MAP2K2: Difference between revisions

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{{main|Mitogen-activated protein kinase kinase}}
{{main|Mitogen-activated protein kinase kinase}}
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{{Infobox_gene}}
{{PBB_Controls
'''Dual specificity mitogen-activated protein kinase kinase 2''' is an [[enzyme]] that in humans is encoded by the ''MAP2K2'' [[gene]].<ref name="pmid8388392">{{cite journal | vauthors = Zheng CF, Guan KL | title = Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2 | journal = J Biol Chem | volume = 268 | issue = 15 | pages = 11435–9 |date=Jun 1993 | pmid = 8388392 | pmc =  | doi =  }}</ref> It is more commonly known as MEK2, but has many alternative names including CFC4, MKK2, MAPKK2 and PRKMK2. <ref>{{Cite web|title = MAP2K2 mitogen-activated protein kinase kinase 2 [Homo sapiens (human)] - Gene - NCBI|url = https://www.ncbi.nlm.nih.gov/gene/5605|website = www.ncbi.nlm.nih.gov|accessdate = 2015-10-16}}</ref>
| update_page = yes
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| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MAP2K2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1s9i.
| PDB = {{PDB2|1s9i}}
| Name = Mitogen-activated protein kinase kinase 2
| HGNCid = 6842
| Symbol = MAP2K2
| AltSymbols =; MAPKK2; MEK2; MKK2; PRKMK2
| OMIM = 601263
| ECnumber = 
| Homologene = 48591
| MGIid = 1346867
| GeneAtlas_image1 = PBB_GE_MAP2K2_202424_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAP2K2_213490_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine 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:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5605
    | Hs_Ensembl = ENSG00000126934
    | Hs_RefseqProtein = NP_109587
    | Hs_RefseqmRNA = NM_030662
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 4041331
    | Hs_GenLoc_end = 4075126
    | Hs_Uniprot = P36507
    | Mm_EntrezGene = 26396
    | Mm_Ensembl = ENSMUSG00000035027
    | Mm_RefseqmRNA = XM_987766
    | Mm_RefseqProtein = XP_992860
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 80509092
    | Mm_GenLoc_end = 80527465
    | Mm_Uniprot = Q3USU3
  }}
}}
'''Mitogen-activated protein kinase kinase 2''', also known as '''MAP2K2''', 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 dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is known to play a critical role in [[MAPK/ERK pathway|mitogen growth factor signal transduction]]. It phosphorylates and thus activates [[MAPK1]]/ERK2 and [[MAPK3]]/ERK1.
{{PBB_Summary
 
| section_title =
The activation of this kinase itself is dependent on the Ser/Thr phosphorylation by [[MAP kinase kinase kinase]]s.
| summary_text = The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is known to play a critical role in mitogen growth factor signal transduction. It phosphorylates and thus activates MAPK1/ERK2 and MAPK2/ERK3. The activation of this kinase itself is dependent on the Ser/Thr phosphorylation by MAP kinase kinase kinases. The inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax.<ref>{{cite web | title = Entrez Gene: MAP2K2 mitogen-activated protein kinase kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5605| accessdate = }}</ref>
 
}}
The inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax.<ref>{{cite web | title = Entrez Gene: MAP2K2 mitogen-activated protein kinase kinase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5605| accessdate = }}</ref>
 
==Interactions==
MAP2K2 has been shown to [[Protein-protein interaction|interact]] with [[MAPK3]]<ref name=pmid9006895>{{cite journal |last=Marti |first=A |authorlink= |author2=Luo Z |author3=Cunningham C |author4=Ohta Y |author5=Hartwig J |author6=Stossel T P |author7=Kyriakis J M |author8=Avruch J  |date=Jan 1997 |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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9006895 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.272.5.2620 }}</ref><ref name=pmid8626767>{{cite journal |last=Butch |first=E R |authorlink= |author2=Guan K L  |date=Feb 1996 |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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 8626767 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.271.8.4230 }}</ref><ref name=pmid8226933>{{cite journal |last=Zheng |first=C F |authorlink= |author2=Guan K L  |date=Nov 1993 |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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 8226933 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[ARAF]].<ref name=pmid11909642>{{cite journal |last=Yin |first=Xiang L |authorlink= |author2=Chen She |author3=Yan Jun |author4=Hu Yun |author5=Gu Jian X  |date=Feb 2002 |title=Identification of interaction between MEK2 and A-Raf-1 |journal=Biochim. Biophys. Acta |volume=1589 |issue=1 |pages=71–6 |publisher= |location = Netherlands| issn = 0006-3002| pmid = 11909642 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi=10.1016/S0167-4889(01)00188-4}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87–94 |year= 2005 |pmid= 15638726 |doi=10.2174/1570162052773013 }}
| citations =
*{{cite journal  | vauthors=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57–64 |year= 2006 |pmid= 16454711 |doi=10.2174/157016206775197583 }}
*{{cite journal  | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi=  }}
*{{cite journal   |vauthors=Charest DL, Mordret G, Harder KW, etal |title=Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1 |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4679–90 |year= 1993 |pmid= 7687743 |doi= | pmc=360094 }}
*{{cite journal  | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi=  }}
*{{cite journal   |vauthors=Dérijard B, Raingeaud J, Barrett T, etal |title=Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms |journal=Science |volume=267 |issue= 5198 |pages= 682–5 |year= 1995 |pmid= 7839144 |doi=10.1126/science.7839144 }}
*{{cite journal | author=Charest DL, Mordret G, Harder KW, ''et al.'' |title=Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1. |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4679-90 |year= 1993 |pmid= 7687743 |doi=  }}
*{{cite journal   |vauthors=Alessi DR, Saito Y, Campbell DG, etal |title=Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1 |journal=EMBO J. |volume=13 |issue= 7 |pages= 1610–9 |year= 1994 |pmid= 8157000 |doi= | pmc=394991 }}
*{{cite journal | author=Dérijard B, Raingeaud J, Barrett T, ''et al.'' |title=Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. |journal=Science |volume=267 |issue= 5198 |pages= 682-5 |year= 1995 |pmid= 7839144 |doi=  }}
*{{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 |year= 1993 |pmid= 8226933 |doi=  }}
*{{cite journal | author=Alessi DR, Saito Y, Campbell DG, ''et al.'' |title=Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1. |journal=EMBO J. |volume=13 |issue= 7 |pages= 1610-9 |year= 1994 |pmid= 8157000 |doi=  }}
*{{cite journal   |vauthors=Wu J, Harrison JK, Dent P, etal |title=Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2 |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4539–48 |year= 1993 |pmid= 8393135 |doi= | pmc=360070 }}
*{{cite journal  | author=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 |year= 1993 |pmid= 8226933 |doi=  }}
*{{cite journal  | vauthors=Moriguchi T, Gotoh Y, Nishida E |title=Activation of two isoforms of mitogen-activated protein kinase kinase in response to epidermal growth factor and nerve growth factor |journal=Eur. J. Biochem. |volume=234 |issue= 1 |pages= 32–8 |year= 1996 |pmid= 8529659 |doi=10.1111/j.1432-1033.1995.032_c.x }}
*{{cite journal | author=Zheng CF, Guan KL |title=Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2. |journal=J. Biol. Chem. |volume=268 |issue= 15 |pages= 11435-9 |year= 1993 |pmid= 8388392 |doi=  }}
*{{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 |year= 1996 |pmid= 8626767 |doi=10.1074/jbc.271.8.4230 }}
*{{cite journal  | author=Wu J, Harrison JK, Dent P, ''et al.'' |title=Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2. |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4539-48 |year= 1993 |pmid= 8393135 |doi=  }}
*{{cite journal  | vauthors =Papin C, Denouel A, Calothy G, Eychène A |title=Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system |journal=Oncogene |volume=12 |issue= 10 |pages= 2213–21 |year= 1996 |pmid= 8668348 |doi=  }}
*{{cite journal  | author=Moriguchi T, Gotoh Y, Nishida E |title=Activation of two isoforms of mitogen-activated protein kinase kinase in response to epidermal growth factor and nerve growth factor. |journal=Eur. J. Biochem. |volume=234 |issue= 1 |pages= 32-8 |year= 1996 |pmid= 8529659 |doi=  }}
*{{cite journal   |vauthors=Downey GP, Butler JR, Brumell J, etal |title=Chemotactic peptide-induced activation of MEK-2, the predominant isoform in human neutrophils. Inhibition by wortmannin |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21005–1011 |year= 1996 |pmid= 8702863 |doi=10.1074/jbc.271.35.21005 }}
*{{cite journal  | author=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 |year= 1996 |pmid= 8626767 |doi=  }}
*{{cite journal  | vauthors=Khoo S, Cobb MH |title=Activation of mitogen-activating protein kinase by glucose is not required for insulin secretion |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5599–604 |year= 1997 |pmid= 9159118 |doi=10.1073/pnas.94.11.5599  | pmc=20824 }}
*{{cite journal | author=Papin C, Denouel A, Calothy G, Eychène A |title=Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system. |journal=Oncogene |volume=12 |issue= 10 |pages= 2213-21 |year= 1996 |pmid= 8668348 |doi=  }}
*{{cite journal   |vauthors=Li CJ, Ueda Y, Shi B |title=Tat protein induces self-perpetuating permissivity for productive HIV-1 infection |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 15 |pages= 8116–20 |year= 1997 |pmid= 9223324 |doi=10.1073/pnas.94.15.8116  | pmc=21566  }}
*{{cite journal  | author=Downey GP, Butler JR, Brumell J, ''et al.'' |title=Chemotactic peptide-induced activation of MEK-2, the predominant isoform in human neutrophils. Inhibition by wortmannin. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21005-1011 |year= 1996 |pmid= 8702863 |doi=  }}
*{{cite journal  | vauthors =Menegon A, Leoni C, Benfenati F, Valtorta F |title=Tat protein from HIV-1 activates MAP kinase in granular neurons and glial cells from rat cerebellum |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 3 |pages= 800–5 |year= 1997 |pmid= 9325171 |doi= 10.1006/bbrc.1997.7393 }}
*{{cite journal | author=Khoo S, Cobb MH |title=Activation of mitogen-activating protein kinase by glucose is not required for insulin secretion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5599-604 |year= 1997 |pmid= 9159118 |doi= }}
*{{cite journal   |vauthors=Denouel-Galy A, Douville EM, Warne PH |title=Murine Ksr interacts with MEK and inhibits Ras-induced transformation |journal=Curr. Biol. |volume=8 |issue= 1 |pages= 46–55 |year= 1998 |pmid= 9427625 |doi=10.1016/S0960-9822(98)70019-3  }}
*{{cite journal  | author=Li CJ, Ueda Y, Shi B, ''et al.'' |title=Tat protein induces self-perpetuating permissivity for productive HIV-1 infection. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 15 |pages= 8116-20 |year= 1997 |pmid= 9223324 |doi= }}
*{{cite journal   |vauthors=Gibellini D, Bassini A, Pierpaoli S |title=Extracellular HIV-1 Tat protein induces the rapid Ser133 phosphorylation and activation of CREB transcription factor in both Jurkat lymphoblastoid T cells and primary peripheral blood mononuclear cells |journal=J. Immunol. |volume=160 |issue= 8 |pages= 3891–8 |year= 1998 |pmid= 9558095 |doi=  }}
*{{cite journal | author=Menegon A, Leoni C, Benfenati F, Valtorta F |title=Tat protein from HIV-1 activates MAP kinase in granular neurons and glial cells from rat cerebellum. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 3 |pages= 800-5 |year= 1997 |pmid= 9325171 |doi= 10.1006/bbrc.1997.7393 }}
*{{cite journal   |vauthors=Duesbery NS, Webb CP, Leppla SH |title=Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor |journal=Science |volume=280 |issue= 5364 |pages= 734–7 |year= 1998 |pmid= 9563949 |doi=10.1126/science.280.5364.734 }}
*{{cite journal | author=Denouel-Galy A, Douville EM, Warne PH, ''et al.'' |title=Murine Ksr interacts with MEK and inhibits Ras-induced transformation. |journal=Curr. Biol. |volume=8 |issue= 1 |pages= 46-55 |year= 1998 |pmid= 9427625 |doi=  }}
*{{cite journal   |vauthors=Ganju RK, Munshi N, Nair BC |title=Human Immunodeficiency Virus Tat Modulates the Flk-1/KDR Receptor, Mitogen-Activated Protein Kinases, and Components of Focal Adhesion in Kaposi's Sarcoma Cells |journal=J. Virol. |volume=72 |issue= 7 |pages= 6131–7 |year= 1998 |pmid= 9621077 |doi=  | pmc=110419 }}
*{{cite journal | author=Gibellini D, Bassini A, Pierpaoli S, ''et al.'' |title=Extracellular HIV-1 Tat protein induces the rapid Ser133 phosphorylation and activation of CREB transcription factor in both Jurkat lymphoblastoid T cells and primary peripheral blood mononuclear cells. |journal=J. Immunol. |volume=160 |issue= 8 |pages= 3891-8 |year= 1998 |pmid= 9558095 |doi=  }}
*{{cite journal   |vauthors=Tanimura S, Chatani Y, Hoshino R |title=Activation of the 41/43 kDa mitogen-activated protein kinase signaling pathway is required for hepatocyte growth factor-induced cell scattering |journal=Oncogene |volume=17 |issue= 1 |pages= 57–65 |year= 1998 |pmid= 9671314 |doi= 10.1038/sj.onc.1201905 }}
*{{cite journal | author=Duesbery NS, Webb CP, Leppla SH, ''et al.'' |title=Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. |journal=Science |volume=280 |issue= 5364 |pages= 734-7 |year= 1998 |pmid= 9563949 |doi=  }}
*{{cite journal  | author=Ganju RK, Munshi N, Nair BC, ''et al.'' |title=Human immunodeficiency virus tat modulates the Flk-1/KDR receptor, mitogen-activated protein kinases, and components of focal adhesion in Kaposi's sarcoma cells. |journal=J. Virol. |volume=72 |issue= 7 |pages= 6131-7 |year= 1998 |pmid= 9621077 |doi=  }}
*{{cite journal | author=Tanimura S, Chatani Y, Hoshino R, ''et al.'' |title=Activation of the 41/43 kDa mitogen-activated protein kinase signaling pathway is required for hepatocyte growth factor-induced cell scattering. |journal=Oncogene |volume=17 |issue= 1 |pages= 57-65 |year= 1998 |pmid= 9671314 |doi= 10.1038/sj.onc.1201905 }}
}}
{{refend}}
{{refend}}
==External links==
* [https://www.ncbi.nlm.nih.gov/books/NBK1186/  GeneReviews/NCBI/NIH/UW entry on Cardiofaciocutaneous Syndrome]
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Revision as of 06:04, 4 September 2017

Main article: Mitogen-activated protein kinase kinase
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Dual specificity mitogen-activated protein kinase kinase 2 is an enzyme that in humans is encoded by the MAP2K2 gene.[1] It is more commonly known as MEK2, but has many alternative names including CFC4, MKK2, MAPKK2 and PRKMK2. [2]

Function

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is known to play a critical role in mitogen growth factor signal transduction. It phosphorylates and thus activates MAPK1/ERK2 and MAPK3/ERK1.

The activation of this kinase itself is dependent on the Ser/Thr phosphorylation by MAP kinase kinase kinases.

The inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax.[3]

Interactions

MAP2K2 has been shown to interact with MAPK3[4][5][6] and ARAF.[7]

References

  1. ↑ Zheng CF, Guan KL (Jun 1993). "Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2". J Biol Chem. 268 (15): 11435–9. PMID 8388392.
  2. ↑ "MAP2K2 mitogen-activated protein kinase kinase 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2015-10-16.
  3. ↑ "Entrez Gene: MAP2K2 mitogen-activated protein kinase kinase 2".
  4. ↑ Marti, A; Luo Z; Cunningham C; Ohta Y; Hartwig J; Stossel T P; Kyriakis J M; Avruch J (Jan 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. UNITED STATES. 272 (5): 2620–8. doi:10.1074/jbc.272.5.2620. ISSN 0021-9258. PMID 9006895.
  5. ↑ Butch, E R; Guan K L (Feb 1996). "Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2". J. Biol. Chem. UNITED STATES. 271 (8): 4230–5. doi:10.1074/jbc.271.8.4230. ISSN 0021-9258. PMID 8626767.
  6. ↑ Zheng, C F; Guan K L (Nov 1993). "Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases". J. Biol. Chem. UNITED STATES. 268 (32): 23933–9. ISSN 0021-9258. PMID 8226933.
  7. ↑ Yin, Xiang L; Chen She; Yan Jun; Hu Yun; Gu Jian X (Feb 2002). "Identification of interaction between MEK2 and A-Raf-1". Biochim. Biophys. Acta. Netherlands. 1589 (1): 71–6. doi:10.1016/S0167-4889(01)00188-4. ISSN 0006-3002. PMID 11909642.

Further reading

External links


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