ヒストンアセチルトランスフェラーゼ (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "ヒストンアセチルトランスフェラーゼ" in Japanese language version.

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archive.org

Voet, Donald; Voet, Judith G (2004). Biochemistry (3rd ed.). Hoboken, N.J.: John Wiley & Sons. ISBN 978-0-471-19350-0

doi.org

Zeng, Lei; Zhou, Ming Ming (2002-02-20). “Bromodomain: an acetyl-lysine binding domain”. FEBS letters 513 (1): 124–128. doi:10.1016/s0014-5793(01)03309-9. ISSN 0014-5793. PMID 11911891.
“Histone acetyltransferases”. Annual Review of Biochemistry 70: 81–120. (2001). doi:10.1146/annurev.biochem.70.1.81. PMID 11395403.
“Histone acetyltransferase complexes: one size doesn't fit all”. Nature Reviews. Molecular Cell Biology 8 (4): 284–95. (April 2007). doi:10.1038/nrm2145. PMID 17380162.
“Histone acetylation in chromatin structure and transcription”. Nature 389 (6649): 349–52. (September 1997). Bibcode: 1997Natur.389..349G. doi:10.1038/38664. PMID 9311776.
“Expression homeostasis during DNA replication”. Science 351 (6277): 1087–90. (March 2016). Bibcode: 2016Sci...351.1087V. doi:10.1126/science.aad1162. PMID 26941319.
“Structure and ligand of a histone acetyltransferase bromodomain”. Nature 399 (6735): 491–6. (June 1999). Bibcode: 1999Natur.399..491D. doi:10.1038/20974. PMID 10365964.
“Acetylation of histones and transcription-related factors”. Microbiology and Molecular Biology Reviews 64 (2): 435–59. (June 2000). doi:10.1128/MMBR.64.2.435-459.2000. PMC 98999. PMID 10839822.
“Structure of histone acetyltransferases”. Journal of Molecular Biology 311 (3): 433–44. (August 2001). doi:10.1006/jmbi.2001.4859. PMID 11492997.
“Histone acetyltransferases: Rising ancient counterparts to protein kinases”. Biopolymers 99 (2): 98–111. (February 2013). doi:10.1002/bip.22128. PMC 4017165. PMID 23175385.
“Histone modifying enzymes: structures, mechanisms, and specificities”. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1789 (1): 58–68. (January 2009). doi:10.1016/j.bbagrm.2008.07.009. PMC 4059211. PMID 18722564.
“Mammalian histone acetyltransferases and their complexes”. Cellular and Molecular Life Sciences 58 (5–6): 683–92. (May 2001). doi:10.1007/PL00000892. PMID 11437230.
“Circadian regulator CLOCK is a histone acetyltransferase”. Cell 125 (3): 497–508. (May 2006). doi:10.1016/j.cell.2006.03.033. PMID 16678094.
“A decade of histone acetylation: marking eukaryotic chromosomes with specific codes”. Journal of Biochemistry 138 (6): 647–62. (December 2005). doi:10.1093/jb/mvi184. PMID 16428293.
“Histone acetyltransferases: function, structure, and catalysis”. Current Opinion in Genetics & Development 11 (2): 155–61. (April 2001). doi:10.1016/S0959-437X(00)00173-8. PMID 11250138.
“Lessons from genome-wide studies: an integrated definition of the coactivator function of histone acetyl transferases”. Epigenetics & Chromatin 3 (1): 18. (October 2010). doi:10.1186/1756-8935-3-18. PMC 2972259. PMID 20961410.
“The diverse functions of histone acetyltransferase complexes”. Trends in Genetics 19 (6): 321–9. (June 2003). doi:10.1016/S0168-9525(03)00115-X. PMID 12801725.
“Histone acetyltransferase proteins contribute to transcriptional processes at multiple levels”. Proteins in Eukaryotic Transcription. Advances in Protein Chemistry. 67. (2004). pp. 181–99. doi:10.1016/S0065-3233(04)67007-0. ISBN 9780120342679. PMID 14969728
“Tuning acetylated chromatin with HAT inhibitors: a novel tool for therapy”. Epigenetics 5 (2): 105–11. (February 2010). doi:10.4161/epi.5.2.10942. PMID 20160510.
“Catalytic mechanism of a MYST family histone acetyltransferase”. Biochemistry 46 (3): 623–9. (January 2007). doi:10.1021/bi602513x. PMC 2752042. PMID 17223684.
“Catalysis and substrate selection by histone/protein lysine acetyltransferases”. Current Opinion in Structural Biology 18 (6): 682–9. (December 2008). doi:10.1016/j.sbi.2008.11.004. PMC 2723715. PMID 19056256.
“Lysine acetylation and the bromodomain: a new partnership for signaling”. BioEssays 26 (10): 1076–87. (October 2004). doi:10.1002/bies.20104. PMID 15382140.
“Acetylation and deacetylation of non-histone proteins”. Gene 363: 15–23. (December 2005). doi:10.1016/j.gene.2005.09.010. PMID 16289629.
“A novel acetylation cycle of transcription co-activator Yes-associated protein that is downstream of Hippo pathway is triggered in response to SN2 alkylating agents”. The Journal of Biological Chemistry 287 (26): 22089–98. (June 2012). doi:10.1074/jbc.M111.334714. PMC 3381167. PMID 22544757.
“The structural basis of protein acetylation by the p300/CBP transcriptional coactivator”. Nature 451 (7180): 846–50. (February 2008). Bibcode: 2008Natur.451..846L. doi:10.1038/nature06546. PMID 18273021.
“Autoacetylation of the histone acetyltransferase Rtt109”. The Journal of Biological Chemistry 286 (28): 24694–701. (July 2011). doi:10.1074/jbc.M111.251579. PMC 3137045. PMID 21606491.
“Epigenetic modifications in double-strand break DNA damage signaling and repair”. Clinical Cancer Research 16 (18): 4543–52. (September 2010). doi:10.1158/1078-0432.CCR-10-0513. PMC 2940951. PMID 20823147.
“Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice”. Proc. Natl. Acad. Sci. U.S.A. 108 (30): 12325–30. (July 2011). Bibcode: 2011PNAS..10812325K. doi:10.1073/pnas.1102789108. PMC 3145730. PMID 21746928.
“LANP mediates neuritic pathology in Spinocerebellar ataxia type 1”. Neurobiol. Dis. 48 (3): 526–32. (December 2012). doi:10.1016/j.nbd.2012.07.024. PMC 3987943. PMID 22884877.
“Small molecule inhibitors of histone acetyltransferases as epigenetic tools and drug candidates”. Archiv der Pharmazie 345 (1): 7–21. (January 2012). doi:10.1002/ardp.201100209. PMID 22234972.
“Garcinol, a histone acetyltransferase inhibitor, radiosensitizes cancer cells by inhibiting non-homologous end joining”. International Journal of Radiation Oncology, Biology, Physics 84 (3): 815–21. (November 2012). doi:10.1016/j.ijrobp.2012.01.017. PMID 22417805.

harvard.edu

ui.adsabs.harvard.edu

“Histone acetylation in chromatin structure and transcription”. Nature 389 (6649): 349–52. (September 1997). Bibcode: 1997Natur.389..349G. doi:10.1038/38664. PMID 9311776.
“Expression homeostasis during DNA replication”. Science 351 (6277): 1087–90. (March 2016). Bibcode: 2016Sci...351.1087V. doi:10.1126/science.aad1162. PMID 26941319.
“Structure and ligand of a histone acetyltransferase bromodomain”. Nature 399 (6735): 491–6. (June 1999). Bibcode: 1999Natur.399..491D. doi:10.1038/20974. PMID 10365964.
“The structural basis of protein acetylation by the p300/CBP transcriptional coactivator”. Nature 451 (7180): 846–50. (February 2008). Bibcode: 2008Natur.451..846L. doi:10.1038/nature06546. PMID 18273021.
“Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice”. Proc. Natl. Acad. Sci. U.S.A. 108 (30): 12325–30. (July 2011). Bibcode: 2011PNAS..10812325K. doi:10.1073/pnas.1102789108. PMC 3145730. PMID 21746928.

nih.gov

pubmed.ncbi.nlm.nih.gov

Zeng, Lei; Zhou, Ming Ming (2002-02-20). “Bromodomain: an acetyl-lysine binding domain”. FEBS letters 513 (1): 124–128. doi:10.1016/s0014-5793(01)03309-9. ISSN 0014-5793. PMID 11911891.
“Histone acetyltransferases”. Annual Review of Biochemistry 70: 81–120. (2001). doi:10.1146/annurev.biochem.70.1.81. PMID 11395403.
“Histone acetyltransferase complexes: one size doesn't fit all”. Nature Reviews. Molecular Cell Biology 8 (4): 284–95. (April 2007). doi:10.1038/nrm2145. PMID 17380162.
“Histone acetylation in chromatin structure and transcription”. Nature 389 (6649): 349–52. (September 1997). Bibcode: 1997Natur.389..349G. doi:10.1038/38664. PMID 9311776.
“Expression homeostasis during DNA replication”. Science 351 (6277): 1087–90. (March 2016). Bibcode: 2016Sci...351.1087V. doi:10.1126/science.aad1162. PMID 26941319.
“Structure and ligand of a histone acetyltransferase bromodomain”. Nature 399 (6735): 491–6. (June 1999). Bibcode: 1999Natur.399..491D. doi:10.1038/20974. PMID 10365964.
“Acetylation of histones and transcription-related factors”. Microbiology and Molecular Biology Reviews 64 (2): 435–59. (June 2000). doi:10.1128/MMBR.64.2.435-459.2000. PMC 98999. PMID 10839822.
“Structure of histone acetyltransferases”. Journal of Molecular Biology 311 (3): 433–44. (August 2001). doi:10.1006/jmbi.2001.4859. PMID 11492997.
“Histone acetyltransferases: Rising ancient counterparts to protein kinases”. Biopolymers 99 (2): 98–111. (February 2013). doi:10.1002/bip.22128. PMC 4017165. PMID 23175385.
“Histone modifying enzymes: structures, mechanisms, and specificities”. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1789 (1): 58–68. (January 2009). doi:10.1016/j.bbagrm.2008.07.009. PMC 4059211. PMID 18722564.
“Mammalian histone acetyltransferases and their complexes”. Cellular and Molecular Life Sciences 58 (5–6): 683–92. (May 2001). doi:10.1007/PL00000892. PMID 11437230.
“Circadian regulator CLOCK is a histone acetyltransferase”. Cell 125 (3): 497–508. (May 2006). doi:10.1016/j.cell.2006.03.033. PMID 16678094.
“A decade of histone acetylation: marking eukaryotic chromosomes with specific codes”. Journal of Biochemistry 138 (6): 647–62. (December 2005). doi:10.1093/jb/mvi184. PMID 16428293.
“Histone acetyltransferases: function, structure, and catalysis”. Current Opinion in Genetics & Development 11 (2): 155–61. (April 2001). doi:10.1016/S0959-437X(00)00173-8. PMID 11250138.
“Lessons from genome-wide studies: an integrated definition of the coactivator function of histone acetyl transferases”. Epigenetics & Chromatin 3 (1): 18. (October 2010). doi:10.1186/1756-8935-3-18. PMC 2972259. PMID 20961410.
“The diverse functions of histone acetyltransferase complexes”. Trends in Genetics 19 (6): 321–9. (June 2003). doi:10.1016/S0168-9525(03)00115-X. PMID 12801725.
“Histone acetyltransferase proteins contribute to transcriptional processes at multiple levels”. Proteins in Eukaryotic Transcription. Advances in Protein Chemistry. 67. (2004). pp. 181–99. doi:10.1016/S0065-3233(04)67007-0. ISBN 9780120342679. PMID 14969728
“Tuning acetylated chromatin with HAT inhibitors: a novel tool for therapy”. Epigenetics 5 (2): 105–11. (February 2010). doi:10.4161/epi.5.2.10942. PMID 20160510.
“Catalytic mechanism of a MYST family histone acetyltransferase”. Biochemistry 46 (3): 623–9. (January 2007). doi:10.1021/bi602513x. PMC 2752042. PMID 17223684.
“Catalysis and substrate selection by histone/protein lysine acetyltransferases”. Current Opinion in Structural Biology 18 (6): 682–9. (December 2008). doi:10.1016/j.sbi.2008.11.004. PMC 2723715. PMID 19056256.
“Lysine acetylation and the bromodomain: a new partnership for signaling”. BioEssays 26 (10): 1076–87. (October 2004). doi:10.1002/bies.20104. PMID 15382140.
“Acetylation and deacetylation of non-histone proteins”. Gene 363: 15–23. (December 2005). doi:10.1016/j.gene.2005.09.010. PMID 16289629.
“A novel acetylation cycle of transcription co-activator Yes-associated protein that is downstream of Hippo pathway is triggered in response to SN2 alkylating agents”. The Journal of Biological Chemistry 287 (26): 22089–98. (June 2012). doi:10.1074/jbc.M111.334714. PMC 3381167. PMID 22544757.
“The structural basis of protein acetylation by the p300/CBP transcriptional coactivator”. Nature 451 (7180): 846–50. (February 2008). Bibcode: 2008Natur.451..846L. doi:10.1038/nature06546. PMID 18273021.
“Autoacetylation of the histone acetyltransferase Rtt109”. The Journal of Biological Chemistry 286 (28): 24694–701. (July 2011). doi:10.1074/jbc.M111.251579. PMC 3137045. PMID 21606491.
“Epigenetic modifications in double-strand break DNA damage signaling and repair”. Clinical Cancer Research 16 (18): 4543–52. (September 2010). doi:10.1158/1078-0432.CCR-10-0513. PMC 2940951. PMID 20823147.
“Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice”. Proc. Natl. Acad. Sci. U.S.A. 108 (30): 12325–30. (July 2011). Bibcode: 2011PNAS..10812325K. doi:10.1073/pnas.1102789108. PMC 3145730. PMID 21746928.
“LANP mediates neuritic pathology in Spinocerebellar ataxia type 1”. Neurobiol. Dis. 48 (3): 526–32. (December 2012). doi:10.1016/j.nbd.2012.07.024. PMC 3987943. PMID 22884877.
“Small molecule inhibitors of histone acetyltransferases as epigenetic tools and drug candidates”. Archiv der Pharmazie 345 (1): 7–21. (January 2012). doi:10.1002/ardp.201100209. PMID 22234972.
“Garcinol, a histone acetyltransferase inhibitor, radiosensitizes cancer cells by inhibiting non-homologous end joining”. International Journal of Radiation Oncology, Biology, Physics 84 (3): 815–21. (November 2012). doi:10.1016/j.ijrobp.2012.01.017. PMID 22417805.

ncbi.nlm.nih.gov

worldcat.org

search.worldcat.org

Zeng, Lei; Zhou, Ming Ming (2002-02-20). “Bromodomain: an acetyl-lysine binding domain”. FEBS letters 513 (1): 124–128. doi:10.1016/s0014-5793(01)03309-9. ISSN 0014-5793. PMID 11911891.