ハンチンチン (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "ハンチンチン" in Japanese language version.

refsWebsite

Global rank Japanese rank

54nih.gov

4^th place

24^th place

35doi.org

2^nd place

6^th place

5harvard.edu

18^th place

107^th place

2ensembl.org

1,626^th place

2,625^th place

2wikipedia.org

low place

1umich.edu

459^th place

1,980^th place

1handle.net

102^nd place

78^th place

1neurology.org

9,919^th place

low place

doi.org

The Huntington's Disease Collaborative Research Group (Mar 1993). “A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group”. Cell 72 (6): 971–83. doi:10.1016/0092-8674(93)90585-E. hdl:2027.42/30901. PMID 8458085.
“Huntingtin is critical both pre- and postsynaptically for long-term learning-related synaptic plasticity in Aplysia”. PLOS ONE 9 (7): e103004. (July 23, 2014). Bibcode: 2014PLoSO...9j3004C. doi:10.1371/journal.pone.0103004. PMC 4108396. PMID 25054562.
“Analysis of a very large trinucleotide repeat in a patient with juvenile Huntington's disease”. Neurology 52 (2): 392–4. (Jan 1999). doi:10.1212/wnl.52.2.392. PMID 9932964.
“Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes”. Cell 81 (5): 811–23. (Jun 1995). doi:10.1016/0092-8674(95)90542-1. PMID 7774020.
“Traffic signaling: new functions of huntingtin and axonal transport in neurological disease”. Current Opinion in Neurobiology 63: 122–130. (August 2020). doi:10.1016/j.conb.2020.04.001. PMID 32408142.
“Normal huntingtin function: an alternative approach to Huntington's disease”. Nature Reviews. Neuroscience 6 (12): 919–30. (December 2005). doi:10.1038/nrn1806. PMID 16288298.
“Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease”. Science 293 (5529): 493–8. (July 2001). doi:10.1126/science.1059581. PMID 11408619.
“Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease”. Journal of Cell Science 115 (Pt 5): 941–8. (March 2002). doi:10.1242/jcs.115.5.941. PMID 11870213.
“Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons”. Neuron 14 (5): 1075–81. (May 1995). doi:10.1016/0896-6273(95)90346-1. PMID 7748555.
“Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways”. Experimental Neurology 152 (1): 34–40. (July 1998). doi:10.1006/exnr.1998.6832. PMID 9682010.
“The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis”. Human Molecular Genetics 10 (17): 1807–17. (August 2001). doi:10.1093/hmg/10.17.1807. PMID 11532990.
“Huntingtin Is Required for Epithelial Polarity through RAB11A-Mediated Apical Trafficking of PAR3-aPKC”. PLOS Biology 13 (5): e1002142. (May 2015). doi:10.1371/journal.pbio.1002142. PMC 4420272. PMID 25942483.
“The hunt for huntingtin function: interaction partners tell many different stories”. Trends in Biochemical Sciences 28 (8): 425–33. (Aug 2003). doi:10.1016/S0968-0004(03)00168-3. PMID 12932731.
“A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease”. Molecular Cell 15 (6): 853–65. (Sep 2004). doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
“HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system”. Human Molecular Genetics 6 (3): 487–95. (Mar 1997). doi:10.1093/hmg/6.3.487. PMID 9147654.
“SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes”. The Journal of Biological Chemistry 272 (13): 8121–4. (Mar 1997). doi:10.1074/jbc.272.13.8121. PMID 9079622.
“The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription”. Proceedings of the National Academy of Sciences of the United States of America 97 (12): 6763–8. (Jun 2000). Bibcode: 2000PNAS...97.6763S. doi:10.1073/pnas.100110097. PMC 18731. PMID 10823891.
“PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains”. Human Molecular Genetics 11 (21): 2547–58. (Oct 2002). doi:10.1093/hmg/11.21.2547. PMID 12354780.
“SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates”. Molecular Cell 2 (4): 427–36. (Oct 1998). doi:10.1016/S1097-2765(00)80142-2. PMID 9809064.
“Interaction of Huntington disease protein with transcriptional activator Sp1”. Molecular and Cellular Biology 22 (5): 1277–87. (Mar 2002). doi:10.1128/MCB.22.5.1277-1287.2002. PMC 134707. PMID 11839795.
“Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme”. The Journal of Biological Chemistry 271 (32): 19385–94. (Aug 1996). doi:10.1074/jbc.271.32.19385. PMID 8702625.
“Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin”. The Journal of Biological Chemistry 275 (25): 19035–40. (Jun 2000). doi:10.1074/jbc.C000180200. PMID 10801775.
“FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis”. Current Biology 10 (24): 1603–6. (2000). doi:10.1016/S0960-9822(00)00864-2. PMID 11137014.
“Huntingtin interacts with a family of WW domain proteins”. Human Molecular Genetics 7 (9): 1463–74. (Sep 1998). doi:10.1093/hmg/7.9.1463. PMID 9700202.
“Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease”. Proceedings of the National Academy of Sciences of the United States of America 100 (5): 2712–7. (Mar 2003). Bibcode: 2003PNAS..100.2712H. doi:10.1073/pnas.0437967100. PMC 151406. PMID 12604778.
“HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis”. Human Molecular Genetics 11 (23): 2815–28. (Nov 2002). doi:10.1093/hmg/11.23.2815. PMID 12393793.
“Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications”. Oxid Med Cell Longev 2017: 2525967. (2017). doi:10.1155/2017/2525967. PMC 5529664. PMID 28785371.
Maiuri, Tamara; Mocle, Andrew J.; Hung, Claudia L.; Xia, Jianrun; van Roon-Mom, Willeke M. C.; Truant, Ray (25 December 2016). “Huntingtin is a scaffolding protein in the ATM oxidative DNA damage response complex”. Human Molecular Genetics 26 (2): 395–406. doi:10.1093/hmg/ddw395. PMID 28017939.
“Role of oxidative DNA damage in mitochondrial dysfunction and Huntington's disease pathogenesis”. Free Radic. Biol. Med. 62: 102–10. (September 2013). doi:10.1016/j.freeradbiomed.2013.04.017. PMC 3722255. PMID 23602907.
“Huntington's disease”. Lancet 369 (9557): 218–28. (Jan 2007). doi:10.1016/S0140-6736(07)60111-1. PMID 17240289.
“Contribution of DNA sequence and CAG size to mutation frequencies of intermediate alleles for Huntington disease: evidence from single sperm analyses”. Human Molecular Genetics 6 (2): 301–9. (Feb 1997). doi:10.1093/hmg/6.2.301. PMID 9063751.
“Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation”. Cell 90 (3): 537–48. (Aug 1997). doi:10.1016/S0092-8674(00)80513-9. PMID 9267033.
“Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death”. Nature 431 (7010): 805–10. (Oct 2004). Bibcode: 2004Natur.431..805A. doi:10.1038/nature02998. PMID 15483602.
“Delayed Emergence of Subdiffraction-Sized Mutant Huntingtin Fibrils Following Inclusion Body Formation”. Q Rev Biophys 49: e2. (2016). doi:10.1017/S0033583515000219. PMC 4785097. PMID 26350150.
“Neurodegenerative disease: neuron protection agency”. Nature 431 (7010): 747–8. (Oct 2004). Bibcode: 2004Natur.431..747O. doi:10.1038/431747a. PMID 15483586.

ensembl.org

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000197386 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000029104 - Ensembl, May 2017

handle.net

hdl.handle.net

The Huntington's Disease Collaborative Research Group (Mar 1993). “A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group”. Cell 72 (6): 971–83. doi:10.1016/0092-8674(93)90585-E. hdl:2027.42/30901. PMID 8458085.

harvard.edu

ui.adsabs.harvard.edu

“Huntingtin is critical both pre- and postsynaptically for long-term learning-related synaptic plasticity in Aplysia”. PLOS ONE 9 (7): e103004. (July 23, 2014). Bibcode: 2014PLoSO...9j3004C. doi:10.1371/journal.pone.0103004. PMC 4108396. PMID 25054562.
“The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription”. Proceedings of the National Academy of Sciences of the United States of America 97 (12): 6763–8. (Jun 2000). Bibcode: 2000PNAS...97.6763S. doi:10.1073/pnas.100110097. PMC 18731. PMID 10823891.
“Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease”. Proceedings of the National Academy of Sciences of the United States of America 100 (5): 2712–7. (Mar 2003). Bibcode: 2003PNAS..100.2712H. doi:10.1073/pnas.0437967100. PMC 151406. PMID 12604778.
“Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death”. Nature 431 (7010): 805–10. (Oct 2004). Bibcode: 2004Natur.431..805A. doi:10.1038/nature02998. PMID 15483602.
“Neurodegenerative disease: neuron protection agency”. Nature 431 (7010): 747–8. (Oct 2004). Bibcode: 2004Natur.431..747O. doi:10.1038/431747a. PMID 15483586.

neurology.org

“Analysis of a very large trinucleotide repeat in a patient with juvenile Huntington's disease”. Neurology 52 (2): 392–4. (Jan 1999). doi:10.1212/wnl.52.2.392. PMID 9932964.

nih.gov

pubmed.ncbi.nlm.nih.gov

The Huntington's Disease Collaborative Research Group (Mar 1993). “A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group”. Cell 72 (6): 971–83. doi:10.1016/0092-8674(93)90585-E. hdl:2027.42/30901. PMID 8458085.
“Huntingtin is critical both pre- and postsynaptically for long-term learning-related synaptic plasticity in Aplysia”. PLOS ONE 9 (7): e103004. (July 23, 2014). Bibcode: 2014PLoSO...9j3004C. doi:10.1371/journal.pone.0103004. PMC 4108396. PMID 25054562.
“Analysis of a very large trinucleotide repeat in a patient with juvenile Huntington's disease”. Neurology 52 (2): 392–4. (Jan 1999). doi:10.1212/wnl.52.2.392. PMID 9932964.
“Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes”. Cell 81 (5): 811–23. (Jun 1995). doi:10.1016/0092-8674(95)90542-1. PMID 7774020.
“Traffic signaling: new functions of huntingtin and axonal transport in neurological disease”. Current Opinion in Neurobiology 63: 122–130. (August 2020). doi:10.1016/j.conb.2020.04.001. PMID 32408142.
“Normal huntingtin function: an alternative approach to Huntington's disease”. Nature Reviews. Neuroscience 6 (12): 919–30. (December 2005). doi:10.1038/nrn1806. PMID 16288298.
“Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease”. Science 293 (5529): 493–8. (July 2001). doi:10.1126/science.1059581. PMID 11408619.
“Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease”. Journal of Cell Science 115 (Pt 5): 941–8. (March 2002). doi:10.1242/jcs.115.5.941. PMID 11870213.
“Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons”. Neuron 14 (5): 1075–81. (May 1995). doi:10.1016/0896-6273(95)90346-1. PMID 7748555.
“Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways”. Experimental Neurology 152 (1): 34–40. (July 1998). doi:10.1006/exnr.1998.6832. PMID 9682010.
“The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis”. Human Molecular Genetics 10 (17): 1807–17. (August 2001). doi:10.1093/hmg/10.17.1807. PMID 11532990.
“Huntingtin Is Required for Epithelial Polarity through RAB11A-Mediated Apical Trafficking of PAR3-aPKC”. PLOS Biology 13 (5): e1002142. (May 2015). doi:10.1371/journal.pbio.1002142. PMC 4420272. PMID 25942483.
“The hunt for huntingtin function: interaction partners tell many different stories”. Trends in Biochemical Sciences 28 (8): 425–33. (Aug 2003). doi:10.1016/S0968-0004(03)00168-3. PMID 12932731.
“A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease”. Molecular Cell 15 (6): 853–65. (Sep 2004). doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
“HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system”. Human Molecular Genetics 6 (3): 487–95. (Mar 1997). doi:10.1093/hmg/6.3.487. PMID 9147654.
“SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes”. The Journal of Biological Chemistry 272 (13): 8121–4. (Mar 1997). doi:10.1074/jbc.272.13.8121. PMID 9079622.
“The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription”. Proceedings of the National Academy of Sciences of the United States of America 97 (12): 6763–8. (Jun 2000). Bibcode: 2000PNAS...97.6763S. doi:10.1073/pnas.100110097. PMC 18731. PMID 10823891.
“PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains”. Human Molecular Genetics 11 (21): 2547–58. (Oct 2002). doi:10.1093/hmg/11.21.2547. PMID 12354780.
“SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates”. Molecular Cell 2 (4): 427–36. (Oct 1998). doi:10.1016/S1097-2765(00)80142-2. PMID 9809064.
“Interaction of Huntington disease protein with transcriptional activator Sp1”. Molecular and Cellular Biology 22 (5): 1277–87. (Mar 2002). doi:10.1128/MCB.22.5.1277-1287.2002. PMC 134707. PMID 11839795.
“Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme”. The Journal of Biological Chemistry 271 (32): 19385–94. (Aug 1996). doi:10.1074/jbc.271.32.19385. PMID 8702625.
“Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin”. The Journal of Biological Chemistry 275 (25): 19035–40. (Jun 2000). doi:10.1074/jbc.C000180200. PMID 10801775.
“FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis”. Current Biology 10 (24): 1603–6. (2000). doi:10.1016/S0960-9822(00)00864-2. PMID 11137014.
“Huntingtin interacts with a family of WW domain proteins”. Human Molecular Genetics 7 (9): 1463–74. (Sep 1998). doi:10.1093/hmg/7.9.1463. PMID 9700202.
“Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease”. Proceedings of the National Academy of Sciences of the United States of America 100 (5): 2712–7. (Mar 2003). Bibcode: 2003PNAS..100.2712H. doi:10.1073/pnas.0437967100. PMC 151406. PMID 12604778.
“HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis”. Human Molecular Genetics 11 (23): 2815–28. (Nov 2002). doi:10.1093/hmg/11.23.2815. PMID 12393793.
“Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications”. Oxid Med Cell Longev 2017: 2525967. (2017). doi:10.1155/2017/2525967. PMC 5529664. PMID 28785371.
Maiuri, Tamara; Mocle, Andrew J.; Hung, Claudia L.; Xia, Jianrun; van Roon-Mom, Willeke M. C.; Truant, Ray (25 December 2016). “Huntingtin is a scaffolding protein in the ATM oxidative DNA damage response complex”. Human Molecular Genetics 26 (2): 395–406. doi:10.1093/hmg/ddw395. PMID 28017939.
“Role of oxidative DNA damage in mitochondrial dysfunction and Huntington's disease pathogenesis”. Free Radic. Biol. Med. 62: 102–10. (September 2013). doi:10.1016/j.freeradbiomed.2013.04.017. PMC 3722255. PMID 23602907.
“Huntington's disease”. Lancet 369 (9557): 218–28. (Jan 2007). doi:10.1016/S0140-6736(07)60111-1. PMID 17240289.
“Contribution of DNA sequence and CAG size to mutation frequencies of intermediate alleles for Huntington disease: evidence from single sperm analyses”. Human Molecular Genetics 6 (2): 301–9. (Feb 1997). doi:10.1093/hmg/6.2.301. PMID 9063751.
“Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation”. Cell 90 (3): 537–48. (Aug 1997). doi:10.1016/S0092-8674(00)80513-9. PMID 9267033.
“Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death”. Nature 431 (7010): 805–10. (Oct 2004). Bibcode: 2004Natur.431..805A. doi:10.1038/nature02998. PMID 15483602.
“Delayed Emergence of Subdiffraction-Sized Mutant Huntingtin Fibrils Following Inclusion Body Formation”. Q Rev Biophys 49: e2. (2016). doi:10.1017/S0033583515000219. PMC 4785097. PMID 26350150.
“Neurodegenerative disease: neuron protection agency”. Nature 431 (7010): 747–8. (Oct 2004). Bibcode: 2004Natur.431..747O. doi:10.1038/431747a. PMID 15483586.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

ghr.nlm.nih.gov

“HTT gene”. 2023年3月11日閲覧。

umich.edu

deepblue.lib.umich.edu

The Huntington's Disease Collaborative Research Group (Mar 1993). “A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group”. Cell 72 (6): 971–83. doi:10.1016/0092-8674(93)90585-E. hdl:2027.42/30901. PMID 8458085.

wikipedia.org

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000197386 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000029104 - Ensembl, May 2017