposide and calicheamicin, we found that only 10% of etoposide-induced DSBs resulted in histone H2AX phosphorylation and toxicity.	Etoposide	132-141	H2A.X variant histone	Homo sapiens	175-179
19516899-6	2009	By comparing the level of DSBs, H2AX phosphorylation and toxicity induced by etoposide and calicheamicin, we found that only 10% of etoposide-induced DSBs resulted in histone H2AX phosphorylation and toxicity.	dsbs	150-154	H2A.X variant histone	Homo sapiens	175-179
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	calicheamicin T	78-91	H2A.X variant histone	Homo sapiens	53-57
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	calicheamicin T	78-91	H2A.X variant histone	Homo sapiens	168-172
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	Etoposide	96-105	H2A.X variant histone	Homo sapiens	53-57
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	Etoposide	96-105	H2A.X variant histone	Homo sapiens	168-172
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	Etoposide	130-139	H2A.X variant histone	Homo sapiens	53-57
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	Etoposide	130-139	H2A.X variant histone	Homo sapiens	168-172
19516899-7	2009	There was a close match between toxicity and histone H2AX phosphorylation for calicheamicin and etoposide suggesting that the few etoposide-induced DSBs that activated H2AX phosphorylation were responsible for toxicity.	dsbs	148-152	H2A.X variant histone	Homo sapiens	168-172
19516899-8	2009	CONCLUSIONS/SIGNIFICANCE: These results show that only 0.3% of all strand breaks produced by etoposide activate H2AX phosphorylation and suggests that over 99% of the etoposide induced DNA damage does not contribute to its toxicity.	Etoposide	93-102	H2A.X variant histone	Homo sapiens	112-116
19516899-8	2009	CONCLUSIONS/SIGNIFICANCE: These results show that only 0.3% of all strand breaks produced by etoposide activate H2AX phosphorylation and suggests that over 99% of the etoposide induced DNA damage does not contribute to its toxicity.	Etoposide	167-176	H2A.X variant histone	Homo sapiens	112-116
19351884-1	2009	In mammalian cells, the DNA damage-related histone H2A variant H2A.X is characterized by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an atypical kinase, WSTF.	cyclo(tyrosyl-tyrosyl)	102-109	H2A.X variant histone	Homo sapiens	63-68
19351884-1	2009	In mammalian cells, the DNA damage-related histone H2A variant H2A.X is characterized by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an atypical kinase, WSTF.	Tyrosine	119-122	H2A.X variant histone	Homo sapiens	63-68
19351884-2	2009	The phosphorylation status of Tyr-142 in H2A.X has been shown to be an important regulator of the DNA damage response by controlling the formation of gammaH2A.X foci, which are platforms for recruiting molecules involved in DNA damage repair and signaling.	Tyrosine	30-33	H2A.X variant histone	Homo sapiens	41-46
19351884-4	2009	We demonstrate that EYA2 and EYA3 displayed specificity for Tyr-142 of H2A.X in assays in vitro.	Tyrosine	60-63	H2A.X variant histone	Homo sapiens	71-76
19351884-5	2009	Suppression of eya3 by RNA interference resulted in elevated basal phosphorylation and inhibited DNA damage-induced dephosphorylation of Tyr-142 of H2A.X in vivo.	Tyrosine	137-140	H2A.X variant histone	Homo sapiens	148-153
19486862-3	2009	In this study, we showed that CSS generated phosphorylated histone H2AX (gamma-H2AX), recently considered as a sensitive marker of the generation of DSBs, in a human pulmonary epithelial cell model, A549.	thiocysteine	30-33	H2A.X variant histone	Homo sapiens	59-71
19486862-3	2009	In this study, we showed that CSS generated phosphorylated histone H2AX (gamma-H2AX), recently considered as a sensitive marker of the generation of DSBs, in a human pulmonary epithelial cell model, A549.	thiocysteine	30-33	H2A.X variant histone	Homo sapiens	73-83
19486862-3	2009	In this study, we showed that CSS generated phosphorylated histone H2AX (gamma-H2AX), recently considered as a sensitive marker of the generation of DSBs, in a human pulmonary epithelial cell model, A549.	dsbs	149-153	H2A.X variant histone	Homo sapiens	59-71
19486862-3	2009	In this study, we showed that CSS generated phosphorylated histone H2AX (gamma-H2AX), recently considered as a sensitive marker of the generation of DSBs, in a human pulmonary epithelial cell model, A549.	dsbs	149-153	H2A.X variant histone	Homo sapiens	73-83
19486862-4	2009	Treatment with CSS drastically induced discrete foci of gamma-H2AX within the nucleus in a dose-dependent manner.	thiocysteine	15-18	H2A.X variant histone	Homo sapiens	56-66
19486862-5	2009	CSS increased intracellular oxidation, and N-acetylcysteine (NAC), an antioxidant, significantly attenuated the formation of gamma-H2AX, suggesting that reactive oxygen species produced from CSS partially contributed to the phosphorylation.	Acetylcysteine	43-59	H2A.X variant histone	Homo sapiens	125-135
19486862-5	2009	CSS increased intracellular oxidation, and N-acetylcysteine (NAC), an antioxidant, significantly attenuated the formation of gamma-H2AX, suggesting that reactive oxygen species produced from CSS partially contributed to the phosphorylation.	Acetylcysteine	61-64	H2A.X variant histone	Homo sapiens	125-135
19486862-5	2009	CSS increased intracellular oxidation, and N-acetylcysteine (NAC), an antioxidant, significantly attenuated the formation of gamma-H2AX, suggesting that reactive oxygen species produced from CSS partially contributed to the phosphorylation.	Reactive Oxygen Species	153-176	H2A.X variant histone	Homo sapiens	125-135
19486862-5	2009	CSS increased intracellular oxidation, and N-acetylcysteine (NAC), an antioxidant, significantly attenuated the formation of gamma-H2AX, suggesting that reactive oxygen species produced from CSS partially contributed to the phosphorylation.	thiocysteine	191-194	H2A.X variant histone	Homo sapiens	125-135
19428384-0	2009	Acetaldehyde stimulates FANCD2 monoubiquitination, H2AX phosphorylation, and BRCA1 phosphorylation in human cells in vitro: implications for alcohol-related carcinogenesis.	Acetaldehyde	0-12	H2A.X variant histone	Homo sapiens	51-55
19401701-4	2009	Immunoblot studies revealed increased phosphorylation of H2A.X at Ser-139 and Chk1 at Ser-280 and a decrease in DNA polymerase-beta level in curcumin-treated cells.	Serine	66-69	H2A.X variant histone	Homo sapiens	57-62
19401701-4	2009	Immunoblot studies revealed increased phosphorylation of H2A.X at Ser-139 and Chk1 at Ser-280 and a decrease in DNA polymerase-beta level in curcumin-treated cells.	Serine	86-89	H2A.X variant histone	Homo sapiens	57-62
19360330-5	2009	In the present study we observed that hyaluronic acid (HA) of average molecular weight (MW) 5.4x10(6) and 2x10(6) at 0.1% (w/v) concentration significantly attenuated H2AX phosphorylation and ATM activation induced in leukocytes during oxidative burst.	Hyaluronic Acid	38-53	H2A.X variant histone	Homo sapiens	167-171
19401701-4	2009	Immunoblot studies revealed increased phosphorylation of H2A.X at Ser-139 and Chk1 at Ser-280 and a decrease in DNA polymerase-beta level in curcumin-treated cells.	Curcumin	141-149	H2A.X variant histone	Homo sapiens	57-62
19234442-0	2009	Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions.	Tyrosine	0-8	H2A.X variant histone	Homo sapiens	30-34
19273466-7	2009	The H2AX phosphorylation level increased 8-fold compared with the background level with 1.0 microg/ml (3 microM) 3,6-DNBeP-treatment in HepG2 cells.	3,6-dinitrobenzopyrene	113-122	H2A.X variant histone	Homo sapiens	4-8
19377482-0	2009	miR-24-mediated downregulation of H2AX suppresses DNA repair in terminally differentiated blood cells.	mir-24	0-6	H2A.X variant histone	Homo sapiens	34-38
19377482-5	2009	miR-24-mediated suppression of H2AX renders cells hypersensitive to gamma-irradiation and genotoxic drugs, a phenotype that is fully rescued by overexpression of miR-24-insensitive H2AX.	mir-24	0-6	H2A.X variant histone	Homo sapiens	31-35
19377482-5	2009	miR-24-mediated suppression of H2AX renders cells hypersensitive to gamma-irradiation and genotoxic drugs, a phenotype that is fully rescued by overexpression of miR-24-insensitive H2AX.	mir-24	0-6	H2A.X variant histone	Homo sapiens	181-185
19377482-5	2009	miR-24-mediated suppression of H2AX renders cells hypersensitive to gamma-irradiation and genotoxic drugs, a phenotype that is fully rescued by overexpression of miR-24-insensitive H2AX.	mir-24	162-168	H2A.X variant histone	Homo sapiens	31-35
19383846-9	2009	The trapping of Top1 cleavage complexes by indenoisoquinolines in cells results in the rapid and sustained phosphorylation of histone H2AX (gamma-H2AX).	indenoisoquinolines	43-62	H2A.X variant histone	Homo sapiens	126-138
19234442-3	2009	Here we report that a protein tyrosine phosphatase, EYA, is involved in promoting efficient DNA repair rather than apoptosis in response to genotoxic stress in mammalian embryonic kidney cells by executing a damage-signal-dependent dephosphorylation of an H2AX carboxy-terminal tyrosine phosphate (Y142).	Phosphotyrosine	278-296	H2A.X variant histone	Homo sapiens	256-260
19234442-4	2009	This post-translational modification determines the relative recruitment of either DNA repair or pro-apoptotic factors to the tail of serine phosphorylated histone H2AX (gamma-H2AX) and allows it to function as an active determinant of repair/survival versus apoptotic responses to DNA damage, revealing an additional phosphorylation-dependent mechanism that modulates survival/apoptotic decisions during mammalian organogenesis.	Serine	134-140	H2A.X variant histone	Homo sapiens	164-168
19234442-4	2009	This post-translational modification determines the relative recruitment of either DNA repair or pro-apoptotic factors to the tail of serine phosphorylated histone H2AX (gamma-H2AX) and allows it to function as an active determinant of repair/survival versus apoptotic responses to DNA damage, revealing an additional phosphorylation-dependent mechanism that modulates survival/apoptotic decisions during mammalian organogenesis.	Serine	134-140	H2A.X variant histone	Homo sapiens	170-180
19397442-0	2009	Forskolin decreases phosphorylation of histone H2AX in human cells induced by ionizing radiation.	Colforsin	0-9	H2A.X variant histone	Homo sapiens	39-51
19397442-3	2009	It is unknown whether forskolin can effect cellular responses to ionizing radiation, such as induction of phosphorylation of histone H2AX (gamma-H2AX) in megabase chromatin domains near DNA double-strand breaks (DSBs).	Colforsin	22-31	H2A.X variant histone	Homo sapiens	125-137
19280549-2	2009	MATERIALS AND METHODS: The method is based on the phosphorylation of the histone variant H 2AX (gamma-H2AX) after formation of DSBs.	dsbs	127-131	H2A.X variant histone	Homo sapiens	89-94
19397442-3	2009	It is unknown whether forskolin can effect cellular responses to ionizing radiation, such as induction of phosphorylation of histone H2AX (gamma-H2AX) in megabase chromatin domains near DNA double-strand breaks (DSBs).	Colforsin	22-31	H2A.X variant histone	Homo sapiens	139-149
19397442-4	2009	Here we report that treatment with forskolin decreases H2AX phosphorylation after irradiation detected by immunoblotting or by analysis of the overall gamma-H2AX-associated fluorescence in the nuclei.	Colforsin	35-44	H2A.X variant histone	Homo sapiens	55-59
19397442-4	2009	Here we report that treatment with forskolin decreases H2AX phosphorylation after irradiation detected by immunoblotting or by analysis of the overall gamma-H2AX-associated fluorescence in the nuclei.	Colforsin	35-44	H2A.X variant histone	Homo sapiens	151-161
19397442-6	2009	We suggest that the overall decrease of H2AX phosphorylation after treatment with forskolin in irradiated cells reflects a lesser extent of apparent H2AX modification at individual DSBs that may be caused by inhibition of the initial spread of gamma-H2AX and/or by stimulation of elimination of gamma-H2AX from chromatin after DSB rejoining.	Colforsin	82-91	H2A.X variant histone	Homo sapiens	40-44
19397442-6	2009	We suggest that the overall decrease of H2AX phosphorylation after treatment with forskolin in irradiated cells reflects a lesser extent of apparent H2AX modification at individual DSBs that may be caused by inhibition of the initial spread of gamma-H2AX and/or by stimulation of elimination of gamma-H2AX from chromatin after DSB rejoining.	Colforsin	82-91	H2A.X variant histone	Homo sapiens	244-254
19397442-6	2009	We suggest that the overall decrease of H2AX phosphorylation after treatment with forskolin in irradiated cells reflects a lesser extent of apparent H2AX modification at individual DSBs that may be caused by inhibition of the initial spread of gamma-H2AX and/or by stimulation of elimination of gamma-H2AX from chromatin after DSB rejoining.	Colforsin	82-91	H2A.X variant histone	Homo sapiens	295-305
19305155-2	2009	Phosphorylation of histone H2AX at serine 139 is a critical event in the response to DNA damage, but the functional implications of this modification are not yet clear.	Serine	35-41	H2A.X variant histone	Homo sapiens	19-31
19159633-8	2009	Interestingly, DNA double-strand breaks, as measured by the phosphorylation of H2AX, were remarkably accumulated in berberine-treated cells in a dose-dependent manner.	Berberine	116-125	H2A.X variant histone	Homo sapiens	79-83
19305155-12	2009	Taken together these results demonstrate a role for H2AX Serine 139 phosphorylation in cell cycle regulation and apoptosis, and for Lysine 119 in the control of H2AX turnover.	Serine	57-63	H2A.X variant histone	Homo sapiens	52-56
19305155-12	2009	Taken together these results demonstrate a role for H2AX Serine 139 phosphorylation in cell cycle regulation and apoptosis, and for Lysine 119 in the control of H2AX turnover.	Lysine	132-138	H2A.X variant histone	Homo sapiens	161-165
19252467-3	2009	The formation of nuclear DSBs triggers phosphorylation of H2AX at Ser139; phosphorylated H2AX is named gamma H2AX.	dsbs	25-29	H2A.X variant histone	Homo sapiens	58-62
19157440-2	2009	The phosphorylation of histone H2AX at serine 139 (gamma-H2AX) is associated with DNA breaks.	Serine	39-45	H2A.X variant histone	Homo sapiens	31-35
19157440-2	2009	The phosphorylation of histone H2AX at serine 139 (gamma-H2AX) is associated with DNA breaks.	Serine	39-45	H2A.X variant histone	Homo sapiens	57-61
19049966-4	2009	Because H2AX has been shown to play a facilitative role in homologous recombination, we hypothesized that H2AX participates in Rad51-mediated suppression of DSBs generated in the absence of ATR.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	157-161	H2A.X variant histone	Homo sapiens	8-12
19049966-4	2009	Because H2AX has been shown to play a facilitative role in homologous recombination, we hypothesized that H2AX participates in Rad51-mediated suppression of DSBs generated in the absence of ATR.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	157-161	H2A.X variant histone	Homo sapiens	106-110
19049966-6	2009	Importantly, the ATM and DNA-PK phosphorylation site on H2AX (Ser(139)) is required for genome stabilization in the absence of ATR; therefore, phosphorylation of H2AX by ATM and DNA-PKcs plays a pivotal role in suppressing DSBs during DNA synthesis in instances of ATR pathway failure.	Serine	62-65	H2A.X variant histone	Homo sapiens	56-60
19049966-6	2009	Importantly, the ATM and DNA-PK phosphorylation site on H2AX (Ser(139)) is required for genome stabilization in the absence of ATR; therefore, phosphorylation of H2AX by ATM and DNA-PKcs plays a pivotal role in suppressing DSBs during DNA synthesis in instances of ATR pathway failure.	Serine	62-65	H2A.X variant histone	Homo sapiens	162-166
19049966-6	2009	Importantly, the ATM and DNA-PK phosphorylation site on H2AX (Ser(139)) is required for genome stabilization in the absence of ATR; therefore, phosphorylation of H2AX by ATM and DNA-PKcs plays a pivotal role in suppressing DSBs during DNA synthesis in instances of ATR pathway failure.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	223-227	H2A.X variant histone	Homo sapiens	56-60
19049966-6	2009	Importantly, the ATM and DNA-PK phosphorylation site on H2AX (Ser(139)) is required for genome stabilization in the absence of ATR; therefore, phosphorylation of H2AX by ATM and DNA-PKcs plays a pivotal role in suppressing DSBs during DNA synthesis in instances of ATR pathway failure.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	223-227	H2A.X variant histone	Homo sapiens	162-166
19137017-8	2009	In the Mapo1-defective mutant cells treated with MNU, the mitochondrial membrane depolarization and caspase-3 activation were severely suppressed, although phosphorylation of p53, CHK1 and histone H2AX was observed.	Methylnitrosourea	49-52	H2A.X variant histone	Homo sapiens	189-201
19252467-3	2009	The formation of nuclear DSBs triggers phosphorylation of H2AX at Ser139; phosphorylated H2AX is named gamma H2AX.	dsbs	25-29	H2A.X variant histone	Homo sapiens	89-93
19252467-3	2009	The formation of nuclear DSBs triggers phosphorylation of H2AX at Ser139; phosphorylated H2AX is named gamma H2AX.	dsbs	25-29	H2A.X variant histone	Homo sapiens	89-93
19252467-5	2009	H2AX is phosphorylated by members of phosphoinositide 3-kinase-related protein kinases (PIKKs), such as ATM (ataxia teleangiectasia mutated), which is the main mediator of H2AX phosphorylation in response to DSB induction.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	208-211	H2A.X variant histone	Homo sapiens	0-4
19252467-5	2009	H2AX is phosphorylated by members of phosphoinositide 3-kinase-related protein kinases (PIKKs), such as ATM (ataxia teleangiectasia mutated), which is the main mediator of H2AX phosphorylation in response to DSB induction.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	208-211	H2A.X variant histone	Homo sapiens	172-176
19190126-6	2009	RESULTS: The selected Dbait molecules activate H2AX phosphorylation in cell culture and in xenografted tumors.	dbait	22-27	H2A.X variant histone	Homo sapiens	47-51
19190126-12	2009	The induction of H2AX phosphorylation in tumors treated with Dbait suggests that it acts in vivo through the induction of "false" DNA damage signaling and repair inhibition.	dbait	61-66	H2A.X variant histone	Homo sapiens	17-21
19028473-6	2009	Kaempferol also induced ATM and H2AX phosphorylation in HCT116 cells, inhibition of ATM by a chemical inhibitor resulted in abrogation of the downstream apoptotic cascades.	kaempferol	0-10	H2A.X variant histone	Homo sapiens	32-36
19203579-5	2009	We show that RNF168 interacts with ubiquitylated H2A, assembles at DSBs in an RNF8-dependent manner, and, by targeting H2A and H2AX, amplifies local concentration of lysine 63-linked ubiquitin conjugates to the threshold required for retention of 53BP1 and BRCA1.	Lysine	166-172	H2A.X variant histone	Homo sapiens	127-131
19763948-2	2009	DNA damage, particularly induction of DSBs, manifests by phosphorylation of histone H2AX on Ser-139 which is mediated by one of the protein kinases of the phosphoinositide kinase family, namely ATM, ATR, and/or DNA-PK.	Serine	92-95	H2A.X variant histone	Homo sapiens	84-88
19127257-14	2009	Apoptosis in melanoma cells induced by TMZ and fotemustine was accompanied by double-strand break (DSB) formation (as determined by H2AX phosphorylation) and caspase-3 and -7 activation as well as PARP cleavage.	Temozolomide	39-42	H2A.X variant histone	Homo sapiens	132-136
19127257-14	2009	Apoptosis in melanoma cells induced by TMZ and fotemustine was accompanied by double-strand break (DSB) formation (as determined by H2AX phosphorylation) and caspase-3 and -7 activation as well as PARP cleavage.	fotemustine	47-58	H2A.X variant histone	Homo sapiens	132-136
18848825-0	2009	H2AX phosphorylation in A549 cells induced by the bulky and stable DNA adducts of benzo[a]pyrene and dibenzo[a,l]pyrene diol epoxides.	Benzo(a)pyrene	82-96	H2A.X variant histone	Homo sapiens	0-4
18848825-0	2009	H2AX phosphorylation in A549 cells induced by the bulky and stable DNA adducts of benzo[a]pyrene and dibenzo[a,l]pyrene diol epoxides.	dibenzo(a,l)pyrene diol epoxide	101-133	H2A.X variant histone	Homo sapiens	0-4
18848825-7	2009	Visualisation of H2AXgamma formation demonstrated that the proportion of cells exhibiting H2AXgamma staining at 1h differed between BPDE, 40% followed by a decline, and DBPDE, <10% followed by an increase.	Hydrogen	112-114	H2A.X variant histone	Homo sapiens	17-26
18848825-7	2009	Visualisation of H2AXgamma formation demonstrated that the proportion of cells exhibiting H2AXgamma staining at 1h differed between BPDE, 40% followed by a decline, and DBPDE, <10% followed by an increase.	Hydrogen	112-114	H2A.X variant histone	Homo sapiens	90-99
18848825-7	2009	Visualisation of H2AXgamma formation demonstrated that the proportion of cells exhibiting H2AXgamma staining at 1h differed between BPDE, 40% followed by a decline, and DBPDE, <10% followed by an increase.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	132-136	H2A.X variant histone	Homo sapiens	17-26
18848825-7	2009	Visualisation of H2AXgamma formation demonstrated that the proportion of cells exhibiting H2AXgamma staining at 1h differed between BPDE, 40% followed by a decline, and DBPDE, <10% followed by an increase.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	132-136	H2A.X variant histone	Homo sapiens	90-99
18848825-10	2009	The kinetics of H2AXgamma formation correlated with the previously observed kinetics of elimination of BPDE and DBPDE adducts.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	103-107	H2A.X variant histone	Homo sapiens	16-25
18848825-10	2009	The kinetics of H2AXgamma formation correlated with the previously observed kinetics of elimination of BPDE and DBPDE adducts.	dibenzo(a,l)pyrene diol epoxide	112-117	H2A.X variant histone	Homo sapiens	16-25
19381940-1	2009	Phosphorylation of histone H2AX on Ser 139 is a sensitive reporter of DNA damage, particularly if the damage involves induction of DNA double-strand breaks (DSBs).	Serine	35-38	H2A.X variant histone	Homo sapiens	19-31
19381940-4	2009	This chapter presents the protocols and outlines applications of multiparameter cytometry in analysis of H2AX phosphorylation as a reporter of the presence of DSBs.	dsbs	159-163	H2A.X variant histone	Homo sapiens	105-109
19763948-3	2009	The presence of Ser-139 phosphorylated H2AX (gammaH2AX) is thus a reporter of DNA damage.	Serine	16-19	H2A.X variant histone	Homo sapiens	39-43
19092802-3	2009	During the double-strand break response, mammalian chromatin undergoes reorganization demarcated by H2A.X Ser 139 phosphorylation (gamma-H2A.X).	Serine	106-109	H2A.X variant histone	Homo sapiens	100-105
19092802-3	2009	During the double-strand break response, mammalian chromatin undergoes reorganization demarcated by H2A.X Ser 139 phosphorylation (gamma-H2A.X).	Serine	106-109	H2A.X variant histone	Homo sapiens	137-142
19092802-7	2009	We show that WSTF phosphorylates Tyr 142 of H2A.X, and that WSTF activity has an important role in regulating several events that are critical for the DNA damage response.	Tyrosine	33-36	H2A.X variant histone	Homo sapiens	44-49
19424844-4	2008	In response to the formation of double-stranded breaks in chromosomal DNA, serine 139 on H2AX, a 14-kDa protein that is a member of the H2A histone family and part of the nucleosome structure, becomes rapidly phosphorylated to generate gamma H2AX.	Serine	75-81	H2A.X variant histone	Homo sapiens	89-93
19224683-6	2009	RESULTS: After treatment with different doses of silica for 12 h, the levels of H2AX and the percentages of tail DNA increased in concentration-dependent manner.	Silicon Dioxide	49-55	H2A.X variant histone	Homo sapiens	80-84
19224683-7	2009	After treatment with 200 microg/ml silica for different times, the levels of H2AX increased in a time-dependent manner.	Silicon Dioxide	35-41	H2A.X variant histone	Homo sapiens	77-81
19224683-9	2009	After treatment with silica at 12 h, the level of H2AX was lower in HELF-PKcs than in HELF-NC, and the percentages of tail DNA increased obviously in both HELF-PKcs and HELF-NC compared with non-treated cells, but no significant difference was found in the percentages of tail DNA between them.	Silicon Dioxide	21-27	H2A.X variant histone	Homo sapiens	50-54
19224683-13	2009	Silica-induced histone H2AX phosphorylation was dependent on DNA-PKcs.	Silicon Dioxide	0-6	H2A.X variant histone	Homo sapiens	23-27
19007111-3	2008	The metabolically released formaldehyde from the prodrugs was the dominant factor affecting cell viability by a ROS-dependent mechanism and was responsible for rapid phosphorylation of H2AX, suppression of the cell survival protein c-myc, and transient elevation in the expression of p21.	Formaldehyde	27-39	H2A.X variant histone	Homo sapiens	185-189
19007111-3	2008	The metabolically released formaldehyde from the prodrugs was the dominant factor affecting cell viability by a ROS-dependent mechanism and was responsible for rapid phosphorylation of H2AX, suppression of the cell survival protein c-myc, and transient elevation in the expression of p21.	ros	112-115	H2A.X variant histone	Homo sapiens	185-189
19424844-4	2008	In response to the formation of double-stranded breaks in chromosomal DNA, serine 139 on H2AX, a 14-kDa protein that is a member of the H2A histone family and part of the nucleosome structure, becomes rapidly phosphorylated to generate gamma H2AX.	Serine	75-81	H2A.X variant histone	Homo sapiens	242-246
18835433-0	2008	Generation of phosphorylated histone H2AX by benzene metabolites.	Benzene	45-52	H2A.X variant histone	Homo sapiens	29-41
19005492-1	2008	Histone H2AX phosphorylation on a serine four residues from the carboxyl terminus (producing gammaH2AX) is a sensitive marker for DNA double-strand breaks (DSBs).	Serine	34-40	H2A.X variant histone	Homo sapiens	0-12
18949412-2	2008	DNA double-strand breaks (DSBs) are thought to be caused by the deleterious effects of ionizing radiation, and gammaH2AX (serine 139 phosphorylated form of histone H2AX) is reported to be a significant marker for DSBs.	Serine	122-128	H2A.X variant histone	Homo sapiens	156-168
18765297-2	2008	An immunocytochemical assay using antibodies capable of recognizing histone H2AX phosphorylated at serine 139 (gammaH2AX) is very sensitive and is a specific indicator for the existence of a DNA double strand break.	Serine	99-105	H2A.X variant histone	Homo sapiens	76-80
18645678-0	2008	Adriamycin induces H2AX phosphorylation in human spermatozoa.	Doxorubicin	0-10	H2A.X variant histone	Homo sapiens	19-23
18829552-5	2008	Cellular responses to both DSBs and stalled replication forks are marked by H2AX phosphorylation on Ser(139) (gamma-H2AX), which forms nuclear foci at sites of DNA damage.	Serine	100-103	H2A.X variant histone	Homo sapiens	76-80
18829552-5	2008	Cellular responses to both DSBs and stalled replication forks are marked by H2AX phosphorylation on Ser(139) (gamma-H2AX), which forms nuclear foci at sites of DNA damage.	Serine	100-103	H2A.X variant histone	Homo sapiens	116-120
18829552-7	2008	Using gamma-H2AX as a marker for changes in chromatin structure, we show that Mre11, Rad50, Nbs1, and phosphorylated ATM respond to nucleoside analogue-induced stalled replication forks by forming nuclear foci that colocalize with gamma-H2AX within 2 hours.	Nucleosides	132-142	H2A.X variant histone	Homo sapiens	12-16
18829552-7	2008	Using gamma-H2AX as a marker for changes in chromatin structure, we show that Mre11, Rad50, Nbs1, and phosphorylated ATM respond to nucleoside analogue-induced stalled replication forks by forming nuclear foci that colocalize with gamma-H2AX within 2 hours.	Nucleosides	132-142	H2A.X variant histone	Homo sapiens	237-241
18772227-2	2008	In higher eukaryotic cells, DSBs in chromatin promptly initiate the phosphorylation of the histone H2A variant, H2AX, at Serine 139 to generate gamma-H2AX.	dsbs	28-32	H2A.X variant histone	Homo sapiens	112-116
18772227-2	2008	In higher eukaryotic cells, DSBs in chromatin promptly initiate the phosphorylation of the histone H2A variant, H2AX, at Serine 139 to generate gamma-H2AX.	dsbs	28-32	H2A.X variant histone	Homo sapiens	150-154
18772227-2	2008	In higher eukaryotic cells, DSBs in chromatin promptly initiate the phosphorylation of the histone H2A variant, H2AX, at Serine 139 to generate gamma-H2AX.	Serine	121-127	H2A.X variant histone	Homo sapiens	112-116
18772227-2	2008	In higher eukaryotic cells, DSBs in chromatin promptly initiate the phosphorylation of the histone H2A variant, H2AX, at Serine 139 to generate gamma-H2AX.	Serine	121-127	H2A.X variant histone	Homo sapiens	150-154
18772227-4	2008	Regions in chromatin with gamma-H2AX are conveniently detected by immunofluorescence microscopy and serve as beacons of DSBs.	dsbs	120-124	H2A.X variant histone	Homo sapiens	32-36
18802408-8	2008	The maximal increase in p53-Ser15(P) expression, rising up to 2.5-fold above the level of its constitutive expression, was observed in cells treated with TPT or MXT for 4-6 h. This maximum expression of p53-Ser15(P) coincided in time with the peak of Chk2 activation but not with ATM activation and H2AX phosphorylation, both of which crested 1-2 h after the treatment with TPT or MXT.	Topotecan	154-157	H2A.X variant histone	Homo sapiens	299-303
18802408-8	2008	The maximal increase in p53-Ser15(P) expression, rising up to 2.5-fold above the level of its constitutive expression, was observed in cells treated with TPT or MXT for 4-6 h. This maximum expression of p53-Ser15(P) coincided in time with the peak of Chk2 activation but not with ATM activation and H2AX phosphorylation, both of which crested 1-2 h after the treatment with TPT or MXT.	Mitoxantrone	161-164	H2A.X variant histone	Homo sapiens	299-303
18802408-8	2008	The maximal increase in p53-Ser15(P) expression, rising up to 2.5-fold above the level of its constitutive expression, was observed in cells treated with TPT or MXT for 4-6 h. This maximum expression of p53-Ser15(P) coincided in time with the peak of Chk2 activation but not with ATM activation and H2AX phosphorylation, both of which crested 1-2 h after the treatment with TPT or MXT.	Topotecan	374-377	H2A.X variant histone	Homo sapiens	299-303
18542054-4	2008	Cellular sensitivity to two monofunctional alkylating agents (methyl methane sulfonate and N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)) was dependent on H2AX dosage, and H2AX null cells were more sensitive than heterozygous cells.	Methyl Methanesulfonate	62-86	H2A.X variant histone	Homo sapiens	153-157
18542054-4	2008	Cellular sensitivity to two monofunctional alkylating agents (methyl methane sulfonate and N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)) was dependent on H2AX dosage, and H2AX null cells were more sensitive than heterozygous cells.	Methyl Methanesulfonate	62-86	H2A.X variant histone	Homo sapiens	170-174
18542054-4	2008	Cellular sensitivity to two monofunctional alkylating agents (methyl methane sulfonate and N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)) was dependent on H2AX dosage, and H2AX null cells were more sensitive than heterozygous cells.	Methylnitronitrosoguanidine	91-127	H2A.X variant histone	Homo sapiens	153-157
18542054-4	2008	Cellular sensitivity to two monofunctional alkylating agents (methyl methane sulfonate and N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)) was dependent on H2AX dosage, and H2AX null cells were more sensitive than heterozygous cells.	Methylnitronitrosoguanidine	129-133	H2A.X variant histone	Homo sapiens	153-157
18542054-4	2008	Cellular sensitivity to two monofunctional alkylating agents (methyl methane sulfonate and N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)) was dependent on H2AX dosage, and H2AX null cells were more sensitive than heterozygous cells.	Methylnitronitrosoguanidine	129-133	H2A.X variant histone	Homo sapiens	170-174
18542054-8	2008	Consistent with this, increased activities of PARP and poly(ADP) ribose (PAR) polymer synthesis were detected in both H2AX heterozygous and null cells.	Poly Adenosine Diphosphate Ribose	55-71	H2A.X variant histone	Homo sapiens	118-122
18542054-8	2008	Consistent with this, increased activities of PARP and poly(ADP) ribose (PAR) polymer synthesis were detected in both H2AX heterozygous and null cells.	Poly Adenosine Diphosphate Ribose	46-49	H2A.X variant histone	Homo sapiens	118-122
18645678-1	2008	AIM: To investigate whether adriamycin induces DNA damage and the formation of gammaH2AX (the phosphorylated form of histone H2AX) foci in mature spermatozoa.	Doxorubicin	28-38	H2A.X variant histone	Homo sapiens	117-129
18645678-1	2008	AIM: To investigate whether adriamycin induces DNA damage and the formation of gammaH2AX (the phosphorylated form of histone H2AX) foci in mature spermatozoa.	gammah2ax	79-88	H2A.X variant histone	Homo sapiens	117-129
18645678-8	2008	CONCLUSION: Human mature spermatozoa have the same response to DSB-induced H2AX phosphorylation and subsequent recruitment of DNA maintenance/repair proteins as somatic cells.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	63-66	H2A.X variant histone	Homo sapiens	75-79
18729329-11	2008	HPLC analysis clarified that several compounds with increased hydrophilicity were produced from 3,3"-diClBPA by UVB irradiation, not from BPA, suggesting the chlorinated chemical structure to be important for the degradation and generation of products related to the phosphorylation of histone H2AX.	3,3'-dichlorobisphenol A	96-108	H2A.X variant histone	Homo sapiens	286-298
18729329-12	2008	In separated peaks of 3,3"-diClBPA exposed to UVB, peak fluctuation of 3-hydroxybisphenol A (3-OHBPA) was consistent with the UVB dose-dependent appearance of phosphorylated histone H2AX.	3,3'-dichlorobisphenol A	22-34	H2A.X variant histone	Homo sapiens	174-186
18729329-0	2008	UVB-exposed chlorinated bisphenol A generates phosphorylated histone H2AX in human skin cells.	bisphenol A	24-35	H2A.X variant histone	Homo sapiens	61-73
18729329-12	2008	In separated peaks of 3,3"-diClBPA exposed to UVB, peak fluctuation of 3-hydroxybisphenol A (3-OHBPA) was consistent with the UVB dose-dependent appearance of phosphorylated histone H2AX.	3-hydroxybisphenol A	71-91	H2A.X variant histone	Homo sapiens	174-186
18729329-8	2008	In this study using human keratinocytes and skin fibroblasts, we found that 3,3"-dichlorobisphenol A (3,3"-diClBPA) exposed to UVB induces phosphorylation of histone H2AX, the event considered to be a marker of formation of DNA double strand breaks.	3,3'-dichlorobisphenol A	76-100	H2A.X variant histone	Homo sapiens	158-170
18729329-8	2008	In this study using human keratinocytes and skin fibroblasts, we found that 3,3"-dichlorobisphenol A (3,3"-diClBPA) exposed to UVB induces phosphorylation of histone H2AX, the event considered to be a marker of formation of DNA double strand breaks.	3,3'-dichlorobisphenol A	102-114	H2A.X variant histone	Homo sapiens	158-170
18729329-9	2008	The cells treated with the UVB-exposed 3,3"-diClBPA formed clear foci of phosphorylated histone H2AX in the nucleus.	3,3'-dichlorobisphenol A	39-51	H2A.X variant histone	Homo sapiens	88-100
18729329-12	2008	In separated peaks of 3,3"-diClBPA exposed to UVB, peak fluctuation of 3-hydroxybisphenol A (3-OHBPA) was consistent with the UVB dose-dependent appearance of phosphorylated histone H2AX.	3-hydroxybisphenol A	93-100	H2A.X variant histone	Homo sapiens	174-186
18647348-4	2008	The C-terminal tail of histone 2AX (H2AX) is hyperphosphorylated in the same mutants, and Pph3p is found to interact with phosphorylated H2AX (gammaH2AX).	gammah2ax	143-152	H2A.X variant histone	Homo sapiens	23-34
18602349-10	2008	These results confirm the importance of homologous recombination in the accurate repair of double-strand breaks in mES cells, they help explain the chromosome abnormalities associated with deficiencies in H2AX and ATM, and they add to the growing list of differences in the way rodent and human cells deal with DNA damage.	2-(N-morpholino)ethanesulfonic acid	115-118	H2A.X variant histone	Homo sapiens	205-209
18030472-9	2008	Formaldehyde-releasing prodrugs abrogated c-myc protein expression and elevated c-Jun and H2AX phosphorylation, N-acetylcysteine partially reversed these changes.	Formaldehyde	0-12	H2A.X variant histone	Homo sapiens	90-94
18647348-4	2008	The C-terminal tail of histone 2AX (H2AX) is hyperphosphorylated in the same mutants, and Pph3p is found to interact with phosphorylated H2AX (gammaH2AX).	gammah2ax	143-152	H2A.X variant histone	Homo sapiens	36-40
18647348-4	2008	The C-terminal tail of histone 2AX (H2AX) is hyperphosphorylated in the same mutants, and Pph3p is found to interact with phosphorylated H2AX (gammaH2AX).	gammah2ax	143-152	H2A.X variant histone	Homo sapiens	137-141
18632984-3	2008	Here we show that Et743 induces both transcription- and replication-coupled DNA double-strand breaks (DSBs) that are detectible by neutral COMET assay and as gamma-H2AX foci that colocalize with 53BP1, Mre11, Ser(1981)-pATM, and Thr(68)-pChk2.	Trabectedin	18-23	H2A.X variant histone	Homo sapiens	164-168
18632984-4	2008	The transcription coupled-DSBs (TC-DSBs) induced by Et743 depended both on TCR and Mre11-Rad50-Nbs1 (MRN) and were associated with DNA-PK-dependent gamma-H2AX foci.	dsbs	26-30	H2A.X variant histone	Homo sapiens	154-158
18632984-4	2008	The transcription coupled-DSBs (TC-DSBs) induced by Et743 depended both on TCR and Mre11-Rad50-Nbs1 (MRN) and were associated with DNA-PK-dependent gamma-H2AX foci.	tc-dsbs	32-39	H2A.X variant histone	Homo sapiens	154-158
18632984-4	2008	The transcription coupled-DSBs (TC-DSBs) induced by Et743 depended both on TCR and Mre11-Rad50-Nbs1 (MRN) and were associated with DNA-PK-dependent gamma-H2AX foci.	Trabectedin	52-57	H2A.X variant histone	Homo sapiens	154-158
18790767-5	2008	Biochemically, bortezomib treatment activated the p38 and c-Jun NH2-termnial kinase stress-activated mitogen-activated protein kinase (MAPK) pathways and induced phospho-H2AX activity.	Bortezomib	15-25	H2A.X variant histone	Homo sapiens	170-174
18262646-9	2008	While phosphorylation of H2A.X 1h after irradiation was detected by both confocal microscopy and Western blot, phosphorylation of Nbs1 on serine 343 was not detectable in MOLT-4 cells.	Hydrogen	31-33	H2A.X variant histone	Homo sapiens	25-30
18616816-7	2008	Cells manipulated to stably express H2AX did not contain soluble H2AX, however, short-term treatment with aphidicolin (1 h) resulted in detectable amounts of H2AX in the soluble nuclear fraction and enhanced apoptosis.	Aphidicolin	106-117	H2A.X variant histone	Homo sapiens	36-40
18632822-0	2008	Relationship between induction of phosphorylated H2AX and survival in breast cancer cells exposed to 111In-DTPA-hEGF.	111in-dtpa	101-111	H2A.X variant histone	Homo sapiens	49-53
18632822-14	2008	The number of gamma-H2AX foci per nucleus in MDA-MB-468 cells correlated with the concentration, specific activity, and incubation time of 111In-DTPA-hEGF.	Pentetic Acid	145-149	H2A.X variant histone	Homo sapiens	20-24
18632822-16	2008	The gamma-H2AX assay may be a useful biomarker to predict and monitor the outcome of treatment with 111In-DTPA-hEGF.	111in-dtpa	100-110	H2A.X variant histone	Homo sapiens	10-14
18636201-8	2008	Combination treatment with As2O3 and sulindac induced oxidative DNA damage in a time-dependent fashion, which was evaluated by H2AX phosphorylation along with HO-1 induction.	Arsenic Trioxide	27-32	H2A.X variant histone	Homo sapiens	127-131
18636201-8	2008	Combination treatment with As2O3 and sulindac induced oxidative DNA damage in a time-dependent fashion, which was evaluated by H2AX phosphorylation along with HO-1 induction.	Sulindac	37-45	H2A.X variant histone	Homo sapiens	127-131
18616816-7	2008	Cells manipulated to stably express H2AX did not contain soluble H2AX, however, short-term treatment with aphidicolin (1 h) resulted in detectable amounts of H2AX in the soluble nuclear fraction and enhanced apoptosis.	Aphidicolin	106-117	H2A.X variant histone	Homo sapiens	65-69
18616816-7	2008	Cells manipulated to stably express H2AX did not contain soluble H2AX, however, short-term treatment with aphidicolin (1 h) resulted in detectable amounts of H2AX in the soluble nuclear fraction and enhanced apoptosis.	Aphidicolin	106-117	H2A.X variant histone	Homo sapiens	65-69
18594007-14	2008	Moreover, moscatilin induces DNA damage, phosphorylation of H2AX and p53, and up-regulation of p21.	dendrophenol	10-20	H2A.X variant histone	Homo sapiens	60-64
18459160-0	2008	Kinetics of histone H2AX phosphorylation and Chk2 activation in A549 cells treated with topotecan and mitoxantrone in relation to the cell cycle phase.	Topotecan	88-97	H2A.X variant histone	Homo sapiens	20-24
18499365-0	2008	Regulation of gamma-H2AX and securin contribute to apoptosis by oxaliplatin via a p38 mitogen-activated protein kinase-dependent pathway in human colorectal cancer cells.	Oxaliplatin	64-75	H2A.X variant histone	Homo sapiens	20-24
18499365-5	2008	Treatment of oxaliplatin (1-10 microM for 6-24h) persistently induced gamma-H2AX formation and inhibited securin protein expression via a time- and concentration-dependent manner in HCT116 securin-wild type colorectal cancer cells.	Oxaliplatin	13-24	H2A.X variant histone	Homo sapiens	76-80
18499365-6	2008	Compared with HCT116 securin-wild type cells, the induction of apoptosis and persistent gamma-H2AX formation by oxaliplatin was reduced in the HCT116 securin-null colorectal cancer cells.	Oxaliplatin	112-123	H2A.X variant histone	Homo sapiens	94-98
18499365-8	2008	The gene knockdown of H2AX by transfection with a short interfering RNA of H2AX enhanced the oxaliplatin-induced cell death.	Oxaliplatin	93-104	H2A.X variant histone	Homo sapiens	22-26
18499365-8	2008	The gene knockdown of H2AX by transfection with a short interfering RNA of H2AX enhanced the oxaliplatin-induced cell death.	Oxaliplatin	93-104	H2A.X variant histone	Homo sapiens	75-79
18499365-10	2008	Pre-treatment of a specific p38 MAPK inhibitor SB202190 reduced gamma-H2AX proteins and increased securin protein expression in the oxaliplatin-treated cells.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	47-55	H2A.X variant histone	Homo sapiens	70-74
18499365-11	2008	Our findings suggest that p38 MAPK may oppositely regulate securin protein expression and gamma-H2AX formation in the oxaliplatin-induced apoptosis of human colorectal cancer cells.	Oxaliplatin	118-129	H2A.X variant histone	Homo sapiens	96-100
18395832-3	2008	The levels of H3Ser10P and Ser28P decreased between 15 and 60 min after H(2)O(2) addition in an inverse correlation manner with H2AX Ser139 phosphorylation (gammaH2AX).	h3ser10p	14-22	H2A.X variant histone	Homo sapiens	128-132
18459160-0	2008	Kinetics of histone H2AX phosphorylation and Chk2 activation in A549 cells treated with topotecan and mitoxantrone in relation to the cell cycle phase.	Mitoxantrone	102-114	H2A.X variant histone	Homo sapiens	20-24
18395832-3	2008	The levels of H3Ser10P and Ser28P decreased between 15 and 60 min after H(2)O(2) addition in an inverse correlation manner with H2AX Ser139 phosphorylation (gammaH2AX).	ser28p	27-33	H2A.X variant histone	Homo sapiens	128-132
18459160-5	2008	In the present study we explored a relationship between H2AX phosphorylation and activation of checkpoint kinase 2 (Chk2) in human lung carcinoma A549 cells treated with TPT or with MXT.	Topotecan	170-173	H2A.X variant histone	Homo sapiens	56-60
18459160-9	2008	H2AX phosphorylation whether induced by TPT or MXT was rapid, with the maximal rate occurring during the initial 2 h and peaking at 2 h of treatment.	Topotecan	40-43	H2A.X variant histone	Homo sapiens	0-4
18459160-9	2008	H2AX phosphorylation whether induced by TPT or MXT was rapid, with the maximal rate occurring during the initial 2 h and peaking at 2 h of treatment.	Mitoxantrone	47-50	H2A.X variant histone	Homo sapiens	0-4
18459160-10	2008	TPT or MXT induced Chk2 activation occurred at a distinctly slower pace, peaking at 4 h. While TPT-induced H2AX phosphorylation and Chk2 activation were maximal in S-phase cells, Chk2 activation was also much pronounced in G(2)M cells; the least affected by TPT were G(1) cells.	Topotecan	0-3	H2A.X variant histone	Homo sapiens	107-111
18459160-10	2008	TPT or MXT induced Chk2 activation occurred at a distinctly slower pace, peaking at 4 h. While TPT-induced H2AX phosphorylation and Chk2 activation were maximal in S-phase cells, Chk2 activation was also much pronounced in G(2)M cells; the least affected by TPT were G(1) cells.	Mitoxantrone	7-10	H2A.X variant histone	Homo sapiens	107-111
18459160-10	2008	TPT or MXT induced Chk2 activation occurred at a distinctly slower pace, peaking at 4 h. While TPT-induced H2AX phosphorylation and Chk2 activation were maximal in S-phase cells, Chk2 activation was also much pronounced in G(2)M cells; the least affected by TPT were G(1) cells.	Topotecan	95-98	H2A.X variant histone	Homo sapiens	107-111
18459160-10	2008	TPT or MXT induced Chk2 activation occurred at a distinctly slower pace, peaking at 4 h. While TPT-induced H2AX phosphorylation and Chk2 activation were maximal in S-phase cells, Chk2 activation was also much pronounced in G(2)M cells; the least affected by TPT were G(1) cells.	Topotecan	95-98	H2A.X variant histone	Homo sapiens	107-111
18459160-11	2008	MTX-induced H2AX phosphorylation was maximal in G(1) cells while Chk2 activation was maximal in G(2)M and minimal in G(1) cells.	Methotrexate	0-3	H2A.X variant histone	Homo sapiens	12-16
18610740-5	2008	DSBs can be induced by mechanisms such as ionizing radiation or cytotoxic agents and subsequently, gamma-H2AX foci quickly form.	dsbs	0-4	H2A.X variant histone	Homo sapiens	105-109
18445521-5	2008	In contrast to irinotecan, ST1968 still showed an excellent, persisting activity in models less susceptible to apoptosis induction (KB, Caski and SiHa), in which drug treatment elicited a persistent DNA damage response, as documented by phosphorylation of p53, RPA-2 and histone H2AX, resulting in delayed apoptosis and senescence.	namitecan	27-33	H2A.X variant histone	Homo sapiens	271-283
18497977-7	2008	HA of average MW 5.4 million (high MW) and 2 million (medium MW) at 0.1% (w/v) in culture medium totally prevented the H2O2-induced H2AX phosphorylation in both cell types whereas effect of 60,000 average MW (low MW) HA was somewhat less pronounced.	Hydrogen Peroxide	119-123	H2A.X variant histone	Homo sapiens	132-136
18497997-8	2008	Furthermore, quantitative real-time PCR demonstrated that mRNA changes of selected novel genes (CENPB, H2AFX, MCM5, ZADH1 and NGB) in irinotecan-resistant clones vs. parental clone were in agreement with array-CGH results.	Irinotecan	134-144	H2A.X variant histone	Homo sapiens	103-108
18607506-8	2008	Radiosensitization by gemcitabine was accompanied by early S-phase arrest and induction/persistence of gamma-H2AX protein, which were unaltered by oxaliplatin.	gemcitabine	22-33	H2A.X variant histone	Homo sapiens	103-113
18285460-3	2008	The depletion of Rvb1 increases the amount and persistence of phosphorylation on chromatin-associated H2AX after the exposure of cells to UV irradiation or to mitomycin C, cisplatin, camptothecin, or etoposide, without increasing the amount of DNA damage.	Mitomycin	159-170	H2A.X variant histone	Homo sapiens	102-106
18285460-3	2008	The depletion of Rvb1 increases the amount and persistence of phosphorylation on chromatin-associated H2AX after the exposure of cells to UV irradiation or to mitomycin C, cisplatin, camptothecin, or etoposide, without increasing the amount of DNA damage.	Cisplatin	172-181	H2A.X variant histone	Homo sapiens	102-106
18285460-3	2008	The depletion of Rvb1 increases the amount and persistence of phosphorylation on chromatin-associated H2AX after the exposure of cells to UV irradiation or to mitomycin C, cisplatin, camptothecin, or etoposide, without increasing the amount of DNA damage.	Camptothecin	183-195	H2A.X variant histone	Homo sapiens	102-106
18285460-3	2008	The depletion of Rvb1 increases the amount and persistence of phosphorylation on chromatin-associated H2AX after the exposure of cells to UV irradiation or to mitomycin C, cisplatin, camptothecin, or etoposide, without increasing the amount of DNA damage.	Etoposide	200-209	H2A.X variant histone	Homo sapiens	102-106
18179804-2	2008	This is to determine whether cell cycle related changes in chromatin structure might influence the gamma-H2AX assay which depends on extensive phosphorylation and dephosphorylation of the H2AX histone variant surrounding DSBs.	dsbs	221-225	H2A.X variant histone	Homo sapiens	188-200
18406329-0	2008	FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16.	Adenosine Diphosphate	88-91	H2A.X variant histone	Homo sapiens	42-46
18406329-6	2008	In contrast, poly-ADP-ribosylation of Spt16 by PARP1 significantly inhibits FACT activities for H2AX exchange.	poly-adp	13-21	H2A.X variant histone	Homo sapiens	96-100
17879944-4	2008	The presence of DNA double-strand breaks in the bleomycin-treated cells was examined by Western analysis using antibody against phosphorylated histone H2AX (gamma-H2AX).	Bleomycin	48-57	H2A.X variant histone	Homo sapiens	143-155
18059176-3	2008	DSBs trigger Ser-139 phosphorylation of histone H2AX (gammaH2AX) by PI-3-like kinases including ATM; gammaH2AX can serve as a marker of DNA damage when measured in situ using immunocytochemistry and flow cytometry.	Serine	13-16	H2A.X variant histone	Homo sapiens	40-52
18160332-0	2008	Solar-simulated light-exposed benzo[a]pyrene induces phosphorylation of histone H2AX.	Benzo(a)pyrene	30-44	H2A.X variant histone	Homo sapiens	80-84
18160332-3	2008	In this study, we found that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL)-induced phosphorylation of histone H2AX (gamma-H2AX), which was recently identified as an early event after the induction of DNA double strand breaks (DSBs).	Benzo(a)pyrene	29-43	H2A.X variant histone	Homo sapiens	116-128
18160332-3	2008	In this study, we found that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL)-induced phosphorylation of histone H2AX (gamma-H2AX), which was recently identified as an early event after the induction of DNA double strand breaks (DSBs).	Benzo(a)pyrene	29-43	H2A.X variant histone	Homo sapiens	130-140
18160332-3	2008	In this study, we found that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL)-induced phosphorylation of histone H2AX (gamma-H2AX), which was recently identified as an early event after the induction of DNA double strand breaks (DSBs).	Benzo(a)pyrene	45-48	H2A.X variant histone	Homo sapiens	116-128
18160332-3	2008	In this study, we found that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL)-induced phosphorylation of histone H2AX (gamma-H2AX), which was recently identified as an early event after the induction of DNA double strand breaks (DSBs).	Benzo(a)pyrene	45-48	H2A.X variant histone	Homo sapiens	130-140
18160332-3	2008	In this study, we found that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL)-induced phosphorylation of histone H2AX (gamma-H2AX), which was recently identified as an early event after the induction of DNA double strand breaks (DSBs).	dsbs	240-244	H2A.X variant histone	Homo sapiens	116-128
18160332-3	2008	In this study, we found that benzo[a]pyrene (BaP) exposed to solar-simulated light (SSL)-induced phosphorylation of histone H2AX (gamma-H2AX), which was recently identified as an early event after the induction of DNA double strand breaks (DSBs).	dsbs	240-244	H2A.X variant histone	Homo sapiens	130-140
18160332-4	2008	Although BaP itself did not produce gamma-H2AX, SSL-exposed BaP significantly generated gamma-H2AX depending on the period of exposure.	Benzo(a)pyrene	60-63	H2A.X variant histone	Homo sapiens	88-98
18160332-5	2008	Furthermore, we revealed that reactive oxygen species produced by the SSL-exposed BaP mainly contributed to the generation of gamma-H2AX.	Reactive Oxygen Species	30-53	H2A.X variant histone	Homo sapiens	126-136
18160332-5	2008	Furthermore, we revealed that reactive oxygen species produced by the SSL-exposed BaP mainly contributed to the generation of gamma-H2AX.	ssl	70-73	H2A.X variant histone	Homo sapiens	126-136
18160332-5	2008	Furthermore, we revealed that reactive oxygen species produced by the SSL-exposed BaP mainly contributed to the generation of gamma-H2AX.	Benzo(a)pyrene	82-85	H2A.X variant histone	Homo sapiens	126-136
18160332-6	2008	The appearance of gamma-H2AX means the induction of the most serious form of DNA damage, DSBs, suggesting the potential risk of carcinogenesis.	dsbs	89-93	H2A.X variant histone	Homo sapiens	18-28
18095327-3	2008	In response to DSBs, H2A.X is phosphorylated and this phosphorylation is required for DSB signaling and the retention of repair proteins at the break site.	dsbs	15-19	H2A.X variant histone	Homo sapiens	21-26
17879239-5	2007	Thirty- to 60-min exposure of cells to 100 or 200 microM H2O2 led to an increase in the level of H2AX phosphorylation and ATM activation, particularly pronounced (nearly fivefold) in S-phase cells.	Hydrogen Peroxide	57-61	H2A.X variant histone	Homo sapiens	97-101
18603118-3	2008	Because phosphorylation of H2AX at Ser 139 correlates well with each DSB, phospho-H2AX is a sensitive marker to used to examine the DNA damage and its repair.	Serine	35-38	H2A.X variant histone	Homo sapiens	27-31
18603118-3	2008	Because phosphorylation of H2AX at Ser 139 correlates well with each DSB, phospho-H2AX is a sensitive marker to used to examine the DNA damage and its repair.	Serine	35-38	H2A.X variant histone	Homo sapiens	82-86
18600224-1	2008	Phosphorylation of histone protein H2AX on serine 139 (gamma-H2AX) occurs at sites flanking DNA double-stranded breaks (DSBs) and can provide a measure of the number of DSBs within a cell.	Serine	43-49	H2A.X variant histone	Homo sapiens	35-39
18600224-1	2008	Phosphorylation of histone protein H2AX on serine 139 (gamma-H2AX) occurs at sites flanking DNA double-stranded breaks (DSBs) and can provide a measure of the number of DSBs within a cell.	Serine	43-49	H2A.X variant histone	Homo sapiens	61-65
18600224-4	2008	The method is based on the fact that H2AX like other histone proteins are retained in the nucleus when cells are lysed at physiological salt concentrations.	Salts	136-140	H2A.X variant histone	Homo sapiens	37-41
18600224-5	2008	Cells are therefore added without fixation to a solution containing detergent to lyse the cells along with a fluorescein isothiocyanate-labeled monoclonal gamma-H2AX antibody, DNA staining dye and blocking agents.	Fluorescein-5-isothiocyanate	109-135	H2A.X variant histone	Homo sapiens	161-165
17910628-6	2007	Bortezomib/PXD101 treatment markedly triggered reactive oxygen species (ROS) generation that was accompanied by p53, H2A.X and p38-mitogen-activated protein kinase phosphorylation.	Bortezomib	0-10	H2A.X variant histone	Homo sapiens	117-122
17957241-9	2007	In this study, treatment of S-phase cells with hydroxyurea lead to efficient H2AX phosphorylation in both euchromatin and heterochromatin at times when these chromatin compartments were undergoing replication.	Hydroxyurea	47-58	H2A.X variant histone	Homo sapiens	77-81
17969164-3	2007	Flow cytometry was used to quantify gammaH2AX (serine 139 phosphorylated form of histone H2AX) expression of antibody-stained cells as a marker for deoxyribonucleic acid (DNA) DSBs one hour and 24 hours after magnetic field exposure.	gammah2ax	36-45	H2A.X variant histone	Homo sapiens	81-93
17903033-3	2007	Here we studied the phosphorylation status of the histone H2AX in micronuclei after exposure of cultured cells to ionizing radiation or treatment with colchicine.	Colchicine	151-161	H2A.X variant histone	Homo sapiens	50-62
17912033-6	2007	Consistent with this hypothesis, we observed higher levels of Serine 139 H2AX phosphorylation in Plk2-deficient as compared to control cells before and after aphidicolin treatment indicating that there is more DNA damage when Plk2 is depleted.	Serine	62-68	H2A.X variant histone	Homo sapiens	73-77
17912033-6	2007	Consistent with this hypothesis, we observed higher levels of Serine 139 H2AX phosphorylation in Plk2-deficient as compared to control cells before and after aphidicolin treatment indicating that there is more DNA damage when Plk2 is depleted.	Aphidicolin	158-169	H2A.X variant histone	Homo sapiens	73-77
17940040-9	2007	The attenuation of BER in myotubes was associated with significant accumulation of DNA damage as detected by increased DNA single-strand breaks and phosphorylated H2AX nuclear foci upon exposure to hydrogen peroxide.	Hydrogen Peroxide	198-215	H2A.X variant histone	Homo sapiens	163-167
17635668-4	2007	We show that aminoindan (0.1-1 mumol/L) significantly reduced the apoptosis-associated phosphorylated protein, H2A.X (Ser139), decreased the cleavage of caspase 9 and caspase 3, while increasing the anti-apoptotic proteins, Bcl-2 and Bcl-xl.	1-aminoindan	13-23	H2A.X variant histone	Homo sapiens	111-116
17540426-0	2007	Activation of p38 mitogen-activated protein kinase by celecoxib oppositely regulates survivin and gamma-H2AX in human colorectal cancer cells.	Celecoxib	54-63	H2A.X variant histone	Homo sapiens	104-108
17908043-3	2007	M-30 and EGCG decreased apoptosis of human SH-SY5Y neuroblastoma cells in a neurorescue, serum deprivation model, via multiple protection mechanisms including: reduction of the pro-apoptotic proteins, Bad and Bax, reduction of apoptosis-associated Ser139 phosphorylated H2A.X and inhibition of the cleavage and activation of caspase-3.	epigallocatechin gallate	9-13	H2A.X variant histone	Homo sapiens	270-275
17512204-6	2007	The activation of DNA damage response as indicated by phosphorylation of H2AX histone, RPA-2 protein, and p53 at serine 15 by the most apoptotic compounds provides additional support to the hypothesis that the genotoxic stress is a critical event mediating apoptosis induction by compounds of this group.	Serine	113-119	H2A.X variant histone	Homo sapiens	73-85
17372987-0	2007	Water soluble fraction of solar-simulated light-exposed crude oil generates phosphorylation of histone H2AX in human skin cells under UVA exposure.	Water	0-5	H2A.X variant histone	Homo sapiens	103-107
17372987-0	2007	Water soluble fraction of solar-simulated light-exposed crude oil generates phosphorylation of histone H2AX in human skin cells under UVA exposure.	Oils	62-65	H2A.X variant histone	Homo sapiens	103-107
17372987-3	2007	In this study, we found that the water soluble fraction (WSF) of crude oil irradiated with solar-simulated light (SSL) generated phosphorylation of histone H2AX (gamma-H2AX) in human skin cells under UVA irradiation, which was due to the formation of DNA double strand breaks (DSBs).	Water	33-38	H2A.X variant histone	Homo sapiens	148-160
17372987-3	2007	In this study, we found that the water soluble fraction (WSF) of crude oil irradiated with solar-simulated light (SSL) generated phosphorylation of histone H2AX (gamma-H2AX) in human skin cells under UVA irradiation, which was due to the formation of DNA double strand breaks (DSBs).	Water	33-38	H2A.X variant histone	Homo sapiens	162-172
17372987-10	2007	These findings demonstrate that exposure of crude oil to sunlight makes the WSF phototoxic, generating DSBs accompanying the appearance of gamma-H2AX in human skin cells.	Oils	50-53	H2A.X variant histone	Homo sapiens	139-149
17875720-8	2007	In vitro pretreatment with NS-123 resulted in accumulation of unrepaired IR-induced DNA strand breaks and prolonged phosphorylation of the surrogate markers of DNA damage H2AX, ataxia telangiectasia mutated protein, DNA-dependent protein kinase, and CHK2 after IR, suggesting that NS-123 inhibits a critical step in the DNA repair pathway.	4'-bromo-3'-nitropropiophenone	27-33	H2A.X variant histone	Homo sapiens	171-214
19746219-8	2007	TSA induces phosphorylation of serine 1981 of ATM, accumulation of phosphorylated H2AX and Chk2, and formation of H2AX foci, in a manner analogous to genotoxic DNA damage.	trichostatin A	0-3	H2A.X variant histone	Homo sapiens	82-86
19746219-8	2007	TSA induces phosphorylation of serine 1981 of ATM, accumulation of phosphorylated H2AX and Chk2, and formation of H2AX foci, in a manner analogous to genotoxic DNA damage.	trichostatin A	0-3	H2A.X variant histone	Homo sapiens	114-118
17611684-9	2007	Following treatment with zoledronate, phosphorylated histone H2AX (gamma-H2AX) displayed patterns of nuclear foci in HOS cells.	Zoledronic Acid	25-36	H2A.X variant histone	Homo sapiens	53-65
17540426-5	2007	Celecoxib blocked the survivin protein expression and increased the phosphorylation of H2AX at serine-193 (gamma-H2AX).	Celecoxib	0-9	H2A.X variant histone	Homo sapiens	87-91
17540426-5	2007	Celecoxib blocked the survivin protein expression and increased the phosphorylation of H2AX at serine-193 (gamma-H2AX).	Celecoxib	0-9	H2A.X variant histone	Homo sapiens	113-117
17540426-5	2007	Celecoxib blocked the survivin protein expression and increased the phosphorylation of H2AX at serine-193 (gamma-H2AX).	Serine	95-101	H2A.X variant histone	Homo sapiens	87-91
17953227-2	2007	It is reported that DNA double-strand breaks (DSB) could induce phosphorylation of H2AX at conservative C-terminal region of serine 139 and the formation of gamma-H2AX.	Serine	125-131	H2A.X variant histone	Homo sapiens	83-87
17540426-5	2007	Celecoxib blocked the survivin protein expression and increased the phosphorylation of H2AX at serine-193 (gamma-H2AX).	Serine	95-101	H2A.X variant histone	Homo sapiens	113-117
17953227-2	2007	It is reported that DNA double-strand breaks (DSB) could induce phosphorylation of H2AX at conservative C-terminal region of serine 139 and the formation of gamma-H2AX.	Serine	125-131	H2A.X variant histone	Homo sapiens	163-167
17540426-10	2007	SB203580, a specific p38 MAP kinase inhibitor, protected the survivin protein expression and decreased the levels of gamma-H2AX and apoptosis in the celecoxib-exposed cells.	SB 203580	0-8	H2A.X variant histone	Homo sapiens	123-127
17540426-10	2007	SB203580, a specific p38 MAP kinase inhibitor, protected the survivin protein expression and decreased the levels of gamma-H2AX and apoptosis in the celecoxib-exposed cells.	Celecoxib	149-158	H2A.X variant histone	Homo sapiens	123-127
17540426-12	2007	Our results provide for the first time that p38 MAP kinase participates in the down-regulation of survivin and subsequently induces the activation of gamma-H2AX for mediating apoptosis following treatment with celecoxib in human colorectal cancer cells.	Celecoxib	210-219	H2A.X variant histone	Homo sapiens	156-160
17498657-1	2007	Double-strand breaks in mammalian DNA lead to rapid phosphorylation of C-terminal serines in histone H2AX (gamma-H2AX) and formation of large nuclear gamma-H2AX foci.	Serine	82-89	H2A.X variant histone	Homo sapiens	93-105
17498657-1	2007	Double-strand breaks in mammalian DNA lead to rapid phosphorylation of C-terminal serines in histone H2AX (gamma-H2AX) and formation of large nuclear gamma-H2AX foci.	Serine	82-89	H2A.X variant histone	Homo sapiens	107-117
17498657-1	2007	Double-strand breaks in mammalian DNA lead to rapid phosphorylation of C-terminal serines in histone H2AX (gamma-H2AX) and formation of large nuclear gamma-H2AX foci.	Serine	82-89	H2A.X variant histone	Homo sapiens	150-160
17594478-4	2007	RESULTS: We report here that H2AX phosphorylation in A549 cells induced by CS was accompanied by activation of ATM, as revealed by ATM phosphorylation on Ser1981 (ATM-S1981P) detected immunocytochemically and by Western blotting.	Cesium	75-77	H2A.X variant histone	Homo sapiens	29-33
17594478-6	2007	When cells were exposed to CS from cigarettes with different tobacco and filter combinations, the expression levels of ATM-S1981P correlated well with the increase in expression of phosphorylated H2AX (gammaH2AX) (R = 0.89).	Cesium	27-29	H2A.X variant histone	Homo sapiens	196-200
17594478-8	2007	CONCLUSION: These data implicate ATM as the PIKK that phosphorylates H2AX in response to DNA damage caused by CS.	Cesium	110-112	H2A.X variant histone	Homo sapiens	69-73
17428792-5	2007	Using potent PARP inhibitors and PARP-1 knock-out cells, we demonstrate a functional interplay between ATM and poly(ADP-ribose) that is important for the phosphorylation of p53, SMC1, and H2AX.	Poly Adenosine Diphosphate Ribose	111-127	H2A.X variant histone	Homo sapiens	188-192
17545612-4	2007	As evidenced by increased Ser(139)-phosphorylated histone H2AX (gammaH2AX), impaired Ku70 function diminished cellular capability to repair DNA DSBs induced by bleomycin, doxorubicin, and etoposide, thereby enhancing their cell-killing effect.	Serine	26-29	H2A.X variant histone	Homo sapiens	50-62
17545612-4	2007	As evidenced by increased Ser(139)-phosphorylated histone H2AX (gammaH2AX), impaired Ku70 function diminished cellular capability to repair DNA DSBs induced by bleomycin, doxorubicin, and etoposide, thereby enhancing their cell-killing effect.	Bleomycin	160-169	H2A.X variant histone	Homo sapiens	50-62
17545612-4	2007	As evidenced by increased Ser(139)-phosphorylated histone H2AX (gammaH2AX), impaired Ku70 function diminished cellular capability to repair DNA DSBs induced by bleomycin, doxorubicin, and etoposide, thereby enhancing their cell-killing effect.	Doxorubicin	171-182	H2A.X variant histone	Homo sapiens	50-62
17545612-4	2007	As evidenced by increased Ser(139)-phosphorylated histone H2AX (gammaH2AX), impaired Ku70 function diminished cellular capability to repair DNA DSBs induced by bleomycin, doxorubicin, and etoposide, thereby enhancing their cell-killing effect.	Etoposide	188-197	H2A.X variant histone	Homo sapiens	50-62
17563398-4	2007	Notably, the time-dependent accumulation of DFO-induced phosphorylation of Ser-139-H2AX (gamma-H2AX), a hallmark for DNA damage, was altered by sh-PKCdelta, and sh-PKCdelta completely abrogated the activation of caspase-3 in DFO-treated cells.	Deferoxamine	44-47	H2A.X variant histone	Homo sapiens	83-87
17563398-4	2007	Notably, the time-dependent accumulation of DFO-induced phosphorylation of Ser-139-H2AX (gamma-H2AX), a hallmark for DNA damage, was altered by sh-PKCdelta, and sh-PKCdelta completely abrogated the activation of caspase-3 in DFO-treated cells.	Deferoxamine	44-47	H2A.X variant histone	Homo sapiens	95-99
17563398-4	2007	Notably, the time-dependent accumulation of DFO-induced phosphorylation of Ser-139-H2AX (gamma-H2AX), a hallmark for DNA damage, was altered by sh-PKCdelta, and sh-PKCdelta completely abrogated the activation of caspase-3 in DFO-treated cells.	Serine	75-78	H2A.X variant histone	Homo sapiens	83-87
17563398-4	2007	Notably, the time-dependent accumulation of DFO-induced phosphorylation of Ser-139-H2AX (gamma-H2AX), a hallmark for DNA damage, was altered by sh-PKCdelta, and sh-PKCdelta completely abrogated the activation of caspase-3 in DFO-treated cells.	Serine	75-78	H2A.X variant histone	Homo sapiens	95-99
17563398-4	2007	Notably, the time-dependent accumulation of DFO-induced phosphorylation of Ser-139-H2AX (gamma-H2AX), a hallmark for DNA damage, was altered by sh-PKCdelta, and sh-PKCdelta completely abrogated the activation of caspase-3 in DFO-treated cells.	Deferoxamine	225-228	H2A.X variant histone	Homo sapiens	83-87
17563398-4	2007	Notably, the time-dependent accumulation of DFO-induced phosphorylation of Ser-139-H2AX (gamma-H2AX), a hallmark for DNA damage, was altered by sh-PKCdelta, and sh-PKCdelta completely abrogated the activation of caspase-3 in DFO-treated cells.	Deferoxamine	225-228	H2A.X variant histone	Homo sapiens	95-99
17167777-2	2007	The results showed that MMC treatment arrested the cells in S-phase and induced the appearance of gamma-H2AX and Rad51 nuclear foci, accompanied with a sequestering of Rad51 to the nuclear matrix.	Mitomycin	24-27	H2A.X variant histone	Homo sapiens	104-108
17505006-5	2007	RESULTS: ABT-888 reduced clonogenic survival in H460 lung cancer cells, and inhibited DNA repair as shown by enhanced expression of DNA strand break marker histone gamma-H2AX.	2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid	9-12	H2A.X variant histone	Homo sapiens	170-174
17363589-5	2007	We found that untreated GIST cells down-regulate H2AX in a pathway that involves KIT, phosphoinositide-3-kinase, and the ubiquitin/proteasome machinery, and that the imatinib-mediated H2AX up-regulation correlates with imatinib sensitivity.	Imatinib Mesylate	219-227	H2A.X variant histone	Homo sapiens	184-188
17406032-0	2007	H2AX phosphorylation marks gemcitabine-induced stalled replication forks and their collapse upon S-phase checkpoint abrogation.	gemcitabine	27-38	H2A.X variant histone	Homo sapiens	0-4
17406032-2	2007	The histone variant H2AX is phosphorylated on Ser(139) (gamma-H2AX) and forms nuclear foci at sites of DNA damage.	Serine	46-49	H2A.X variant histone	Homo sapiens	20-24
17406032-2	2007	The histone variant H2AX is phosphorylated on Ser(139) (gamma-H2AX) and forms nuclear foci at sites of DNA damage.	Serine	46-49	H2A.X variant histone	Homo sapiens	62-66
17406032-3	2007	Here, we characterize the concentration- and time-dependent phosphorylation of H2AX in response to gemcitabine-induced stalled replication forks.	gemcitabine	99-110	H2A.X variant histone	Homo sapiens	79-83
17406032-4	2007	The number of gamma-H2AX foci increased with time up to 2 to 6 h after exposure to gemcitabine, whereas longer exposures did not cause greater phosphorylation or increase cell death.	gemcitabine	83-94	H2A.X variant histone	Homo sapiens	20-24
17406032-5	2007	The percentage of gamma-H2AX-positive cells increased with concentrations of gemcitabine up to 0.1 micromol/L, and gamma-H2AX was most evident in the S-phase fraction.	gemcitabine	77-88	H2A.X variant histone	Homo sapiens	24-28
17406032-6	2007	Phosphorylation of ataxia-telangiectasia mutated (ATM) on Ser(1981) was also associated with S-phase cells and colocalized in the nucleus with phosphorylated H2AX foci after gemcitabine exposure.	Serine	58-61	H2A.X variant histone	Homo sapiens	158-162
17406032-9	2007	Exposure of previously gemcitabine-treated cultures to the Chk1 inhibitor 7-hydroxystaurosporine (UCN-01) caused a 10-fold increase in H2AX phosphorylation, which was displayed as an even pan-nuclear staining.	gemcitabine	23-34	H2A.X variant histone	Homo sapiens	135-139
17406032-9	2007	Exposure of previously gemcitabine-treated cultures to the Chk1 inhibitor 7-hydroxystaurosporine (UCN-01) caused a 10-fold increase in H2AX phosphorylation, which was displayed as an even pan-nuclear staining.	7-hydroxystaurosporine	74-96	H2A.X variant histone	Homo sapiens	135-139
17363589-0	2007	Histone H2AX is a mediator of gastrointestinal stromal tumor cell apoptosis following treatment with imatinib mesylate.	Imatinib Mesylate	101-118	H2A.X variant histone	Homo sapiens	0-12
17363589-4	2007	We report here that imatinib triggers GIST cell apoptosis in part through the up-regulation of soluble histone H2AX, a core histone H2A variant.	Imatinib Mesylate	20-28	H2A.X variant histone	Homo sapiens	111-115
17363589-5	2007	We found that untreated GIST cells down-regulate H2AX in a pathway that involves KIT, phosphoinositide-3-kinase, and the ubiquitin/proteasome machinery, and that the imatinib-mediated H2AX up-regulation correlates with imatinib sensitivity.	Imatinib Mesylate	166-174	H2A.X variant histone	Homo sapiens	184-188
17406032-9	2007	Exposure of previously gemcitabine-treated cultures to the Chk1 inhibitor 7-hydroxystaurosporine (UCN-01) caused a 10-fold increase in H2AX phosphorylation, which was displayed as an even pan-nuclear staining.	7-hydroxystaurosporine	98-104	H2A.X variant histone	Homo sapiens	135-139
17406032-11	2007	Thus, H2AX becomes phosphorylated and forms nuclear foci in response to gemcitabine-induced stalled replication forks, and this is greatly increased upon checkpoint abrogation.	gemcitabine	72-83	H2A.X variant histone	Homo sapiens	6-10
17363589-5	2007	We found that untreated GIST cells down-regulate H2AX in a pathway that involves KIT, phosphoinositide-3-kinase, and the ubiquitin/proteasome machinery, and that the imatinib-mediated H2AX up-regulation correlates with imatinib sensitivity.	Imatinib Mesylate	219-227	H2A.X variant histone	Homo sapiens	49-53
17363589-6	2007	Depletion of H2AX attenuated the apoptotic response of GIST cells to imatinib.	Imatinib Mesylate	69-77	H2A.X variant histone	Homo sapiens	13-17
17363589-8	2007	Our results underscore the importance of H2AX as a human tumor suppressor protein, provide mechanistic insights into imatinib-induced tumor cell apoptosis and establish H2AX as a novel target in cancer therapy.	Imatinib Mesylate	117-125	H2A.X variant histone	Homo sapiens	41-45
17363589-8	2007	Our results underscore the importance of H2AX as a human tumor suppressor protein, provide mechanistic insights into imatinib-induced tumor cell apoptosis and establish H2AX as a novel target in cancer therapy.	Imatinib Mesylate	117-125	H2A.X variant histone	Homo sapiens	169-173
17297310-0	2007	Induction of ATM activation, histone H2AX phosphorylation and apoptosis by etoposide: relation to cell cycle phase.	Etoposide	75-84	H2A.X variant histone	Homo sapiens	37-41
17220276-7	2007	Likewise, the DNA polymerase inhibitor aphidicolin triggered increased cell death, chromosomal aberrations, and H2AX phosphorylation, a marker for double-stranded DNA breaks, in Hus1(neo/neo) and Hus1(neo/Delta1) cultures compared to controls.	Aphidicolin	39-50	H2A.X variant histone	Homo sapiens	112-116
17327276-1	2007	Human histone H2AX is rapidly phosphorylated on serine 139 in response to DNA double-strand breaks and plays a crucial role in tethering the factors involved in DNA repair and damage signaling.	Serine	48-54	H2A.X variant histone	Homo sapiens	6-18
17327276-5	2007	The treatment of cytosine-beta-D-arabinofuranoside strikingly enhances the NER-dependent H2AX phosphorylation and induces the accumulation of replication protein A (RPA) and ATR-interacting protein (ATRIP) at locally UV-damaged subnuclear regions.	Cytarabine	17-50	H2A.X variant histone	Homo sapiens	89-93
17172468-9	2007	Taken together, these data suggest that E4orf6 disrupts cellular DSBR signaling by inhibiting PP2A, leading to prolonged H2AX phosphorylation, hyperactivation of PARP, and AIF translocation to the nucleus.	dsbr	65-69	H2A.X variant histone	Homo sapiens	121-125
17227291-1	2007	OBJECTIVES: We recently postulated that constitutive activation of Ataxia Telangiectasia, Mutated (CAA) and constitutive histone H2AX phosphorylation (CHP) seen in cells not treated with genotoxic agents are the events triggered by DNA damage caused by endogenous reactive oxygen species (ROS), the product of mitochondrial oxidative metabolism.	Reactive Oxygen Species	264-287	H2A.X variant histone	Homo sapiens	121-133
17227291-1	2007	OBJECTIVES: We recently postulated that constitutive activation of Ataxia Telangiectasia, Mutated (CAA) and constitutive histone H2AX phosphorylation (CHP) seen in cells not treated with genotoxic agents are the events triggered by DNA damage caused by endogenous reactive oxygen species (ROS), the product of mitochondrial oxidative metabolism.	Reactive Oxygen Species	289-292	H2A.X variant histone	Homo sapiens	121-133
17297310-7	2007	The extent of etoposide-induced H2AX phosphorylation was partially reduced by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Etoposide	14-23	H2A.X variant histone	Homo sapiens	32-36
17297310-7	2007	The extent of etoposide-induced H2AX phosphorylation was partially reduced by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Reactive Oxygen Species	120-143	H2A.X variant histone	Homo sapiens	32-36
17297310-7	2007	The extent of etoposide-induced H2AX phosphorylation was partially reduced by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Reactive Oxygen Species	145-148	H2A.X variant histone	Homo sapiens	32-36
17200364-2	2007	EXPERIMENTAL DESIGN: Enhancement of temozolomide via methoxyamine and MPG overexpression was analyzed using in vitro assays, including 3-(4-5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium salt (MTS) assay, apoptosis via Annexin staining, and Western blotting for H2AX phosphorylation to quantitate DNA damage.	Temozolomide	36-48	H2A.X variant histone	Homo sapiens	299-303
17245119-5	2007	Correspondingly, in PANC-1 cells, EXEL-9844 increased gemcitabine-induced H2AX phosphorylation, blocked Cdc25A phosphorylation, and induced premature mitotic entry.	gemcitabine	54-65	H2A.X variant histone	Homo sapiens	74-78
17431330-2	2007	In several organisms, gamma-H2AX presence has been demonstrated in meiotic processes such as recombination and sex chromosome inactivation during prophase I (from leptotene to pachytene).	leptotene	163-172	H2A.X variant histone	Homo sapiens	28-32
17431330-2	2007	In several organisms, gamma-H2AX presence has been demonstrated in meiotic processes such as recombination and sex chromosome inactivation during prophase I (from leptotene to pachytene).	pachytene	176-185	H2A.X variant histone	Homo sapiens	28-32
17431330-5	2007	During the first meiotic division, gamma-H2AX is associated with i) recombination, as deduced from its presence in leptotene-zygotene over all chromosome length, ii) X chromosome inactivation, since at pachytene gamma-H2AX is present in the X chromosome only, and iii) chromosome segregation, as deduced from gamma-H2AX presence in centromere regions at first metaphase-anaphase.	leptotene-zygotene	115-133	H2A.X variant histone	Homo sapiens	41-45
17284459-7	2007	Interindividual difference in the gamma-H2AX signal in response to ionizing radiation and the DSB-inducing drug calicheamicin was almost 2-fold in blood cells from patients, indicating that the amount of gamma-H2AX produced in response to a given dose of radiation varies significantly in the human population.	calicheamicin T	112-125	H2A.X variant histone	Homo sapiens	210-214
17284459-1	2007	Phosphorylation of histone H2AX on serine 139 (gamma-H2AX, gammaH2AX) occurs at sites flanking DNA double-strand breaks (DSBs) and can provide a measure of the number of DSBs within a cell.	Serine	35-41	H2A.X variant histone	Homo sapiens	27-31
17874213-1	2007	Double-strand DNA breaks (DSBs) induced by ionizing radiation can be visualized in human cells using antibodies against Ser-139 phosphorylated histone H2AX (gamma-H2AX).	Serine	120-123	H2A.X variant histone	Homo sapiens	143-155
17874213-1	2007	Double-strand DNA breaks (DSBs) induced by ionizing radiation can be visualized in human cells using antibodies against Ser-139 phosphorylated histone H2AX (gamma-H2AX).	Serine	120-123	H2A.X variant histone	Homo sapiens	157-167
17874213-3	2007	We estimated whether transcription is affected in chromatin domains containing gamma-H2AX by following in vivo incorporation of 5-bromouridine triphosphate (BrUTP) loaded by cell scratching (run-on assay).	5-bromouridine triphosphate	128-155	H2A.X variant histone	Homo sapiens	79-89
17284459-1	2007	Phosphorylation of histone H2AX on serine 139 (gamma-H2AX, gammaH2AX) occurs at sites flanking DNA double-strand breaks (DSBs) and can provide a measure of the number of DSBs within a cell.	Serine	35-41	H2A.X variant histone	Homo sapiens	53-57
17111099-3	2007	Another approach was aimed at determining possible correlations between the extent of hydroxyurea-induced phosphorylation of H2AX histones and the quantities of root meristem cells induced by caffeine to enter aberrant mitotic division (premature chromosome condensation).	Hydroxyurea	86-97	H2A.X variant histone	Homo sapiens	125-129
17284459-6	2007	We found that all nucleated blood cell types examined, including the short-lived neutrophils induce gamma-H2AX in response to DSBs.	dsbs	126-130	H2A.X variant histone	Homo sapiens	106-110
17284459-7	2007	Interindividual difference in the gamma-H2AX signal in response to ionizing radiation and the DSB-inducing drug calicheamicin was almost 2-fold in blood cells from patients, indicating that the amount of gamma-H2AX produced in response to a given dose of radiation varies significantly in the human population.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	94-97	H2A.X variant histone	Homo sapiens	210-214
17085668-8	2006	Pretreatment with 2ME enhanced H2AX phosphorylation, its foci, and phosphorylation of ATM kinase and delayed re-entry of cell cycle progression after ionizing radiation.	2-Methoxyestradiol	18-21	H2A.X variant histone	Homo sapiens	31-35
17185671-1	2007	PURPOSE: To prospectively determine if gammaH2AX (phosphorylated form of H2AX histone variant)-based visualization and quantification of DNA damage induced in peripheral blood mononuclear cells (PBMCs) can be used to estimate the radiation dose received by adult patients who undergo multidetector computed tomography (CT).	gammah2ax	39-48	H2A.X variant histone	Homo sapiens	73-85
17145805-12	2006	CONCLUSIONS: TOPK binds with histone H2AX and inhibits As(3+)-induced apoptosis through phosphorylation of histone H2AX.	Arsenic(3+) ion	55-61	H2A.X variant histone	Homo sapiens	29-41
17145805-12	2006	CONCLUSIONS: TOPK binds with histone H2AX and inhibits As(3+)-induced apoptosis through phosphorylation of histone H2AX.	Arsenic(3+) ion	55-61	H2A.X variant histone	Homo sapiens	37-41
17172433-5	2006	Further upstream, gallic acid also induced phosphorylation of both cdc25A and cdc25C via ataxia telangiectasia mutated (ATM)-checkpoint kinase 2 (Chk2) activation as a DNA damage response evidenced by increased phospho-histone 2AX (H2A.X) that is phosphorylated by ATM in response to DNA damage.	Gallic Acid	18-29	H2A.X variant histone	Homo sapiens	211-230
17172433-5	2006	Further upstream, gallic acid also induced phosphorylation of both cdc25A and cdc25C via ataxia telangiectasia mutated (ATM)-checkpoint kinase 2 (Chk2) activation as a DNA damage response evidenced by increased phospho-histone 2AX (H2A.X) that is phosphorylated by ATM in response to DNA damage.	Gallic Acid	18-29	H2A.X variant histone	Homo sapiens	232-237
17172433-6	2006	Time kinetics of ATM phosphorylation, together with those of H2A.X and Chk2, was in accordance with an inactivating phosphorylation of cdc25A and cdc25C phosphatases and cdc2 kinase, suggesting that gallic acid increases cdc25A/C-cdc2 phosphorylation and thereby inactivation via ATM-Chk2 pathway following DNA damage that induces cell cycle arrest.	Gallic Acid	199-210	H2A.X variant histone	Homo sapiens	61-66
17172433-7	2006	Caffeine, an ATM/ataxia telangiectasia-rad3-related inhibitor, reversed gallic acid-caused ATM and H2A.X phosphorylation and cell cycle arrest, supporting the role of ATM pathway in gallic acid-induced cell cycle arrest.	Caffeine	0-8	H2A.X variant histone	Homo sapiens	99-104
17172433-7	2006	Caffeine, an ATM/ataxia telangiectasia-rad3-related inhibitor, reversed gallic acid-caused ATM and H2A.X phosphorylation and cell cycle arrest, supporting the role of ATM pathway in gallic acid-induced cell cycle arrest.	Gallic Acid	72-83	H2A.X variant histone	Homo sapiens	99-104
17064697-2	2006	In human spermatozoa, the present study showed that H(2)O(2) induced H2AX phosphorylation in a time- and dose-dependent manner.	Hydrogen Peroxide	52-60	H2A.X variant histone	Homo sapiens	69-73
17064697-4	2006	Meanwhile, the neutral comet assay also revealed DSBs production in correlation with H2AX phosphorylation assessed by flow cytometry.	dsbs	49-53	H2A.X variant histone	Homo sapiens	85-89
17064697-8	2006	Collectively, these results demonstrate that oxidative stress can induce H2AX phosphorylation in human spermatozoa through DSB induction, and that gammaH2AX may be used as a sensitive, novel marker for such DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	123-126	H2A.X variant histone	Homo sapiens	73-77
17064697-8	2006	Collectively, these results demonstrate that oxidative stress can induce H2AX phosphorylation in human spermatozoa through DSB induction, and that gammaH2AX may be used as a sensitive, novel marker for such DSBs.	gammah2ax	147-156	H2A.X variant histone	Homo sapiens	73-77
17106266-0	2006	Phosphorylation of histone H2AX on Ser 139 and activation of ATM during oxidative burst in phorbol ester-treated human leukocytes.	Serine	35-38	H2A.X variant histone	Homo sapiens	27-31
17106266-0	2006	Phosphorylation of histone H2AX on Ser 139 and activation of ATM during oxidative burst in phorbol ester-treated human leukocytes.	Phorbol Esters	91-104	H2A.X variant histone	Homo sapiens	27-31
17106266-5	2006	We now present the evidence that induction of oxidative stress in human peripheral blood leukocytes by phorbol myristate acetate (PMA) was associated with intense phosphorylation of histone H2AX and with ATM activation, seen already 60 min after exposure to PMA.	Tetradecanoylphorbol Acetate	103-128	H2A.X variant histone	Homo sapiens	190-194
17106266-5	2006	We now present the evidence that induction of oxidative stress in human peripheral blood leukocytes by phorbol myristate acetate (PMA) was associated with intense phosphorylation of histone H2AX and with ATM activation, seen already 60 min after exposure to PMA.	Tetradecanoylphorbol Acetate	130-133	H2A.X variant histone	Homo sapiens	190-194
17106266-9	2006	The observed H2AX phosphorylation in lymphocytes may reflect their DNA damage by the superoxide ions propagating from the neighboring granulocytes and/or monocytes.	Superoxides	85-95	H2A.X variant histone	Homo sapiens	13-17
17145805-0	2006	Lymphokine-activated killer T-cell-originated protein kinase phosphorylation of histone H2AX prevents arsenite-induced apoptosis in RPMI7951 melanoma cells.	arsenite	102-110	H2A.X variant histone	Homo sapiens	80-92
17145805-5	2006	Immunofluorescence, Western blot, and flow cytometry were used to assess the effect of arsenic on TOPK, histone H2AX, and apoptosis in RPMI7951 cells.	Arsenic	87-94	H2A.X variant histone	Homo sapiens	104-116
16557274-3	2006	However, only doxorubicin and cisplatin induced activation of H2AX, a marker for double-strand break formation.	Doxorubicin	14-25	H2A.X variant histone	Homo sapiens	62-66
16557274-3	2006	However, only doxorubicin and cisplatin induced activation of H2AX, a marker for double-strand break formation.	Cisplatin	30-39	H2A.X variant histone	Homo sapiens	62-66
17085668-9	2006	Augmentation of both radiosensitivity and H2AX phosphorylation was substantially reduced by SP600125 or overexpression of a dominant-negative mutant SEK1.	pyrazolanthrone	92-100	H2A.X variant histone	Homo sapiens	42-46
16940754-4	2006	Sensitive reporters of DNA damage, particularly the induction of DNA double-strand breaks (DSBs), are activation of ATM, through its phosphorylation on Ser 1981, and phosphorylation of histone H2AX on Ser 139; the phosphorylated form of H2AX has been named gammaH2AX.	Serine	201-204	H2A.X variant histone	Homo sapiens	193-197
17056792-4	2006	BITC (10 micromol/L) treatment caused marked phosphorylation of H2A.x (2.6-fold) and permanent damage to Capan-2 cells.	benzyl isothiocyanate	0-4	H2A.X variant histone	Homo sapiens	64-69
16872365-0	2006	Extent of constitutive histone H2AX phosphorylation on Ser-139 varies in cells with different TP53 status.	Serine	55-58	H2A.X variant histone	Homo sapiens	31-35
16969115-4	2006	Here, we show that a short-term treatment with roscovitine is sufficient to inhibit DNA synthesis, and to activate a DNA damage checkpoint response, as indicated by phosphorylation of p53-Ser15, replication protein A, and histone H2AX.	Roscovitine	47-58	H2A.X variant histone	Homo sapiens	222-234
16760673-0	2006	Activation of ATM and histone H2AX phosphorylation induced by mitoxantrone but not by topotecan is prevented by the antioxidant N-acetyl-L-cysteine.	Mitoxantrone	62-74	H2A.X variant histone	Homo sapiens	22-34
16760673-0	2006	Activation of ATM and histone H2AX phosphorylation induced by mitoxantrone but not by topotecan is prevented by the antioxidant N-acetyl-L-cysteine.	Acetylcysteine	128-147	H2A.X variant histone	Homo sapiens	22-34
16760673-3	2006	In the present study we observed that treatment of human lung carcinoma A549 or promyelocytic leukemic HL-60 cells with MXT led to ATM activation and phosphorylation of histone H2AX on Ser-139, the reporters of induction of DSBs, in all phases of the cell-cycle.	Serine	185-188	H2A.X variant histone	Homo sapiens	169-181
16760673-5	2006	Unlike MXT, the treatment with TP induced ATM activation and H2AX phosphorylation almost exclusively in S-phase cells and only S phase cells underwent apoptosis.	Topotecan	31-33	H2A.X variant histone	Homo sapiens	61-65
16861926-0	2006	Nitrogen oxide-releasing aspirin induces histone H2AX phosphorylation, ATM activation and apoptosis preferentially in S-phase cells: involvement of reactive oxygen species.	Nitrogen	0-8	H2A.X variant histone	Homo sapiens	49-53
16872365-1	2006	In response to DNA damage by genotoxic agents, histone H2AX is phosphorylated on Ser-139.	Serine	81-84	H2A.X variant histone	Homo sapiens	47-59
16861926-0	2006	Nitrogen oxide-releasing aspirin induces histone H2AX phosphorylation, ATM activation and apoptosis preferentially in S-phase cells: involvement of reactive oxygen species.	Aspirin	25-32	H2A.X variant histone	Homo sapiens	49-53
16760673-6	2006	The induction of both ATM activation and H2AX phosphorylation by MXT was prevented to a large extent by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Mitoxantrone	65-68	H2A.X variant histone	Homo sapiens	41-45
16872365-3	2006	This constitutive H2AX phosphorylation is markedly reduced by exposure of cells to the reactive oxygen species scavenger N-acetyl-L-cysteine.	Reactive Oxygen Species	87-110	H2A.X variant histone	Homo sapiens	18-22
16760673-6	2006	The induction of both ATM activation and H2AX phosphorylation by MXT was prevented to a large extent by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Acetylcysteine	104-123	H2A.X variant histone	Homo sapiens	41-45
16760673-6	2006	The induction of both ATM activation and H2AX phosphorylation by MXT was prevented to a large extent by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Reactive Oxygen Species	146-169	H2A.X variant histone	Homo sapiens	41-45
16861926-4	2006	We observed that even brief (1 h) treatment of human B-lymphoblastoid TK6 cells with >or=5 microM NO-ASA led to DNA damage revealed by the alkaline and neutral comet assays, histone H2AX phosphorylation on Ser 139, and ATM phosphorylation on Ser 1981, a marker of activation of this kinase.	Aspirin	104-107	H2A.X variant histone	Homo sapiens	185-189
16861926-8	2006	The induction of phosphorylation of H2AX on Ser 139 by NO-ASA was markedly attenuated in the presence of N-acetyl-L-cysteine, a scavenger of reactive oxygen species (ROS).	Serine	44-47	H2A.X variant histone	Homo sapiens	36-40
16861926-8	2006	The induction of phosphorylation of H2AX on Ser 139 by NO-ASA was markedly attenuated in the presence of N-acetyl-L-cysteine, a scavenger of reactive oxygen species (ROS).	Aspirin	58-61	H2A.X variant histone	Homo sapiens	36-40
16861926-8	2006	The induction of phosphorylation of H2AX on Ser 139 by NO-ASA was markedly attenuated in the presence of N-acetyl-L-cysteine, a scavenger of reactive oxygen species (ROS).	Acetylcysteine	105-124	H2A.X variant histone	Homo sapiens	36-40
16861926-8	2006	The induction of phosphorylation of H2AX on Ser 139 by NO-ASA was markedly attenuated in the presence of N-acetyl-L-cysteine, a scavenger of reactive oxygen species (ROS).	Reactive Oxygen Species	141-164	H2A.X variant histone	Homo sapiens	36-40
16861926-8	2006	The induction of phosphorylation of H2AX on Ser 139 by NO-ASA was markedly attenuated in the presence of N-acetyl-L-cysteine, a scavenger of reactive oxygen species (ROS).	Reactive Oxygen Species	166-169	H2A.X variant histone	Homo sapiens	36-40
16760673-6	2006	The induction of both ATM activation and H2AX phosphorylation by MXT was prevented to a large extent by N-acetyl-L-cysteine (NAC), a scavenger of reactive oxygen species (ROS).	Reactive Oxygen Species	171-174	H2A.X variant histone	Homo sapiens	41-45
16872365-3	2006	This constitutive H2AX phosphorylation is markedly reduced by exposure of cells to the reactive oxygen species scavenger N-acetyl-L-cysteine.	Acetylcysteine	121-140	H2A.X variant histone	Homo sapiens	18-22
16872365-4	2006	Therefore, it appears likely that constitutive H2AX phosphorylation reflects the ongoing oxidative DNA damage induced by the reactive oxygen species during progression through the cell cycle.	Reactive Oxygen Species	125-148	H2A.X variant histone	Homo sapiens	47-51
16872365-9	2006	Also, the degree of attenuation of constitutive H2AX phosphorylation by N-acetyl-L-cysteine was less pronounced in NH32, WTK1, and HL-60, compared to TK6 cells.	Acetylcysteine	72-91	H2A.X variant histone	Homo sapiens	48-52
16772334-5	2006	The ability of cells expressing these mutants to form DNA repair foci comprising phosphorylated H2AX in response to mild doses of cisplatin or UV irradiation was markedly diminished, unlike the nearly normal response of cells expressing wild-type GFP-lamin A or disease-causing H222P and R482L mutants.	Cisplatin	130-139	H2A.X variant histone	Homo sapiens	96-100
16820894-0	2006	Constitutive histone H2AX phosphorylation on Ser-139 in cells untreated by genotoxic agents is cell-cycle phase specific and attenuated by scavenging reactive oxygen species.	Serine	45-48	H2A.X variant histone	Homo sapiens	21-25
16820894-0	2006	Constitutive histone H2AX phosphorylation on Ser-139 in cells untreated by genotoxic agents is cell-cycle phase specific and attenuated by scavenging reactive oxygen species.	Reactive Oxygen Species	150-173	H2A.X variant histone	Homo sapiens	21-25
16820894-1	2006	DNA damage, particularly when it involves formation of double-strand breaks (DSBs), triggers phosphorylation of histone H2AX on Ser-139.	Serine	128-131	H2A.X variant histone	Homo sapiens	112-124
16820894-2	2006	Phosphorylated H2AX has been named gammaH2AX, and induction of gammaH2AX in cells exposed to genotoxic agents is considered a sensitive and specific reporter of DNA damage.	gammah2ax	35-44	H2A.X variant histone	Homo sapiens	15-19
16820894-2	2006	Phosphorylated H2AX has been named gammaH2AX, and induction of gammaH2AX in cells exposed to genotoxic agents is considered a sensitive and specific reporter of DNA damage.	gammah2ax	63-72	H2A.X variant histone	Homo sapiens	15-19
16820894-5	2006	Furthermore, constitutive H2AX phosphorylation in human pulmonary carcinoma A549, lymphoblastoid TK6, and in normal bronchial epithelial cells was reduced following cell exposure to N-acetyl-L-cysteine, a scavenger of reactive oxygen intermediates; the reduction was most pronounced for G(2)M cells.	Acetylcysteine	182-201	H2A.X variant histone	Homo sapiens	26-30
16820894-5	2006	Furthermore, constitutive H2AX phosphorylation in human pulmonary carcinoma A549, lymphoblastoid TK6, and in normal bronchial epithelial cells was reduced following cell exposure to N-acetyl-L-cysteine, a scavenger of reactive oxygen intermediates; the reduction was most pronounced for G(2)M cells.	reactive oxygen intermediates	218-247	H2A.X variant histone	Homo sapiens	26-30
16820894-6	2006	Growth of A549 cells in the presence of buthionine sulfoximine, an inhibitor of glutathione synthetase, amplified the level of constitutive H2AX phosphorylation in A549 cells.	Buthionine Sulfoximine	40-62	H2A.X variant histone	Homo sapiens	140-144
16820894-7	2006	The observed constitutive H2AX phosphorylation may be a reflection of the ongoing DNA damage mediated by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle, leading to formation of DSBs during the S phase.	Reactive Oxygen Species	105-128	H2A.X variant histone	Homo sapiens	26-30
16820894-7	2006	The observed constitutive H2AX phosphorylation may be a reflection of the ongoing DNA damage mediated by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle, leading to formation of DSBs during the S phase.	Reactive Oxygen Species	130-133	H2A.X variant histone	Homo sapiens	26-30
16820894-7	2006	The observed constitutive H2AX phosphorylation may be a reflection of the ongoing DNA damage mediated by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle, leading to formation of DSBs during the S phase.	dsbs	234-238	H2A.X variant histone	Homo sapiens	26-30
16928830-6	2006	In support of these findings, PXD101 was shown to increase the acetylation of alpha-tubulin induced by docetaxel and the phosphorylation of H2AX induced by carboplatin.	Carboplatin	156-167	H2A.X variant histone	Homo sapiens	140-144
16751067-2	2006	To explore their effects on ionizing radiation (IR), we examined whether the HDAC inhibitors m-carboxycinnamic acid bis-hydroxamide (CBHA) and depsipeptide FK228 affect H2AX phosphorylation (gamma-H2AX), a landmark of DNA double-strand breaks after IR exposure.	carboxycinnamic acid bishydroxamide	93-131	H2A.X variant histone	Homo sapiens	169-173
16751067-2	2006	To explore their effects on ionizing radiation (IR), we examined whether the HDAC inhibitors m-carboxycinnamic acid bis-hydroxamide (CBHA) and depsipeptide FK228 affect H2AX phosphorylation (gamma-H2AX), a landmark of DNA double-strand breaks after IR exposure.	romidepsin	156-161	H2A.X variant histone	Homo sapiens	169-173
16751067-7	2006	CBHA and FK228, but not 5-fluorouracil, enhanced IR-induced gamma-H2AX in A549 and other cancer cell lines.	carboxycinnamic acid bishydroxamide	0-4	H2A.X variant histone	Homo sapiens	66-70
16751067-7	2006	CBHA and FK228, but not 5-fluorouracil, enhanced IR-induced gamma-H2AX in A549 and other cancer cell lines.	romidepsin	9-14	H2A.X variant histone	Homo sapiens	66-70
16818713-7	2006	Analysis of the radiation-induced H2AX phosphorylation revealed that BIBX, as well as the PI3K inhibitor LY294002, leads to a marked reduction of P-H2AX in K-RAS(mt)-A549 and MDA-MB-231 cells, but not in K-RAS(wt)-FaDu and HH4ded cells.	BIBX 1382BS	69-73	H2A.X variant histone	Homo sapiens	34-38
16818713-7	2006	Analysis of the radiation-induced H2AX phosphorylation revealed that BIBX, as well as the PI3K inhibitor LY294002, leads to a marked reduction of P-H2AX in K-RAS(mt)-A549 and MDA-MB-231 cells, but not in K-RAS(wt)-FaDu and HH4ded cells.	BIBX 1382BS	69-73	H2A.X variant histone	Homo sapiens	148-152
16818713-7	2006	Analysis of the radiation-induced H2AX phosphorylation revealed that BIBX, as well as the PI3K inhibitor LY294002, leads to a marked reduction of P-H2AX in K-RAS(mt)-A549 and MDA-MB-231 cells, but not in K-RAS(wt)-FaDu and HH4ded cells.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	105-113	H2A.X variant histone	Homo sapiens	148-152
16628006-0	2006	2-deoxy-D-glucose reduces the level of constitutive activation of ATM and phosphorylation of histone H2AX.	Deoxyglucose	0-17	H2A.X variant histone	Homo sapiens	93-105
16563640-10	2006	The dramatic reduction in RNA synthesis upon actinomycin D treatment was associated with two important cellular events, heterochromatin silencing and formation of DNA damage/repair nuclear foci, demonstrated by the expression of tri-methylated histone H4 and phosphorylated H2AX, respectively.	Dactinomycin	45-58	H2A.X variant histone	Homo sapiens	274-278
16678501-2	2006	Following treatment with a psoralen derivative and ultraviolet A radiation doses that produce significant numbers of crosslinks, gamma-H2AX levels in nucleotide excision repair-deficient XP-A fibroblasts (XP12RO-SV) increased to levels that were twice those observed in normal control GM637 fibroblasts.	Ficusin	27-35	H2A.X variant histone	Homo sapiens	129-139
16678501-4	2006	XP-F fibroblasts (XP2YO-SV and XP3YO) that are also repair-deficient exhibited gamma-H2AX levels below even control fibroblasts following treatment with psoralen and ultraviolet A radiation.	Ficusin	153-161	H2A.X variant histone	Homo sapiens	79-89
16678501-7	2006	Angelicin, a furocoumarin which forms only monoadducts and not crosslinks following ultraviolet A radiation, as well as ultraviolet C radiation, resulted only in weak induction of gamma-H2AX in all cells, suggesting that the double strand breaks observed with psoralen and ultraviolet A treatment result preferentially following crosslink formation.	angelicin	0-9	H2A.X variant histone	Homo sapiens	180-190
16672000-3	2006	We have now observed that HL-60 cells exposed to inhibitors of DNA replication (thymidine, aphidicolin and hydroxyurea), at concentrations commonly used to synchronize cell populations, had histone H2AX phosphorylated on Ser-139.	Thymidine	80-89	H2A.X variant histone	Homo sapiens	198-202
16672000-3	2006	We have now observed that HL-60 cells exposed to inhibitors of DNA replication (thymidine, aphidicolin and hydroxyurea), at concentrations commonly used to synchronize cell populations, had histone H2AX phosphorylated on Ser-139.	Aphidicolin	91-102	H2A.X variant histone	Homo sapiens	198-202
16672000-3	2006	We have now observed that HL-60 cells exposed to inhibitors of DNA replication (thymidine, aphidicolin and hydroxyurea), at concentrations commonly used to synchronize cell populations, had histone H2AX phosphorylated on Ser-139.	Hydroxyurea	107-118	H2A.X variant histone	Homo sapiens	198-202
16672000-3	2006	We have now observed that HL-60 cells exposed to inhibitors of DNA replication (thymidine, aphidicolin and hydroxyurea), at concentrations commonly used to synchronize cell populations, had histone H2AX phosphorylated on Ser-139.	Serine	221-224	H2A.X variant histone	Homo sapiens	198-202
16786700-3	2006	We have previously found that phosphorylation of histone H2AX (gamma-H2AX), which accompanied the induction of DNA double strand breaks (DSBs), was significantly induced by low concentrations of benzo[a]pyrene (10(-9)-10(-7) M) and UVA (0.6 J/cm2) in CHO-K1 cells.	dsbs	137-141	H2A.X variant histone	Homo sapiens	49-61
16786700-3	2006	We have previously found that phosphorylation of histone H2AX (gamma-H2AX), which accompanied the induction of DNA double strand breaks (DSBs), was significantly induced by low concentrations of benzo[a]pyrene (10(-9)-10(-7) M) and UVA (0.6 J/cm2) in CHO-K1 cells.	benzo[a	195-202	H2A.X variant histone	Homo sapiens	49-61
16786700-3	2006	We have previously found that phosphorylation of histone H2AX (gamma-H2AX), which accompanied the induction of DNA double strand breaks (DSBs), was significantly induced by low concentrations of benzo[a]pyrene (10(-9)-10(-7) M) and UVA (0.6 J/cm2) in CHO-K1 cells.	pyrene	203-209	H2A.X variant histone	Homo sapiens	49-61
16786700-3	2006	We have previously found that phosphorylation of histone H2AX (gamma-H2AX), which accompanied the induction of DNA double strand breaks (DSBs), was significantly induced by low concentrations of benzo[a]pyrene (10(-9)-10(-7) M) and UVA (0.6 J/cm2) in CHO-K1 cells.	CAV protocol	251-254	H2A.X variant histone	Homo sapiens	49-61
16786700-10	2006	These findings suggest that histone H2AX is a potential moleculartargetfor detecting the phototoxicity of PAHs more sensitively than the detection of cell viability and DSBs.	Polycyclic Aromatic Hydrocarbons	106-110	H2A.X variant histone	Homo sapiens	28-40
16778179-7	2006	Treatment of K-ras-transformed cells with bortezomib resulted in translocation of MST1 from cytoplasm into the nucleus and an increase of phosphorylated histone H2B and histone H2AX.	Bortezomib	42-52	H2A.X variant histone	Homo sapiens	177-181
16778179-8	2006	Moreover, pretreatment with leptomycin B, an inhibitor of the nuclear export signal receptor, dramatically enhanced bortezomib-mediated MST1 activation, phosphorylation of histones H2B and H2AX, and apoptosis induction in K-ras-transformed cells.	leptomycin B	28-40	H2A.X variant histone	Homo sapiens	189-193
16778179-8	2006	Moreover, pretreatment with leptomycin B, an inhibitor of the nuclear export signal receptor, dramatically enhanced bortezomib-mediated MST1 activation, phosphorylation of histones H2B and H2AX, and apoptosis induction in K-ras-transformed cells.	Bortezomib	116-126	H2A.X variant histone	Homo sapiens	189-193
16685450-2	2006	Induction of DSBs triggers phosphorylation of histone H2AX on Ser-139.	dsbs	13-17	H2A.X variant histone	Homo sapiens	54-58
16685450-2	2006	Induction of DSBs triggers phosphorylation of histone H2AX on Ser-139.	Serine	62-65	H2A.X variant histone	Homo sapiens	54-58
16685450-3	2006	Phosphorylated H2AX (gammaH2AX) can be detected immunocytochemically, and the intensity of gammaH2AX immunofluorescence (IF), reflecting the number of gammaH2AX-IF foci per nucleus, reveals the frequency of DSBs.	gammah2ax	21-30	H2A.X variant histone	Homo sapiens	15-19
16567133-1	2006	The phosphorylation of histone H2AX at serine 139 is one of the earliest responses of mammalian cells to ionizing radiation-induced DNA breaks.	Serine	39-45	H2A.X variant histone	Homo sapiens	31-35
16628006-1	2006	Histone H2AX phosphorylated on Ser-139, defined as gammaH2AX, is a reporter of DNA double-strand breaks (DSBs).	Serine	31-34	H2A.X variant histone	Homo sapiens	0-12
16628006-3	2006	We recently reported that this constitutive H2AX phosphorylation (CHP) is markedly reduced by the antioxidant N-acetyl-L-cysteine (NAC), and postulated that it reflects the oxidative DNA damage ("endogenous DSBs") induced by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle.	Acetylcysteine	110-129	H2A.X variant histone	Homo sapiens	44-48
16528719-4	2006	Histone H2AX is phosphorylated on Ser 139 in response to DSBs and one of the protein kinases that phosphorylate H2AX is ataxia telangiectasia mutated (ATM); activation of ATM is through its phosphorylation of Ser 1981.	Serine	34-37	H2A.X variant histone	Homo sapiens	8-12
16528719-4	2006	Histone H2AX is phosphorylated on Ser 139 in response to DSBs and one of the protein kinases that phosphorylate H2AX is ataxia telangiectasia mutated (ATM); activation of ATM is through its phosphorylation of Ser 1981.	Serine	34-37	H2A.X variant histone	Homo sapiens	112-116
16628006-3	2006	We recently reported that this constitutive H2AX phosphorylation (CHP) is markedly reduced by the antioxidant N-acetyl-L-cysteine (NAC), and postulated that it reflects the oxidative DNA damage ("endogenous DSBs") induced by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle.	dsbs	207-211	H2A.X variant histone	Homo sapiens	44-48
16528719-4	2006	Histone H2AX is phosphorylated on Ser 139 in response to DSBs and one of the protein kinases that phosphorylate H2AX is ataxia telangiectasia mutated (ATM); activation of ATM is through its phosphorylation of Ser 1981.	Serine	209-212	H2A.X variant histone	Homo sapiens	8-12
16628006-3	2006	We recently reported that this constitutive H2AX phosphorylation (CHP) is markedly reduced by the antioxidant N-acetyl-L-cysteine (NAC), and postulated that it reflects the oxidative DNA damage ("endogenous DSBs") induced by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle.	Reactive Oxygen Species	225-248	H2A.X variant histone	Homo sapiens	44-48
16528719-4	2006	Histone H2AX is phosphorylated on Ser 139 in response to DSBs and one of the protein kinases that phosphorylate H2AX is ataxia telangiectasia mutated (ATM); activation of ATM is through its phosphorylation of Ser 1981.	Serine	209-212	H2A.X variant histone	Homo sapiens	112-116
16528736-0	2006	Sequential phosphorylation of Ser-10 on histone H3 and ser-139 on histone H2AX and ATM activation during premature chromosome condensation: relationship to cell-cycle phase and apoptosis.	Serine	30-33	H2A.X variant histone	Homo sapiens	66-78
16528736-0	2006	Sequential phosphorylation of Ser-10 on histone H3 and ser-139 on histone H2AX and ATM activation during premature chromosome condensation: relationship to cell-cycle phase and apoptosis.	Serine	55-58	H2A.X variant histone	Homo sapiens	66-78
16528736-3	2006	The aim of the present study was to reveal the status of histone H3 and H2AX phosphorylation on Ser-10 and Ser-139, respectively, as well as ATM activation through phosphorylation on Ser-1981, during PCC, and relate these events to cell-cycle phase and to initiation of apoptosis.	Serine	96-99	H2A.X variant histone	Homo sapiens	72-76
16528736-3	2006	The aim of the present study was to reveal the status of histone H3 and H2AX phosphorylation on Ser-10 and Ser-139, respectively, as well as ATM activation through phosphorylation on Ser-1981, during PCC, and relate these events to cell-cycle phase and to initiation of apoptosis.	Serine	107-110	H2A.X variant histone	Homo sapiens	72-76
16528736-3	2006	The aim of the present study was to reveal the status of histone H3 and H2AX phosphorylation on Ser-10 and Ser-139, respectively, as well as ATM activation through phosphorylation on Ser-1981, during PCC, and relate these events to cell-cycle phase and to initiation of apoptosis.	Serine	107-110	H2A.X variant histone	Homo sapiens	72-76
16628006-3	2006	We recently reported that this constitutive H2AX phosphorylation (CHP) is markedly reduced by the antioxidant N-acetyl-L-cysteine (NAC), and postulated that it reflects the oxidative DNA damage ("endogenous DSBs") induced by reactive oxygen species (ROS) generated by metabolic activity during progression through the cell cycle.	Reactive Oxygen Species	250-253	H2A.X variant histone	Homo sapiens	44-48
16426422-3	2006	Activation of ATM and/or H2AX phosphorylation in HL-60 or Jurkat cells treated with topotecan (Tpt) was detected immunocytochemically in relation to cell cycle phase, by multiparameter cytometry.	Topotecan	84-93	H2A.X variant histone	Homo sapiens	25-29
16494516-0	2006	Quantitative analysis reveals asynchronous and more than DSB-associated histone H2AX phosphorylation after exposure to ionizing radiation.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	57-60	H2A.X variant histone	Homo sapiens	72-84
16552174-1	2006	Phosphorylation of histone H2AX at Serine 139 is one of the earliest events after DNA damage and is required for the retention of factors involved in repair at the site of the break.	Serine	35-41	H2A.X variant histone	Homo sapiens	27-31
16426422-3	2006	Activation of ATM and/or H2AX phosphorylation in HL-60 or Jurkat cells treated with topotecan (Tpt) was detected immunocytochemically in relation to cell cycle phase, by multiparameter cytometry.	Topotecan	95-98	H2A.X variant histone	Homo sapiens	25-29
16426422-4	2006	Exposure to Tpt led to concurrent phosphorylation of ATM and H2AX in S-phase cells, whereas G1 cells were unaffected.	Topotecan	12-15	H2A.X variant histone	Homo sapiens	61-65
16299494-1	2006	One of the earliest marks of a double-strand break (DSB) in eukaryotes is serine phosphorylation of the histone variant H2AX at the carboxy-terminal SQE motif to create gammaH2AX-containing nucleosomes.	Serine	74-80	H2A.X variant histone	Homo sapiens	120-124
16263812-9	2006	CEP-751 induced a loss in the induction of the DNA repair program marked by phospho-H2AX and the checkpoint pathway marked by the activated Chk1 pathway.	CEP 751	0-7	H2A.X variant histone	Homo sapiens	84-88
16129552-2	2005	Since it has been reported that DNA double-strand breaks (DSBs) induce phosphorylation of H2AX at serine 139 (gammaH2AX), an immunocytochemical assay with antibodies recognizing gammaH2AX has become the gold standard for the detection of DSBs.	Serine	98-104	H2A.X variant histone	Homo sapiens	90-94
16673875-1	2006	DNA damage that leads to formation of DNA double-strand breaks (DSBs) induces phosphorylation of histone H2AX on Ser-139 at sites flanking the breakage.	Serine	113-116	H2A.X variant histone	Homo sapiens	97-109
16148027-3	2005	Propargylamine (0.1-10 microM) dose-dependently reduced the levels of the early apoptosis-associated phosphorylated protein, H2A-X (ser 139), as well as decreased the cleavage of caspase-3 and its substrate poly-ADP ribose polymerase (PARP).	propargylamine	0-14	H2A.X variant histone	Homo sapiens	125-130
16170376-3	2005	Formation of DSBs induces the phosphorylation of the tumor suppressor protein, histone H2AX and this phosphorylated form, named gamma-H2AX, forms foci at DSB sites.	dsbs	13-17	H2A.X variant histone	Homo sapiens	79-91
16170376-3	2005	Formation of DSBs induces the phosphorylation of the tumor suppressor protein, histone H2AX and this phosphorylated form, named gamma-H2AX, forms foci at DSB sites.	dsbs	13-17	H2A.X variant histone	Homo sapiens	87-91
15975956-5	2005	The involvement of these molecules in resveratrol-induced S phase was also supported by the studies showing that addition of ATM/ATR inhibitor caffeine reverses resveratrol-caused activation of ATM/ATR-Chk1/2 as well as phosphorylation of Cdc25C, Cdc2 and H2A.X, and S phase arrest.	Resveratrol	38-49	H2A.X variant histone	Homo sapiens	256-261
15975956-5	2005	The involvement of these molecules in resveratrol-induced S phase was also supported by the studies showing that addition of ATM/ATR inhibitor caffeine reverses resveratrol-caused activation of ATM/ATR-Chk1/2 as well as phosphorylation of Cdc25C, Cdc2 and H2A.X, and S phase arrest.	Caffeine	143-151	H2A.X variant histone	Homo sapiens	256-261
15975956-5	2005	The involvement of these molecules in resveratrol-induced S phase was also supported by the studies showing that addition of ATM/ATR inhibitor caffeine reverses resveratrol-caused activation of ATM/ATR-Chk1/2 as well as phosphorylation of Cdc25C, Cdc2 and H2A.X, and S phase arrest.	Resveratrol	161-172	H2A.X variant histone	Homo sapiens	256-261
15975956-6	2005	In additional studies assessing whether observed effects of resveratrol are specific to Ovcar-3 cells, we observed that it also induces S phase arrest and H2A.X (Ser139) phosphorylation in other ovarian cancer cell lines PA-1 and SKOV-3, albeit at different levels; whereas, resveratrol showed only marginal S phase arrest in normal human foreskin fibroblasts with undetectable level of phospho-H2A.X (Ser139).	Resveratrol	60-71	H2A.X variant histone	Homo sapiens	155-160
15975956-6	2005	In additional studies assessing whether observed effects of resveratrol are specific to Ovcar-3 cells, we observed that it also induces S phase arrest and H2A.X (Ser139) phosphorylation in other ovarian cancer cell lines PA-1 and SKOV-3, albeit at different levels; whereas, resveratrol showed only marginal S phase arrest in normal human foreskin fibroblasts with undetectable level of phospho-H2A.X (Ser139).	Resveratrol	60-71	H2A.X variant histone	Homo sapiens	395-400
16256111-0	2005	Co-exposure to benzo[a]pyrene and UVA induces phosphorylation of histone H2AX.	Benzo(a)pyrene	15-29	H2A.X variant histone	Homo sapiens	73-77
16256111-6	2005	NaN(3) effectively inhibited the formation of gamma-H2AX induced by co-exposure, indicating the contribution of singlet oxygen.	Sodium Azide	0-6	H2A.X variant histone	Homo sapiens	46-56
16256111-6	2005	NaN(3) effectively inhibited the formation of gamma-H2AX induced by co-exposure, indicating the contribution of singlet oxygen.	Singlet Oxygen	112-126	H2A.X variant histone	Homo sapiens	46-56
16271620-4	2005	This response may have been triggered by DNA damage since juglone induced a rapid and strong phosphorylation of H2AX in all phases of the cell cycle.	juglone	58-65	H2A.X variant histone	Homo sapiens	112-116
16112599-9	2005	The H2A.X protein becomes rapidly phosphorylated on residue serine 139 in cells when DSBs are introduced into the DNA by ionizing radiation.	Serine	60-66	H2A.X variant histone	Homo sapiens	4-9
16184611-0	2005	Assessment of ATM phosphorylation on Ser-1981 induced by DNA topoisomerase I and II inhibitors in relation to Ser-139-histone H2AX phosphorylation, cell cycle phase, and apoptosis.	Serine	37-40	H2A.X variant histone	Homo sapiens	126-130
16184611-0	2005	Assessment of ATM phosphorylation on Ser-1981 induced by DNA topoisomerase I and II inhibitors in relation to Ser-139-histone H2AX phosphorylation, cell cycle phase, and apoptosis.	Serine	110-113	H2A.X variant histone	Homo sapiens	126-130
16184611-3	2005	The aim of the present study was to reveal a possible correlation between activation of ATM vis-a-vis H2AX phosphorylation, cell cycle phase, and apoptosis in cells treated with DNA topoisomerase (topo) I (topotecan; Tpt) or topo2 (mitoxantrone; Mtx) inhibitor.	Topotecan	206-215	H2A.X variant histone	Homo sapiens	102-106
16184611-3	2005	The aim of the present study was to reveal a possible correlation between activation of ATM vis-a-vis H2AX phosphorylation, cell cycle phase, and apoptosis in cells treated with DNA topoisomerase (topo) I (topotecan; Tpt) or topo2 (mitoxantrone; Mtx) inhibitor.	9 alpha,11 alpha,15 alpha-trihydroxy-16-phenoxy-17,18,19,20-tetranorprosta-4,5,13-trienoic acid	217-220	H2A.X variant histone	Homo sapiens	102-106
16184611-3	2005	The aim of the present study was to reveal a possible correlation between activation of ATM vis-a-vis H2AX phosphorylation, cell cycle phase, and apoptosis in cells treated with DNA topoisomerase (topo) I (topotecan; Tpt) or topo2 (mitoxantrone; Mtx) inhibitor.	topo2	225-230	H2A.X variant histone	Homo sapiens	102-106
16184611-3	2005	The aim of the present study was to reveal a possible correlation between activation of ATM vis-a-vis H2AX phosphorylation, cell cycle phase, and apoptosis in cells treated with DNA topoisomerase (topo) I (topotecan; Tpt) or topo2 (mitoxantrone; Mtx) inhibitor.	Mitoxantrone	232-244	H2A.X variant histone	Homo sapiens	102-106
16184611-5	2005	ATM or H2AX phosphorylation was detected immunocytochemically, using Ab specific for ATM phosphorylated on Ser-1981 (ATM-S1981(P)) or for H2AX (gammaH2AX) phosphorylated on Ser-139, respectively, concurrent with the analysis of cellular DNA content.	Serine	107-110	H2A.X variant histone	Homo sapiens	7-11
16184611-5	2005	ATM or H2AX phosphorylation was detected immunocytochemically, using Ab specific for ATM phosphorylated on Ser-1981 (ATM-S1981(P)) or for H2AX (gammaH2AX) phosphorylated on Ser-139, respectively, concurrent with the analysis of cellular DNA content.	Serine	173-176	H2A.X variant histone	Homo sapiens	7-11
16184611-8	2005	Exposure of cells to 150 nM Tpt induced ATM phosphorylation concurrent with phosphorylation of H2AX within 10 min; phosphorylation of both proteins was essentially limited to S-phase and was suppressed by caffeine and wortmannin, inhibitors of PI-3-like kinases.	9 alpha,11 alpha,15 alpha-trihydroxy-16-phenoxy-17,18,19,20-tetranorprosta-4,5,13-trienoic acid	28-31	H2A.X variant histone	Homo sapiens	95-99
16184611-11	2005	CONCLUSIONS: The data are consistent with the role of ATM as a mediator of H2AX phosphorylation in response to DNA damage by topo1 (Tpt) or topo 2 (Mtx) inhibitor.	topo1	125-130	H2A.X variant histone	Homo sapiens	75-79
16184611-11	2005	CONCLUSIONS: The data are consistent with the role of ATM as a mediator of H2AX phosphorylation in response to DNA damage by topo1 (Tpt) or topo 2 (Mtx) inhibitor.	9 alpha,11 alpha,15 alpha-trihydroxy-16-phenoxy-17,18,19,20-tetranorprosta-4,5,13-trienoic acid	132-135	H2A.X variant histone	Homo sapiens	75-79
16112599-9	2005	The H2A.X protein becomes rapidly phosphorylated on residue serine 139 in cells when DSBs are introduced into the DNA by ionizing radiation.	dsbs	85-89	H2A.X variant histone	Homo sapiens	4-9
16046194-4	2005	H2AX kinase and phosphatase activity were maintained in the presence of high salt.	Salts	77-81	H2A.X variant histone	Homo sapiens	0-4
15905198-0	2005	Novel genotoxicity assays identify norethindrone to activate p53 and phosphorylate H2AX.	Norethindrone	35-48	H2A.X variant histone	Homo sapiens	83-87
15905198-2	2005	We applied a novel and particularly sensitive method to screen for DNA damage with special attention to double-strand breaks (DSBs) and identified norethindrone to be likely genotoxic and therefore potentially mutagenic: a p53-reporter assay served as a first, high-throughput screening method and was followed by the immunofluorescent detection of phosphorylated H2AX as a sensitive assay for the presence of DSBs.	Norethindrone	147-160	H2A.X variant histone	Homo sapiens	364-368
15905198-3	2005	Norethindrone at concentrations of 2-100 microg/ml activated p53 and phosphorylated H2AX specifically and in a dose-dependent manner.	Norethindrone	0-13	H2A.X variant histone	Homo sapiens	84-88
16030261-1	2005	H2AX is a core histone H2A variant that contains an absolutely conserved serine/glutamine (SQ) motif within an extended carboxy-terminal tail.	Serine	73-79	H2A.X variant histone	Homo sapiens	0-4
16030261-1	2005	H2AX is a core histone H2A variant that contains an absolutely conserved serine/glutamine (SQ) motif within an extended carboxy-terminal tail.	Glutamine	80-89	H2A.X variant histone	Homo sapiens	0-4
16187759-0	2005	Induction and repair of DNA double-strand breaks in human cells: dephosphorylation of histone H2AX and its inhibition by calyculin A. Phosphorylation of histone H2AX at serine 139 (gamma-H2AX) represents one of the earliest steps in DNA DSB signaling and repair, but the mechanisms of coupling this histone modification to DSB processing remain to be established.	Serine	169-175	H2A.X variant histone	Homo sapiens	86-98
16187759-0	2005	Induction and repair of DNA double-strand breaks in human cells: dephosphorylation of histone H2AX and its inhibition by calyculin A. Phosphorylation of histone H2AX at serine 139 (gamma-H2AX) represents one of the earliest steps in DNA DSB signaling and repair, but the mechanisms of coupling this histone modification to DSB processing remain to be established.	Serine	169-175	H2A.X variant histone	Homo sapiens	153-165
16187760-1	2005	We studied the spatial and temporal distributions of foci of the phosphorylated form of the histone protein H2AX (gamma-H2AX), which is known to be activated by double-strand breaks after irradiation of human fibroblast cells with high-energy silicon (54 keV/microm) and iron (176 keV/microm) ions.	Silicon	243-250	H2A.X variant histone	Homo sapiens	108-112
16187760-1	2005	We studied the spatial and temporal distributions of foci of the phosphorylated form of the histone protein H2AX (gamma-H2AX), which is known to be activated by double-strand breaks after irradiation of human fibroblast cells with high-energy silicon (54 keV/microm) and iron (176 keV/microm) ions.	Silicon	243-250	H2A.X variant histone	Homo sapiens	114-124
16187760-1	2005	We studied the spatial and temporal distributions of foci of the phosphorylated form of the histone protein H2AX (gamma-H2AX), which is known to be activated by double-strand breaks after irradiation of human fibroblast cells with high-energy silicon (54 keV/microm) and iron (176 keV/microm) ions.	Iron	271-275	H2A.X variant histone	Homo sapiens	108-112
16187760-1	2005	We studied the spatial and temporal distributions of foci of the phosphorylated form of the histone protein H2AX (gamma-H2AX), which is known to be activated by double-strand breaks after irradiation of human fibroblast cells with high-energy silicon (54 keV/microm) and iron (176 keV/microm) ions.	Iron	271-275	H2A.X variant histone	Homo sapiens	114-124
16199871-9	2005	Following camptothecin treatment, T99p-BLM colocalized with gamma-H2AX but not with Top3alpha or PML.	Camptothecin	10-22	H2A.X variant histone	Homo sapiens	66-70
16199871-11	2005	A defect in gamma-H2AX signaling in response to unrepaired replication-mediated double-strand breaks might, at least in part, explain the camptothecin-sensitivity of BLM-deficient cells.	Camptothecin	138-150	H2A.X variant histone	Homo sapiens	18-22
16094454-6	2005	At the structural level, these processes involve the phosphorylation of serine at the SQE motif, which is present at the very end of the C-terminal domain of H2AX, and possibly other PTMs, some of which have recently started to be defined.	Serine	72-78	H2A.X variant histone	Homo sapiens	158-162
16049003-1	2005	MDC1 (mediator of DNA damage checkpoint protein 1) regulates the recognition and repair of DNA double strand breaks in mammalian cells through its interactions with nuclear foci containing the COOH-terminally phosphorylated form of the histone variant, H2AX.	Carbonic Acid	193-197	H2A.X variant histone	Homo sapiens	253-257
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	Serine	106-109	H2A.X variant histone	Homo sapiens	101-105
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	Glutamine	113-116	H2A.X variant histone	Homo sapiens	101-105
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	Glutamic Acid	117-120	H2A.X variant histone	Homo sapiens	101-105
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	Tyrosine	121-124	H2A.X variant histone	Homo sapiens	101-105
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	carboxylate	179-190	H2A.X variant histone	Homo sapiens	101-105
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	Carbonic Acid	204-208	H2A.X variant histone	Homo sapiens	101-105
16049003-2	2005	Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue.	Tyrosine	218-221	H2A.X variant histone	Homo sapiens	101-105
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Arginine	100-108	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Arginine	127-130	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Arginine	141-144	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Carbonic Acid	169-173	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Glutamic Acid	225-228	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Glutamine	244-247	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Carbonic Acid	297-301	H2A.X variant histone	Homo sapiens	232-236
16049003-4	2005	By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr.	Tyrosine	311-314	H2A.X variant histone	Homo sapiens	232-236
15613478-0	2005	Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II.	Dactinomycin	0-13	H2A.X variant histone	Homo sapiens	36-40
16093433-0	2005	Hedamycin, a DNA alkylator, induces (gamma)H2AX and chromosome aberrations: involvement of phosphatidylinositol 3-kinase-related kinases and DNA replication fork movement.	hedamycin	0-9	H2A.X variant histone	Homo sapiens	37-47
16093433-3	2005	This study examined the potential of the monofunctional DNA alkylating agent hedamycin, a powerful inhibitor of DNA replication, to induce DNA strand breaks, phosphorylated H2AX (gammaH2AX) foci, and chromosome aberrations.	hedamycin	77-86	H2A.X variant histone	Homo sapiens	173-177
16093433-4	2005	Hedamycin treatment of HCT116 carcinoma cells resulted in a rapid induction of DNA strand breaks accompanied by increasing H2AX phosphorylation and focalization.	hedamycin	0-9	H2A.X variant histone	Homo sapiens	123-127
16093433-6	2005	Similarly, hedamycin induction of gammaH2AX is not dependent on ataxia telangiectasia mutated or DNA-protein kinase, and pretreatment of cells with the phosphatidylinositol 3-kinase-related kinase inhibitor caffeine did not substantially reduce induction of H2AX phosphorylation by hedamycin.	hedamycin	11-20	H2A.X variant histone	Homo sapiens	39-43
16098182-6	2005	The induction of double-strand DNA breaks (DSBs) by genotoxic agents provides a signal for histone H2AX phosphorylation on Ser139; the phosphorylated H2AX is named gammaH2AX.	gammah2ax	164-173	H2A.X variant histone	Homo sapiens	99-103
16098182-6	2005	The induction of double-strand DNA breaks (DSBs) by genotoxic agents provides a signal for histone H2AX phosphorylation on Ser139; the phosphorylated H2AX is named gammaH2AX.	gammah2ax	164-173	H2A.X variant histone	Homo sapiens	150-154
16024643-10	2005	Furthermore, loss of pol-beta coupled with temozolomide treatment triggered the phosphorylation of H2AX, indicating the activation of the DNA damage response pathway as a result of unrepaired lesions.	Temozolomide	43-55	H2A.X variant histone	Homo sapiens	99-103
15613478-0	2005	Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II.	Dactinomycin	0-13	H2A.X variant histone	Homo sapiens	77-81
15613478-2	2005	Here we show that gamma-H2AX foci were also formed when cells were incubated with 0.5 microg/ml DNA intercalating agent actinomycin D.	Dactinomycin	120-133	H2A.X variant histone	Homo sapiens	24-28
15613478-8	2005	Congruently, after actinomycin D treatment, NDH II accumulated in RNA-containing nuclear bodies that predominantly co-localized with gamma-H2AX foci.	Dactinomycin	19-32	H2A.X variant histone	Homo sapiens	139-143
15655354-1	2005	Damage to DNA that engenders double-strand breaks (DSBs) triggers phosphorylation of histone H2AX on Ser-139.	Serine	101-104	H2A.X variant histone	Homo sapiens	85-97
15655354-2	2005	Expression of phosphorylated H2AX (gammaH2AX) can be revealed immunocytochemically; the intensity of gammaH2AX immunofluorescence (IF) measured by cytometry was reported to correlate with the frequency of DSBs induced by X-ray radiation or by DNA damaging antitumor drugs.	gammah2ax	35-44	H2A.X variant histone	Homo sapiens	29-33
15655354-2	2005	Expression of phosphorylated H2AX (gammaH2AX) can be revealed immunocytochemically; the intensity of gammaH2AX immunofluorescence (IF) measured by cytometry was reported to correlate with the frequency of DSBs induced by X-ray radiation or by DNA damaging antitumor drugs.	dsbs	205-209	H2A.X variant histone	Homo sapiens	29-33
15655354-7	2005	While the suppression of DNA replication, by aphidicolin prevented the induction of H2AX phosphorylation by UV in most S phase cells, it had no effect on a small cohort of cells that appeared to be entering S-phase, that expressed very high levels of gammaH2AX.	Aphidicolin	45-56	H2A.X variant histone	Homo sapiens	84-88
15655354-10	2005	The data are consistent with the notion that H2AX phosphorylation observed throughout S phase reflects formation of DSBs due to the collision of replication forks with the UV-induced primary DNA lesions.	dsbs	116-120	H2A.X variant histone	Homo sapiens	45-49
15603752-10	2005	Further, high NaCl impairs activation of several components of the classical DNA damage response such as Mre11, H2AX and Chk1 leading to inhibition of DNA repair.	Sodium Chloride	14-18	H2A.X variant histone	Homo sapiens	112-116
15389585-1	2005	In eukaryotic cells, DNA double strand breaks (DSBs) cause the prompt phosphorylation of serine 139 at the carboxy terminus of histone H2AX to generate gamma-H2AX, detectable by Western blotting or immunofluorescence.	Serine	89-95	H2A.X variant histone	Homo sapiens	127-139
15389585-1	2005	In eukaryotic cells, DNA double strand breaks (DSBs) cause the prompt phosphorylation of serine 139 at the carboxy terminus of histone H2AX to generate gamma-H2AX, detectable by Western blotting or immunofluorescence.	Serine	89-95	H2A.X variant histone	Homo sapiens	135-139
15389585-2	2005	The consensus sequence at the phosphorylation site implicates the phosphatidylinositol 3-like family of protein kinases in H2AX phosphorylation.	Phosphatidylinositols	66-86	H2A.X variant histone	Homo sapiens	123-127
15389585-6	2005	This is further supported by the observation that initial H2AX phosphorylation is delayed when both kinases are inhibited by wortmannin, as well as when ATM is inhibited by caffeine in DNA-PK deficient cells.	Wortmannin	125-135	H2A.X variant histone	Homo sapiens	58-62
15389585-8	2005	Treatment with wortmannin, caffeine, or UCN-01 produces a strong DNA-PK dependent late global hyperphosphorylation of H2AX, uncoupled from DNA DSB rejoining and compatible with an inhibition of late steps in DNA DSB processing.	Wortmannin	15-25	H2A.X variant histone	Homo sapiens	118-122
15389585-8	2005	Treatment with wortmannin, caffeine, or UCN-01 produces a strong DNA-PK dependent late global hyperphosphorylation of H2AX, uncoupled from DNA DSB rejoining and compatible with an inhibition of late steps in DNA DSB processing.	Caffeine	27-35	H2A.X variant histone	Homo sapiens	118-122
15498771-1	2004	When added for a short period (2-4 h) to cells, the kinase inhibitor staurosporine (STS), can trigger double strand breaks, the formation of nuclear foci containing phosphorylated H2AX, Chk2, and p53, a decrease in transcription, and a minor degree of peripheral chromatin condensation.	Staurosporine	69-82	H2A.X variant histone	Homo sapiens	180-184
15934200-1	2005	We investigated the spatial distribution of the induction of the phosphorylated form of the histone protein H2AX (gamma-H2AX), known to be activated by DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	152-156	H2A.X variant histone	Homo sapiens	108-112
15934200-1	2005	We investigated the spatial distribution of the induction of the phosphorylated form of the histone protein H2AX (gamma-H2AX), known to be activated by DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	152-156	H2A.X variant histone	Homo sapiens	114-124
15934200-2	2005	Following irradiation of human fibroblast cells with 600 MeV/nucleon silicon and 600 MeV/nucleon iron ions we observed the formation of gamma-H2AX aggregates in the shape of streaks stretching over several micrometers in an x/y plane.	Silicon	69-76	H2A.X variant histone	Homo sapiens	136-146
15934200-2	2005	Following irradiation of human fibroblast cells with 600 MeV/nucleon silicon and 600 MeV/nucleon iron ions we observed the formation of gamma-H2AX aggregates in the shape of streaks stretching over several micrometers in an x/y plane.	Iron	97-101	H2A.X variant histone	Homo sapiens	136-146
15498771-1	2004	When added for a short period (2-4 h) to cells, the kinase inhibitor staurosporine (STS), can trigger double strand breaks, the formation of nuclear foci containing phosphorylated H2AX, Chk2, and p53, a decrease in transcription, and a minor degree of peripheral chromatin condensation.	Staurosporine	84-87	H2A.X variant histone	Homo sapiens	180-184
15610743-3	2004	After DNA breakage, H2AX is phosphorylated on serine 139 in chromatin near the break.	Serine	46-52	H2A.X variant histone	Homo sapiens	20-24
15610743-4	2004	We show here that H2AX serine 139 enforces efficient homologous recombinational repair of a chromosomal double-strand break (DSB) by using the sister chromatid as a template.	Serine	23-29	H2A.X variant histone	Homo sapiens	18-22
15610743-7	2004	Therefore, the chromatin response around a chromosomal DSB, in which H2AX serine 139 phosphorylation plays a central role, "shapes" the repair process in favor of potentially error-free interchromatid homologous recombination at the expense of error-prone repair.	Serine	74-80	H2A.X variant histone	Homo sapiens	69-73
15455410-0	2004	Histone H2AX phosphorylation induced by selective photolysis of BrdU-labeled DNA with UV light: relation to cell cycle phase.	Bromodeoxyuridine	64-68	H2A.X variant histone	Homo sapiens	0-12
15489221-10	2004	In contrast, preincubation of cells with the hydroxyl radical scavenger, N-acetylcysteine, significantly attenuated the doxorubicin-mediated phosphorylation and accumulation of p53, p53-DNA binding, and the phosphorylation of H2AX, Nbs1, SMC1, Chk1, and Chk2, suggesting that hydroxyl radicals contribute to the doxorubicin-induced activation of ATM-dependent pathways.	Hydroxyl Radical	45-61	H2A.X variant histone	Homo sapiens	226-230
15489221-10	2004	In contrast, preincubation of cells with the hydroxyl radical scavenger, N-acetylcysteine, significantly attenuated the doxorubicin-mediated phosphorylation and accumulation of p53, p53-DNA binding, and the phosphorylation of H2AX, Nbs1, SMC1, Chk1, and Chk2, suggesting that hydroxyl radicals contribute to the doxorubicin-induced activation of ATM-dependent pathways.	Acetylcysteine	73-89	H2A.X variant histone	Homo sapiens	226-230
15489221-10	2004	In contrast, preincubation of cells with the hydroxyl radical scavenger, N-acetylcysteine, significantly attenuated the doxorubicin-mediated phosphorylation and accumulation of p53, p53-DNA binding, and the phosphorylation of H2AX, Nbs1, SMC1, Chk1, and Chk2, suggesting that hydroxyl radicals contribute to the doxorubicin-induced activation of ATM-dependent pathways.	Doxorubicin	120-131	H2A.X variant histone	Homo sapiens	226-230
15604242-1	2004	To identify critical events associated with heat-induced cell killing, we examined foci formation of gammaH2AX (histone H2AX phosphorylated at serine 139) in heat-treated cells.	gammah2ax	101-110	H2A.X variant histone	Homo sapiens	112-124
15604242-1	2004	To identify critical events associated with heat-induced cell killing, we examined foci formation of gammaH2AX (histone H2AX phosphorylated at serine 139) in heat-treated cells.	Serine	143-149	H2A.X variant histone	Homo sapiens	112-124
15489221-6	2004	Treatment of cells with doxorubicin led to the phosphorylation of histone H2AX on serine 139 with dependence on ATM for the initial response.	Doxorubicin	24-35	H2A.X variant histone	Homo sapiens	74-78
15489221-6	2004	Treatment of cells with doxorubicin led to the phosphorylation of histone H2AX on serine 139 with dependence on ATM for the initial response.	Serine	82-88	H2A.X variant histone	Homo sapiens	74-78
15455410-1	2004	BACKGROUND: The induction of DNA double-strand breaks (DSBs) in chromatin triggers histone H2AX phosphorylation (on Ser-139) by ATM-, ATR-, or DNA-dependent protein kinases (DNA-PK).	Serine	116-119	H2A.X variant histone	Homo sapiens	91-95
15455410-2	2004	Phosphorylated H2AX, denoted as gammaH2AX, can be detected immunocytochemically using an antibody that is specific to the Ser-139-phosphorylated epitope.	gammah2ax	32-41	H2A.X variant histone	Homo sapiens	15-19
15455410-2	2004	Phosphorylated H2AX, denoted as gammaH2AX, can be detected immunocytochemically using an antibody that is specific to the Ser-139-phosphorylated epitope.	Serine	122-125	H2A.X variant histone	Homo sapiens	15-19
15455410-12	2004	CONCLUSIONS: Photolysis of BrdU-labeled DNA induces DSBs and leads to H2AX phosphorylation.	Bromodeoxyuridine	27-31	H2A.X variant histone	Homo sapiens	70-74
15374978-8	2004	Conversely, concurrent treatment with SN-38 and UCN-01 resulted in S-phase checkpoint override, an amplified DNA damage response including increased phosphorylation of the DNA double-strand breakage marker H2AX and augmentation of clonogenic inhibition, which was independent of p53.	Irinotecan	38-43	H2A.X variant histone	Homo sapiens	206-210
15199134-7	2004	Treatment of wild-type cells with mitomycin C (MMC) induced gamma-H2AX foci and increased the amount of DSBs detected by pulsed-field gel electrophoresis.	Mitomycin	34-45	H2A.X variant histone	Homo sapiens	60-70
15304327-3	2004	We also studied etoposide-induced phosphorylation of histone H2AX (gamma-H2AX) in human cells in which PrxV activity was downregulated (knockdown, KD-clones) or compromised by overexpression of redox-negative (RD) protein.	Etoposide	16-25	H2A.X variant histone	Homo sapiens	53-65
15199134-7	2004	Treatment of wild-type cells with mitomycin C (MMC) induced gamma-H2AX foci and increased the amount of DSBs detected by pulsed-field gel electrophoresis.	Mitomycin	47-50	H2A.X variant histone	Homo sapiens	60-70
15199134-8	2004	Surprisingly, gamma-H2AX foci were also induced in Ercc1(-/-) cells by MMC treatment.	Mitomycin	71-74	H2A.X variant histone	Homo sapiens	14-24
15199134-11	2004	In Ercc1(-/-) cells, MMC-induced gamma-H2AX foci persisted at least 48 h longer than in wild-type cells, demonstrating that Ercc1 is required for the resolution of cross-link-induced DSBs.	Mitomycin	21-24	H2A.X variant histone	Homo sapiens	33-43
15199134-11	2004	In Ercc1(-/-) cells, MMC-induced gamma-H2AX foci persisted at least 48 h longer than in wild-type cells, demonstrating that Ercc1 is required for the resolution of cross-link-induced DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	183-187	H2A.X variant histone	Homo sapiens	33-43
15197225-5	2004	H2B-(Ser14P) foci formation is not associated with the apoptotic phosphorylation of H2B but is strictly dependent on the phosphorylated isoform of H2AX.	ser14p	5-11	H2A.X variant histone	Homo sapiens	147-151
15177039-0	2004	The isoflavonoids genistein and quercetin activate different stress signaling pathways as shown by analysis of site-specific phosphorylation of ATM, p53 and histone H2AX.	isoflavonoids	4-17	H2A.X variant histone	Homo sapiens	157-169
15173094-8	2004	In addition, l-N-acetylcysteine inhibited the combined therapy-mediated elevation of a proapoptotic BH3-only protein Bim expression, phosphorylation of H2AX, and accumulation of 8-hydroxydeoxyguanosine.	Acetylcysteine	13-31	H2A.X variant histone	Homo sapiens	152-156
15057963-0	2004	Assessment of histone H2AX phosphorylation induced by DNA topoisomerase I and II inhibitors topotecan and mitoxantrone and by the DNA cross-linking agent cisplatin.	Topotecan	92-101	H2A.X variant histone	Homo sapiens	22-26
15057963-0	2004	Assessment of histone H2AX phosphorylation induced by DNA topoisomerase I and II inhibitors topotecan and mitoxantrone and by the DNA cross-linking agent cisplatin.	Mitoxantrone	106-118	H2A.X variant histone	Homo sapiens	22-26
15057963-1	2004	BACKGROUND: DNA double-strand breaks (DSBs) in chromatin, whether induced by radiation, antitumor drugs, or by apoptosis-associated (AA) DNA fragmentation, provide a signal for histone H2AX phosphorylation on Ser-139; the phosphorylated H2AX is denoted gammaH2AX.	Serine	209-212	H2A.X variant histone	Homo sapiens	185-189
15057963-1	2004	BACKGROUND: DNA double-strand breaks (DSBs) in chromatin, whether induced by radiation, antitumor drugs, or by apoptosis-associated (AA) DNA fragmentation, provide a signal for histone H2AX phosphorylation on Ser-139; the phosphorylated H2AX is denoted gammaH2AX.	Serine	209-212	H2A.X variant histone	Homo sapiens	237-241
15059890-4	2004	Here, we show that H2AX phosphorylation after exposure to ionizing radiation (IR) occurs to similar extents in human fibroblasts and in mouse embryo fibroblasts lacking either DNA-PK or ATM but is ablated in ATM-deficient cells treated with LY294002, a drug that specifically inhibits DNA-PK.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	241-249	H2A.X variant histone	Homo sapiens	19-23
15059890-6	2004	We confirm that H2AX phosphorylation induced by DSBs in nonreplicating cells is ATR (ataxia telangiectasia and Rad3-related protein) independent.	dsbs	48-52	H2A.X variant histone	Homo sapiens	16-20
15177039-0	2004	The isoflavonoids genistein and quercetin activate different stress signaling pathways as shown by analysis of site-specific phosphorylation of ATM, p53 and histone H2AX.	Genistein	18-27	H2A.X variant histone	Homo sapiens	157-169
15177039-0	2004	The isoflavonoids genistein and quercetin activate different stress signaling pathways as shown by analysis of site-specific phosphorylation of ATM, p53 and histone H2AX.	Quercetin	32-41	H2A.X variant histone	Homo sapiens	157-169
15177039-5	2004	Also, we show that genistein induces phosphorylation of ATM on serine 1981 and phosphorylation of histone H2AX on serine 139.	Genistein	19-28	H2A.X variant histone	Homo sapiens	98-110
15177039-5	2004	Also, we show that genistein induces phosphorylation of ATM on serine 1981 and phosphorylation of histone H2AX on serine 139.	Serine	114-120	H2A.X variant histone	Homo sapiens	98-110
14504478-1	2003	Histone H2AX is phosphorylated on Ser-139 by ATM kinase in response to damage that induces dsDNA breaks.	Serine	34-37	H2A.X variant histone	Homo sapiens	0-12
15177039-7	2004	Like genistein, quercetin induced phosphorylation of ATM on serine 1981, and ATM-dependent phosphorylation of histone H2AX on serine 139; however, p53 accumulation and phosphorylation on serines 6, 9, 15, 20, 46, and 392 occurred in ATM-deficient cells, indicating that ATM is not required for quercetin-induced phosphorylation of p53.	Serine	126-132	H2A.X variant histone	Homo sapiens	110-122
15476893-2	2004	In response to DNA damage, histone H2AX in the vicinity of DSBs is phosphorylated by ATM.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	59-63	H2A.X variant histone	Homo sapiens	27-39
15493328-2	2004	In response to DNA damage, histone H2AX in the vicinity of DSBs is phosphorylated by ATM.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	59-63	H2A.X variant histone	Homo sapiens	27-39
14643438-6	2003	The DNA-damaging fork-blocking agents, adozelesin and MMS, both induced phosphorylation and focalization of H2AX and RPA.	adozelesin	39-49	H2A.X variant histone	Homo sapiens	108-112
14643438-6	2003	The DNA-damaging fork-blocking agents, adozelesin and MMS, both induced phosphorylation and focalization of H2AX and RPA.	Methyl Methanesulfonate	54-57	H2A.X variant histone	Homo sapiens	108-112
14504478-9	2003	Following treatment with TPT, CPT or MTX the peak of H2AX phosphorylation preceded caspase-3 activation and the appearance of apoptosis-associated DNA fragmentation, both selective to S-phase cells.	Topotecan	25-28	H2A.X variant histone	Homo sapiens	53-57
14504478-9	2003	Following treatment with TPT, CPT or MTX the peak of H2AX phosphorylation preceded caspase-3 activation and the appearance of apoptosis-associated DNA fragmentation, both selective to S-phase cells.	Camptothecin	30-33	H2A.X variant histone	Homo sapiens	53-57
14504478-9	2003	Following treatment with TPT, CPT or MTX the peak of H2AX phosphorylation preceded caspase-3 activation and the appearance of apoptosis-associated DNA fragmentation, both selective to S-phase cells.	Mitoxantrone	37-40	H2A.X variant histone	Homo sapiens	53-57
12926989-1	2003	The induction of DNA double-strand breaks (DSBs) by ionizing radiation in mammalian chromosomes leads to the phosphorylation of Ser-139 in the replacement histone H2AX, but the molecular mechanism(s) of the elimination of phosphorylated H2AX (called gamma-H2AX) from chromatin in the course of DSB repair remains unknown.	Serine	128-131	H2A.X variant histone	Homo sapiens	163-167
12926989-1	2003	The induction of DNA double-strand breaks (DSBs) by ionizing radiation in mammalian chromosomes leads to the phosphorylation of Ser-139 in the replacement histone H2AX, but the molecular mechanism(s) of the elimination of phosphorylated H2AX (called gamma-H2AX) from chromatin in the course of DSB repair remains unknown.	Serine	128-131	H2A.X variant histone	Homo sapiens	237-241
12926989-1	2003	The induction of DNA double-strand breaks (DSBs) by ionizing radiation in mammalian chromosomes leads to the phosphorylation of Ser-139 in the replacement histone H2AX, but the molecular mechanism(s) of the elimination of phosphorylated H2AX (called gamma-H2AX) from chromatin in the course of DSB repair remains unknown.	Serine	128-131	H2A.X variant histone	Homo sapiens	250-260
12926989-3	2003	Here we studied the dynamics of dephosphorylation of gamma-H2AX in vivo and found that more than 50% was dephosphorylated in 3 h, but a significant amount of gamma-H2AX could be detected even 6 h after the induction of DSBs.	dsbs	219-223	H2A.X variant histone	Homo sapiens	53-63
12926989-3	2003	Here we studied the dynamics of dephosphorylation of gamma-H2AX in vivo and found that more than 50% was dephosphorylated in 3 h, but a significant amount of gamma-H2AX could be detected even 6 h after the induction of DSBs.	dsbs	219-223	H2A.X variant histone	Homo sapiens	158-168
12926989-5	2003	However, gamma-H2AX could be detected in some cells treated with methyl methanesulfonate which accumulated RAD18 protein at stalled replication sites.	Methyl Methanesulfonate	65-88	H2A.X variant histone	Homo sapiens	9-19
12926989-6	2003	We also found that calyculin A inhibited early elimination of gamma-H2AX and DSB rejoining in vivo and that protein phosphatase 1 was able to remove phosphate groups from gamma-H2AX-containing chromatin in vitro.	Phosphates	149-158	H2A.X variant histone	Homo sapiens	171-181
12926989-7	2003	Our results confirm the tight association between DSBs and gamma-H2AX and the coupling of its in situ dephosphorylation to DSB repair.	dsbs	50-54	H2A.X variant histone	Homo sapiens	59-69
12697768-6	2003	Moreover, using H2AX-deficient cells reconstituted with wild-type or a phosphorylation-deficient mutant of H2AX, we have shown that phosphorylation of H2AX at serine 140 is critical for efficient 53BP1 foci formation, implying that a direct interaction between 53BP1 and phosphorylated H2AX is required for the accumulation of 53BP1 at DNA break sites.	Serine	159-165	H2A.X variant histone	Homo sapiens	16-20
12766154-4	2003	Consistent with ATM/ATR involvement, selenite was also shown to stimulate Ser-139 phosphorylation of the ATM/ATR substrate H2AX.	Selenious Acid	37-45	H2A.X variant histone	Homo sapiens	123-127
12766154-4	2003	Consistent with ATM/ATR involvement, selenite was also shown to stimulate Ser-139 phosphorylation of the ATM/ATR substrate H2AX.	Serine	74-77	H2A.X variant histone	Homo sapiens	123-127
12914701-5	2003	Restoration of the H2AX null allele with wild-type H2AX restores genomic stability and radiation resistance, but this effect is abolished by substitution of the conserved serine phosphorylation sites in H2AX with alanine or glutamic acid residues.	Serine	171-177	H2A.X variant histone	Homo sapiens	19-23
12914701-5	2003	Restoration of the H2AX null allele with wild-type H2AX restores genomic stability and radiation resistance, but this effect is abolished by substitution of the conserved serine phosphorylation sites in H2AX with alanine or glutamic acid residues.	Serine	171-177	H2A.X variant histone	Homo sapiens	51-55
12914701-5	2003	Restoration of the H2AX null allele with wild-type H2AX restores genomic stability and radiation resistance, but this effect is abolished by substitution of the conserved serine phosphorylation sites in H2AX with alanine or glutamic acid residues.	Serine	171-177	H2A.X variant histone	Homo sapiens	51-55
12914701-5	2003	Restoration of the H2AX null allele with wild-type H2AX restores genomic stability and radiation resistance, but this effect is abolished by substitution of the conserved serine phosphorylation sites in H2AX with alanine or glutamic acid residues.	Glutamic Acid	224-237	H2A.X variant histone	Homo sapiens	19-23
12851679-3	2003	In this study, we show that radioresistant T98G glioblastoma cells can develop sensitivity to DNA damage induced by irradiation and etoposide as a result of the introduction of a DNA repair-associated histone, H2AX.	Etoposide	132-141	H2A.X variant histone	Homo sapiens	210-214
12697768-6	2003	Moreover, using H2AX-deficient cells reconstituted with wild-type or a phosphorylation-deficient mutant of H2AX, we have shown that phosphorylation of H2AX at serine 140 is critical for efficient 53BP1 foci formation, implying that a direct interaction between 53BP1 and phosphorylated H2AX is required for the accumulation of 53BP1 at DNA break sites.	Serine	159-165	H2A.X variant histone	Homo sapiens	107-111
12697768-6	2003	Moreover, using H2AX-deficient cells reconstituted with wild-type or a phosphorylation-deficient mutant of H2AX, we have shown that phosphorylation of H2AX at serine 140 is critical for efficient 53BP1 foci formation, implying that a direct interaction between 53BP1 and phosphorylated H2AX is required for the accumulation of 53BP1 at DNA break sites.	Serine	159-165	H2A.X variant histone	Homo sapiens	107-111
12697768-6	2003	Moreover, using H2AX-deficient cells reconstituted with wild-type or a phosphorylation-deficient mutant of H2AX, we have shown that phosphorylation of H2AX at serine 140 is critical for efficient 53BP1 foci formation, implying that a direct interaction between 53BP1 and phosphorylated H2AX is required for the accumulation of 53BP1 at DNA break sites.	Serine	159-165	H2A.X variant histone	Homo sapiens	107-111
12236816-1	2002	When mammalian cells are exposed to ionizing radiation and other agents that introduce DSBs into DNA, histone H2AX molecules in megabase chromatin regions adjacent to the breaks become phosphorylated within minutes on a specific serine residue.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	87-91	H2A.X variant histone	Homo sapiens	102-114
12533428-1	2003	Within minutes of the induction of DNA double-strand breaks in somatic cells, histone H2AX becomes phosphorylated at serine 139 and forms gamma-H2AX foci at the sites of damage.	Serine	117-123	H2A.X variant histone	Homo sapiens	86-90
12533428-4	2003	Independent of irradiation, gamma-H2AX occurs in all intermediate and B spermatogonia and in preleptotene to zygotene spermatocytes.	preleptotene	93-105	H2A.X variant histone	Homo sapiens	34-38
12533428-4	2003	Independent of irradiation, gamma-H2AX occurs in all intermediate and B spermatogonia and in preleptotene to zygotene spermatocytes.	zygotene	109-117	H2A.X variant histone	Homo sapiens	34-38
12533428-9	2003	Irradiation-independent nuclear gamma-H2AX staining in leptotene spermatocytes demonstrates a function for gamma-H2AX during meiosis.	leptotene	55-64	H2A.X variant histone	Homo sapiens	38-42
12533428-9	2003	Irradiation-independent nuclear gamma-H2AX staining in leptotene spermatocytes demonstrates a function for gamma-H2AX during meiosis.	leptotene	55-64	H2A.X variant histone	Homo sapiens	113-117
12372432-1	2002	The Ser-139 phosphorylated form of replacement histone H2AX (gamma-H2AX) is induced within large chromatin domains by double-strand DNA breaks (DSBs) in mammalian chromosomes.	Serine	4-7	H2A.X variant histone	Homo sapiens	47-59
12372432-1	2002	The Ser-139 phosphorylated form of replacement histone H2AX (gamma-H2AX) is induced within large chromatin domains by double-strand DNA breaks (DSBs) in mammalian chromosomes.	Serine	4-7	H2A.X variant histone	Homo sapiens	61-71
12236816-1	2002	When mammalian cells are exposed to ionizing radiation and other agents that introduce DSBs into DNA, histone H2AX molecules in megabase chromatin regions adjacent to the breaks become phosphorylated within minutes on a specific serine residue.	Serine	229-235	H2A.X variant histone	Homo sapiens	102-114
12236816-2	2002	An antibody to this phosphoserine motif of human H2AX (gamma-H2AX) demonstrates that gamma-H2AX molecules appear in discrete nuclear foci.	Phosphoserine	20-33	H2A.X variant histone	Homo sapiens	49-53
12236816-2	2002	An antibody to this phosphoserine motif of human H2AX (gamma-H2AX) demonstrates that gamma-H2AX molecules appear in discrete nuclear foci.	Phosphoserine	20-33	H2A.X variant histone	Homo sapiens	55-65
12236816-2	2002	An antibody to this phosphoserine motif of human H2AX (gamma-H2AX) demonstrates that gamma-H2AX molecules appear in discrete nuclear foci.	Phosphoserine	20-33	H2A.X variant histone	Homo sapiens	85-95
12236816-7	2002	Based on these findings, we conclude that gamma-H2AX antibody may form the basis of a sensitive quantitative method for the detection of DNA DSBs in eukaryotic cells.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	141-145	H2A.X variant histone	Homo sapiens	42-52
11896765-2	2002	We demonstrate that the Haemophilus ducreyi CDT (HdCDT) induces phosphorylation of the histone H2AX as early as 1 h after intoxication and re-localization of the DNA repair complex Mre11 in HeLa cells with kinetics similar to those observed upon ionizing radiation.	hdcdt	49-54	H2A.X variant histone	Homo sapiens	95-99
12220643-2	2002	This type of DNA break is followed by the rapid phosphorylation of Ser-139 in the histone variant H2AX to form gamma-H2AX.	Serine	67-70	H2A.X variant histone	Homo sapiens	98-102
12220643-2	2002	This type of DNA break is followed by the rapid phosphorylation of Ser-139 in the histone variant H2AX to form gamma-H2AX.	Serine	67-70	H2A.X variant histone	Homo sapiens	117-121
12220643-5	2002	During the end-joining reaction H2AX is phosphorylated at Ser-139 as detected by immunoblot with specific antibodies and this phosphorylation is inhibited by wortmannin.	Serine	58-61	H2A.X variant histone	Homo sapiens	32-36
12220643-5	2002	During the end-joining reaction H2AX is phosphorylated at Ser-139 as detected by immunoblot with specific antibodies and this phosphorylation is inhibited by wortmannin.	Wortmannin	158-168	H2A.X variant histone	Homo sapiens	32-36
11893489-3	2002	H2AX is phosphorylated on a serine four residues from the carboxyl terminus in response to the introduction of DNA double-strand breaks, whether these breaks are a result of environmental insult, metabolic mistake, or programmed process.	Serine	28-34	H2A.X variant histone	Homo sapiens	0-4
11896765-6	2002	H2AX phosphorylation and Mre11 re-localization were induced also in HdCDT-treated, non-proliferating dendritic cells (DCs) in a differentiation dependent manner, and resulted in cell death.	hdcdt	68-73	H2A.X variant histone	Homo sapiens	0-4
11571274-1	2001	A very early step in the response of mammalian cells to DNA double-strand breaks is the phosphorylation of histone H2AX at serine 139 at the sites of DNA damage.	Serine	123-129	H2A.X variant histone	Homo sapiens	115-119
11673449-3	2001	Here we report that inhibition of DNA replication by hydroxyurea or ultraviolet irradiation also induces phosphorylation and foci formation of H2AX.	Hydroxyurea	53-64	H2A.X variant histone	Homo sapiens	143-147
11571274-6	2001	The minimal H2AX phosphorylation in Atm-/- fibroblasts can be abolished by low concentrations of wortmannin suggesting that DNA-PK, rather than ATR, is responsible for low levels of H2AX phosphorylation in the absence of ATM.	Wortmannin	97-107	H2A.X variant histone	Homo sapiens	12-16
10477747-1	1999	The loss of chromosomal integrity from DNA double-strand breaks introduced into mammalian cells by ionizing radiation results in the specific phosphorylation of histone H2AX on serine residue 139, yielding a specific modified form named gamma-H2AX.	Serine	177-183	H2A.X variant histone	Homo sapiens	161-173
10959836-7	2000	Wortmannin treatment was effective only when it was added early enough to prevent gamma-H2AX formation, indicating that gamma-H2AX is necessary for the recruitment of other factors to the sites of DNA damage.	Wortmannin	0-10	H2A.X variant histone	Homo sapiens	82-92
10959836-7	2000	Wortmannin treatment was effective only when it was added early enough to prevent gamma-H2AX formation, indicating that gamma-H2AX is necessary for the recruitment of other factors to the sites of DNA damage.	Wortmannin	0-10	H2A.X variant histone	Homo sapiens	120-130
10734083-0	2000	Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139.	Serine	92-98	H2A.X variant histone	Homo sapiens	76-88
10734083-5	2000	gamma-H2AX formation is inhibited by N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone and the inhibitor of caspase-activated DNase, and it is induced when DNase I and restriction enzymes are introduced into cells, suggesting that any apoptotic endonuclease is sufficient to induce gamma-H2AX formation.	Caspase Inhibitor VI	37-88	H2A.X variant histone	Homo sapiens	6-10
10477747-1	1999	The loss of chromosomal integrity from DNA double-strand breaks introduced into mammalian cells by ionizing radiation results in the specific phosphorylation of histone H2AX on serine residue 139, yielding a specific modified form named gamma-H2AX.	Serine	177-183	H2A.X variant histone	Homo sapiens	169-173
34771723-2	2021	In response to DSB induction, phosphorylation of the histone variant H2AX to gammaH2AX was observed in the form of foci visualized by specific antibodies.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	15-18	H2A.X variant histone	Homo sapiens	69-73
33805713-9	2021	Western blot analysis indicated increased apoptotic markers cleaved Parp, cleaved caspase 3 and phosphorylated H2AX in NAs-HSA-Dox treated DIPG neurospheres.	nas	119-122	H2A.X variant histone	Homo sapiens	111-115
33805713-9	2021	Western blot analysis indicated increased apoptotic markers cleaved Parp, cleaved caspase 3 and phosphorylated H2AX in NAs-HSA-Dox treated DIPG neurospheres.	Doxorubicin	127-130	H2A.X variant histone	Homo sapiens	111-115
9488723-0	1998	DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139.	Serine	66-72	H2A.X variant histone	Homo sapiens	34-46
33941661-5	2021	VCP/p97 inhibition also reduces the etoposide-induced phosphorylation of histone H2AX, indicative of fewer DSBs .	Etoposide	36-45	H2A.X variant histone	Homo sapiens	73-85
33941661-5	2021	VCP/p97 inhibition also reduces the etoposide-induced phosphorylation of histone H2AX, indicative of fewer DSBs .	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	107-111	H2A.X variant histone	Homo sapiens	73-85
34783124-8	2022	Moreover, ginsenoside Rg1 treatment before doxorubicin activates the DNA damage response elements (ATM, H2AX, RAD51, and XRCC1) and subsequent apoptosis-related gene expression (p21, TP53.	Doxorubicin	43-54	H2A.X variant histone	Homo sapiens	104-108
34938381-5	2021	However, phosphorylated H2A.X occurs during apoptosis, which is associated with exposure to cold plasma and ROS.	ros	108-111	H2A.X variant histone	Homo sapiens	24-29
34777693-5	2021	In this process, reactive oxygen species (ROS) and phosphorylation of H2A histone family member X (H2A.X), forming gamma-H2A.X, were enhanced.	gamma-h2a	115-124	H2A.X variant histone	Homo sapiens	70-97
34777693-5	2021	In this process, reactive oxygen species (ROS) and phosphorylation of H2A histone family member X (H2A.X), forming gamma-H2A.X, were enhanced.	gamma-h2a	115-124	H2A.X variant histone	Homo sapiens	99-104
34348893-3	2021	GRB2-SH2 domain targets the GM complex to phosphorylated H2AX at DSBs.	gm	28-30	H2A.X variant histone	Homo sapiens	57-61
34429760-7	2021	In addition, the impact of GADD45alpha overexpression on cell viability was evaluated in vitro and in vivo, and the levels of Ser-139 phosphorylated H2A histone family member X (gamma-H2AX), which is associated with DNA damage, were detected.	Serine	126-129	H2A.X variant histone	Homo sapiens	149-176
34659543-0	2021	miR-328-3p promotes migration and invasion by targeting H2AFX in head and neck squamous cell carcinoma.	mir-328-3p	0-10	H2A.X variant histone	Homo sapiens	56-61
34659543-7	2021	Moreover, H2AFX could partially reverse the migration and invasion of HNSCC caused by miR-328-3p.	mir-328-3p	86-96	H2A.X variant histone	Homo sapiens	10-15
34659543-8	2021	Overall, our results indicated that miR-328-3p enhanced migration and invasion of HNSCC through targeting H2AFX and activated the mTOR pathway.	mir-328-3p	36-46	H2A.X variant histone	Homo sapiens	106-111
34733488-5	2021	In addition, the transduction of upstream extrinsic (Fasl-Fas-caspase-8) and intrinsic (loss of Bcl-2 and mitochondrial membrane potential, DeltaPsim) apoptosis pathways, as well as phosphorylated (p)-H2AX (Ser139), an epigenetic marker contributing to DNA fragmentation and PARP1 activity, was partially suppressed.	(p)	197-200	H2A.X variant histone	Homo sapiens	201-205
34153406-2	2021	The present study investigated the effects of 1,2-DCP on the expression of histone family member X (H2AX) phosphorylated on Ser 139 (gamma-H2AX), a marker of DNA double strand break, in human immortalized cholangiocytes MMNK-1 cells.	Serine	124-127	H2A.X variant histone	Homo sapiens	100-104
34146926-7	2021	Delta9-THC and Delta8-THC also downregulated cyclin D1, p53, NOXA, PUMAalpha, and DRAM expressions but increased p21 and H2AX expression.	Dronabinol	7-10	H2A.X variant histone	Homo sapiens	121-125
34146926-7	2021	Delta9-THC and Delta8-THC also downregulated cyclin D1, p53, NOXA, PUMAalpha, and DRAM expressions but increased p21 and H2AX expression.	Dronabinol	22-25	H2A.X variant histone	Homo sapiens	121-125
34348893-3	2021	GRB2-SH2 domain targets the GM complex to phosphorylated H2AX at DSBs.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	65-69	H2A.X variant histone	Homo sapiens	57-61
34277626-5	2021	After LASSO and Cox regression analyses, a six ARG-based signature (APOC3, EPOR, H2AFX, MXD1, PLCG2, and YWHAZ) was constructed using TCGA dataset that significantly stratified cases into high- and low-risk groups in terms of overall survival (OS).	Arginine	47-50	H2A.X variant histone	Homo sapiens	81-86
34405020-7	2021	The results showed that 5-Aza differentially inhibited spontaneous proliferation, arrested the cell cycle at S phase in DU145, at G1 phase in 22RV1 and LNCaP cells, and G2 phase in normal RWPE-1 cells, as well as induced the expression of phospho-H2A.X and tumor suppressive mammary serine protease inhibitor (maspin) in all three types of CaP cells.	Azacitidine	24-29	H2A.X variant histone	Homo sapiens	247-252
34235927-8	2021	The accumulation of C-rich U-bearing particles induced DNA damage and cytotoxicity as indicated by the increased phosphorylation of the histone H2AX and cell death, respectively.	u-bearing	27-36	H2A.X variant histone	Homo sapiens	136-148
35006630-7	2022	CAPE enhanced the level of ionizing radiation (IR)-induced gamma H2AX foci and cell death by apoptosis.	caffeic acid phenethyl ester	0-4	H2A.X variant histone	Homo sapiens	65-69
34282773-1	2021	Histone H2AX phosphorylated at serine 139 (gamma-H2AX) is a hallmark of DNA damage, signaling the presence of DNA double-strand breaks and global replication stress in mammalian cells.	Serine	31-37	H2A.X variant histone	Homo sapiens	0-12
35568224-6	2022	Expressions of genes responses to DNA damage, ATM, ATR, p53, p21, Bax, H2AX, and GADD45A were disturbed by NIT treatment.	nitenpyram	107-110	H2A.X variant histone	Homo sapiens	71-75
35566199-3	2022	Thouracil amide compounds 5a and 5e inhibited the catalytical activity of PARP1, enhanced cleavage of PARP1, enhanced phosphorylation of H2AX, and increased CASPASE 3/7 activity.	thouracil amide	0-15	H2A.X variant histone	Homo sapiens	137-141
35456987-5	2022	Noteworthy is that while direct irradiation activated only ATM, both ATM and ATR were activated by two factors known to induce the replication stress: hydroxyurea and camptothecin (with subsequent phosphorylation of gamma H2A.X).	Hydroxyurea	151-162	H2A.X variant histone	Homo sapiens	222-227
35456022-0	2022	Apoptotic and DNA Damage Effect of 1,2,3,4,6-Penta-O-galloyl-beta-D-glucose in Cisplatin-Resistant Non-Small Lung Cancer Cells via Phosphorylation of H2AX, CHK2 and p53.	Glucose	68-75	H2A.X variant histone	Homo sapiens	150-154
35456022-0	2022	Apoptotic and DNA Damage Effect of 1,2,3,4,6-Penta-O-galloyl-beta-D-glucose in Cisplatin-Resistant Non-Small Lung Cancer Cells via Phosphorylation of H2AX, CHK2 and p53.	Cisplatin	79-88	H2A.X variant histone	Homo sapiens	150-154
35517402-6	2022	The phosphorylation of H2AX was increased after treatment with DCZ0415 or TRIP13 knockdown.	DCZ0415	63-70	H2A.X variant histone	Homo sapiens	23-27
35456987-5	2022	Noteworthy is that while direct irradiation activated only ATM, both ATM and ATR were activated by two factors known to induce the replication stress: hydroxyurea and camptothecin (with subsequent phosphorylation of gamma H2A.X).	Camptothecin	167-179	H2A.X variant histone	Homo sapiens	222-227
35131362-5	2022	By using immunofluorescence, we found that AC (0.5, 1 and 5 mM) induced the formation of both phosphorylated form of the histone H2 variant H2AX (gH2AX) and p53-binding protein 1 (53BP1) foci.	Acrylamide	43-45	H2A.X variant histone	Homo sapiens	140-144
35235704-0	2022	Genetic variations in ATM and H2AX loci contribute to risk of hematological abnormalities in individuals exposed to BTEX chemicals.	btex	116-120	H2A.X variant histone	Homo sapiens	30-34
35235704-2	2022	The aim of the current study was to determine the relationship of functional polymorphisms ATM-rs228589 A>T, WRN-rs1800392 G>T and H2AX-rs7759 A>G in DBS repair loci with the abnormal hematological indices in workers who exposed to BTEXs.	btexs	232-237	H2A.X variant histone	Homo sapiens	131-135
35191521-6	2022	In vitro, the AZD6738/5-FU combination increased the number of mitotic cells according to flow cytometry, decreased the checkpoint kinase 1 phosphorylation levels and increased cleaved caspase-3 and phosphorylated form of H2A.X variant histone levels according to western blotting, and decreased the proliferation rate of four colon cancer cell lines according to cell viability experiments.	Fluorouracil	22-26	H2A.X variant histone	Homo sapiens	222-227
35199383-7	2022	Importantly, we found that PRV-encoded serine/threonine kinase UL13 interacts with and subsequently phosphorylates H2AX.	Serine	39-45	H2A.X variant histone	Homo sapiens	115-119
35007525-6	2022	Comet assay demonstrated that mollugin induced DNA damage in HepG2 cells, as well as an increase in the expression of p-H2AX.	rubimaillin	30-38	H2A.X variant histone	Homo sapiens	120-124
35137086-10	2022	The phosphorylation of C-terminal of histone H2AX at amino acid Ser 139 (gamma-H2AX), which occurs at the DNA double strand break focus, was evaluated.	Serine	64-67	H2A.X variant histone	Homo sapiens	37-49
35163819-7	2022	Interestingly, a transient induction of phosphor-histone gamma-H2Ax, which is associated with genotoxic damages, was observed.	phosphor-histone	40-56	H2A.X variant histone	Homo sapiens	63-67
35163354-9	2022	Further mechanistic studies performed with the use of flow cytometry showed that under hypoxia, BrdU increased the level of histone H2A.X phosphorylation after X-ray exposure to a greater extent than under normal oxygenation conditions.	Bromodeoxyuridine	96-100	H2A.X variant histone	Homo sapiens	124-137
35163511-4	2022	Treatment with MHY2245 decreased SIRT1 activity and caused DNA damage, leading to the upregulation of p53 acetylation, and increased levels of p53, phosphorylation of H2A histone family member X, ataxia telangiectasia and Rad3-related kinase, checkpoint kinase 1 (Chk1), and Chk2.	mhy2245	15-22	H2A.X variant histone	Homo sapiens	167-241