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{{main|Extracellular signal-regulated kinases}}
{{main|Extracellular signal-regulated kinases}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Mitogen-activated protein kinase 3''', also known as '''p44MAPK''' and '''ERK1''',<ref>{{Cite journal|last=Thomas|first=Gareth M.|last2=Huganir|first2=Richard L.|date=1 March 2004|title=MAPK cascade signalling and synaptic plasticity|url=https://www.nature.com/articles/nrn1346|journal=Nature Reviews Neuroscience|volume=5|issue=3|pages=173–183|doi=10.1038/nrn1346|issn=1471-003X|via=}}</ref> is an [[enzyme]] that in humans is encoded by the ''MAPK3'' [[gene]].<ref name="pmid9628824">{{cite journal | vauthors = García F, Zalba G, Páez G, Encío I, de Miguel C | title = Molecular cloning and characterization of the human p44 mitogen-activated protein kinase gene | journal = Genomics | volume = 50 | issue = 1 | pages = 69–78 | date = 15 May 1998 | pmid = 9628824 | pmc = | doi = 10.1006/geno.1998.5315 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Mitogen-activated protein kinase 3
| HGNCid = 6877
| Symbol = MAPK3
| AltSymbols =; ERK1; HS44KDAP; HUMKER1A; MGC20180; P44ERK1; P44MAPK; PRKM3
| OMIM = 601795
| ECnumber = 
| Homologene = 55682
| MGIid = 1346859
| GeneAtlas_image1 = PBB_GE_MAPK3_212046_x_at_tn.png
<!-- The Following entry is a time stamp of the last bot update.  It is typically hidden data -->
| DateOfBotUpdate = 07:39, 9 October 2007 (UTC)
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0001784 |text = phosphotyrosine binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004707 |text = MAP kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0019233 |text = sensory perception of pain}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5595
    | Hs_Ensembl = ENSG00000102882
    | Hs_RefseqProtein = NP_001035145
    | Hs_RefseqmRNA = NM_001040056
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 30032951
    | Hs_GenLoc_end = 30042116
    | Hs_Uniprot = P27361
    | Mm_EntrezGene = 26417
    | Mm_Ensembl = ENSMUSG00000063065
    | Mm_RefseqmRNA = NM_011952
    | Mm_RefseqProtein = NP_036082
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 126550780
    | Mm_GenLoc_end = 126556964
    | Mm_Uniprot = Q63844
  }}
}}
'''Mitogen-activated protein kinase 3''', also known as '''MAPK3''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the [[mitogen-activated protein kinase]] (MAP kinase) family. MAP kinases, also known as [[extracellular signal-regulated kinases]] (ERKs), act in a signaling cascade that regulates various cellular processes such as [[Cell growth|proliferation]], [[Cellular differentiation|differentiation]], and [[cell cycle]] progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it [[phosphorylates]] nuclear targets. Alternatively spliced transcript variants encoding different protein [[isoforms]] have been described.<ref>{{cite web | title = Entrez Gene: MAPK3 mitogen-activated protein kinase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5595| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act in a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms have been described.<ref>{{cite web | title = Entrez Gene: MAPK3 mitogen-activated protein kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5595| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
It has been suggested that MAPK3, along with the gene [[IRAK1]], is turned off by two [[microRNA]]s that were activated after the [[influenza A]] virus had been made to infect human lung cells.<ref name="pmid22822053">{{cite journal | vauthors = Buggele WA, Johnson KE, Horvath CM | title = Influenza A virus infection of human respiratory cells induces primary microRNA expression | journal = J. Biol. Chem. | volume = 287 | issue = 37 | pages = 31027–40 | year = 2012 | pmid = 22822053 | pmc = 3438935 | doi = 10.1074/jbc.M112.387670 }}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== Signaling pathways ==
| citations =  
 
*{{cite journal  | author=Peruzzi F, Gordon J, Darbinian N, Amini S |title=Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway. |journal=J. Neurovirol. |volume=8 Suppl 2 |issue= |pages= 91-6 |year= 2003 |pmid= 12491158 |doi= 10.1080/13550280290167885 }}
Pharmacological inhibition of ERK1/2 restores [[GSK3β]] activity and protein synthesis levels in a model of [[tuberous sclerosis]].<ref name="pmid28646232">{{cite journal | vauthors = Pal R, Bondar VV, Adamski CJ, Rodney GG, Sardiello M | title = Inhibition of ERK1/2 Restores GSK3β Activity and Protein Synthesis Levels in a Model of Tuberous Sclerosis | journal = Sci. Rep. | volume = 7 | issue = 1 | pages = 4174 | year = 2017 | pmid = 28646232 | doi = 10.1038/s41598-017-04528-5 | pmc=5482840}}</ref>
*{{cite journal | author=Meloche S, Pouysségur J |title=The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition. |journal=Oncogene |volume=26 |issue= 22 |pages= 3227-39 |year= 2007 |pmid= 17496918 |doi= 10.1038/sj.onc.1210414 }}
 
*{{cite journal  | author=Ruscica M, Dozio E, Motta M, Magni P |title=Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation. |journal=Adv. Exp. Med. Biol. |volume=604 |issue=  |pages= 96-100 |year= 2007 |pmid= 17695723 |doi= }}
== Interactions ==
}}
 
MAPK3 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[DUSP3]],<ref name = pmid10224087>{{cite journal | vauthors = Todd JL, Tanner KG, Denu JM | title = 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 | journal = J. Biol. Chem. | volume = 274 | issue = 19 | pages = 13271–80  | date = May 1999 | pmid = 10224087 | doi =  10.1074/jbc.274.19.13271}}</ref>
* [[DUSP6]]<ref name = pmid9535927>{{cite journal | vauthors = Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S | title = The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity | journal = J. Biol. Chem. | volume = 273 | issue = 15 | pages = 9323–9  | date = April 1998 | pmid = 9535927 | doi =  10.1074/jbc.273.15.9323}}</ref>
* [[GTF2I]],<ref name = pmid10648599>{{cite journal | vauthors = Kim DW, Cochran BH | title = Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter | journal = Mol. Cell. Biol. | volume = 20 | issue = 4 | pages = 1140–8  | date = February 2000 | pmid = 10648599 | pmc = 85232 | doi = 10.1128/mcb.20.4.1140-1148.2000}}</ref>
* [[HDAC4]],<ref name = pmid11114188>{{cite journal | vauthors = Zhou X, Richon VM, Wang AH, Yang XJ, Rifkind RA, Marks PA | title = Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 26 | pages = 14329–33  | date = December 2000 | pmid = 11114188 | pmc = 18918 | doi = 10.1073/pnas.250494697 }}</ref>
* [[MAP2K1]],<ref name = pmid9006895>{{cite journal | vauthors = Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, Stossel TP, Kyriakis JM, Avruch J | title = Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells | journal = J. Biol. Chem. | volume = 272 | issue = 5 | pages = 2620–8  | date = January 1997 | pmid = 9006895 | doi =  10.1074/jbc.272.5.2620}}</ref><ref name = pmid8626767>{{cite journal | vauthors = Butch ER, Guan KL | title = Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2 | journal = J. Biol. Chem. | volume = 271 | issue = 8 | pages = 4230–5  | date = February 1996 | pmid = 8626767 | doi =  10.1074/jbc.271.8.4230}}</ref><ref name = pmid9733512>{{cite journal | vauthors = Elion EA | title = Routing MAP kinase cascades | journal = Science | volume = 281 | issue = 5383 | pages = 1625–6  | date = September 1998 | pmid = 9767029 | doi =  10.1126/science.281.5383.1625}}</ref><ref name = pmid10748187>{{cite journal | vauthors = Yung Y, Yao Z, Hanoch T, Seger R | title = ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK | journal = J. Biol. Chem. | volume = 275 | issue = 21 | pages = 15799–808  | date = May 2000 | pmid = 10748187 | doi = 10.1074/jbc.M910060199 }}</ref><ref name = pmid8226933>{{cite journal | vauthors = Zheng CF, Guan KL | title = Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases | journal = J. Biol. Chem. | volume = 268 | issue = 32 | pages = 23933–9  | date = November 1993 | pmid = 8226933 | doi =  }}</ref>
* [[MAP2K2]],<ref name = pmid9006895/><ref name = pmid8626767/><ref name = pmid8226933/>
* [[PTPN7]],<ref name = pmid10702794>{{cite journal | vauthors = Pettiford SM, Herbst R | title = The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP | journal = Oncogene | volume = 19 | issue = 7 | pages = 858–69  | date = February 2000 | pmid = 10702794 | doi = 10.1038/sj.onc.1203408 }}</ref><ref name = pmid10559944>{{cite journal | vauthors = Saxena M, Williams S, Taskén K, Mustelin T | title = Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase | journal = Nat. Cell Biol. | volume = 1 | issue = 5 | pages = 305–11  | date = September 1999 | pmid = 10559944 | doi = 10.1038/13024 }}</ref><ref name = pmid10206983>{{cite journal | vauthors = Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T | title = Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP) | journal = J. Biol. Chem. | volume = 274 | issue = 17 | pages = 11693–700  | date = April 1999 | pmid = 10206983 | doi =  10.1074/jbc.274.17.11693}}</ref>
* [[RPS6KA2]],<ref name = pmid12832467>{{cite journal | vauthors = Roux PP, Richards SA, Blenis J | title = Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity | journal = Mol. Cell. Biol. | volume = 23 | issue = 14 | pages = 4796–804  | date = July 2003 | pmid = 12832467 | pmc = 162206 | doi =  10.1128/mcb.23.14.4796-4804.2003}}</ref><ref name = pmid8939914>{{cite journal | vauthors = Zhao Y, Bjorbaek C, Moller DE | title = Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases | journal = J. Biol. Chem. | volume = 271 | issue = 47 | pages = 29773–9  | date = November 1996 | pmid = 8939914 | doi =  10.1074/jbc.271.47.29773}}</ref>  and
* [[SPIB]].<ref name = pmid8632909>{{cite journal | vauthors = Mao C, Ray-Gallet D, Tavitian A, Moreau-Gachelin F | title = Differential phosphorylations of Spi-B and Spi-1 transcription factors | journal = Oncogene | volume = 12 | issue = 4 | pages = 863–73 | date = February 1996 | pmid = 8632909 | doi =  }}</ref>
{{Div col end}}
{{Clear}}
 
== References ==
{{reflist|35em}}
 
== Further reading ==
{{refbegin|35em}}
* {{cite journal | vauthors = Peruzzi F, Gordon J, Darbinian N, Amini S | title = Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway | journal = J. Neurovirol. | volume = 8 Suppl 2 | issue = 2 | pages = 91–6 | year = 2002 | pmid = 12491158 | doi = 10.1080/13550280290167885 }}
* {{cite journal | vauthors = Meloche S, Pouysségur J | title = The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition | journal = Oncogene | volume = 26 | issue = 22 | pages = 3227–39 | year = 2007 | pmid = 17496918 | doi = 10.1038/sj.onc.1210414 }}
* {{citation | vauthors = Ruscica M, Dozio E, Motta M, Magni P | title = Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation | volume = 604 | issue =  | pages = 96–100 | year = 2007 | pmid = 17695723 | doi = 10.1007/978-0-387-69116-9_7 | isbn = 978-0-387-69114-5 | series = Advances In Experimental Medicine And Biology }}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* [http://www.mapkinases.eu MAP Kinase Resource ].
 
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
[[Category:EC 2.7.11]]
 
 
{{gene-16-stub}}

Latest revision as of 09:13, 10 January 2019

Main article: Extracellular signal-regulated kinases
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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Mitogen-activated protein kinase 3, also known as p44MAPK and ERK1,[1] is an enzyme that in humans is encoded by the MAPK3 gene.[2]

Function

The protein encoded by this gene is a member of the mitogen-activated protein kinase (MAP kinase) family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act in a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms have been described.[3]

Clinical significance

It has been suggested that MAPK3, along with the gene IRAK1, is turned off by two microRNAs that were activated after the influenza A virus had been made to infect human lung cells.[4]

Signaling pathways

Pharmacological inhibition of ERK1/2 restores GSK3β activity and protein synthesis levels in a model of tuberous sclerosis.[5]

Interactions

MAPK3 has been shown to interact with:

References

  1. ↑ Thomas, Gareth M.; Huganir, Richard L. (1 March 2004). "MAPK cascade signalling and synaptic plasticity". Nature Reviews Neuroscience. 5 (3): 173–183. doi:10.1038/nrn1346. ISSN 1471-003X.
  2. ↑ García F, Zalba G, Páez G, Encío I, de Miguel C (15 May 1998). "Molecular cloning and characterization of the human p44 mitogen-activated protein kinase gene". Genomics. 50 (1): 69–78. doi:10.1006/geno.1998.5315. PMID 9628824.
  3. ↑ "Entrez Gene: MAPK3 mitogen-activated protein kinase 3".
  4. ↑ Buggele WA, Johnson KE, Horvath CM (2012). "Influenza A virus infection of human respiratory cells induces primary microRNA expression". J. Biol. Chem. 287 (37): 31027–40. doi:10.1074/jbc.M112.387670. PMC 3438935. PMID 22822053.
  5. ↑ Pal R, Bondar VV, Adamski CJ, Rodney GG, Sardiello M (2017). "Inhibition of ERK1/2 Restores GSK3β Activity and Protein Synthesis Levels in a Model of Tuberous Sclerosis". Sci. Rep. 7 (1): 4174. doi:10.1038/s41598-017-04528-5. PMC 5482840. PMID 28646232.
  6. ↑ Todd JL, Tanner KG, Denu JM (May 1999). "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. doi:10.1074/jbc.274.19.13271. PMID 10224087.
  7. ↑ Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S (April 1998). "The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity". J. Biol. Chem. 273 (15): 9323–9. doi:10.1074/jbc.273.15.9323. PMID 9535927.
  8. ↑ Kim DW, Cochran BH (February 2000). "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Mol. Cell. Biol. 20 (4): 1140–8. doi:10.1128/mcb.20.4.1140-1148.2000. PMC 85232. PMID 10648599.
  9. ↑ Zhou X, Richon VM, Wang AH, Yang XJ, Rifkind RA, Marks PA (December 2000). "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. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
  10. ↑ 10.0 10.1 Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, Stossel TP, Kyriakis JM, Avruch J (January 1997). "Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells". J. Biol. Chem. 272 (5): 2620–8. doi:10.1074/jbc.272.5.2620. PMID 9006895.
  11. ↑ 11.0 11.1 Butch ER, Guan KL (February 1996). "Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2". J. Biol. Chem. 271 (8): 4230–5. doi:10.1074/jbc.271.8.4230. PMID 8626767.
  12. ↑ Elion EA (September 1998). "Routing MAP kinase cascades". Science. 281 (5383): 1625–6. doi:10.1126/science.281.5383.1625. PMID 9767029.
  13. ↑ Yung Y, Yao Z, Hanoch T, Seger R (May 2000). "ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK". J. Biol. Chem. 275 (21): 15799–808. doi:10.1074/jbc.M910060199. PMID 10748187.
  14. ↑ 14.0 14.1 Zheng CF, Guan KL (November 1993). "Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases". J. Biol. Chem. 268 (32): 23933–9. PMID 8226933.
  15. ↑ Pettiford SM, Herbst R (February 2000). "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". Oncogene. 19 (7): 858–69. doi:10.1038/sj.onc.1203408. PMID 10702794.
  16. ↑ Saxena M, Williams S, Taskén K, Mustelin T (September 1999). "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase". Nat. Cell Biol. 1 (5): 305–11. doi:10.1038/13024. PMID 10559944.
  17. ↑ Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T (April 1999). "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. 274 (17): 11693–700. doi:10.1074/jbc.274.17.11693. PMID 10206983.
  18. ↑ Roux PP, Richards SA, Blenis J (July 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Mol. Cell. Biol. 23 (14): 4796–804. doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
  19. ↑ Zhao Y, Bjorbaek C, Moller DE (November 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. PMID 8939914.
  20. ↑ Mao C, Ray-Gallet D, Tavitian A, Moreau-Gachelin F (February 1996). "Differential phosphorylations of Spi-B and Spi-1 transcription factors". Oncogene. 12 (4): 863–73. PMID 8632909.

Further reading

  • Peruzzi F, Gordon J, Darbinian N, Amini S (2002). "Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway". J. Neurovirol. 8 Suppl 2 (2): 91–6. doi:10.1080/13550280290167885. PMID 12491158.
  • Meloche S, Pouysségur J (2007). "The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition". Oncogene. 26 (22): 3227–39. doi:10.1038/sj.onc.1210414. PMID 17496918.
  • Ruscica M, Dozio E, Motta M, Magni P (2007), Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation, Advances In Experimental Medicine And Biology, 604, pp. 96–100, doi:10.1007/978-0-387-69116-9_7, ISBN 978-0-387-69114-5, PMID 17695723

External links


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