H2AX (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "H2AX" in Japanese language version.

Last modified: 20:12:04, 28 April 2023 (UTC)

Ref.Un. Ref.Website

Global rank Japanese rank

5839nih.gov

5^th place

11^th place

3021doi.org

2^nd place

3^rd place

62ensembl.org

630^th place

1,132^nd place

22adsabs.harvard.edu

14^th place

60^th place

adsabs.harvard.edu (Global: 14^th place; Japanese: 60^th place)

ui.adsabs.harvard.edu

“HP1-beta mobilization promotes chromatin changes that initiate the DNA damage response”. Nature 453 (7195): 682–6. (2008). Bibcode:2008Natur.453..682A. doi:10.1038/nature06875. PMID 18438399.
“MDC1 is a mediator of the mammalian DNA damage checkpoint”. Nature 421 (6926): 961–6. (Feb 2003). Bibcode:2003Natur.421..961S. doi:10.1038/nature01446. PMID 12607005.

doi.org (Global: 2^nd place; Japanese: 3^rd place)

“Phosphorylated H2Ax is not an unambiguous marker for DNA double strand breaks”. Cell Cycle 10 (19): 3223–4. (2011). doi:10.4161/cc.10.19.17448. PMID 21921674.
“DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139”. J. Biol. Chem. 273 (10): 5858–68. (1998). doi:10.1074/jbc.273.10.5858. PMID 9488723.
“HP1-beta mobilization promotes chromatin changes that initiate the DNA damage response”. Nature 453 (7195): 682–6. (2008). Bibcode:2008Natur.453..682A. doi:10.1038/nature06875. PMID 18438399.
“Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes”. J. Biol. Chem. 278 (22): 20303–12. (2003). doi:10.1074/jbc.M300198200. PMID 12660252.
“Double strand break repair functions of histone H2AX”. Mutat. Res. 750 (1–2): 5–14. (2013). doi:10.1016/j.mrfmmm.2013.07.007. PMC 3818383. PMID 23916969.
“Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks”. J. Cell Biol. 173 (2): 195–206. (2006). doi:10.1083/jcb.200510130. PMC 2063811. PMID 16618811.
“Nuclear dynamics of RAD52 group homologous recombination proteins in response to DNA damage”. EMBO J. 21 (8): 2030–7. (2002). doi:10.1093/emboj/21.8.2030. PMC 125370. PMID 11953322.
“Constitutive histone H2AX phosphorylation and ATM activation, the reporters of DNA damage by endogenous oxidants”. Cell Cycle 5 (17): 1940–5. (2006). doi:10.4161/cc.5.17.3191. PMC 3488278. PMID 16940754.
“RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins”. Cell 131 (5): 887–900. (2007). doi:10.1016/j.cell.2007.09.040. PMID 18001824.
“A new non-catalytic role for ubiquitin ligase RNF8 in unfolding higher-order chromatin structure”. EMBO J. 31 (11): 2511–27. (2012). doi:10.1038/emboj.2012.104. PMC 3365417. PMID 22531782.
“DNA damage foci: Meaning and significance”. Environ. Mol. Mutagen. 56 (6): 491–504. (2015). doi:10.1002/em.21944. PMID 25773265.
“Clustered DNA damage induces pan-nuclear H2AX phosphorylation mediated by ATM and DNA-PK”. Nucleic Acids Res. 41 (12): 6109–18. (2013). doi:10.1093/nar/gkt304. PMC 3695524. PMID 23620287.
“Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains”. The EMBO Journal 21 (24): 6755–62. (Dec 2002). doi:10.1093/emboj/cdf691. PMC 139111. PMID 12485996.
“Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase”. The Journal of Biological Chemistry 277 (24): 22085–92. (Jun 2002). doi:10.1074/jbc.M201252200. PMID 11927591.
“A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage”. Current Biology 10 (15): 886–95. (2000). doi:10.1016/s0960-9822(00)00610-2. PMID 10959836.
“Functional interaction between BLM helicase and 53BP1 in a Chk1-mediated pathway during S-phase arrest”. The Journal of Cell Biology 166 (6): 801–13. (Sep 2004). doi:10.1083/jcb.200405128. PMC 2172115. PMID 15364958.
“MDC1 is a mediator of the mammalian DNA damage checkpoint”. Nature 421 (6926): 961–6. (Feb 2003). Bibcode:2003Natur.421..961S. doi:10.1038/nature01446. PMID 12607005.
“NFBD1/MDC1 regulates ionizing radiation-induced focus formation by DNA checkpoint signaling and repair factors”. FASEB Journal 17 (13): 1842–8. (Oct 2003). doi:10.1096/fj.03-0310com. PMID 14519663.
“NBS1 localizes to γH2AX foci through interaction with the FHA/BRCT domain”. Current Biology 12 (21): 1846–51. (Oct 2002). doi:10.1016/s0960-9822(02)01259-9. PMID 12419185.
“DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1”. Nature Cell Biology 4 (12): 993–7. (Dec 2002). doi:10.1038/ncb884. PMID 12447390.
“Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX”. The Journal of Biological Chemistry 278 (22): 19579–82. (May 2003). doi:10.1074/jbc.C300117200. PMID 12697768.

ensembl.org (Global: 630^th place; Japanese: 1,132^nd place)

may2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000188486 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000049932 - Ensembl, May 2017

nih.gov (Global: 5^th place; Japanese: 11^th place)

pubmed.ncbi.nlm.nih.gov

“Phosphorylated H2Ax is not an unambiguous marker for DNA double strand breaks”. Cell Cycle 10 (19): 3223–4. (2011). doi:10.4161/cc.10.19.17448. PMID 21921674.
“DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139”. J. Biol. Chem. 273 (10): 5858–68. (1998). doi:10.1074/jbc.273.10.5858. PMID 9488723.
“HP1-beta mobilization promotes chromatin changes that initiate the DNA damage response”. Nature 453 (7195): 682–6. (2008). Bibcode:2008Natur.453..682A. doi:10.1038/nature06875. PMID 18438399.
“Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes”. J. Biol. Chem. 278 (22): 20303–12. (2003). doi:10.1074/jbc.M300198200. PMID 12660252.
“Double strand break repair functions of histone H2AX”. Mutat. Res. 750 (1–2): 5–14. (2013). doi:10.1016/j.mrfmmm.2013.07.007. PMC 3818383. PMID 23916969.
“Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks”. J. Cell Biol. 173 (2): 195–206. (2006). doi:10.1083/jcb.200510130. PMC 2063811. PMID 16618811.
“Nuclear dynamics of RAD52 group homologous recombination proteins in response to DNA damage”. EMBO J. 21 (8): 2030–7. (2002). doi:10.1093/emboj/21.8.2030. PMC 125370. PMID 11953322.
“Constitutive histone H2AX phosphorylation and ATM activation, the reporters of DNA damage by endogenous oxidants”. Cell Cycle 5 (17): 1940–5. (2006). doi:10.4161/cc.5.17.3191. PMC 3488278. PMID 16940754.
“RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins”. Cell 131 (5): 887–900. (2007). doi:10.1016/j.cell.2007.09.040. PMID 18001824.
“A new non-catalytic role for ubiquitin ligase RNF8 in unfolding higher-order chromatin structure”. EMBO J. 31 (11): 2511–27. (2012). doi:10.1038/emboj.2012.104. PMC 3365417. PMID 22531782.
“DNA damage foci: Meaning and significance”. Environ. Mol. Mutagen. 56 (6): 491–504. (2015). doi:10.1002/em.21944. PMID 25773265.
“Clustered DNA damage induces pan-nuclear H2AX phosphorylation mediated by ATM and DNA-PK”. Nucleic Acids Res. 41 (12): 6109–18. (2013). doi:10.1093/nar/gkt304. PMC 3695524. PMID 23620287.
“Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains”. The EMBO Journal 21 (24): 6755–62. (Dec 2002). doi:10.1093/emboj/cdf691. PMC 139111. PMID 12485996.
“Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase”. The Journal of Biological Chemistry 277 (24): 22085–92. (Jun 2002). doi:10.1074/jbc.M201252200. PMID 11927591.
“A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage”. Current Biology 10 (15): 886–95. (2000). doi:10.1016/s0960-9822(00)00610-2. PMID 10959836.
“Functional interaction between BLM helicase and 53BP1 in a Chk1-mediated pathway during S-phase arrest”. The Journal of Cell Biology 166 (6): 801–13. (Sep 2004). doi:10.1083/jcb.200405128. PMC 2172115. PMID 15364958.
“MDC1 is a mediator of the mammalian DNA damage checkpoint”. Nature 421 (6926): 961–6. (Feb 2003). Bibcode:2003Natur.421..961S. doi:10.1038/nature01446. PMID 12607005.
“NFBD1/MDC1 regulates ionizing radiation-induced focus formation by DNA checkpoint signaling and repair factors”. FASEB Journal 17 (13): 1842–8. (Oct 2003). doi:10.1096/fj.03-0310com. PMID 14519663.
“NBS1 localizes to γH2AX foci through interaction with the FHA/BRCT domain”. Current Biology 12 (21): 1846–51. (Oct 2002). doi:10.1016/s0960-9822(02)01259-9. PMID 12419185.
“DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1”. Nature Cell Biology 4 (12): 993–7. (Dec 2002). doi:10.1038/ncb884. PMID 12447390.
“Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX”. The Journal of Biological Chemistry 278 (22): 19579–82. (May 2003). doi:10.1074/jbc.C300117200. PMID 12697768.

H2AX (Japanese Wikipedia)

adsabs.harvard.edu (Global: 14th place; Japanese: 60th place)

ui.adsabs.harvard.edu

doi.org (Global: 2nd place; Japanese: 3rd place)

ensembl.org (Global: 630th place; Japanese: 1,132nd place)

may2017.archive.ensembl.org

nih.gov (Global: 5th place; Japanese: 11th place)

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

adsabs.harvard.edu (Global: 14^th place; Japanese: 60^th place)

doi.org (Global: 2^nd place; Japanese: 3^rd place)

ensembl.org (Global: 630^th place; Japanese: 1,132^nd place)

nih.gov (Global: 5^th place; Japanese: 11^th place)