MAPK1 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "MAPK1" in Japanese language version.

refsWebsite

Global rank Japanese rank

65nih.gov

4^th place

24^th place

47doi.org

2^nd place

6^th place

2ensembl.org

1,626^th place

2,625^th place

2wikipedia.org

low place

2harvard.edu

18^th place

107^th place

1phosphosite.org

low place

1mousephenotype.org

low place

1jax.org

low place

1proteinatlas.org

low place

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs”. Biochem. Biophys. Res. Commun. 182 (3): 1416–22. (February 1992). doi:10.1016/0006-291X(92)91891-S. PMID 1540184.
“A conditional knockout resource for the genome-wide study of mouse gene function”. Nature 474 (7351): 337–42. (2011). doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
“Mouse library set to be knockout”. Nature 474 (7351): 262–3. (2011). doi:10.1038/474262a. PMID 21677718.
“A mouse for all reasons”. Cell 128 (1): 9–13. (2007). doi:10.1016/j.cell.2006.12.018. PMID 17218247.
“The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice”. Acta Ophthalmologica 88: 925–7. (2010). doi:10.1111/j.1755-3768.2010.4142.x.
“The mouse genetics toolkit: revealing function and mechanism”. Genome Biol. 12 (6): 224. (2011). doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
“Extracellular signal-regulated protein kinase 2 is required for efficient generation of B cells bearing antigen-specific immunoglobulin G”. Molecular and Cellular Biology 27 (4): 1236–46. (February 2007). doi:10.1128/MCB.01530-06. PMC 1800707. PMID 17145771.
“The influence of the MAPK pathway on T cell lineage commitment”. Immunity 7 (5): 609–18. (November 1997). doi:10.1016/s1074-7613(00)80382-9. PMID 9390685.
“Deletion of ERK2 mitogen-activated protein kinase identifies its key roles in cortical neurogenesis and cognitive function”. The Journal of Neuroscience 28 (27): 6983–95. (July 2008). doi:10.1523/JNEUROSCI.0679-08.2008. PMC 4364995. PMID 18596172.
“Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding”. Mol. Biol. Cell 13 (6): 2031–44. (June 2002). doi:10.1091/mbc.01-11-0561. PMC 117622. PMID 12058067.
“Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator”. J. Biol. Chem. 283 (14): 9031–9. (April 2008). doi:10.1074/jbc.M706487200. PMC 2431044. PMID 18245089.
“Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1”. J. Biol. Chem. 276 (19): 16491–500. (May 2001). doi:10.1074/jbc.M010966200. PMID 11278799.
“Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma”. Cancer Res. 68 (11): 4192–200. (June 2008). doi:10.1158/0008-5472.CAN-07-6157. PMID 18519678.
“Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain”. J. Biol. Chem. 276 (29): 27575–83. (July 2001). doi:10.1074/jbc.M100408200. PMID 11346645.
“Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway”. J. Biol. Chem. 274 (19): 13271–80. (May 1999). doi:10.1074/jbc.274.19.13271. PMID 10224087.
“Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs”. J. Biol. Chem. 278 (17): 14926–35. (April 2003). doi:10.1074/jbc.M300485200. PMID 12594221.
“Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction”. J. Cell Sci. 108 (11): 3599–609. (November 1995). doi:10.1242/jcs.108.11.3599. PMID 8586671.
“Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes”. Mol. Cell. Biol. 24 (3): 1081–95. (February 2004). doi:10.1128/mcb.24.3.1081-1095.2004. PMC 321437. PMID 14729955.
“Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras”. Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14329–33. (December 2000). Bibcode: 2000PNAS...9714329Z. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
“p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels”. Mol. Cell. Biol. 23 (9): 3079–90. (May 2003). doi:10.1128/mcb.23.9.3079-3090.2003. PMC 153192. PMID 12697810.
“Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1”. J. Biol. Chem. 277 (17): 14844–52. (April 2002). doi:10.1074/jbc.M107776200. PMID 11823456.
“Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein”. Mol. Cell. Biol. 20 (9): 3079–85. (May 2000). doi:10.1128/mcb.20.9.3079-3085.2000. PMC 85596. PMID 10757792.
“A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment”. J. Cell Biol. 152 (4): 765–76. (February 2001). doi:10.1083/jcb.152.4.765. PMC 2195784. PMID 11266467.
“Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking”. J. Biol. Chem. 276 (28): 26509–15. (July 2001). doi:10.1074/jbc.M102769200. PMID 11352917.
“Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2”. J. Biol. Chem. 276 (19): 16070–5. (May 2001). doi:10.1074/jbc.M100681200. PMID 11279118.
“MEKK1 binds raf-1 and the ERK2 cascade components”. J. Biol. Chem. 275 (51): 40120–7. (December 2000). doi:10.1074/jbc.M005926200. PMID 10969079.
“Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions”. EMBO J. 20 (3): 466–79. (February 2001). doi:10.1093/emboj/20.3.466. PMC 133461. PMID 11157753.
“Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2”. EMBO J. 16 (8): 1909–20. (April 1997). doi:10.1093/emboj/16.8.1909. PMC 1169794. PMID 9155017.
“The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization”. Mol. Cell. Biol. 23 (16): 5692–705. (August 2003). doi:10.1128/mcb.23.16.5692-5705.2003. PMC 166352. PMID 12897141.
“Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. 279 (38): 40209–19. (September 2004). doi:10.1074/jbc.M404056200. PMID 15210690.
“MAP kinase binds to the NH2-terminal activation domain of c-Myc”. FEBS Lett. 353 (3): 281–5. (October 1994). doi:10.1016/0014-5793(94)01052-8. PMID 7957875.
“Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase”. Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7337–42. (July 1997). Bibcode: 1997PNAS...94.7337T. doi:10.1073/pnas.94.14.7337. PMC 23822. PMID 9207092.
“Nek2A specifies the centrosomal localization of Erk2”. Biochem. Biophys. Res. Commun. 321 (2): 495–501. (August 2004). doi:10.1016/j.bbrc.2004.06.171. PMID 15358203.
“PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase”. Dev. Cell 1 (2): 239–50. (August 2001). doi:10.1016/s1534-5807(01)00035-1. PMID 11702783.
“The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP”. Oncogene 19 (7): 858–69. (February 2000). doi:10.1038/sj.onc.1203408. PMID 10702794.
“Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)”. J. Biol. Chem. 274 (17): 11693–700. (April 1999). doi:10.1074/jbc.274.17.11693. PMID 10206983.
“Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo”. J. Biol. Chem. 274 (5): 2893–8. (January 1999). doi:10.1074/jbc.274.5.2893. PMID 9915826.
“Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity”. Mol. Cell. Biol. 23 (14): 4796–804. (July 2003). doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
“Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases”. J. Biol. Chem. 271 (47): 29773–9. (November 1996). doi:10.1074/jbc.271.47.29773. PMID 8939914.
“Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin”. J. Biol. Chem. 279 (33): 34570–7. (August 2004). doi:10.1074/jbc.M402304200. PMID 15184391.
“Extracellular signal-regulated kinase (ERK) interacts with signal transducer and activator of transcription (STAT) 5a”. Mol. Endocrinol. 13 (4): 555–65. (April 1999). doi:10.1210/mend.13.4.0263. PMID 10194762.
“Growth hormone (GH) induces the formation of protein complexes involving Stat5, Erk2, Shc and serine phosphorylated proteins”. Mol. Cell. Endocrinol. 166 (2): 89–99. (August 2000). doi:10.1016/s0303-7207(00)00277-x. PMID 10996427.
“A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling”. Biochem. Biophys. Res. Commun. 297 (1): 17–23. (September 2002). doi:10.1016/s0006-291x(02)02086-7. PMID 12220502.
“Identification of the Anti-proliferative protein Tob as a MAPK substrate”. J. Biol. Chem. 277 (40): 37783–7. (October 2002). doi:10.1074/jbc.M204506200. PMID 12151396.
“Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis”. Cell 121 (2): 179–93. (April 2005). doi:10.1016/j.cell.2005.02.031. PMID 15851026.
“Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex”. J. Biol. Chem. 271 (43): 26962–70. (October 1996). doi:10.1074/jbc.271.43.26962. PMID 8900182.
“Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”. FEBS Lett. 401 (2–3): 133–7. (January 1997). doi:10.1016/s0014-5793(96)01456-1. PMID 9013873.

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000100030 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000063358 - Ensembl, May 2017

harvard.edu (Global: 18^th place; Japanese: 107^th place)

ui.adsabs.harvard.edu

jax.org (Global: low place; Japanese: low place)

informatics.jax.org

“Mapk1 Targeted Allele Detail MGI Mouse (MGI:4432537)”. www.informatics.jax.org. 2023年7月17日閲覧。

mousephenotype.org (Global: low place; Japanese: low place)

“Mapk1 Mouse Gene Details | mitogen-activated protein kinase 1 | International Mouse Phenotyping Consortium” (英語). www.mousephenotype.org. 2023年7月17日閲覧。

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs”. Biochem. Biophys. Res. Commun. 182 (3): 1416–22. (February 1992). doi:10.1016/0006-291X(92)91891-S. PMID 1540184.
“A conditional knockout resource for the genome-wide study of mouse gene function”. Nature 474 (7351): 337–42. (2011). doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
“Mouse library set to be knockout”. Nature 474 (7351): 262–3. (2011). doi:10.1038/474262a. PMID 21677718.
“A mouse for all reasons”. Cell 128 (1): 9–13. (2007). doi:10.1016/j.cell.2006.12.018. PMID 17218247.
“The mouse genetics toolkit: revealing function and mechanism”. Genome Biol. 12 (6): 224. (2011). doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
“Extracellular signal-regulated protein kinase 2 is required for efficient generation of B cells bearing antigen-specific immunoglobulin G”. Molecular and Cellular Biology 27 (4): 1236–46. (February 2007). doi:10.1128/MCB.01530-06. PMC 1800707. PMID 17145771.
“The influence of the MAPK pathway on T cell lineage commitment”. Immunity 7 (5): 609–18. (November 1997). doi:10.1016/s1074-7613(00)80382-9. PMID 9390685.
“Deletion of ERK2 mitogen-activated protein kinase identifies its key roles in cortical neurogenesis and cognitive function”. The Journal of Neuroscience 28 (27): 6983–95. (July 2008). doi:10.1523/JNEUROSCI.0679-08.2008. PMC 4364995. PMID 18596172.
“Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding”. Mol. Biol. Cell 13 (6): 2031–44. (June 2002). doi:10.1091/mbc.01-11-0561. PMC 117622. PMID 12058067.
“Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator”. J. Biol. Chem. 283 (14): 9031–9. (April 2008). doi:10.1074/jbc.M706487200. PMC 2431044. PMID 18245089.
“Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1”. J. Biol. Chem. 276 (19): 16491–500. (May 2001). doi:10.1074/jbc.M010966200. PMID 11278799.
“Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma”. Cancer Res. 68 (11): 4192–200. (June 2008). doi:10.1158/0008-5472.CAN-07-6157. PMID 18519678.
“Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain”. J. Biol. Chem. 276 (29): 27575–83. (July 2001). doi:10.1074/jbc.M100408200. PMID 11346645.
“Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway”. J. Biol. Chem. 274 (19): 13271–80. (May 1999). doi:10.1074/jbc.274.19.13271. PMID 10224087.
“Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs”. J. Biol. Chem. 278 (17): 14926–35. (April 2003). doi:10.1074/jbc.M300485200. PMID 12594221.
“Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction”. J. Cell Sci. 108 (11): 3599–609. (November 1995). doi:10.1242/jcs.108.11.3599. PMID 8586671.
“Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes”. Mol. Cell. Biol. 24 (3): 1081–95. (February 2004). doi:10.1128/mcb.24.3.1081-1095.2004. PMC 321437. PMID 14729955.
“Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras”. Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14329–33. (December 2000). Bibcode: 2000PNAS...9714329Z. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
“p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels”. Mol. Cell. Biol. 23 (9): 3079–90. (May 2003). doi:10.1128/mcb.23.9.3079-3090.2003. PMC 153192. PMID 12697810.
“Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1”. J. Biol. Chem. 277 (17): 14844–52. (April 2002). doi:10.1074/jbc.M107776200. PMID 11823456.
“Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein”. Mol. Cell. Biol. 20 (9): 3079–85. (May 2000). doi:10.1128/mcb.20.9.3079-3085.2000. PMC 85596. PMID 10757792.
“A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment”. J. Cell Biol. 152 (4): 765–76. (February 2001). doi:10.1083/jcb.152.4.765. PMC 2195784. PMID 11266467.
“Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking”. J. Biol. Chem. 276 (28): 26509–15. (July 2001). doi:10.1074/jbc.M102769200. PMID 11352917.
“Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2”. J. Biol. Chem. 276 (19): 16070–5. (May 2001). doi:10.1074/jbc.M100681200. PMID 11279118.
“MEKK1 binds raf-1 and the ERK2 cascade components”. J. Biol. Chem. 275 (51): 40120–7. (December 2000). doi:10.1074/jbc.M005926200. PMID 10969079.
“Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions”. EMBO J. 20 (3): 466–79. (February 2001). doi:10.1093/emboj/20.3.466. PMC 133461. PMID 11157753.
“Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2”. EMBO J. 16 (8): 1909–20. (April 1997). doi:10.1093/emboj/16.8.1909. PMC 1169794. PMID 9155017.
“The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization”. Mol. Cell. Biol. 23 (16): 5692–705. (August 2003). doi:10.1128/mcb.23.16.5692-5705.2003. PMC 166352. PMID 12897141.
“Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. 279 (38): 40209–19. (September 2004). doi:10.1074/jbc.M404056200. PMID 15210690.
“MAP kinase binds to the NH2-terminal activation domain of c-Myc”. FEBS Lett. 353 (3): 281–5. (October 1994). doi:10.1016/0014-5793(94)01052-8. PMID 7957875.
“Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase”. Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7337–42. (July 1997). Bibcode: 1997PNAS...94.7337T. doi:10.1073/pnas.94.14.7337. PMC 23822. PMID 9207092.
“Nek2A specifies the centrosomal localization of Erk2”. Biochem. Biophys. Res. Commun. 321 (2): 495–501. (August 2004). doi:10.1016/j.bbrc.2004.06.171. PMID 15358203.
“PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase”. Dev. Cell 1 (2): 239–50. (August 2001). doi:10.1016/s1534-5807(01)00035-1. PMID 11702783.
“The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP”. Oncogene 19 (7): 858–69. (February 2000). doi:10.1038/sj.onc.1203408. PMID 10702794.
“Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)”. J. Biol. Chem. 274 (17): 11693–700. (April 1999). doi:10.1074/jbc.274.17.11693. PMID 10206983.
“Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo”. J. Biol. Chem. 274 (5): 2893–8. (January 1999). doi:10.1074/jbc.274.5.2893. PMID 9915826.
“Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity”. Mol. Cell. Biol. 23 (14): 4796–804. (July 2003). doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
“Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases”. J. Biol. Chem. 271 (47): 29773–9. (November 1996). doi:10.1074/jbc.271.47.29773. PMID 8939914.
“Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin”. J. Biol. Chem. 279 (33): 34570–7. (August 2004). doi:10.1074/jbc.M402304200. PMID 15184391.
“Extracellular signal-regulated kinase (ERK) interacts with signal transducer and activator of transcription (STAT) 5a”. Mol. Endocrinol. 13 (4): 555–65. (April 1999). doi:10.1210/mend.13.4.0263. PMID 10194762.
“Growth hormone (GH) induces the formation of protein complexes involving Stat5, Erk2, Shc and serine phosphorylated proteins”. Mol. Cell. Endocrinol. 166 (2): 89–99. (August 2000). doi:10.1016/s0303-7207(00)00277-x. PMID 10996427.
“A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling”. Biochem. Biophys. Res. Commun. 297 (1): 17–23. (September 2002). doi:10.1016/s0006-291x(02)02086-7. PMID 12220502.
“Identification of the Anti-proliferative protein Tob as a MAPK substrate”. J. Biol. Chem. 277 (40): 37783–7. (October 2002). doi:10.1074/jbc.M204506200. PMID 12151396.
“Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis”. Cell 121 (2): 179–93. (April 2005). doi:10.1016/j.cell.2005.02.031. PMID 15851026.
“Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex”. J. Biol. Chem. 271 (43): 26962–70. (October 1996). doi:10.1074/jbc.271.43.26962. PMID 8900182.
“Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”. FEBS Lett. 401 (2–3): 133–7. (January 1997). doi:10.1016/s0014-5793(96)01456-1. PMID 9013873.

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

Human PubMed Reference:
Mouse PubMed Reference:
“Entrez Gene: MAPK1 mitogen-activated protein kinase 1”. 2023年7月17日閲覧。

phosphosite.org (Global: low place; Japanese: low place)

“ERK2 (human)”. www.phosphosite.org. 2020年10月31日閲覧。

proteinatlas.org (Global: low place; Japanese: low place)

“Expression of MAPK1 in cancer - Summary - The Human Protein Atlas”. www.proteinatlas.org. 2023年7月17日閲覧。

wikipedia.org (Global: low place; Japanese: low place)

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000100030 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000063358 - Ensembl, May 2017

MAPK1 (Japanese Wikipedia)

doi.org (Global: 2nd place; Japanese: 6th place)

ensembl.org (Global: 1,626th place; Japanese: 2,625th place)

May2017.archive.ensembl.org

harvard.edu (Global: 18th place; Japanese: 107th place)

ui.adsabs.harvard.edu

jax.org (Global: low place; Japanese: low place)

informatics.jax.org

mousephenotype.org (Global: low place; Japanese: low place)

nih.gov (Global: 4th place; Japanese: 24th place)

pubmed.ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

phosphosite.org (Global: low place; Japanese: low place)

proteinatlas.org (Global: low place; Japanese: low place)

wikipedia.org (Global: low place; Japanese: low place)

en.wikipedia.org

doi.org (Global: 2^nd place; Japanese: 6^th place)

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

harvard.edu (Global: 18^th place; Japanese: 107^th place)

nih.gov (Global: 4^th place; Japanese: 24^th place)