ヒストンH1 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "ヒストンH1" in Japanese language version.

refsWebsite

Global rank Japanese rank

4^th place

24^th place

2^nd place

6^th place

18^th place

107^th place

6^th place

146^th place

archive.org

Jeon, Kwang W.; Berezney, Ronald (1995). Structural and functional organization of the nuclear matrix. Boston: Academic Press. pp. 214–7. ISBN 978-0-12-364565-4

doi.org

“Crystal structure of globular domain of histone H5 and its implications for nucleosome binding”. Nature 362 (6417): 219–23. (March 1993). Bibcode: 1993Natur.362..219R. doi:10.1038/362219a0. PMID 8384699.
“Origin of H1 linker histones”. FASEB Journal 15 (1): 34–42. (January 2001). doi:10.1096/fj.00-0237rev. PMID 11149891.
“The histone H1 family: specific members, specific functions?”. Biological Chemistry 389 (4): 333–43. (April 2008). doi:10.1515/BC.2008.037. PMID 18208346.
“Solenoidal model for superstructure in chromatin”. Proceedings of the National Academy of Sciences of the United States of America 73 (6): 1897–901. (June 1976). Bibcode: 1976PNAS...73.1897F. doi:10.1073/pnas.73.6.1897. PMC 430414. PMID 1064861.
“Influence of histone H1 on chromatin structure”. Cell 12 (1): 101–7. (September 1977). doi:10.1016/0092-8674(77)90188-X. PMID 561660.
“Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin”. The Journal of Cell Biology 83 (2 Pt 1): 403–27. (November 1979). doi:10.1083/jcb.83.2.403. PMC 2111545. PMID 387806.
“What determines the folding of the chromatin fiber?”. Proceedings of the National Academy of Sciences of the United States of America 93 (20): 10548–55. (October 1996). Bibcode: 1996PNAS...9310548V. doi:10.1073/pnas.93.20.10548. PMC 38190. PMID 8855215.
“Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure”. Proceedings of the National Academy of Sciences of the United States of America 105 (26): 8872–7. (July 2008). Bibcode: 2008PNAS..105.8872R. doi:10.1073/pnas.0802336105. PMC 2440727. PMID 18583476.
“Heterogeneity of chromatin subunits in vitro and location of histone H1”. Nucleic Acids Research 3 (2): 477–92. (February 1976). doi:10.1093/nar/3.2.477. PMC 342917. PMID 1257057.
“Removal of histone H1 exposes a fifty base pair DNA segment between nucleosomes”. Biochemistry 15 (15): 3307–14. (July 1976). doi:10.1021/bi00660a022. PMID 952859.
“The structure of histone H1 and its location in chromatin”. Nature 288 (5792): 675–9. (December 1980). Bibcode: 1980Natur.288..675A. doi:10.1038/288675a0. PMID 7453800.
“Footprinting of linker histones H5 and H1 on the nucleosome”. The EMBO Journal 7 (12): 3685–91. (December 1988). doi:10.1002/j.1460-2075.1988.tb03250.x. PMC 454941. PMID 3208745.
“Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin”. Proceedings of the National Academy of Sciences of the United States of America 95 (24): 14173–8. (November 1998). Bibcode: 1998PNAS...9514173B. doi:10.1073/pnas.95.24.14173. PMC 24346. PMID 9826673.
“The maternal histone H1 variant, H1M (B4 protein), is the predominant H1 histone in Xenopus pregastrula embryos”. Developmental Biology 161 (2): 425–39. (February 1994). doi:10.1006/dbio.1994.1042. PMID 8313993.
“Differential effect of H1 variant overexpression on cell cycle progression and gene expression”. Nucleic Acids Research 24 (3): 486–93. (February 1996). doi:10.1093/nar/24.3.486. PMC 145659. PMID 8602362.
“Effects of H1 histone variant overexpression on chromatin structure”. The Journal of Biological Chemistry 274 (53): 37950–6. (December 1999). doi:10.1074/jbc.274.53.37950. PMID 10608862.
“Histone H1 is essential for mitotic chromosome architecture and segregation in Xenopus laevis egg extracts”. The Journal of Cell Biology 169 (6): 859–69. (June 2005). doi:10.1083/jcb.200503031. PMC 2171634. PMID 15967810.
“Functional comparison of H1 histones in Xenopus reveals isoform-specific regulation by Cdk1 and RanGTP”. Current Biology 20 (11): 1048–52. (June 2010). doi:10.1016/j.cub.2010.04.025. PMC 2902237. PMID 20471264.
“Linker histones are not essential and affect chromatin condensation in vivo”. Cell 82 (1): 47–56. (July 1995). doi:10.1016/0092-8674(95)90051-9. PMID 7606784.
“Linker histone H1 is essential for Drosophila development, the establishment of pericentric heterochromatin, and a normal polytene chromosome structure”. Genes & Development 23 (4): 452–65. (February 2009). doi:10.1101/gad.1749309. PMC 2648648. PMID 19196654.
“Dynamic binding of histone H1 to chromatin in living cells”. Nature 408 (6814): 877–81. (December 2000). Bibcode: 2000Natur.408..877M. doi:10.1038/35048610. PMID 11130729.
“Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins”. The Journal of Cell Biology 168 (1): 41–54. (January 2005). doi:10.1083/jcb.200407182. PMC 2171683. PMID 15623580.
“The dynamics of histone H1 function in chromatin”. Molecular Cell 17 (5): 617–20. (March 2005). doi:10.1016/j.molcel.2005.02.019. PMID 15749012.
“Histone H1 compacts DNA under force and during chromatin assembly”. Molecular Biology of the Cell 23 (24): 4864–71. (December 2012). doi:10.1091/mbc.E12-07-0518. PMC 3521692. PMID 23097493.
Cimini, Daniela, ed (September 2010). “Xenopus egg extracts increase dynamics of histone H1 on sperm chromatin”. PLOS One 5 (9): e13111. Bibcode: 2010PLoSO...513111F. doi:10.1371/journal.pone.0013111. PMC 2947519. PMID 20927327.
“Somatic linker histones cause loss of mesodermal competence in Xenopus”. Nature 389 (6649): 395–9. (September 1997). Bibcode: 1997Natur.389..395S. doi:10.1038/38755. PMID 9311783.
“Histone H1 variants differentially inhibit DNA replication through an affinity for chromatin mediated by their carboxyl-terminal domains”. Gene 292 (1–2): 173–81. (June 2002). doi:10.1016/S0378-1119(02)00675-3. PMID 12119111.
“Histone H1 diversity: bridging regulatory signals to linker histone function”. Gene 271 (1): 1–12. (June 2001). doi:10.1016/S0378-1119(01)00495-4. PMID 11410360.
“Cracking the enigmatic linker histone code”. Journal of Biochemistry 143 (3): 287–93. (March 2008). doi:10.1093/jb/mvn013. PMID 18234717.
“Histone H1 and its isoforms: contribution to chromatin structure and function”. Gene 431 (1–2): 1–12. (February 2009). doi:10.1016/j.gene.2008.11.003. PMID 19059319.
“H1 histones: current perspectives and challenges”. Nucleic Acids Research 41 (21): 9593–609. (November 2013). doi:10.1093/nar/gkt700. PMC 3834806. PMID 23945933.

harvard.edu

ui.adsabs.harvard.edu

“Crystal structure of globular domain of histone H5 and its implications for nucleosome binding”. Nature 362 (6417): 219–23. (March 1993). Bibcode: 1993Natur.362..219R. doi:10.1038/362219a0. PMID 8384699.
“Solenoidal model for superstructure in chromatin”. Proceedings of the National Academy of Sciences of the United States of America 73 (6): 1897–901. (June 1976). Bibcode: 1976PNAS...73.1897F. doi:10.1073/pnas.73.6.1897. PMC 430414. PMID 1064861.
“What determines the folding of the chromatin fiber?”. Proceedings of the National Academy of Sciences of the United States of America 93 (20): 10548–55. (October 1996). Bibcode: 1996PNAS...9310548V. doi:10.1073/pnas.93.20.10548. PMC 38190. PMID 8855215.
“Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure”. Proceedings of the National Academy of Sciences of the United States of America 105 (26): 8872–7. (July 2008). Bibcode: 2008PNAS..105.8872R. doi:10.1073/pnas.0802336105. PMC 2440727. PMID 18583476.
“The structure of histone H1 and its location in chromatin”. Nature 288 (5792): 675–9. (December 1980). Bibcode: 1980Natur.288..675A. doi:10.1038/288675a0. PMID 7453800.
“Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin”. Proceedings of the National Academy of Sciences of the United States of America 95 (24): 14173–8. (November 1998). Bibcode: 1998PNAS...9514173B. doi:10.1073/pnas.95.24.14173. PMC 24346. PMID 9826673.
“Dynamic binding of histone H1 to chromatin in living cells”. Nature 408 (6814): 877–81. (December 2000). Bibcode: 2000Natur.408..877M. doi:10.1038/35048610. PMID 11130729.
Cimini, Daniela, ed (September 2010). “Xenopus egg extracts increase dynamics of histone H1 on sperm chromatin”. PLOS One 5 (9): e13111. Bibcode: 2010PLoSO...513111F. doi:10.1371/journal.pone.0013111. PMC 2947519. PMID 20927327.
“Somatic linker histones cause loss of mesodermal competence in Xenopus”. Nature 389 (6649): 395–9. (September 1997). Bibcode: 1997Natur.389..395S. doi:10.1038/38755. PMID 9311783.

nih.gov

pubmed.ncbi.nlm.nih.gov

“Crystal structure of globular domain of histone H5 and its implications for nucleosome binding”. Nature 362 (6417): 219–23. (March 1993). Bibcode: 1993Natur.362..219R. doi:10.1038/362219a0. PMID 8384699.
“Origin of H1 linker histones”. FASEB Journal 15 (1): 34–42. (January 2001). doi:10.1096/fj.00-0237rev. PMID 11149891.
“The histone H1 family: specific members, specific functions?”. Biological Chemistry 389 (4): 333–43. (April 2008). doi:10.1515/BC.2008.037. PMID 18208346.
“Solenoidal model for superstructure in chromatin”. Proceedings of the National Academy of Sciences of the United States of America 73 (6): 1897–901. (June 1976). Bibcode: 1976PNAS...73.1897F. doi:10.1073/pnas.73.6.1897. PMC 430414. PMID 1064861.
“Influence of histone H1 on chromatin structure”. Cell 12 (1): 101–7. (September 1977). doi:10.1016/0092-8674(77)90188-X. PMID 561660.
“Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin”. The Journal of Cell Biology 83 (2 Pt 1): 403–27. (November 1979). doi:10.1083/jcb.83.2.403. PMC 2111545. PMID 387806.
“What determines the folding of the chromatin fiber?”. Proceedings of the National Academy of Sciences of the United States of America 93 (20): 10548–55. (October 1996). Bibcode: 1996PNAS...9310548V. doi:10.1073/pnas.93.20.10548. PMC 38190. PMID 8855215.
“Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure”. Proceedings of the National Academy of Sciences of the United States of America 105 (26): 8872–7. (July 2008). Bibcode: 2008PNAS..105.8872R. doi:10.1073/pnas.0802336105. PMC 2440727. PMID 18583476.
“Heterogeneity of chromatin subunits in vitro and location of histone H1”. Nucleic Acids Research 3 (2): 477–92. (February 1976). doi:10.1093/nar/3.2.477. PMC 342917. PMID 1257057.
“Removal of histone H1 exposes a fifty base pair DNA segment between nucleosomes”. Biochemistry 15 (15): 3307–14. (July 1976). doi:10.1021/bi00660a022. PMID 952859.
“The structure of histone H1 and its location in chromatin”. Nature 288 (5792): 675–9. (December 1980). Bibcode: 1980Natur.288..675A. doi:10.1038/288675a0. PMID 7453800.
“Footprinting of linker histones H5 and H1 on the nucleosome”. The EMBO Journal 7 (12): 3685–91. (December 1988). doi:10.1002/j.1460-2075.1988.tb03250.x. PMC 454941. PMID 3208745.
“Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin”. Proceedings of the National Academy of Sciences of the United States of America 95 (24): 14173–8. (November 1998). Bibcode: 1998PNAS...9514173B. doi:10.1073/pnas.95.24.14173. PMC 24346. PMID 9826673.
“The maternal histone H1 variant, H1M (B4 protein), is the predominant H1 histone in Xenopus pregastrula embryos”. Developmental Biology 161 (2): 425–39. (February 1994). doi:10.1006/dbio.1994.1042. PMID 8313993.
“Differential effect of H1 variant overexpression on cell cycle progression and gene expression”. Nucleic Acids Research 24 (3): 486–93. (February 1996). doi:10.1093/nar/24.3.486. PMC 145659. PMID 8602362.
“Effects of H1 histone variant overexpression on chromatin structure”. The Journal of Biological Chemistry 274 (53): 37950–6. (December 1999). doi:10.1074/jbc.274.53.37950. PMID 10608862.
“Histone H1 is essential for mitotic chromosome architecture and segregation in Xenopus laevis egg extracts”. The Journal of Cell Biology 169 (6): 859–69. (June 2005). doi:10.1083/jcb.200503031. PMC 2171634. PMID 15967810.
“Functional comparison of H1 histones in Xenopus reveals isoform-specific regulation by Cdk1 and RanGTP”. Current Biology 20 (11): 1048–52. (June 2010). doi:10.1016/j.cub.2010.04.025. PMC 2902237. PMID 20471264.
“Linker histones are not essential and affect chromatin condensation in vivo”. Cell 82 (1): 47–56. (July 1995). doi:10.1016/0092-8674(95)90051-9. PMID 7606784.
“A single histone H1 isoform (H1.1) is essential for chromatin silencing and germline development in Caenorhabditis elegans”. Development 128 (7): 1069–80. (April 2001). PMID 11245572.
“Linker histone H1 is essential for Drosophila development, the establishment of pericentric heterochromatin, and a normal polytene chromosome structure”. Genes & Development 23 (4): 452–65. (February 2009). doi:10.1101/gad.1749309. PMC 2648648. PMID 19196654.
“Dynamic binding of histone H1 to chromatin in living cells”. Nature 408 (6814): 877–81. (December 2000). Bibcode: 2000Natur.408..877M. doi:10.1038/35048610. PMID 11130729.
“Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins”. The Journal of Cell Biology 168 (1): 41–54. (January 2005). doi:10.1083/jcb.200407182. PMC 2171683. PMID 15623580.
“The dynamics of histone H1 function in chromatin”. Molecular Cell 17 (5): 617–20. (March 2005). doi:10.1016/j.molcel.2005.02.019. PMID 15749012.
“Histone H1 compacts DNA under force and during chromatin assembly”. Molecular Biology of the Cell 23 (24): 4864–71. (December 2012). doi:10.1091/mbc.E12-07-0518. PMC 3521692. PMID 23097493.
Cimini, Daniela, ed (September 2010). “Xenopus egg extracts increase dynamics of histone H1 on sperm chromatin”. PLOS One 5 (9): e13111. Bibcode: 2010PLoSO...513111F. doi:10.1371/journal.pone.0013111. PMC 2947519. PMID 20927327.
“Somatic linker histones cause loss of mesodermal competence in Xenopus”. Nature 389 (6649): 395–9. (September 1997). Bibcode: 1997Natur.389..395S. doi:10.1038/38755. PMID 9311783.
“Histone H1 variants differentially inhibit DNA replication through an affinity for chromatin mediated by their carboxyl-terminal domains”. Gene 292 (1–2): 173–81. (June 2002). doi:10.1016/S0378-1119(02)00675-3. PMID 12119111.
“Histone H1 diversity: bridging regulatory signals to linker histone function”. Gene 271 (1): 1–12. (June 2001). doi:10.1016/S0378-1119(01)00495-4. PMID 11410360.
“Cracking the enigmatic linker histone code”. Journal of Biochemistry 143 (3): 287–93. (March 2008). doi:10.1093/jb/mvn013. PMID 18234717.
“Histone H1 and its isoforms: contribution to chromatin structure and function”. Gene 431 (1–2): 1–12. (February 2009). doi:10.1016/j.gene.2008.11.003. PMID 19059319.
“H1 histones: current perspectives and challenges”. Nucleic Acids Research 41 (21): 9593–609. (November 2013). doi:10.1093/nar/gkt700. PMC 3834806. PMID 23945933.

ncbi.nlm.nih.gov

“Solenoidal model for superstructure in chromatin”. Proceedings of the National Academy of Sciences of the United States of America 73 (6): 1897–901. (June 1976). Bibcode: 1976PNAS...73.1897F. doi:10.1073/pnas.73.6.1897. PMC 430414. PMID 1064861.
“Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin”. The Journal of Cell Biology 83 (2 Pt 1): 403–27. (November 1979). doi:10.1083/jcb.83.2.403. PMC 2111545. PMID 387806.
“What determines the folding of the chromatin fiber?”. Proceedings of the National Academy of Sciences of the United States of America 93 (20): 10548–55. (October 1996). Bibcode: 1996PNAS...9310548V. doi:10.1073/pnas.93.20.10548. PMC 38190. PMID 8855215.
“Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure”. Proceedings of the National Academy of Sciences of the United States of America 105 (26): 8872–7. (July 2008). Bibcode: 2008PNAS..105.8872R. doi:10.1073/pnas.0802336105. PMC 2440727. PMID 18583476.
“Heterogeneity of chromatin subunits in vitro and location of histone H1”. Nucleic Acids Research 3 (2): 477–92. (February 1976). doi:10.1093/nar/3.2.477. PMC 342917. PMID 1257057.
“Footprinting of linker histones H5 and H1 on the nucleosome”. The EMBO Journal 7 (12): 3685–91. (December 1988). doi:10.1002/j.1460-2075.1988.tb03250.x. PMC 454941. PMID 3208745.
“Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin”. Proceedings of the National Academy of Sciences of the United States of America 95 (24): 14173–8. (November 1998). Bibcode: 1998PNAS...9514173B. doi:10.1073/pnas.95.24.14173. PMC 24346. PMID 9826673.
“Differential effect of H1 variant overexpression on cell cycle progression and gene expression”. Nucleic Acids Research 24 (3): 486–93. (February 1996). doi:10.1093/nar/24.3.486. PMC 145659. PMID 8602362.
“Histone H1 is essential for mitotic chromosome architecture and segregation in Xenopus laevis egg extracts”. The Journal of Cell Biology 169 (6): 859–69. (June 2005). doi:10.1083/jcb.200503031. PMC 2171634. PMID 15967810.
“Functional comparison of H1 histones in Xenopus reveals isoform-specific regulation by Cdk1 and RanGTP”. Current Biology 20 (11): 1048–52. (June 2010). doi:10.1016/j.cub.2010.04.025. PMC 2902237. PMID 20471264.
“Linker histone H1 is essential for Drosophila development, the establishment of pericentric heterochromatin, and a normal polytene chromosome structure”. Genes & Development 23 (4): 452–65. (February 2009). doi:10.1101/gad.1749309. PMC 2648648. PMID 19196654.
“Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins”. The Journal of Cell Biology 168 (1): 41–54. (January 2005). doi:10.1083/jcb.200407182. PMC 2171683. PMID 15623580.
“Histone H1 compacts DNA under force and during chromatin assembly”. Molecular Biology of the Cell 23 (24): 4864–71. (December 2012). doi:10.1091/mbc.E12-07-0518. PMC 3521692. PMID 23097493.
Cimini, Daniela, ed (September 2010). “Xenopus egg extracts increase dynamics of histone H1 on sperm chromatin”. PLOS One 5 (9): e13111. Bibcode: 2010PLoSO...513111F. doi:10.1371/journal.pone.0013111. PMC 2947519. PMID 20927327.
“H1 histones: current perspectives and challenges”. Nucleic Acids Research 41 (21): 9593–609. (November 2013). doi:10.1093/nar/gkt700. PMC 3834806. PMID 23945933.