References analysis of the Wikipedia article "SNAP25" in the Japanese version

doi.org (Global: 2^nd place; Japanese: 3^rd place)

“Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p)”. Mamm. Genome 7 (5): 400–1. (May 1996). doi:10.1007/s003359900120. PMID 8661740.

“Snares and Munc18 in synaptic vesicle fusion”. Nat Rev Neurosci 3 (8): 641–653. (2002). doi:10.1038/nrn898. PMID 12154365.

Georgiev, Danko D; James F . Glazebrook (2007). “Subneuronal processing of information by solitary waves and stochastic processes”. In Lyshevski, Sergey Edward. Nano and Molecular Electronics Handbook. Nano and Microengineering Series. CRC Press. pp. 17–1–17–41. doi:10.1201/9781420008142.ch17. ISBN 978-0-8493-8528-5

“Specificity and regulation of a synaptic vesicle docking complex”. Neuron 13 (2): 353–61. (1994). doi:10.1016/0896-6273(94)90352-2. PMID 8060616.

“Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking”. Science 263 (5150): 1146–9. (1994). Bibcode:1994Sci...263.1146C. doi:10.1126/science.8108733. PMID 8108733.

“SNAP-25”. Int. J. Biochem. Cell Biol. 30 (10): 1069–73. (October 1998). doi:10.1016/S1357-2725(98)00079-X. PMID 9785471.

Chapman, Edwin R. (2002-07). “Synaptotagmin: a Ca(2+) sensor that triggers exocytosis?”. Nature Reviews. Molecular Cell Biology 3 (7): 498–508. doi:10.1038/nrm855. ISSN 1471-0072. PMID 12094216.

“SNAP-25 modulation of calcium dynamics underlies differences in GABAergic and glutamatergic responsiveness to depolarization”. Neuron 41 (4): 599–610. (February 2004). doi:10.1016/S0896-6273(04)00077-7. PMID 14980208.

“Alternative splicing of SNAP-25 regulates secretion through nonconservative substitutions in the SNARE domain”. Mol. Biol. Cell 16 (12): 5675–85. (December 2005). doi:10.1091/mbc.E05-07-0595. PMC 1289412. PMID 16195346.

Bark, Christina (February 1995). “Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development”. Proceedings of the National Academy of Sciences 92 (5): 1510–1514. Bibcode:1995PNAS...92.1510B. doi:10.1073/pnas.92.5.1510. PMC 42549. PMID 7878010.

“Synaptosomal-associated protein 25 (SNAP-25) and attention deficit hyperactivity disorder (ADHD): evidence of linkage and association in the Irish population”. Mol. Psychiatry 7 (8): 913–7. (2002). doi:10.1038/sj.mp.4001092. hdl:2262/36350. PMID 12232787.

“Association study of a SNAP-25 microsatellite and attention deficit hyperactivity disorder”. Am. J. Med. Genet. 114 (3): 269–71. (April 2002). doi:10.1002/ajmg.10253. PMID 11920846.

“Genome-wide association scan for five major dimensions of personality”. Mol. Psychiatry 15 (6): 647–56. (October 2008). doi:10.1038/mp.2008.113. PMC 2874623. PMID 18957941.

“Botulinum toxin type A and other botulinum toxin serotypes: a comparative review of biochemical and pharmacological actions”. Eur. J. Neurol. 8 Suppl 5: 21–9. (November 2001). doi:10.1046/j.1468-1331.2001.00035.x. PMID 11851731.

“Three-dimensional structure of the complexin/SNARE complex”. Neuron 33 (3): 397–409. (January 2002). doi:10.1016/s0896-6273(02)00583-4. PMID 11832227.

“Action of complexin on SNARE complex”. J. Biol. Chem. 277 (44): 41652–6. (November 2002). doi:10.1074/jbc.M205044200. PMID 12200427.

“EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin and SNAP-25. A protein connection between exocytosis and endocytosis?”. J. Biol. Chem. 274 (26): 18446–54. (June 1999). doi:10.1074/jbc.274.26.18446. PMID 10373452.

“The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23”. Biochemistry 41 (50): 14906–15. (Dec 2002). doi:10.1021/bi026417u. PMID 12475239.

“Snapin: a SNARE-associated protein implicated in synaptic transmission”. Nat. Neurosci. 2 (2): 119–24. (February 1999). doi:10.1038/5673. PMID 10195194.

“A human protein-protein interaction network: a resource for annotating the proteome”. Cell 122 (6): 957–68. (September 2005). doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.

“Towards a proteome-scale map of the human protein-protein interaction network”. Nature 437 (7062): 1173–8. (October 2005). Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.

“A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic”. J. Biol. Chem. 270 (22): 13022–8. (June 1995). doi:10.1074/jbc.270.22.13022. PMID 7768895.

“Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues”. J. Biol. Chem. 271 (23): 13300–3. (June 1996). doi:10.1074/jbc.271.23.13300. PMID 8663154.

“Three novel proteins of the syntaxin/SNAP-25 family”. J. Biol. Chem. 273 (51): 34171–9. (Dec 1998). doi:10.1074/jbc.273.51.34171. PMID 9852078.

“A conformational switch in syntaxin during exocytosis: role of munc18”. EMBO J. 18 (16): 4372–82. (August 1999). doi:10.1093/emboj/18.16.4372. PMC 1171512. PMID 10449403.

“Complexins: cytosolic proteins that regulate SNAP receptor function”. Cell 83 (1): 111–9. (October 1995). doi:10.1016/0092-8674(95)90239-2. PMID 7553862.

“Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis”. J. Biol. Chem. 276 (44): 40824–33. (November 2001). doi:10.1074/jbc.M106141200. PMID 11524423.

“Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion”. Blood 93 (8): 2617–26. (April 1999). doi:10.1182/blood.V93.8.2617. PMID 10194441.

“The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes”. J. Biol. Chem. 275 (9): 6328–36. (March 2000). doi:10.1074/jbc.275.9.6328. PMID 10692432.

“Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis”. Neuron 34 (4): 599–611. (May 2002). doi:10.1016/s0896-6273(02)00671-2. PMID 12062043.

“Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes”. J. Neurosci. 17 (5): 1596–603. (March 1997). doi:10.1523/JNEUROSCI.17-05-01596.1997. PMC 6573372. PMID 9030619.

hdl.handle.net (Global: 66^th place; Japanese: 71^st place)

nih.gov (Global: 5^th place; Japanese: 11^th place)

pubmed.ncbi.nlm.nih.gov

“Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p)”. Mamm. Genome 7 (5): 400–1. (May 1996). doi:10.1007/s003359900120. PMID 8661740.

“Snares and Munc18 in synaptic vesicle fusion”. Nat Rev Neurosci 3 (8): 641–653. (2002). doi:10.1038/nrn898. PMID 12154365.

“SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils”. J. Biol. Chem. 269 (44): 27427–32. (1994). PMID 7961655.

“Specificity and regulation of a synaptic vesicle docking complex”. Neuron 13 (2): 353–61. (1994). doi:10.1016/0896-6273(94)90352-2. PMID 8060616.

“SNAP-25”. Int. J. Biochem. Cell Biol. 30 (10): 1069–73. (October 1998). doi:10.1016/S1357-2725(98)00079-X. PMID 9785471.

“Association study of a SNAP-25 microsatellite and attention deficit hyperactivity disorder”. Am. J. Med. Genet. 114 (3): 269–71. (April 2002). doi:10.1002/ajmg.10253. PMID 11920846.

“Genome-wide association scan for five major dimensions of personality”. Mol. Psychiatry 15 (6): 647–56. (October 2008). doi:10.1038/mp.2008.113. PMC 2874623. PMID 18957941.

“Three-dimensional structure of the complexin/SNARE complex”. Neuron 33 (3): 397–409. (January 2002). doi:10.1016/s0896-6273(02)00583-4. PMID 11832227.

“Action of complexin on SNARE complex”. J. Biol. Chem. 277 (44): 41652–6. (November 2002). doi:10.1074/jbc.M205044200. PMID 12200427.

“The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23”. Biochemistry 41 (50): 14906–15. (Dec 2002). doi:10.1021/bi026417u. PMID 12475239.

“Snapin: a SNARE-associated protein implicated in synaptic transmission”. Nat. Neurosci. 2 (2): 119–24. (February 1999). doi:10.1038/5673. PMID 10195194.

“Three novel proteins of the syntaxin/SNAP-25 family”. J. Biol. Chem. 273 (51): 34171–9. (Dec 1998). doi:10.1074/jbc.273.51.34171. PMID 9852078.

“A conformational switch in syntaxin during exocytosis: role of munc18”. EMBO J. 18 (16): 4372–82. (August 1999). doi:10.1093/emboj/18.16.4372. PMC 1171512. PMID 10449403.

“Complexins: cytosolic proteins that regulate SNAP receptor function”. Cell 83 (1): 111–9. (October 1995). doi:10.1016/0092-8674(95)90239-2. PMID 7553862.

“Membrane localization and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells”. J. Cell Sci. 113 (18): 3197–205. (September 2000). PMID 10954418.

“Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis”. J. Biol. Chem. 276 (44): 40824–33. (November 2001). doi:10.1074/jbc.M106141200. PMID 11524423.

“SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils”. J. Biol. Chem. 269 (44): 27427–32. (November 1994). PMID 7961655.

“Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis”. Neuron 34 (4): 599–611. (May 2002). doi:10.1016/s0896-6273(02)00671-2. PMID 12062043.

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SNAP25 (Japanese Wikipedia)

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SNAP25 (Japanese Wikipedia)

adsabs.harvard.edu (Global: 14th place; Japanese: 60th place)

ui.adsabs.harvard.edu

crcnetbase.com (Global: low place; Japanese: low place)

doi.org (Global: 2nd place; Japanese: 3rd place)

ensembl.org (Global: 630th place; Japanese: 1,132nd place)

may2017.archive.ensembl.org

hdl.handle.net (Global: 66th place; Japanese: 71st place)

marquette.edu (Global: 8,736th place; Japanese: low place)

epublications.marquette.edu

nih.gov (Global: 5th place; Japanese: 11th place)

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

worldcat.org (Global: 4th place; Japanese: 12th place)

search.worldcat.org

adsabs.harvard.edu (Global: 14^th place; Japanese: 60^th place)

doi.org (Global: 2^nd place; Japanese: 3^rd place)

ensembl.org (Global: 630^th place; Japanese: 1,132^nd place)

hdl.handle.net (Global: 66^th place; Japanese: 71^st place)

marquette.edu (Global: 8,736^th place; Japanese: low place)

nih.gov (Global: 5^th place; Japanese: 11^th place)

worldcat.org (Global: 4^th place; Japanese: 12^th place)