메뉴 건너뛰기




Volumn 64, Issue 1, 2007, Pages 61-70

Evolution of the metazoan protein phosphatase 2C superfamily

Author keywords

Gene duplication; Phylogeny; Protein phosphatase 2C

Indexed keywords

AMINO ACID; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C; UNCLASSIFIED DRUG;

EID: 33845881426     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00239-006-0033-y     Document Type: Article
Times cited : (36)

References (73)
  • 3
    • 0028111863 scopus 로고
    • PROSITE: Recent developments
    • Bairoch A, Bucher P (1994) PROSITE: recent developments. Nucleic Acids Res 22:3583-3589
    • (1994) Nucleic Acids Res , vol.22 , pp. 3583-3589
    • Bairoch, A.1    Bucher, P.2
  • 4
    • 0028880718 scopus 로고
    • Protein tyrosine phosphatases take o
    • Barford D, Jia Z, Tonks NK (1995) Protein tyrosine phosphatases take o.. Nat Struct Biol 2:1043-1053
    • (1995) Nat Struct Biol , vol.2 , pp. 1043-1053
    • Barford, D.1    Jia, Z.2    Tonks, N.K.3
  • 9
    • 0029040199 scopus 로고
    • Protein tyrosine kinases in the initiation of antigen receptor signaling
    • Bolen JB (1995) Protein tyrosine kinases in the initiation of antigen receptor signaling. Curr Opin Immunol 7:306-311
    • (1995) Curr Opin Immunol , vol.7 , pp. 306-311
    • Bolen, J.B.1
  • 10
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Burnett G, Kennedy EP (1954) The enzymatic phosphorylation of proteins. J Biol Chem 211:969-980
    • (1954) J Biol Chem , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 11
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J (2000) Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol Biol Evol 17:540-552
    • (2000) Mol Biol Evol , vol.17 , pp. 540-552
    • Castresana, J.1
  • 12
    • 0032751695 scopus 로고    scopus 로고
    • Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
    • Cheng A, Ross KE, Kaldis P, Solomon MJ (1999) Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev 13:2946-2957
    • (1999) Genes Dev , vol.13 , pp. 2946-2957
    • Cheng, A.1    Ross, K.E.2    Kaldis, P.3    Solomon, M.J.4
  • 13
    • 0034602268 scopus 로고    scopus 로고
    • Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms
    • Cheng A, Kaldis P, Solomon MJ (2000) Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms. J Biol Chem 275:34744-34749
    • (2000) J Biol Chem , vol.275 , pp. 34744-34749
    • Cheng, A.1    Kaldis, P.2    Solomon, M.J.3
  • 14
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P (1989) The structure and regulation of protein phosphatases. Annu Rev Biochem 58:453-508
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 15
    • 0037389558 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases: New signaling pathways functioning in cellular responses to environmental stress
    • Cowan KJ, Storey KB (2003) Mitogen-activated protein kinases: new signaling pathways functioning in cellular responses to environmental stress. J Exp Biol 206:1107-1115
    • (2003) J Exp Biol , vol.206 , pp. 1107-1115
    • Cowan, K.J.1    Storey, K.B.2
  • 16
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatse 2C at 2.0 A resolution
    • Das AK, Helps NR, Cohen PT, Barford D (1996) Crystal structure of the protein serine/threonine phosphatse 2C at 2.0 A resolution. EMBO J 15:6798-6809
    • (1996) EMBO J , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 17
    • 18744375743 scopus 로고    scopus 로고
    • Selecton: A server for detecting evolutionary forces at a single amino-acid site
    • Doron-Faigenboim A, Stern A, Mayrose I, Bacharach E, Pupko T (2005) Selecton: a server for detecting evolutionary forces at a single amino-acid site. Bioinformatics 21:2101-2103
    • (2005) Bioinformatics , vol.21 , pp. 2101-2103
    • Doron-Faigenboim, A.1    Stern, A.2    Mayrose, I.3    Bacharach, E.4    Pupko, T.5
  • 18
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 19
    • 0000461280 scopus 로고
    • Confidence-limits on phylogenies - an approach using the bootstrap
    • Felsenstein J (1985) Confidence-limits on phylogenies - an approach using the bootstrap. Evolution 39:783-791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 20
    • 0030859025 scopus 로고    scopus 로고
    • Protein phosphatase 2C acts independently of stress-activated kinase cascade to regulate the stress response in fission yeast
    • Gaits F, Shiozaki K, Russell P (1997) Protein phosphatase 2C acts independently of stress-activated kinase cascade to regulate the stress response in fission yeast. J Biol Chem 272:17873-17879
    • (1997) J Biol Chem , vol.272 , pp. 17873-17879
    • Gaits, F.1    Shiozaki, K.2    Russell, P.3
  • 21
    • 33845898552 scopus 로고    scopus 로고
    • Developmental mechanisms of evolutionary change
    • 6th ed. Sinauer Associates, Sunderland, MA, pp
    • Gilbert SF (2001) Developmental mechanisms of evolutionary change. In: Developmental biology, 6th ed. Sinauer Associates, Sunderland, MA, pp 688-689
    • (2001) Developmental biology , pp. 688-689
    • Gilbert, S.F.1
  • 22
    • 23144433822 scopus 로고    scopus 로고
    • PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference
    • Guindon S, Lethiec F, Duroux P, Gascuel O (2005) PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference. Nucleic Acids Res 33:W557-W559
    • (2005) Nucleic Acids Res , vol.33
    • Guindon, S.1    Lethiec, F.2    Duroux, P.3    Gascuel, O.4
  • 23
    • 3242690862 scopus 로고    scopus 로고
    • The new view of animal phylogeny
    • Halanych KM (2004) The new view of animal phylogeny. Annu Rev Ecol Evol Syst 35:229-256
    • (2004) Annu Rev Ecol Evol Syst , vol.35 , pp. 229-256
    • Halanych, K.M.1
  • 26
    • 0032504147 scopus 로고    scopus 로고
    • Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation
    • Huang B, Gudi R, Wu P, Harris RA, Hamilton J, Popov KM (1998) Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation. J Biol Chem 273:17680-17688
    • (1998) J Biol Chem , vol.273 , pp. 17680-17688
    • Huang, B.1    Gudi, R.2    Wu, P.3    Harris, R.A.4    Hamilton, J.5    Popov, K.M.6
  • 27
    • 13444251422 scopus 로고    scopus 로고
    • Hubbard T, Andrews D, Caccamo M, Cameron G, Chen Y, Clamp M, Clarke L, Coates G, Cox T, Cunningham F, Curwen V, Cutts T, Down T, Durbin R, Fernandez-Suarez XM, Gilbert J, Hammond M, Herrero J, Hotz H, Howe K, Iyer V, Jekosch K, Kahari A, Kasprzyk A, Keefe D, Keenan S, Kokocinsci F, London D, Longden I, McVicker G, Melsopp C, Meidl P, Potter S, Proctor G, Rae M, Rios D, Schuster M, Searle S, Severin J, Slater G, Smedley D, Smith J, Spooner W, Stabenau A, Stalker J, Storey R, Trevanion S, Ureta-Vidal A, Vogel J, White S, Woodwark C, Birney E (2005) Ensembl 2005. Nucleic Acids Res 33:D447-D453
    • Hubbard T, Andrews D, Caccamo M, Cameron G, Chen Y, Clamp M, Clarke L, Coates G, Cox T, Cunningham F, Curwen V, Cutts T, Down T, Durbin R, Fernandez-Suarez XM, Gilbert J, Hammond M, Herrero J, Hotz H, Howe K, Iyer V, Jekosch K, Kahari A, Kasprzyk A, Keefe D, Keenan S, Kokocinsci F, London D, Longden I, McVicker G, Melsopp C, Meidl P, Potter S, Proctor G, Rae M, Rios D, Schuster M, Searle S, Severin J, Slater G, Smedley D, Smith J, Spooner W, Stabenau A, Stalker J, Storey R, Trevanion S, Ureta-Vidal A, Vogel J, White S, Woodwark C, Birney E (2005) Ensembl 2005. Nucleic Acids Res 33:D447-D453
  • 28
  • 29
    • 0036226603 scopus 로고    scopus 로고
    • BLAT - the BLAST-like alignment tool
    • Kent WJ (2002) BLAT - the BLAST-like alignment tool. Genome Res 12:656-664
    • (2002) Genome Res , vol.12 , pp. 656-664
    • Kent, W.J.1
  • 31
    • 0037133041 scopus 로고    scopus 로고
    • The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family
    • Koh CG, Tan EJ, Manser E, Lim L (2002) The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Curr Biol 12:317-321
    • (2002) Curr Biol , vol.12 , pp. 317-321
    • Koh, C.G.1    Tan, E.J.2    Manser, E.3    Lim, L.4
  • 33
    • 22044442973 scopus 로고    scopus 로고
    • Tyrosine kinases as targets for cancer therapy
    • Krause DS, Van Etten RA (2005) Tyrosine kinases as targets for cancer therapy. N Engl J Med 353:172-187
    • (2005) N Engl J Med , vol.353 , pp. 172-187
    • Krause, D.S.1    Van Etten, R.A.2
  • 34
    • 0031755555 scopus 로고    scopus 로고
    • A novel phosphatase regulating neurite extension on CNS inhibitors
    • Labes M, Roder J, Roach A (1998) A novel phosphatase regulating neurite extension on CNS inhibitors. Mol Cell Neurosci 12:29-47
    • (1998) Mol Cell Neurosci , vol.12 , pp. 29-47
    • Labes, M.1    Roder, J.2    Roach, A.3
  • 36
    • 0036911725 scopus 로고    scopus 로고
    • The human Hox-bearing chromosome regions did arise by block or chromosome (or even genome) duplications
    • Larhammar D, Lundin LG, Hallbook F (2002) The human Hox-bearing chromosome regions did arise by block or chromosome (or even genome) duplications. Genome Res 12:1910-1920
    • (2002) Genome Res , vol.12 , pp. 1910-1920
    • Larhammar, D.1    Lundin, L.G.2    Hallbook, F.3
  • 37
    • 15444357280 scopus 로고    scopus 로고
    • Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase
    • Lawson JE, Park SH, Mattison AR, Yan J, Reed LJ (1997) Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. J Biol Chem 272:31625-31629
    • (1997) J Biol Chem , vol.272 , pp. 31625-31629
    • Lawson, J.E.1    Park, S.H.2    Mattison, A.R.3    Yan, J.4    Reed, L.J.5
  • 38
    • 0035341207 scopus 로고    scopus 로고
    • Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1
    • Leung-Hagesteijn C, Mahendra A, Naruszewicz I, Hannigan GE (2001) Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1. EMBO J 20:2160-2170
    • (2001) EMBO J , vol.20 , pp. 2160-2170
    • Leung-Hagesteijn, C.1    Mahendra, A.2    Naruszewicz, I.3    Hannigan, G.E.4
  • 39
    • 0037809234 scopus 로고    scopus 로고
    • MG, Katsura K, Nomiyama H, Komaki K, Ninomiya-Tsuji J, Matsumoto K, Kobayashi T, Tamura S (2003) Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon). J Biol Chem 278:12013-12021
    • MG, Katsura K, Nomiyama H, Komaki K, Ninomiya-Tsuji J, Matsumoto K, Kobayashi T, Tamura S (2003) Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon). J Biol Chem 278:12013-12021
  • 40
    • 0026547155 scopus 로고
    • Mammalian protein serine/threonine phosphatase 2C: CDNA cloning and comparative analysis of amino acid sequences
    • Mann DJ, Campbell DG, McGowan CH, Cohen PT (1992) Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences. Biochim Biophys Acta 1130:100-104
    • (1992) Biochim Biophys Acta , vol.1130 , pp. 100-104
    • Mann, D.J.1    Campbell, D.G.2    McGowan, C.H.3    Cohen, P.T.4
  • 45
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods for protein sequences: Empirical Bayesian methods are superior
    • Mayrose I, Graur D, Ben-Tal N, Pupko T (2004) Comparison of site-specific rate-inference methods for protein sequences: empirical Bayesian methods are superior. Mol Biol Evol 21:1781-1791
    • (2004) Mol Biol Evol , vol.21 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Ben-Tal, N.3    Pupko, T.4
  • 46
    • 0036613237 scopus 로고    scopus 로고
    • Extensive genomic duplication during early chordate evolution
    • McLysaght A, Hokamp K, Wolfe KH (2002) Extensive genomic duplication during early chordate evolution. Nat Genet 31:200-204
    • (2002) Nat Genet , vol.31 , pp. 200-204
    • McLysaght, A.1    Hokamp, K.2    Wolfe, K.H.3
  • 48
    • 0035193659 scopus 로고    scopus 로고
    • Divergence pattern of animal gene families and relationship with the Cambrian explosion
    • Miyata T, Suga H (2001) Divergence pattern of animal gene families and relationship with the Cambrian explosion. Bioessays 23:1018-1027
    • (2001) Bioessays , vol.23 , pp. 1018-1027
    • Miyata, T.1    Suga, H.2
  • 49
    • 0032901297 scopus 로고    scopus 로고
    • The type 2C Ser/Thr phosphatase PP2Cgamma is a pre-mRNA splicing factor
    • Murray MV, Kobayashi R, Krainer AR (1999) The type 2C Ser/Thr phosphatase PP2Cgamma is a pre-mRNA splicing factor. Genes Dev 13:87-97
    • (1999) Genes Dev , vol.13 , pp. 87-97
    • Murray, M.V.1    Kobayashi, R.2    Krainer, A.R.3
  • 50
    • 0037515747 scopus 로고    scopus 로고
    • Cell cycle regulation and p53 activation by protein phosphatase 2C alpha
    • Ofek P, Ben-Meir D, Kariv-Inbal Z, Oren M, Lavi S (2003) Cell cycle regulation and p53 activation by protein phosphatase 2C alpha. J Biol Chem 278:14299-14305
    • (2003) J Biol Chem , vol.278 , pp. 14299-14305
    • Ofek, P.1    Ben-Meir, D.2    Kariv-Inbal, Z.3    Oren, M.4    Lavi, S.5
  • 52
    • 0345826130 scopus 로고    scopus 로고
    • Protein phosphatase 2Cbeta association with the IkappaB kinase complex is involved in regulating NF-kappaB activity
    • Prajapati S, Verma U, Yamamoto Y, Kwak YT, Gaynor RB (2004) Protein phosphatase 2Cbeta association with the IkappaB kinase complex is involved in regulating NF-kappaB activity. J Biol Chem 279:1739-1746
    • (2004) J Biol Chem , vol.279 , pp. 1739-1746
    • Prajapati, S.1    Verma, U.2    Yamamoto, Y.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 53
    • 0036382945 scopus 로고    scopus 로고
    • The Hox paradox: More complex(es) than imagined
    • Prince V (2002) The Hox paradox: more complex(es) than imagined. Dev Biol 249:1-15
    • (2002) Dev Biol , vol.249 , pp. 1-15
    • Prince, V.1
  • 54
    • 7944221188 scopus 로고    scopus 로고
    • An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-family Ser/Thr protein phosphatase
    • Pullen KE, Ng HL, Sung PY, Good MC, Smith SM, Alber T (2004) An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-family Ser/Thr protein phosphatase. Structure 12:1947-1954
    • (2004) Structure , vol.12 , pp. 1947-1954
    • Pullen, K.E.1    Ng, H.L.2    Sung, P.Y.3    Good, M.C.4    Smith, S.M.5    Alber, T.6
  • 55
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell RE, Mayrose I, Glaser F, Ben-Tal N (2002) Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 18 (Suppl 1):S71-S77
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 56
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103:211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 58
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases - new avenues for cell regulation
    • Shenolikar S (1994) Protein serine/threonine phosphatases - new avenues for cell regulation. Annu Rev Cell Biol 10:56-86
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 56-86
    • Shenolikar, S.1
  • 59
    • 0029346923 scopus 로고
    • Tyrosine kinases: Modular signaling enzymes with tunable specificities
    • Shokat KM (1995) Tyrosine kinases: modular signaling enzymes with tunable specificities. Chem Biol 2:509-514
    • (1995) Chem Biol , vol.2 , pp. 509-514
    • Shokat, K.M.1
  • 61
    • 0034723073 scopus 로고    scopus 로고
    • Protein phosphatase 2Calpha dephosphorylates axin and activates LEF-1-dependent transcription
    • Strovel ET, Wu D, Sussman DJ (2000) Protein phosphatase 2Calpha dephosphorylates axin and activates LEF-1-dependent transcription. J Biol Chem 275:2399-2403
    • (2000) J Biol Chem , vol.275 , pp. 2399-2403
    • Strovel, E.T.1    Wu, D.2    Sussman, D.J.3
  • 62
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signaling
    • Sun H, Tonks NK (1994) The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem Sci 19:480-485
    • (1994) Trends Biochem Sci , vol.19 , pp. 480-485
    • Sun, H.1    Tonks, N.K.2
  • 63
    • 0034383398 scopus 로고    scopus 로고
    • p53-inducible wip1 phosphatase mediates a negative feedback regulation of p38 MAPKp53 signaling in response to UV radiation
    • Takekawa M, Adachi M, Nakahata A, Nakayama I, Itoh F, Tsukuda H, Taya Y, Imai K (2000) p53-inducible wip1 phosphatase mediates a negative feedback regulation of p38 MAPKp53 signaling in response to UV radiation. EMBO J 19:6517-6526
    • (2000) EMBO J , vol.19 , pp. 6517-6526
    • Takekawa, M.1    Adachi, M.2    Nakahata, A.3    Nakayama, I.4    Itoh, F.5    Tsukuda, H.6    Taya, Y.7    Imai, K.8
  • 64
    • 0032541227 scopus 로고    scopus 로고
    • Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways
    • Takekawa M, Maeda T, Saito H (1998) Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J 17:4744-4752
    • (1998) EMBO J , vol.17 , pp. 4744-4752
    • Takekawa, M.1    Maeda, T.2    Saito, H.3
  • 67
    • 0030851204 scopus 로고    scopus 로고
    • PP2C gamma: A human protein phosphatase with a unique acidic domain
    • Travis SM, Welsh MJ (1997) PP2C gamma: a human protein phosphatase with a unique acidic domain. FEBS Lett 412:415-419
    • (1997) FEBS Lett , vol.412 , pp. 415-419
    • Travis, S.M.1    Welsh, M.J.2
  • 68
    • 18944395674 scopus 로고    scopus 로고
    • Clathrin heavy and light chain isoforms originated by independent mechanisms of gene duplication during chordate evolution
    • Wakeham DE, Abi-Rached L, Towler MC, Wilbur JD, Parham P, Brodsky FM (2005) Clathrin heavy and light chain isoforms originated by independent mechanisms of gene duplication during chordate evolution. Proc Natl Acad Sci USA 102:7209-7214
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7209-7214
    • Wakeham, D.E.1    Abi-Rached, L.2    Towler, M.C.3    Wilbur, J.D.4    Parham, P.5    Brodsky, F.M.6
  • 70
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera S, Hemmings BA (1995) Serine/threonine protein phosphatases. Biochem J 311(Pt 1):17-29
    • (1995) Biochem J , vol.311 , Issue.PART 1 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 72
    • 0034097381 scopus 로고    scopus 로고
    • Codonsubstitution models for heterogeneous selection pressure at amino acid sites
    • Yang Z, Nielsen R, Goldman N, Pedersen AM (2000) Codonsubstitution models for heterogeneous selection pressure at amino acid sites. Genetics 155:431-449
    • (2000) Genetics , vol.155 , pp. 431-449
    • Yang, Z.1    Nielsen, R.2    Goldman, N.3    Pedersen, A.M.4
  • 73
    • 0032863261 scopus 로고    scopus 로고
    • The Janus kinase family of protein tyrosine kinases and their role in signaling
    • Yeh TC, Pellegrini S (1999) The Janus kinase family of protein tyrosine kinases and their role in signaling. Cell Mol Life Sci 55:1523-1534
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1523-1534
    • Yeh, T.C.1    Pellegrini, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.