ヒストンH2A (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "ヒストンH2A" in Japanese language version.

refsWebsite

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20nih.gov

4^th place

24^th place

11doi.org

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6^th place

2harvard.edu

18^th place

107^th place

1archive.org

6^th place

146^th place

1zenodo.org

621^st place

4,635^th place

archive.org

Cox, Michael M; Lehninger, Albert L; Nelson, David L (2005). Lehninger principles of biochemistry (4th ed.). New York: W.H. Freeman. ISBN 978-0-7167-4339-2

doi.org

“The nucleosome: from genomic organization to genomic regulation”. Cell 116 (2): 259–72. (January 2004). doi:10.1016/s0092-8674(04)00044-3. PMID 14744436.
“Crystal structure of a nucleosome core particle containing the variant histone H2A.Z”. Nature Structural Biology 7 (12): 1121–4. (December 2000). doi:10.1038/81971. PMID 11101893.
“ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex”. Science 303 (5656): 343–8. (January 2004). Bibcode: 2004Sci...303..343M. doi:10.1126/science.1090701. PMID 14645854. https://zenodo.org/record/1230842.
“DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin”. Nucleic Acids Research 39 (15): 6489–99. (August 2011). doi:10.1093/nar/gkr230. PMC 3159438. PMID 21511815.
“Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals”. Nature 393 (6685): 599–601. (June 1998). Bibcode: 1998Natur.393..599C. doi:10.1038/31275. PMID 9634239.
“Multiple independent evolutionary solutions to core histone gene regulation”. Genome Biology 7 (12): R122. (2006). doi:10.1186/gb-2006-7-12-r122. PMC 1794435. PMID 17184543.
“The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A”. Journal of Molecular Biology 330 (3): 503–11. (July 2003). doi:10.1016/s0022-2836(03)00473-x. PMID 12842467.
“A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B”. The EMBO Journal 21 (23): 6527–38. (December 2002). doi:10.1093/emboj/cdf647. PMC 136951. PMID 12456659.
“The Histone Database: an integrated resource for histones and histone fold-containing proteins”. Database 2011: bar048. (2011). doi:10.1093/database/bar048. PMC 3199919. PMID 22025671.
“An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: analysis of immune properties”. Fish & Shellfish Immunology 35 (5): 1511–22. (November 2013). doi:10.1016/j.fsi.2013.08.018. PMID 23994279.
“Histone variants--ancient wrap artists of the epigenome”. Nature Reviews. Molecular Cell Biology 11 (4): 264–75. (April 2010). doi:10.1038/nrm2861. PMID 20197778.

harvard.edu

ui.adsabs.harvard.edu

“ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex”. Science 303 (5656): 343–8. (January 2004). Bibcode: 2004Sci...303..343M. doi:10.1126/science.1090701. PMID 14645854. https://zenodo.org/record/1230842.
“Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals”. Nature 393 (6685): 599–601. (June 1998). Bibcode: 1998Natur.393..599C. doi:10.1038/31275. PMID 9634239.

nih.gov

pubmed.ncbi.nlm.nih.gov

“The nucleosome: from genomic organization to genomic regulation”. Cell 116 (2): 259–72. (January 2004). doi:10.1016/s0092-8674(04)00044-3. PMID 14744436.
“Changes in core histone variant composition in differentiating neurons: the roles of differential turnover and synthesis rates”. European Journal of Cell Biology 68 (3): 220–5. (November 1995). PMID 8603674.
“Crystal structure of a nucleosome core particle containing the variant histone H2A.Z”. Nature Structural Biology 7 (12): 1121–4. (December 2000). doi:10.1038/81971. PMID 11101893.
“ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex”. Science 303 (5656): 343–8. (January 2004). Bibcode: 2004Sci...303..343M. doi:10.1126/science.1090701. PMID 14645854. https://zenodo.org/record/1230842.
“DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin”. Nucleic Acids Research 39 (15): 6489–99. (August 2011). doi:10.1093/nar/gkr230. PMC 3159438. PMID 21511815.
“Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals”. Nature 393 (6685): 599–601. (June 1998). Bibcode: 1998Natur.393..599C. doi:10.1038/31275. PMID 9634239.
“Multiple independent evolutionary solutions to core histone gene regulation”. Genome Biology 7 (12): R122. (2006). doi:10.1186/gb-2006-7-12-r122. PMC 1794435. PMID 17184543.
“The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A”. Journal of Molecular Biology 330 (3): 503–11. (July 2003). doi:10.1016/s0022-2836(03)00473-x. PMID 12842467.
“A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B”. The EMBO Journal 21 (23): 6527–38. (December 2002). doi:10.1093/emboj/cdf647. PMC 136951. PMID 12456659.
“The Histone Database: an integrated resource for histones and histone fold-containing proteins”. Database 2011: bar048. (2011). doi:10.1093/database/bar048. PMC 3199919. PMID 22025671.
“An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: analysis of immune properties”. Fish & Shellfish Immunology 35 (5): 1511–22. (November 2013). doi:10.1016/j.fsi.2013.08.018. PMID 23994279.
“Histone variants--ancient wrap artists of the epigenome”. Nature Reviews. Molecular Cell Biology 11 (4): 264–75. (April 2010). doi:10.1038/nrm2861. PMID 20197778.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

zenodo.org

“ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex”. Science 303 (5656): 343–8. (January 2004). Bibcode: 2004Sci...303..343M. doi:10.1126/science.1090701. PMID 14645854. https://zenodo.org/record/1230842.