메뉴 건너뛰기




Volumn 204, Issue 1, 2014, Pages 95-109

Cytoplasmic protein methylation is essential for neural crest migration

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSYLHOMOCYSTEINASE; CYTOPLASM PROTEIN; ELONGATION FACTOR 1ALPHA; LYSINE; MESSENGER RNA;

EID: 84891896208     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201306071     Document Type: Article
Times cited : (28)

References (89)
  • 1
    • 42149176677 scopus 로고    scopus 로고
    • Discovery of transcription factors and other candidate regulators of neural crest development
    • Adams, M.S., L.S. Gammill, and M. Bronner-Fraser. 2008. Discovery of transcription factors and other candidate regulators of neural crest development. Dev. Dyn. 237:1021-1033. http://dx.doi.org/10.1002/dvdy.21513
    • (2008) Dev. Dyn. , vol.237 , pp. 1021-1033
    • Adams, M.S.1    Gammill, L.S.2    Bronner-Fraser, M.3
  • 2
    • 50649090270 scopus 로고    scopus 로고
    • Cortactin branches out: roles in regulating protrusive actin dynamics
    • Ammer, A.G., and S.A. Weed. 2008. Cortactin branches out: roles in regulating protrusive actin dynamics. Cell Motil. Cytoskeleton. 65:687-707. http://dx.doi.org/10.1002/cm.20296
    • (2008) Cell Motil. Cytoskeleton. , vol.65 , pp. 687-707
    • Ammer, A.G.1    Weed, S.A.2
  • 4
    • 78049246250 scopus 로고    scopus 로고
    • Fast signals and slow marks: the dynamics of histone modifications
    • Barth, T.K., and A. Imhof. 2010. Fast signals and slow marks: the dynamics of histone modifications. Trends Biochem. Sci. 35:618-626. http://dx.doi.org/10.1016/j.tibs.2010.05.006
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 618-626
    • Barth, T.K.1    Imhof, A.2
  • 5
    • 33646595985 scopus 로고    scopus 로고
    • Specification of the neural crest occurs during gastrulation and requires Pax7
    • Basch, M.L., M. Bronner-Fraser, and M.I. García-Castro. 2006. Specification of the neural crest occurs during gastrulation and requires Pax7. Nature. 441:218-222. http://dx.doi.org/10.1038/nature04684
    • (2006) Nature. , vol.441 , pp. 218-222
    • Basch, M.L.1    Bronner-Fraser, M.2    García-Castro, M.I.3
  • 6
    • 84873198265 scopus 로고    scopus 로고
    • Detection of the Wolbachia-encoded DNA binding protein, HU beta, in mosquito gonads
    • Beckmann, J.F., T.W. Markowski, B.A. Witthuhn, and A.M. Fallon. 2013. Detection of the Wolbachia-encoded DNA binding protein, HU beta, in mosquito gonads. Insect Biochem. Mol. Biol. 43:272-279. http://dx.doi.org/10.1016/j.ibmb.2012.12.007
    • (2013) Insect Biochem. Mol. Biol. , vol.43 , pp. 272-279
    • Beckmann, J.F.1    Markowski, T.W.2    Witthuhn, B.A.3    Fallon, A.M.4
  • 7
    • 56449110468 scopus 로고    scopus 로고
    • Rho-kinase and myosin II affect dynamic neural crest cell behaviors during epithelial to mesenchymal transition in vivo
    • Berndt, J.D., M.R. Clay, T. Langenberg, and M.C. Halloran. 2008. Rho-kinase and myosin II affect dynamic neural crest cell behaviors during epithelial to mesenchymal transition in vivo. Dev. Biol. 324:236-244. http://dx.doi.org/10.1016/j.ydbio.2008.09.013
    • (2008) Dev. Biol. , vol.324 , pp. 236-244
    • Berndt, J.D.1    Clay, M.R.2    Langenberg, T.3    Halloran, M.C.4
  • 8
    • 84856531511 scopus 로고    scopus 로고
    • Offthe beaten paths: alternative and crosstalk regulation of Rho GTPases
    • Boulter, E., S. Estrach, R. Garcia-Mata, and C.C. Féral. 2012. Offthe beaten paths: alternative and crosstalk regulation of Rho GTPases. FASEB J. 26:469-479. http://dx.doi.org/10.1096/fj.11-192252
    • (2012) FASEB J. , vol.26 , pp. 469-479
    • Boulter, E.1    Estrach, S.2    Garcia-Mata, R.3    Féral, C.C.4
  • 9
    • 43149111032 scopus 로고    scopus 로고
    • Manipulations of neural crest cells or their migratory pathways
    • Bronner-Fraser, M., and M. García-Castro. 2008. Manipulations of neural crest cells or their migratory pathways. Methods Cell Biol. 87:75-96. http://dx.doi.org/10.1016/S0091-679X(08)00204-5
    • (2008) Methods Cell Biol. , vol.87 , pp. 75-96
    • Bronner-Fraser, M.1    García-Castro, M.2
  • 11
    • 0027406211 scopus 로고
    • Characterization of yeast EF-1 alpha: non-conservation of post-translational modifications
    • Cavallius, J., W. Zoll, K. Chakraburtty, and W.C. Merrick. 1993. Characterization of yeast EF-1 alpha: non-conservation of post-translational modifications. Biochim. Biophys. Acta. 1163:75-80. http://dx.doi.org/10.1016/0167-4838(93)90281-U
    • (1993) Biochim. Biophys. Acta. , vol.1163 , pp. 75-80
    • Cavallius, J.1    Zoll, W.2    Chakraburtty, K.3    Merrick, W.C.4
  • 12
    • 0031588970 scopus 로고    scopus 로고
    • Site-directed mutants of posttranslationally modified sites of yeast eEF1A using a shuttle vector containing a chromogenic switch
    • Cavallius, J., A.P. Popkie, and W.C. Merrick. 1997. Site-directed mutants of posttranslationally modified sites of yeast eEF1A using a shuttle vector containing a chromogenic switch. Biochim. Biophys. Acta. 1350:345-358. http://dx.doi.org/10.1016/S0167-4781(96)00181-9
    • (1997) Biochim. Biophys. Acta. , vol.1350 , pp. 345-358
    • Cavallius, J.1    Popkie, A.P.2    Merrick, W.C.3
  • 13
    • 0034733795 scopus 로고    scopus 로고
    • Chick sox10, a transcription factor expressed in both early neural crest cells and central nervous system
    • Cheng, Y., M. Cheung, M.M. Abu-Elmagd, A. Orme, and P.J. Scotting. 2000. Chick sox10, a transcription factor expressed in both early neural crest cells and central nervous system. Brain Res. Dev. Brain Res. 121:233-241. http://dx.doi.org/10.1016/S0165-3806(00)00049-3
    • (2000) Brain Res. Dev. Brain Res. , vol.121 , pp. 233-241
    • Cheng, Y.1    Cheung, M.2    Abu-Elmagd, M.M.3    Orme, A.4    Scotting, P.J.5
  • 15
    • 84867026199 scopus 로고    scopus 로고
    • Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B
    • Cho, H.S., T. Shimazu, G. Toyokawa, Y. Daigo, Y. Maehara, S. Hayami, A. Ito, K. Masuda, N. Ikawa, H.I. Field, et al. 2012. Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B. Nat Commun. 3:1072. http://dx.doi.org/10.1038/ncomms2074
    • (2012) Nat Commun. , vol.3 , pp. 1072
    • Cho, H.S.1    Shimazu, T.2    Toyokawa, G.3    Daigo, Y.4    Maehara, Y.5    Hayami, S.6    Ito, A.7    Masuda, K.8    Ikawa, N.9    Field, H.I.10
  • 17
    • 79952071213 scopus 로고    scopus 로고
    • Regulation of cell adhesions and motility during initiation of neural crest migration
    • Clay, M.R., and M.C. Halloran. 2011. Regulation of cell adhesions and motility during initiation of neural crest migration. Curr. Opin. Neurobiol. 21:17-22. http://dx.doi.org/10.1016/j.conb.2010.09.013
    • (2011) Curr. Opin. Neurobiol. , vol.21 , pp. 17-22
    • Clay, M.R.1    Halloran, M.C.2
  • 18
    • 0028670656 scopus 로고
    • Elongation factor 1 alpha is a component of the subcortical actin bundles of characean algae
    • Collings, D.A., G.O. Wasteneys, M. Miyazaki, and R.E. Williamson. 1994. Elongation factor 1 alpha is a component of the subcortical actin bundles of characean algae. Cell Biol. Int. 18:1019-1024. http://dx.doi.org/10.1006/cbir.1994.1025
    • (1994) Cell Biol. Int. , vol.18 , pp. 1019-1024
    • Collings, D.A.1    Wasteneys, G.O.2    Miyazaki, M.3    Williamson, R.E.4
  • 19
    • 13544257399 scopus 로고    scopus 로고
    • How and why does beta-actin mRNA target?
    • Condeelis, J., and R.H. Singer. 2005. How and why does beta-actin mRNA target? Biol. Cell. 97:97-110. http://dx.doi.org/10.1042/BC20040063
    • (2005) Biol. Cell. , vol.97 , pp. 97-110
    • Condeelis, J.1    Singer, R.H.2
  • 20
    • 84859998371 scopus 로고    scopus 로고
    • Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases
    • Couttas, T.A., M.J. Raftery, M.P. Padula, B.R. Herbert, and M.R. Wilkins. 2012. Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases. Proteomics. 12:960-972. http://dx.doi.org/10.1002/pmic.201100570
    • (2012) Proteomics. , vol.12 , pp. 960-972
    • Couttas, T.A.1    Raftery, M.J.2    Padula, M.P.3    Herbert, B.R.4    Wilkins, M.R.5
  • 21
    • 21244479003 scopus 로고    scopus 로고
    • Essential role of non-canonical Wnt signalling in neural crest migration
    • De Calisto, J., C. Araya, L. Marchant, C.F. Riaz, and R. Mayor. 2005. Essential role of non-canonical Wnt signalling in neural crest migration. Development. 132:2587-2597. http://dx.doi.org/10.1242/dev.01857
    • (2005) Development. , vol.132 , pp. 2587-2597
    • De Calisto, J.1    Araya, C.2    Marchant, L.3    Riaz, C.F.4    Mayor, R.5
  • 22
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine trimethyllysine, and glycerylphosphorylethanolamine
    • Dever, T.E., C.E. Costello, C.L. Owens, T.L. Rosenberry, and W.C. Merrick. 1989. Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. J. Biol. Chem. 264:20518-20525.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.E.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 23
    • 0026320055 scopus 로고
    • Compartmentalization and actin binding properties of ABP-50: the elongation factor-1 alpha of Dictyostelium
    • Dharmawardhane, S., M. Demma, F. Yang, and J. Condeelis. 1991. Compartmentalization and actin binding properties of ABP-50: the elongation factor-1 alpha of Dictyostelium. Cell Motil. Cytoskeleton. 20:279-288. http://dx.doi.org/10.1002/cm.970200404
    • (1991) Cell Motil. Cytoskeleton. , vol.20 , pp. 279-288
    • Dharmawardhane, S.1    Demma, M.2    Yang, F.3    Condeelis, J.4
  • 24
    • 84916639710 scopus 로고    scopus 로고
    • Methylation: From DNA RNA, Histones to Diseases and Treatment
    • E. Dricu, editor. InTech. Rijeka, Croatia
    • Dricu, E. 2012 Methylation: From DNA, RNA and Histones to Diseases and Treatment. E. Dricu, editor. InTech. Rijeka, Croatia. 301 pp.
    • (2012) , pp. 301
    • Dricu, E.1
  • 25
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha
    • Edmonds, B.T., J. Murray, and J. Condeelis. 1995. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha. J. Biol. Chem. 270:15222-15230. http://dx.doi.org/10.1074/jbc.270.25.15222
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 26
    • 80053418255 scopus 로고    scopus 로고
    • Primary culture of chick, mouse or human neural crest cells
    • Etchevers, H. 2011. Primary culture of chick, mouse or human neural crest cells. Nat. Protoc. 6:1568-1577. http://dx.doi.org/10.1038/nprot.2011.398
    • (2011) Nat. Protoc. , vol.6 , pp. 1568-1577
    • Etchevers, H.1
  • 27
    • 0028142918 scopus 로고
    • Effects of novel anti-viral adenosine analogues on the activity of S-adenosylhomocysteine hydrolase from human liver
    • Fabianowska-Majewska, K., J.A. Duley, and H.A. Simmonds. 1994. Effects of novel anti-viral adenosine analogues on the activity of S-adenosylhomocysteine hydrolase from human liver. Biochem. Pharmacol. 48:897-903. http://dx.doi.org/10.1016/0006-2952(94)90360-3
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 897-903
    • Fabianowska-Majewska, K.1    Duley, J.A.2    Simmonds, H.A.3
  • 28
    • 0036927690 scopus 로고    scopus 로고
    • Genomic analysis of neural crest induction
    • Gammill, L.S., and M. Bronner-Fraser. 2002. Genomic analysis of neural crest induction. Development. 129:5731-5741. http://dx.doi.org/10.1242/dev.00175
    • (2002) Development. , vol.129 , pp. 5731-5741
    • Gammill, L.S.1    Bronner-Fraser, M.2
  • 29
    • 80052937400 scopus 로고    scopus 로고
    • Embryological and genetic manipulation of chick development
    • Gammill, L.S., and C.E. Krull. 2011. Embryological and genetic manipulation of chick development. Methods Mol. Biol. 770:119-137. http://dx.doi.org/10.1007/978-1-61779-210-6_5
    • (2011) Methods Mol. Biol. , vol.770 , pp. 119-137
    • Gammill, L.S.1    Krull, C.E.2
  • 30
    • 0031021578 scopus 로고    scopus 로고
    • Structure and transcription of the gene for translation elongation factor 1 subunit alpha of zebrafish (Danio rerio)
    • Gao, D., Z. Li, T. Murphy, and W. Sauerbier. 1997. Structure and transcription of the gene for translation elongation factor 1 subunit alpha of zebrafish (Danio rerio). Biochim. Biophys. Acta. 1350:1-5. http://dx.doi.org/10.1016/S0167-4781(96)00179-0
    • (1997) Biochim. Biophys. Acta. , vol.1350 , pp. 1-5
    • Gao, D.1    Li, Z.2    Murphy, T.3    Sauerbier, W.4
  • 31
    • 77956194960 scopus 로고    scopus 로고
    • Methylation of the tumor suppressor protein, BRCA1, influences its transcriptional cofactor function
    • Guendel, I., L. Carpio, C. Pedati, A. Schwartz, C. Teal, F. Kashanchi, and K. Kehn-Hall. 2010. Methylation of the tumor suppressor protein, BRCA1, influences its transcriptional cofactor function. PLoS ONE. 5:e11379. http://dx.doi.org/10.1371/journal.pone.0011379
    • (2010) PLoS ONE. , vol.5
    • Guendel, I.1    Carpio, L.2    Pedati, C.3    Schwartz, A.4    Teal, C.5    Kashanchi, F.6    Kehn-Hall, K.7
  • 32
    • 69449100707 scopus 로고    scopus 로고
    • The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis
    • Guerrier, S., J. Coutinho-Budd, T. Sassa, A. Gresset, N.V. Jordan, K. Chen, W.L. Jin, A. Frost, and F. Polleux. 2009. The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis. Cell. 138:990-1004. http://dx.doi.org/10.1016/j.cell.2009.06.047
    • (2009) Cell. , vol.138 , pp. 990-1004
    • Guerrier, S.1    Coutinho-Budd, J.2    Sassa, T.3    Gresset, A.4    Jordan, N.V.5    Chen, K.6    Jin, W.L.7    Frost, A.8    Polleux, F.9
  • 33
    • 78049388286 scopus 로고    scopus 로고
    • srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization
    • Guo, S., and S. Bao. 2010. srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization. J. Biol. Chem. 285:35133-35141. http://dx.doi.org/10.1074/jbc. M110.153429
    • (2010) J. Biol. Chem. , vol.285 , pp. 35133-35141
    • Guo, S.1    Bao, S.2
  • 34
    • 0027018236 scopus 로고
    • A series of normal stages in the development of the chick embryo
    • Hamburger, V., and H.L. Hamilton. 1992. A series of normal stages in the development of the chick embryo. 1951. Dev. Dyn. 195:231-272. http://dx.doi.org/10.1002/aja.1001950404
    • (1992) 1951. Dev. Dyn. , vol.195 , pp. 231-272
    • Hamburger, V.1    Hamilton, H.L.2
  • 35
    • 80053451459 scopus 로고    scopus 로고
    • The motility of a human parasite, Toxoplasma gondii, is regulated by a novel lysine methyltransferase
    • Heaslip, A.T., M. Nishi, B. Stein, and K. Hu. 2011. The motility of a human parasite, Toxoplasma gondii, is regulated by a novel lysine methyltransferase. PLoS Pathog. 7:e1002201. http://dx.doi.org/10.1371/journal.ppat.1002201
    • (2011) PLoS Pathog. , vol.7
    • Heaslip, A.T.1    Nishi, M.2    Stein, B.3    Hu, K.4
  • 36
    • 0018075296 scopus 로고
    • S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity
    • Hershfield, M.S., and N.M. Krodich. 1978. S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity. Science. 202:757-760. http://dx.doi.org/10.1126/science.715439
    • (1978) Science. , vol.202 , pp. 757-760
    • Hershfield, M.S.1    Krodich, N.M.2
  • 37
    • 0019932647 scopus 로고
    • Methylation of elongation factor 1 alpha from the fungus Mucor
    • Hiatt, W.R., R. Garcia, W.C. Merrick, and P.S. Sypherd. 1982. Methylation of elongation factor 1 alpha from the fungus Mucor. Proc. Natl. Acad. Sci. USA. 79:3433-3437. http://dx.doi.org/10.1073/pnas.79.11.3433
    • (1982) Proc. Natl. Acad. Sci. USA. , vol.79 , pp. 3433-3437
    • Hiatt, W.R.1    Garcia, R.2    Merrick, W.C.3    Sypherd, P.S.4
  • 38
    • 84868519673 scopus 로고    scopus 로고
    • DNA methyltransferase3A as a molecular switch mediating the neural tubeto-neural crest fate transition
    • Hu, N., P. Strobl-Mazzulla, T. Sauka-Spengler, and M.E. Bronner. 2012. DNA methyltransferase3A as a molecular switch mediating the neural tubeto-neural crest fate transition. Genes Dev. 26:2380-2385. http://dx.doi.org/10.1101/gad.198747.112
    • (2012) Genes Dev. , vol.26 , pp. 2380-2385
    • Hu, N.1    Strobl-Mazzulla, P.2    Sauka-Spengler, T.3    Bronner, M.E.4
  • 39
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of non-histone proteins
    • Huang, J., and S.L. Berger. 2008. The emerging field of dynamic lysine methylation of non-histone proteins. Curr. Opin. Genet. Dev. 18:152-158. http://dx.doi.org/10.1016/j.gde.2008.01.012
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 40
    • 65249146059 scopus 로고    scopus 로고
    • Lysine methylation of nuclear co-repressor receptor interacting protein 140
    • Huq, M.D., S.G. Ha, H. Barcelona, and L.N. Wei. 2009. Lysine methylation of nuclear co-repressor receptor interacting protein 140. J. Proteome Res. 8:1156-1167. http://dx.doi.org/10.1021/pr800569c
    • (2009) J. Proteome Res. , vol.8 , pp. 1156-1167
    • Huq, M.D.1    Ha, S.G.2    Barcelona, H.3    Wei, L.N.4
  • 41
    • 29544438797 scopus 로고    scopus 로고
    • Proteomic analysis of organspecific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies
    • Iwabata, H., M. Yoshida, and Y. Komatsu. 2005. Proteomic analysis of organspecific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies. Proteomics. 5:4653-4664. http://dx.doi.org/10.1002/pmic.200500042
    • (2005) Proteomics. , vol.5 , pp. 4653-4664
    • Iwabata, H.1    Yoshida, M.2    Komatsu, Y.3
  • 43
    • 0028027909 scopus 로고
    • Sequences responsible for intracellular localization of beta-actin messenger RNA also affect cell phenotype
    • Kislauskis, E.H., X. Zhu, and R.H. Singer. 1994. Sequences responsible for intracellular localization of beta-actin messenger RNA also affect cell phenotype. J. Cell Biol. 127:441-451. http://dx.doi.org/10.1083/jcb.127.2.441
    • (1994) J. Cell Biol. , vol.127 , pp. 441-451
    • Kislauskis, E.H.1    Zhu, X.2    Singer, R.H.3
  • 44
    • 0030766557 scopus 로고    scopus 로고
    • beta-Actin messenger RNA localization and protein synthesis augment cell motility
    • Kislauskis, E.H., X. Zhu, and R.H. Singer. 1997. beta-Actin messenger RNA localization and protein synthesis augment cell motility. J. Cell Biol. 136:1263-1270. http://dx.doi.org/10.1083/jcb.136.6.1263
    • (1997) J. Cell Biol. , vol.136 , pp. 1263-1270
    • Kislauskis, E.H.1    Zhu, X.2    Singer, R.H.3
  • 45
    • 0032992945 scopus 로고    scopus 로고
    • ATP depletion, purine riboside triphosphate accumulation and rat thymocyte death induced by purine riboside
    • Kozlowska, M., R.T. Smolenski, W. Makarewicz, C. Hoffmann, B. Jastorff, and J. Swierczynski. 1999. ATP depletion, purine riboside triphosphate accumulation and rat thymocyte death induced by purine riboside. Toxicol. Lett. 104:171-181. http://dx.doi.org/10.1016/S0378-4274(98)00369-5
    • (1999) Toxicol. Lett. , vol.104 , pp. 171-181
    • Kozlowska, M.1    Smolenski, R.T.2    Makarewicz, W.3    Hoffmann, C.4    Jastorff, B.5    Swierczynski, J.6
  • 46
    • 0034034793 scopus 로고    scopus 로고
    • In ovo time-lapse analysis of chick hindbrain neural crest cell migration shows cell interactions during migration to the branchial arches
    • Kulesa, P.M., and S.E. Fraser. 2000. In ovo time-lapse analysis of chick hindbrain neural crest cell migration shows cell interactions during migration to the branchial arches. Development. 127:1161-1172.
    • (2000) Development. , vol.127 , pp. 1161-1172
    • Kulesa, P.M.1    Fraser, S.E.2
  • 47
    • 77955280367 scopus 로고    scopus 로고
    • Neural crest migration: patterns, phases and signals
    • Kulesa, P.M., and L.S. Gammill. 2010. Neural crest migration: patterns, phases and signals. Dev. Biol. 344:566-568. http://dx.doi.org/10.1016/j.ydbio.2010.05.005
    • (2010) Dev. Biol. , vol.344 , pp. 566-568
    • Kulesa, P.M.1    Gammill, L.S.2
  • 48
    • 84863066260 scopus 로고    scopus 로고
    • Nuclear targeting of methyl-recycling enzymes in Arabidopsis thaliana is mediated by specific protein interactions
    • Lee, S., A.C. Doxey, B.J. McConkey, and B.A. Moffatt. 2012. Nuclear targeting of methyl-recycling enzymes in Arabidopsis thaliana is mediated by specific protein interactions. Mol. Plant. 5:231-248. http://dx.doi.org/10.1093/mp/ssr083
    • (2012) Mol. Plant. , vol.5 , pp. 231-248
    • Lee, S.1    Doxey, A.C.2    McConkey, B.J.3    Moffatt, B.A.4
  • 49
    • 43149124178 scopus 로고    scopus 로고
    • Neural crest, sensory neuron, and muscle cultures
    • Lee, V.M., and P.Y. Lwigale. 2008. Neural crest, sensory neuron, and muscle cultures. Methods Cell Biol. 87:115-133. http://dx.doi.org/10.1016/S0091-679X(08)00206-9
    • (2008) Methods Cell Biol. , vol.87 , pp. 115-133
    • Lee, V.M.1    Lwigale, P.Y.2
  • 50
    • 80054815567 scopus 로고    scopus 로고
    • A proteomic approach for the identification of novel lysine methyltransferase substrates
    • Levy, D., C.L. Liu, Z. Yang, A.M. Newman, A.A. Alizadeh, P.J. Utz, and O. Gozani. 2011. A proteomic approach for the identification of novel lysine methyltransferase substrates. Epigenetics Chromatin. 4:19. http://dx.doi.org/10.1186/1756-8935-4-19
    • (2011) Epigenetics Chromatin. , vol.4 , pp. 19
    • Levy, D.1    Liu, C.L.2    Yang, Z.3    Newman, A.M.4    Alizadeh, A.A.5    Utz, P.J.6    Gozani, O.7
  • 51
    • 84872057373 scopus 로고    scopus 로고
    • Re-evaluation of the role of calcium homeostasis endoplasmic reticulum protein (CHERP) in cellular calcium signaling
    • Lin-Moshier, Y., P.J. Sebastian, L. Higgins, N.D. Sampson, J.E. Hewitt, and J.S. Marchant. 2013. Re-evaluation of the role of calcium homeostasis endoplasmic reticulum protein (CHERP) in cellular calcium signaling. J. Biol. Chem. 288:355-367. http://dx.doi.org/10.1074/jbc. M112.405761
    • (2013) J. Biol. Chem. , vol.288 , pp. 355-367
    • Lin-Moshier, Y.1    Sebastian, P.J.2    Higgins, L.3    Sampson, N.D.4    Hewitt, J.E.5    Marchant, J.S.6
  • 52
    • 77954621487 scopus 로고    scopus 로고
    • Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae
    • Lipson, R.S., K.J. Webb, and S.G. Clarke. 2010. Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 500:137-143. http://dx.doi.org/10.1016/j.abb.2010.05.023
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 137-143
    • Lipson, R.S.1    Webb, K.J.2    Clarke, S.G.3
  • 53
    • 0036175770 scopus 로고    scopus 로고
    • Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions
    • Liu, G., W.M. Grant, D. Persky, V.M. Latham Jr., R.H. Singer, and J. Condeelis. 2002. Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions. Mol. Biol. Cell. 13:579-592. http://dx.doi.org/10.1091/mbc.01-03-0140
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 579-592
    • Liu, G.1    Grant, W.M.2    Persky, D.3    Latham Jr., V.M.4    Singer, R.H.5    Condeelis, J.6
  • 54
    • 79960976768 scopus 로고    scopus 로고
    • UniProt Knowledgebase: a hub of integrated protein data
    • Database (Oxford).
    • Magrane, M., and U. Consortium. 2011. UniProt Knowledgebase: a hub of integrated protein data. Database (Oxford). 2011:bar009.
    • (2011) , pp. 009
    • Magrane, M.1    Consortium, U.2
  • 55
    • 49949088657 scopus 로고    scopus 로고
    • Directional migration of neural crest cells in vivo is regulated by Syndecan-4/Rac1 and non-canonical Wnt signaling/RhoA
    • Matthews, H.K., L. Marchant, C. Carmona-Fontaine, S. Kuriyama, J. Larraín, M.R. Holt, M. Parsons, and R. Mayor. 2008. Directional migration of neural crest cells in vivo is regulated by Syndecan-4/Rac1 and non-canonical Wnt signaling/RhoA. Development. 135:1771-1780. http://dx.doi.org/10.1242/dev.017350
    • (2008) Development. , vol.135 , pp. 1771-1780
    • Matthews, H.K.1    Marchant, L.2    Carmona-Fontaine, C.3    Kuriyama, S.4    Larraín, J.5    Holt, M.R.6    Parsons, M.7    Mayor, R.8
  • 56
    • 84887203696 scopus 로고    scopus 로고
    • A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation
    • Moore, K.E., S.M. Carlson, N.D. Camp, P. Cheung, R.G. James, K.F. Chua, A. Wolf-Yadlin, and O. Gozani. 2013. A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation. Mol. Cell. 50:444-456. http://dx.doi.org/10.1016/j.molcel.2013.03.005
    • (2013) Mol. Cell. , vol.50 , pp. 444-456
    • Moore, K.E.1    Carlson, S.M.2    Camp, N.D.3    Cheung, P.4    James, R.G.5    Chua, K.F.6    Wolf-Yadlin, A.7    Gozani, O.8
  • 57
    • 0030471363 scopus 로고    scopus 로고
    • Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends
    • Murray, J.W., B.T. Edmonds, G. Liu, and J. Condeelis. 1996. Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends. J. Cell Biol. 135:1309-1321. http://dx.doi.org/10.1083/jcb.135.5.1309
    • (1996) J. Cell Biol. , vol.135 , pp. 1309-1321
    • Murray, J.W.1    Edmonds, B.T.2    Liu, G.3    Condeelis, J.4
  • 58
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S.E., G. Mittler, and M. Mann. 2004. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods. 1:119-126. http://dx.doi.org/10.1038/nmeth715
    • (2004) Nat. Methods. , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 59
    • 77649090565 scopus 로고    scopus 로고
    • Identification of arginineand lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications
    • Pang, C.N., E. Gasteiger, and M.R. Wilkins. 2010. Identification of arginineand lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications. BMC Genomics. 11:92. http://dx.doi.org/10.1186/1471-2164-11-92
    • (2010) BMC Genomics. , vol.11 , pp. 92
    • Pang, C.N.1    Gasteiger, E.2    Wilkins, M.R.3
  • 60
    • 34447581084 scopus 로고    scopus 로고
    • Methylation of proteins involved in translation
    • Polevoda, B., and F. Sherman. 2007. Methylation of proteins involved in translation. Mol. Microbiol. 65:590-606. http://dx.doi.org/10.1111/j.1365-2958.2007.05831.x
    • (2007) Mol. Microbiol. , vol.65 , pp. 590-606
    • Polevoda, B.1    Sherman, F.2
  • 61
    • 84860838210 scopus 로고    scopus 로고
    • Induction of the neural crest state: control of stem cell attributes by gene regulatory, posttranscriptional and epigenetic interactions
    • Prasad, M.S., T. Sauka-Spengler, and C. LaBonne. 2012. Induction of the neural crest state: control of stem cell attributes by gene regulatory, posttranscriptional and epigenetic interactions. Dev. Biol. 366:10-21. http://dx.doi.org/10.1016/j.ydbio.2012.03.014
    • (2012) Dev. Biol. , vol.366 , pp. 10-21
    • Prasad, M.S.1    Sauka-Spengler, T.2    LaBonne, C.3
  • 62
    • 84891900340 scopus 로고    scopus 로고
    • R Development Core Team. R: A Language Environment for Statistical Computing. Vienna Austria: R Foundation for Statistical Computing. Retrieved from
    • R Development Core Team. 2011. R: A Language and Environment for Statistical Computing. Vienna, Austria: R Foundation for Statistical Computing. Retrieved from http://www. R-project.org.
    • (2011)
  • 63
    • 0032734241 scopus 로고    scopus 로고
    • Nuclear accumulation of Sadenosylhomocysteine hydrolase in transcriptionally active cells during development of Xenopus laevis
    • Radomski, N., C. Kaufmann, and C. Dreyer. 1999. Nuclear accumulation of Sadenosylhomocysteine hydrolase in transcriptionally active cells during development of Xenopus laevis. Mol. Biol. Cell. 10:4283-4298. http://dx.doi.org/10.1091/mbc.10.12.4283
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 4283-4298
    • Radomski, N.1    Kaufmann, C.2    Dreyer, C.3
  • 64
    • 0037067183 scopus 로고    scopus 로고
    • Interaction of S-adenosylhomocysteine hydrolase of Xenopus laevis with mRNA(guanine-7-)methyltransferase: implication on its nuclear compartmentalisation and on cap methylation of hnRNA
    • Radomski, N., G. Barreto, C. Kaufmann, J. Yokoska, K. Mizumoto, and C. Dreyer. 2002. Interaction of S-adenosylhomocysteine hydrolase of Xenopus laevis with mRNA(guanine-7-)methyltransferase: implication on its nuclear compartmentalisation and on cap methylation of hnRNA. Biochim. Biophys. Acta. 1590:93-102. http://dx.doi.org/10.1016/S0167-4889(02)00205-7
    • (2002) Biochim. Biophys. Acta. , vol.1590 , pp. 93-102
    • Radomski, N.1    Barreto, G.2    Kaufmann, C.3    Yokoska, J.4    Mizumoto, K.5    Dreyer, C.6
  • 65
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J., Y. Ishihama, and M. Mann. 2003. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75:663-670. http://dx.doi.org/10.1021/ac026117i
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 66
    • 0025027287 scopus 로고
    • Eukaryotic protein elongation factors
    • Riis, B., S.I. Rattan, B.F. Clark, and W.C. Merrick. 1990. Eukaryotic protein elongation factors. Trends Biochem. Sci. 15:420-424. http://dx.doi.org/10.1016/0968-0004(90)90279-K
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 420-424
    • Riis, B.1    Rattan, S.I.2    Clark, B.F.3    Merrick, W.C.4
  • 67
    • 84867142212 scopus 로고    scopus 로고
    • Paladin is an antiphosphatase that regulates neural crest cell formation and migration
    • Roffers-Agarwal, J., K.J. Hutt, and L.S. Gammill. 2012. Paladin is an antiphosphatase that regulates neural crest cell formation and migration. Dev. Biol. 371:180-190. http://dx.doi.org/10.1016/j.ydbio.2012.08.007
    • (2012) Dev. Biol. , vol.371 , pp. 180-190
    • Roffers-Agarwal, J.1    Hutt, K.J.2    Gammill, L.S.3
  • 68
    • 80053328974 scopus 로고    scopus 로고
    • Actin dynamics and turnover in cell motility
    • Rottner, K., and T.E. Stradal. 2011. Actin dynamics and turnover in cell motility. Curr. Opin. Cell Biol. 23:569-578. http://dx.doi.org/10.1016/j.ceb.2011.07.003
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 569-578
    • Rottner, K.1    Stradal, T.E.2
  • 69
    • 84856267593 scopus 로고    scopus 로고
    • Ubiquitin links to cytoskeletal dynamics, cell adhesion and migration
    • Schaefer, A., M. Nethe, and P.L. Hordijk. 2012. Ubiquitin links to cytoskeletal dynamics, cell adhesion and migration. Biochem. J. 442:13-25. http://dx.doi.org/10.1042/BJ20111815
    • (2012) Biochem. J. , vol.442 , pp. 13-25
    • Schaefer, A.1    Nethe, M.2    Hordijk, P.L.3
  • 70
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., W.S. Rasband, and K.W. Eliceiri. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods. 9:671-675. http://dx.doi.org/10.1038/nmeth.2089
    • (2012) Nat. Methods. , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 71
    • 0024805295 scopus 로고
    • Role of lysine methylation in the activities of elongation factor 1 alpha
    • Sherman, M., and P.S. Sypherd. 1989. Role of lysine methylation in the activities of elongation factor 1 alpha. Arch. Biochem. Biophys. 275:371-378. http://dx.doi.org/10.1016/0003-9861(89)90384-6
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 371-378
    • Sherman, M.1    Sypherd, P.S.2
  • 72
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:850-858. http://dx.doi.org/10.1021/ac950914h
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 73
    • 33845940683 scopus 로고    scopus 로고
    • S-adenosylhomocysteine hydrolase is localized at the front of chemotaxing cells, suggesting a role for transmethylation during migration
    • Shu, S., D.C. Mahadeo, X. Liu, W. Liu, C.A. Parent, and E.D. Korn. 2006. S-adenosylhomocysteine hydrolase is localized at the front of chemotaxing cells, suggesting a role for transmethylation during migration. Proc. Natl. Acad. Sci. USA. 103:19788-19793. http://dx.doi.org/10.1073/pnas.0609385103
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 19788-19793
    • Shu, S.1    Mahadeo, D.C.2    Liu, X.3    Liu, W.4    Parent, C.A.5    Korn, E.D.6
  • 74
    • 77952614701 scopus 로고    scopus 로고
    • Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF
    • Sinha, R., E. Allemand, Z. Zhang, R. Karni, M.P. Myers, and A.R. Krainer. 2010. Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF. Mol. Cell. Biol. 30:2762-2774. http://dx.doi.org/10.1128/MCB.01270-09
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2762-2774
    • Sinha, R.1    Allemand, E.2    Zhang, Z.3    Karni, R.4    Myers, M.P.5    Krainer, A.R.6
  • 75
    • 0019062683 scopus 로고
    • The role of eucaryotic factor Tu in protein synthesis. The measurement of the elongation factor Tu content of rabbit reticulocytes and other mammalian cells by a sensitive radioimmunoassay
    • Slobin, L.I. 1980. The role of eucaryotic factor Tu in protein synthesis. The measurement of the elongation factor Tu content of rabbit reticulocytes and other mammalian cells by a sensitive radioimmunoassay. Eur. J. Biochem. 110:555-563. http://dx.doi.org/10.1111/j.1432-1033.1980.tb04898.x
    • (1980) Eur. J. Biochem. , vol.110 , pp. 555-563
    • Slobin, L.I.1
  • 76
    • 77956571712 scopus 로고    scopus 로고
    • Histone demethylase JmjD2A regulates neural crest specification
    • Strobl-Mazzulla, P.H., T. Sauka-Spengler, and M. Bronner-Fraser. 2010. Histone demethylase JmjD2A regulates neural crest specification. Dev. Cell. 19:460-468. http://dx.doi.org/10.1016/j.devcel.2010.08.009
    • (2010) Dev. Cell. , vol.19 , pp. 460-468
    • Strobl-Mazzulla, P.H.1    Sauka-Spengler, T.2    Bronner-Fraser, M.3
  • 78
    • 0035336675 scopus 로고    scopus 로고
    • Sparking new frontiers: using in vivo electroporation for genetic manipulations
    • Swartz, M., J. Eberhart, G.S. Mastick, and C.E. Krull. 2001. Sparking new frontiers: using in vivo electroporation for genetic manipulations. Dev. Biol. 233:13-21. http://dx.doi.org/10.1006/dbio.2001.0181
    • (2001) Dev. Biol. , vol.233 , pp. 13-21
    • Swartz, M.1    Eberhart, J.2    Mastick, G.S.3    Krull, C.E.4
  • 79
    • 12344271451 scopus 로고    scopus 로고
    • In vivo evidence for short- and long-range cell communication in cranial neural crest cells
    • Teddy, J.M., and P.M. Kulesa. 2004. In vivo evidence for short- and long-range cell communication in cranial neural crest cells. Development. 131:6141-6151. http://dx.doi.org/10.1242/dev.01534
    • (2004) Development. , vol.131 , pp. 6141-6151
    • Teddy, J.M.1    Kulesa, P.M.2
  • 80
    • 79952046499 scopus 로고    scopus 로고
    • Integrating chemotaxis and contact-inhibition during collective cell migration: Small GTPases at work
    • Theveneau, E., and R. Mayor. 2010. Integrating chemotaxis and contact-inhibition during collective cell migration: Small GTPases at work. Small GTPases. 1:113-117. http://dx.doi.org/10.4161/sgtp.1.2.13673
    • (2010) Small GTPases. , vol.1 , pp. 113-117
    • Theveneau, E.1    Mayor, R.2
  • 81
    • 84860841774 scopus 로고    scopus 로고
    • Neural crest delamination and migration: from epithelium-to-mesenchyme transition to collective cell migration
    • Theveneau, E., and R. Mayor. 2012. Neural crest delamination and migration: from epithelium-to-mesenchyme transition to collective cell migration. Dev. Biol. 366:34-54. http://dx.doi.org/10.1016/j.ydbio.2011.12.041
    • (2012) Dev. Biol. , vol.366 , pp. 34-54
    • Theveneau, E.1    Mayor, R.2
  • 82
    • 0021111516 scopus 로고
    • Binding of adenosine to intracellular S-adenosylhomocysteine hydrolase in isolated rat hepatocytes
    • Ueland, P.M., and S. Helland. 1983. Binding of adenosine to intracellular S-adenosylhomocysteine hydrolase in isolated rat hepatocytes. J. Biol. Chem. 258:747-752.
    • (1983) J. Biol. Chem. , vol.258 , pp. 747-752
    • Ueland, P.M.1    Helland, S.2
  • 83
    • 84891894507 scopus 로고    scopus 로고
    • Expression of actin-binding proteins and requirement for actin depolymerizing factor in chick neural crest cells
    • In press.
    • Vermillion, K.L., K. Lidberg, and L.S. Gammill. 2013. Expression of actin-binding proteins and requirement for actin depolymerizing factor in chick neural crest cells. Dev. Dyn. In press.
    • (2013) Dev. Dyn.
    • Vermillion, K.L.1    Lidberg, K.2    Gammill, L.S.3
  • 84
    • 70349797209 scopus 로고    scopus 로고
    • Chemotaxis: how bacteria use memory
    • Vladimirov, N., and V. Sourjik. 2009. Chemotaxis: how bacteria use memory. Biol. Chem. 390:1097-1104.
    • (2009) Biol. Chem. , vol.390 , pp. 1097-1104
    • Vladimirov, N.1    Sourjik, V.2
  • 85
    • 0003496492 scopus 로고
    • In Situ Hybridization: A Practical Approach.
    • IRL Press Oxford, England
    • Wilkinson, D.G. 1992. In Situ Hybridization: A Practical Approach. IRL Press, Oxford, England. 224 pp.
    • (1992) , vol.224
    • Wilkinson, D.G.1
  • 86
    • 73649118866 scopus 로고    scopus 로고
    • Post-translational modifications to Toxoplasma gondii alpha- and beta-tubulins include novel C-terminal methylation
    • Xiao, H., K. El Bissati, P. Verdier-Pinard, B. Burd, H. Zhang, K. Kim, A. Fiser, R.H. Angeletti, and L.M. Weiss. 2010. Post-translational modifications to Toxoplasma gondii alpha- and beta-tubulins include novel C-terminal methylation. J. Proteome Res. 9:359-372. http://dx.doi.org/10.1021/pr900699a
    • (2010) J. Proteome Res. , vol.9 , pp. 359-372
    • Xiao, H.1    El Bissati, K.2    Verdier-Pinard, P.3    Burd, B.4    Zhang, H.5    Kim, K.6    Fiser, A.7    Angeletti, R.H.8    Weiss, L.M.9
  • 87
    • 78651277061 scopus 로고    scopus 로고
    • The significance, development and progress of high-throughput combinatorial histone code analysis
    • Young, N.L., P.A. DiMaggio, and B.A. Garcia. 2010. The significance, development and progress of high-throughput combinatorial histone code analysis. Cell. Mol. Life Sci. 67:3983-4000. http://dx.doi.org/10.1007/s00018-010-0475-7
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3983-4000
    • Young, N.L.1    DiMaggio, P.A.2    Garcia, B.A.3
  • 89
    • 84855303522 scopus 로고    scopus 로고
    • Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity
    • Zhang, Y., T.H. Kim, and L. Niswander. 2012. Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity. Genes Dev. 26:69-81. http://dx.doi.org/10.1101/gad.179283.111
    • (2012) Genes Dev. , vol.26 , pp. 69-81
    • Zhang, Y.1    Kim, T.H.2    Niswander, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.