Sign In

Login

Password

Forgot Password ? Sign Up

Histone H2A (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "Histone H2A" in French language version.

refsWebsite
Global rank French rank
13nih.gov
4th place
12th place
10doi.org
2nd place
3rd place
1science.org
1,160th place
1,188th place
1epigenie.com
low place
low place

doi.org

dx.doi.org

  • Suto, M. J. Clarkson, D. J. Tremethick et K Luger, « Crystal structure of a nucleosome core particle containing the variant histone H2A.Z », Nature Structural Biology, vol. 7, no 12,‎ , p. 1121–4 (PMID 11101893, DOI 10.1038/81971)
  • Mizuguchi, X Shen, J Landry et W. H. Wu, « ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex », Science, vol. 303, no 5656,‎ , p. 343–8 (PMID 14645854, DOI 10.1126/science.1090701)
  • Jakob, J Splinter, S Conrad et K. O. Voss, « DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin », Nucleic Acids Research, vol. 39, no 15,‎ , p. 6489–99 (PMID 21511815, PMCID 3159438, DOI 10.1093/nar/gkr230)
  • Costanzi et J. R. Pehrson, « Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals », Nature, vol. 393, no 6685,‎ , p. 599–601 (PMID 9634239, DOI 10.1038/31275)
  • Mariño-Ramírez, I. K. Jordan et D Landsman, « Multiple independent evolutionary solutions to core histone gene regulation », Genome Biology, vol. 7, no 12,‎ , R122 (PMID 17184543, PMCID 1794435, DOI 10.1186/gb-2006-7-12-r122)
  • Allen, A. M. Buckle, S. C. Cordell et J Löwe, « The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A », Journal of molecular biology, vol. 330, no 3,‎ , p. 503–11 (PMID 12842467, DOI 10.1016/s0022-2836(03)00473-x)
  • Mosammaparast, C. S. Ewart et L. F. Pemberton, « A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B », The EMBO journal, vol. 21, no 23,‎ , p. 6527–38 (PMID 12456659, PMCID 136951, DOI 10.1093/emboj/cdf647)
  • Mariño-Ramírez, K. M. Levine, M Morales et S Zhang, « The Histone Database: An integrated resource for histones and histone fold-containing proteins », Database, vol. 2011,‎ , bar048 (PMID 22025671, PMCID 3199919, DOI 10.1093/database/bar048)
  • Jesu Arockiaraj, Annie J Gnanam, Venkatesh Kumaresan, Rajesh Palanisamy, Annie J Gnanam, Annie J Gnanam, Annie J Gnanam, Annie J Gnanam, Annie J Gnanam et Annie J Gnanam, « An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: Analysis of immune properties », Fish & Shellfish Immunology, vol. 35, no 5,‎ , p. 1511–1522 (PMID 23994279, DOI 10.1016/j.fsi.2013.08.018)
  • Talbert et S Henikoff, « Histone variants--ancient wrap artists of the epigenome », Nature Reviews Molecular Cell Biology, vol. 11, no 4,‎ , p. 264–75 (PMID 20197778, DOI 10.1038/nrm2861)

epigenie.com

nih.gov

ncbi.nlm.nih.gov

  • Khorasanizadeh, « The nucleosome: From genomic organization to genomic regulation », Cell, vol. 116, no 2,‎ , p. 259–72 (PMID 14744436)
  • Bosch et P Suau, « Changes in core histone variant composition in differentiating neurons: The roles of differential turnover and synthesis rates », European journal of cell biology, vol. 68, no 3,‎ , p. 220–5 (PMID 8603674)
  • Suto, M. J. Clarkson, D. J. Tremethick et K Luger, « Crystal structure of a nucleosome core particle containing the variant histone H2A.Z », Nature Structural Biology, vol. 7, no 12,‎ , p. 1121–4 (PMID 11101893, DOI 10.1038/81971)
  • Mizuguchi, X Shen, J Landry et W. H. Wu, « ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex », Science, vol. 303, no 5656,‎ , p. 343–8 (PMID 14645854, DOI 10.1126/science.1090701)
  • Jakob, J Splinter, S Conrad et K. O. Voss, « DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin », Nucleic Acids Research, vol. 39, no 15,‎ , p. 6489–99 (PMID 21511815, PMCID 3159438, DOI 10.1093/nar/gkr230)
  • Costanzi et J. R. Pehrson, « Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals », Nature, vol. 393, no 6685,‎ , p. 599–601 (PMID 9634239, DOI 10.1038/31275)
  • Mariño-Ramírez, I. K. Jordan et D Landsman, « Multiple independent evolutionary solutions to core histone gene regulation », Genome Biology, vol. 7, no 12,‎ , R122 (PMID 17184543, PMCID 1794435, DOI 10.1186/gb-2006-7-12-r122)
  • Allen, A. M. Buckle, S. C. Cordell et J Löwe, « The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A », Journal of molecular biology, vol. 330, no 3,‎ , p. 503–11 (PMID 12842467, DOI 10.1016/s0022-2836(03)00473-x)
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5791885/
  • Mosammaparast, C. S. Ewart et L. F. Pemberton, « A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B », The EMBO journal, vol. 21, no 23,‎ , p. 6527–38 (PMID 12456659, PMCID 136951, DOI 10.1093/emboj/cdf647)
  • Mariño-Ramírez, K. M. Levine, M Morales et S Zhang, « The Histone Database: An integrated resource for histones and histone fold-containing proteins », Database, vol. 2011,‎ , bar048 (PMID 22025671, PMCID 3199919, DOI 10.1093/database/bar048)
  • Jesu Arockiaraj, Annie J Gnanam, Venkatesh Kumaresan, Rajesh Palanisamy, Annie J Gnanam, Annie J Gnanam, Annie J Gnanam, Annie J Gnanam, Annie J Gnanam et Annie J Gnanam, « An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: Analysis of immune properties », Fish & Shellfish Immunology, vol. 35, no 5,‎ , p. 1511–1522 (PMID 23994279, DOI 10.1016/j.fsi.2013.08.018)
  • Talbert et S Henikoff, « Histone variants--ancient wrap artists of the epigenome », Nature Reviews Molecular Cell Biology, vol. 11, no 4,‎ , p. 264–75 (PMID 20197778, DOI 10.1038/nrm2861)

science.org