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H-NS (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "H-NS" in French language version.

refsWebsite
Global rank French rank
8nih.gov
4th place
12th place
8doi.org
2nd place
3rd place
1sciencedirect.com
149th place
80th place
1wiley.com
222nd place
129th place
1springer.com
274th place
223rd place
1nature.com
234th place
147th place
1oup.com
485th place
416th place
1plos.org
2,112th place
666th place
1cshlp.org
low place
3,952nd place
1jbc.org
4,455th place
1,915th place

cshlp.org

genesdev.cshlp.org

  • (en) William Wiley Navarre, Michael McClelland, Stephen J. Libby et Ferric C. Fang, « Silencing of xenogeneic DNA by H-NS—facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA », Genes & Development, vol. 21, no 12,‎ , p. 1456-1471 (PMID 17575047, DOI 10.1101/gad.1543107, lire en ligne)

doi.org

dx.doi.org

  • (en) Diego Esposito, Arsen Petrovic, Richard Harris, Shusuke Ono, John F. Eccleston, Amina Mbabaali, Ihtshamul Haq, Christopher F. Higgins, Jay C. D. Hinton, Paul C. Driscoll et John E.Ladbury, « H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein », Journal of Molecular Biology, vol. 324, no 4,‎ , p. 841-850 (PMID 12460581, DOI 10.1016/S0022-2836(02)01141-5, lire en ligne)
  • (en) Heisaburo Shindo, Takanobu Iwaki, Ryoichi Ieda, Hitoshi Kurumizaka, Chiharu Ueguchi, Takeshi Mizuno, Soichi Morikawa, Haruki Nakamura et Hitoshi Kuboniwa, « Solution structure of the DNA binding domain of a nucleoid‐associated protein, H‐NS, from Escherichia coli », FEBS Letters, vol. 360, no 2,‎ , p. 125-131 (PMID 7875316, DOI 10.1016/0014-5793%2895%2900079-O, lire en ligne)
  • (en) C. Beloin, P. Deighan, M. Doyle et C. J. Dorman, « Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein », Molecular Genetics and Genomics, vol. 270, no 1,‎ , p. 66-77 (PMID 12898223, DOI 10.1007/s00438-003-0897-0, lire en ligne)
  • (en) Charles J. Dorman, « H-NS: a universal regulator for a dynamic genome », Nature Reviews. Microbiology, vol. 2, no 5,‎ , p. 391-400 (PMID 15100692, DOI 10.1038/nrmicro883, lire en ligne)
  • (en) Remus Thei Dame, Claire Wyman, Nora Goosen, « H-NS mediated compaction of DNA visualised by atomic force microscopy », Nucleic Acids Research, vol. 28, no 18,‎ , p. 3504-3510 (PMID 10982869, PMCID 110753, DOI 10.1093/nar/28.18.3504, lire en ligne)
  • (en) Sacha Lucchini, Gary Rowley, Martin D. Goldberg, Douglas Hurd, Marcus Harrison et Jay C. D. Hinton, « H-NS Mediates the Silencing of Laterally Acquired Genes in Bacteria », PLoS Pathogens, vol. 2, no 8,‎ , article no e81 (PMID 16933988, PMCID 1550270, DOI 10.1371/journal.ppat.0020081, lire en ligne)
  • (en) William Wiley Navarre, Michael McClelland, Stephen J. Libby et Ferric C. Fang, « Silencing of xenogeneic DNA by H-NS—facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA », Genes & Development, vol. 21, no 12,‎ , p. 1456-1471 (PMID 17575047, DOI 10.1101/gad.1543107, lire en ligne)
  • (en) Gina M. Donato et Thomas H. Kawula, « Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli », The Journal of Biological Chemistry, vol. 273, no 37,‎ , p. 24030-24036 (PMID 9727020, DOI 10.1074/jbc.273.37.24030, lire en ligne)

jbc.org

  • (en) Gina M. Donato et Thomas H. Kawula, « Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli », The Journal of Biological Chemistry, vol. 273, no 37,‎ , p. 24030-24036 (PMID 9727020, DOI 10.1074/jbc.273.37.24030, lire en ligne)

nature.com

nih.gov

ncbi.nlm.nih.gov

  • (en) Diego Esposito, Arsen Petrovic, Richard Harris, Shusuke Ono, John F. Eccleston, Amina Mbabaali, Ihtshamul Haq, Christopher F. Higgins, Jay C. D. Hinton, Paul C. Driscoll et John E.Ladbury, « H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein », Journal of Molecular Biology, vol. 324, no 4,‎ , p. 841-850 (PMID 12460581, DOI 10.1016/S0022-2836(02)01141-5, lire en ligne)
  • (en) Heisaburo Shindo, Takanobu Iwaki, Ryoichi Ieda, Hitoshi Kurumizaka, Chiharu Ueguchi, Takeshi Mizuno, Soichi Morikawa, Haruki Nakamura et Hitoshi Kuboniwa, « Solution structure of the DNA binding domain of a nucleoid‐associated protein, H‐NS, from Escherichia coli », FEBS Letters, vol. 360, no 2,‎ , p. 125-131 (PMID 7875316, DOI 10.1016/0014-5793%2895%2900079-O, lire en ligne)
  • (en) C. Beloin, P. Deighan, M. Doyle et C. J. Dorman, « Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein », Molecular Genetics and Genomics, vol. 270, no 1,‎ , p. 66-77 (PMID 12898223, DOI 10.1007/s00438-003-0897-0, lire en ligne)
  • (en) Charles J. Dorman, « H-NS: a universal regulator for a dynamic genome », Nature Reviews. Microbiology, vol. 2, no 5,‎ , p. 391-400 (PMID 15100692, DOI 10.1038/nrmicro883, lire en ligne)
  • (en) Remus Thei Dame, Claire Wyman, Nora Goosen, « H-NS mediated compaction of DNA visualised by atomic force microscopy », Nucleic Acids Research, vol. 28, no 18,‎ , p. 3504-3510 (PMID 10982869, PMCID 110753, DOI 10.1093/nar/28.18.3504, lire en ligne)
  • (en) Sacha Lucchini, Gary Rowley, Martin D. Goldberg, Douglas Hurd, Marcus Harrison et Jay C. D. Hinton, « H-NS Mediates the Silencing of Laterally Acquired Genes in Bacteria », PLoS Pathogens, vol. 2, no 8,‎ , article no e81 (PMID 16933988, PMCID 1550270, DOI 10.1371/journal.ppat.0020081, lire en ligne)
  • (en) William Wiley Navarre, Michael McClelland, Stephen J. Libby et Ferric C. Fang, « Silencing of xenogeneic DNA by H-NS—facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA », Genes & Development, vol. 21, no 12,‎ , p. 1456-1471 (PMID 17575047, DOI 10.1101/gad.1543107, lire en ligne)
  • (en) Gina M. Donato et Thomas H. Kawula, « Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli », The Journal of Biological Chemistry, vol. 273, no 37,‎ , p. 24030-24036 (PMID 9727020, DOI 10.1074/jbc.273.37.24030, lire en ligne)

oup.com

academic.oup.com

plos.org

journals.plos.org

sciencedirect.com

  • (en) Diego Esposito, Arsen Petrovic, Richard Harris, Shusuke Ono, John F. Eccleston, Amina Mbabaali, Ihtshamul Haq, Christopher F. Higgins, Jay C. D. Hinton, Paul C. Driscoll et John E.Ladbury, « H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein », Journal of Molecular Biology, vol. 324, no 4,‎ , p. 841-850 (PMID 12460581, DOI 10.1016/S0022-2836(02)01141-5, lire en ligne)

springer.com

link.springer.com

  • (en) C. Beloin, P. Deighan, M. Doyle et C. J. Dorman, « Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein », Molecular Genetics and Genomics, vol. 270, no 1,‎ , p. 66-77 (PMID 12898223, DOI 10.1007/s00438-003-0897-0, lire en ligne)

wiley.com

febs.onlinelibrary.wiley.com

  • (en) Heisaburo Shindo, Takanobu Iwaki, Ryoichi Ieda, Hitoshi Kurumizaka, Chiharu Ueguchi, Takeshi Mizuno, Soichi Morikawa, Haruki Nakamura et Hitoshi Kuboniwa, « Solution structure of the DNA binding domain of a nucleoid‐associated protein, H‐NS, from Escherichia coli », FEBS Letters, vol. 360, no 2,‎ , p. 125-131 (PMID 7875316, DOI 10.1016/0014-5793%2895%2900079-O, lire en ligne)