메뉴 건너뛰기




Volumn 34, Issue 3, 2014, Pages 374-385

Regulation of ras localization and cell transformation by evolutionarily conserved palmitoyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

PALMITOYLTRANSFERASE; RAS PROTEIN; SCHIZOSACCHAROMYCES POMBE ERF2 PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; SHORT HAIRPIN RNA; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84892467472     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01248-13     Document Type: Article
Times cited : (23)

References (67)
  • 1
    • 84255195028 scopus 로고    scopus 로고
    • Regulating the regulator: post-translational modification of RAS
    • Ahearn IM, Haigis K, Bar-Sagi D, Philips MR. 2012. Regulating the regulator: post-translational modification of RAS. Nat. Rev. Mol. Cell. Biol. 13:39-51. http://dx.doi.org/10.1038/nrm3255.
    • (2012) Nat. Rev. Mol. Cell. Biol. , vol.13 , pp. 39-51
    • Ahearn, I.M.1    Haigis, K.2    Bar-Sagi, D.3    Philips, M.R.4
  • 2
    • 79952263402 scopus 로고    scopus 로고
    • Compartmentalized Ras proteins transform NIH 3T3 cells with different efficiencies
    • Cheng CM, Li H, Gasman S, Huang J, Schiff R, Chang EC. 2011. Compartmentalized Ras proteins transform NIH 3T3 cells with different efficiencies. Mol. Cell. Biol. 31:983-997. http://dx.doi.org/10.1128/MCB.00137-10.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 983-997
    • Cheng, C.M.1    Li, H.2    Gasman, S.3    Huang, J.4    Schiff, R.5    Chang, E.C.6
  • 3
    • 77951729960 scopus 로고    scopus 로고
    • Palmitoylation of oncogenic NRAS is essential for leukemogenesis
    • Cuiffo B, Ren R. 2010. Palmitoylation of oncogenic NRAS is essential for leukemogenesis. Blood 115:3598-3605. http://dx.doi.org/10.1182/blood -2009-03-213876.
    • (2010) Blood , vol.115 , pp. 3598-3605
    • Cuiffo, B.1    Ren, R.2
  • 5
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels DJ, Mitchell DA, Dong X, Deschenes RJ. 1999. Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:6775-6787.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 7
    • 24744466287 scopus 로고    scopus 로고
    • DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras
    • Swarthout JT, Lobo S, Farh L, Croke MR, Greentree WK, Deschenes RJ, Linder ME. 2005. DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J. Biol. Chem. 280: 31141-31148. http://dx.doi.org/10.1074/jbc.M504113200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31141-31148
    • Swarthout, J.T.1    Lobo, S.2    Farh, L.3    Croke, M.R.4    Greentree, W.K.5    Deschenes, R.J.6    Linder, M.E.7
  • 8
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • Mitchell DA, Vasudevan A, Linder ME, Deschenes RJ. 2006. Protein palmitoylation by a family of DHHC protein S-acyltransferases. J. Lipid Res. 47:1118-1127. http://dx.doi.org/10.1194/jlr.R600007-JLR200.
    • (2006) J. Lipid Res. , vol.47 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 9
    • 33748931133 scopus 로고    scopus 로고
    • Spatial segregation of Ras signaling: new evidence from fission yeast
    • Chang EC, Philips MR. 2006. Spatial segregation of Ras signaling: new evidence from fission yeast. Cell Cycle 5:1936-1939. http://dx.doi.org/10.4161/cc.5.17.3187.
    • (2006) Cell Cycle , vol.5 , pp. 1936-1939
    • Chang, E.C.1    Philips, M.R.2
  • 11
    • 0025806672 scopus 로고
    • byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype
    • Wang Y, Xu HP, Riggs M, Rodgers L, Wigler M. 1991. byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype. Mol. Cell. Biol. 11:3554-3563.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3554-3563
    • Wang, Y.1    Xu, H.P.2    Riggs, M.3    Rodgers, L.4    Wigler, M.5
  • 12
    • 0027937264 scopus 로고
    • Cooperative interaction of S. pombe proteins required for mating and morphogenesis
    • Chang EC, Barr M, Wang Y, Jung V, Xu HP, Wigler MH. 1994. Cooperative interaction of S. pombe proteins required for mating and morphogenesis. Cell 79:131-141. http://dx.doi.org/10.1016/0092 -8674(94)90406-5.
    • (1994) Cell , vol.79 , pp. 131-141
    • Chang, E.C.1    Barr, M.2    Wang, Y.3    Jung, V.4    Xu, H.P.5    Wigler, M.H.6
  • 13
    • 0024206818 scopus 로고
    • Isolation and characterization of Schizosaccharomyces pombe mutants phenotypically similar to ras1
    • Fukui Y, Yamamoto M. 1988. Isolation and characterization of Schizosaccharomyces pombe mutants phenotypically similar to ras1. Mol. Gen. Genet. 215:26-31. http://dx.doi.org/10.1007/BF00331298.
    • (1988) Mol. Gen. Genet. , vol.215 , pp. 26-31
    • Fukui, Y.1    Yamamoto, M.2
  • 14
    • 23944500847 scopus 로고    scopus 로고
    • A rapid and simple procedure for highefficiency lithium acetate transformation of cryopreserved Schizosaccharomyces pombe cells
    • Suga M, Hatakeyama T. 2005. A rapid and simple procedure for highefficiency lithium acetate transformation of cryopreserved Schizosaccharomyces pombe cells. Yeast 22:799-804. http://dx.doi.org/10.1002/yea.1247.
    • (2005) Yeast , vol.22 , pp. 799-804
    • Suga, M.1    Hatakeyama, T.2
  • 17
    • 0027757725 scopus 로고
    • Antigen localization in fission yeast
    • Alfa CE, Gallagher IM, Hyams JS. 1993. Antigen localization in fission yeast. Methods Cell Biol. 37:201-222. http://dx.doi.org/10.1016/S0091 -679X(08)60251-4.
    • (1993) Methods Cell Biol , vol.37 , pp. 201-222
    • Alfa, C.E.1    Gallagher, I.M.2    Hyams, J.S.3
  • 18
    • 39049127908 scopus 로고    scopus 로고
    • Transcriptional regulatory network for sexual differentiation in fission yeast
    • Mata J, Wilbrey A, Bahler J. 2007. Transcriptional regulatory network for sexual differentiation in fission yeast. Genome Biol. 8:R217. http://dx.doi.org/10.1186/gb-2007-8-10-r217.
    • (2007) Genome Biol , vol.8
    • Mata, J.1    Wilbrey, A.2    Bahler, J.3
  • 20
    • 79951508532 scopus 로고    scopus 로고
    • Int6 regulates both proteasomal degradation and translation initiation and is critical for proper formation of acini by human mammary epithelium
    • Suo J, Snider SJ, Mills GB, Creighton CJ, Chen AC, Schiff R, Lloyd RE, Chang EC. 2011. Int6 regulates both proteasomal degradation and translation initiation and is critical for proper formation of acini by human mammary epithelium. Oncogene 30:724-736. http://dx.doi.org/10.1038 /onc.2010.445.
    • (2011) Oncogene , vol.30 , pp. 724-736
    • Suo, J.1    Snider, S.J.2    Mills, G.B.3    Creighton, C.J.4    Chen, A.C.5    Schiff, R.6    Lloyd, R.E.7    Chang, E.C.8
  • 21
    • 0030950042 scopus 로고    scopus 로고
    • General purpose tagging vectors for fission yeast
    • Forsburg SL, Sherman DA. 1997. General purpose tagging vectors for fission yeast. Gene 191:191-195. http://dx.doi.org/10.1016/S0378 -1119(97)00058-9.
    • (1997) Gene , vol.191 , pp. 191-195
    • Forsburg, S.L.1    Sherman, D.A.2
  • 22
    • 66849138215 scopus 로고    scopus 로고
    • S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p
    • Codlin S, Mole SE. 2009. S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p. J. Cell Sci. 122:1163-1173. http://dx.doi.org/10.1242 /jcs.038323.
    • (2009) J. Cell Sci. , vol.122 , pp. 1163-1173
    • Codlin, S.1    Mole, S.E.2
  • 24
    • 74549130263 scopus 로고    scopus 로고
    • Int6 and Moe1 interact with Cdc48 to regulate ERAD and proper chromosome segregation
    • Otero JH, Suo J, Gordon C, Chang EC. 2010. Int6 and Moe1 interact with Cdc48 to regulate ERAD and proper chromosome segregation. Cell Cycle 9:147-161. http://dx.doi.org/10.4161/cc.9.1.10312.
    • (2010) Cell Cycle , vol.9 , pp. 147-161
    • Otero, J.H.1    Suo, J.2    Gordon, C.3    Chang, E.C.4
  • 25
    • 0015792521 scopus 로고
    • Processing of adenovirus 2-induced proteins
    • Anderson CW, Baum PR, Gesteland RF. 1973. Processing of adenovirus 2-induced proteins. J. Virol. 12:241-252.
    • (1973) J. Virol. , vol.12 , pp. 241-252
    • Anderson, C.W.1    Baum, P.R.2    Gesteland, R.F.3
  • 26
    • 53349107573 scopus 로고    scopus 로고
    • Low- copy episomal vector pFY20 and high-saturation coverage genomic libraries for the fission yeast Schizosaccharomyces pombe
    • Wahls WP, Davidson MK. 2008. Low-copy episomal vector pFY20 and high-saturation coverage genomic libraries for the fission yeast Schizosaccharomyces pombe. Yeast 25:643-650. http://dx.doi.org/10.1002/yea.1605.
    • (2008) Yeast , vol.25 , pp. 643-650
    • Wahls, W.P.1    Davidson, M.K.2
  • 27
    • 84855962805 scopus 로고    scopus 로고
    • Evolutionary trace for prediction and redesign of protein functional sites
    • Wilkins A, Erdin S, Lua R, Lichtarge O. 2012. Evolutionary trace for prediction and redesign of protein functional sites. Methods Mol. Biol. 819:29-42. http://dx.doi.org/10.1007/978-1-61779-465-0_3.
    • (2012) Methods Mol. Biol. , vol.819 , pp. 29-42
    • Wilkins, A.1    Erdin, S.2    Lua, R.3    Lichtarge, O.4
  • 28
    • 58149178579 scopus 로고    scopus 로고
    • NCBI Reference Sequences: current status, policy and new initiatives
    • Pruitt KD, Tatusova T, Klimke W, Maglott DR. 2009. NCBI Reference Sequences: current status, policy and new initiatives. Nucleic Acids Res. 37:D32-36. http://dx.doi.org/10.1093/nar/gkn721.
    • (2009) Nucleic Acids Res , vol.37
    • Pruitt, K.D.1    Tatusova, T.2    Klimke, W.3    Maglott, D.R.4
  • 29
    • 1242339659 scopus 로고    scopus 로고
    • A family of evolution-entropy hybrid methods for ranking protein residues by importance
    • Mihalek I, Res Lichtarge IO. 2004. A family of evolution-entropy hybrid methods for ranking protein residues by importance. J. Mol. Biol. 336: 1265-1282. http://dx.doi.org/10.1016/j.jmb.2003.12.078.
    • (2004) J. Mol. Biol. , vol.336 , pp. 1265-1282
    • Mihalek, I.1    Res Lichtarge, I.O.2
  • 30
    • 34547590429 scopus 로고    scopus 로고
    • PROMALS web server for accurate multiple protein sequence alignments
    • Pei J, Kim BH, Tang M, Grishin NV. 2007. PROMALS web server for accurate multiple protein sequence alignments. Nucleic Acids Res. 35: W649-652. http://dx.doi.org/10.1093/nar/gkm227.
    • (2007) Nucleic Acids Res , vol.35
    • Pei, J.1    Kim, B.H.2    Tang, M.3    Grishin, N.V.4
  • 31
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno S, Klar A, Nurse P. 1991. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194:795-823. http: //dx.doi.org/10.1016/0076-6879(91)94059-L.
    • (1991) Methods Enzymol , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 32
    • 0032539775 scopus 로고    scopus 로고
    • The Byr2 kinase translocates to the plasma membrane in a Ras1-dependent manner
    • Bauman P, Cheng QC, Albright CF. 1998. The Byr2 kinase translocates to the plasma membrane in a Ras1-dependent manner. Biochem. Biophys. Res. Commun. 244:468-474. http://dx.doi.org/10.1006/bbrc.1998.8292.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 468-474
    • Bauman, P.1    Cheng, Q.C.2    Albright, C.F.3
  • 33
    • 0042594438 scopus 로고    scopus 로고
    • Characterization of vps33_, a gene required for vacuolar biogenesis and protein sorting in Schizosaccharomyces pombe
    • Iwaki T, Osawa F, Onishi M, Koga T, Fujita Y, Hosomi A, Tanaka N, Fukui Y, Takegawa K. 2003. Characterization of vps33_, a gene required for vacuolar biogenesis and protein sorting in Schizosaccharomyces pombe. Yeast 20:845-855. http://dx.doi.org/10.1002/yea.1011.
    • (2003) Yeast , vol.20 , pp. 845-855
    • Iwaki, T.1    Osawa, F.2    Onishi, M.3    Koga, T.4    Fujita, Y.5    Hosomi, A.6    Tanaka, N.7    Fukui, Y.8    Takegawa, K.9
  • 35
    • 0036729529 scopus 로고    scopus 로고
    • The transcriptional program of meiosis and sporulation in fission yeast
    • Mata J, Lyne R, Burns G, Bahler J. 2002. The transcriptional program of meiosis and sporulation in fission yeast. Nat. Genet. 32:143-147. http://dx.doi.org/10.1038/ng951.
    • (2002) Nat. Genet. , vol.32 , pp. 143-147
    • Mata, J.1    Lyne, R.2    Burns, G.3    Bahler, J.4
  • 36
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo S, Greentree WK, Linder ME, Deschenes RJ. 2002. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277:41268-41273. http://dx.doi.org/10.1074/jbc.M206573200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 37
    • 84880959257 scopus 로고    scopus 로고
    • Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast
    • Zhang MM, Wu PY, Kelly FD, Nurse P, Hang HC. 2013. Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast. PLoS Biol. 11:e1001597. http://dx.doi.org/10.1371/journal.pbio.1001597.
    • (2013) PLoS Biol , vol.11
    • Zhang, M.M.1    Wu, P.Y.2    Kelly, F.D.3    Nurse, P.4    Hang, H.C.5
  • 38
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O, Bourne HR, Cohen FE. 1996. An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 257: 342-358. http://dx.doi.org/10.1006/jmbi.1996.0167.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 39
    • 80053453491 scopus 로고    scopus 로고
    • Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites
    • Adikesavan AK, Katsonis P, Marciano DC, Lua R, Herman C, Lichtarge O. 2011. Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites. PLoS Genet. 7:e1002244. http://dx.doi.org/10.1371/journal.pgen.1002244.
    • (2011) PLoS Genet , vol.7
    • Adikesavan, A.K.1    Katsonis, P.2    Marciano, D.C.3    Lua, R.4    Herman, C.5    Lichtarge, O.6
  • 40
    • 34247194102 scopus 로고    scopus 로고
    • Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions
    • Ribes-Zamora A, Mihalek I, Lichtarge O, Bertuch AA. 2007. Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions. Nat. Struct. Mol. Biol. 14:301-307. http://dx.doi.org/10.1038/nsmb1214.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 301-307
    • Ribes-Zamora, A.1    Mihalek, I.2    Lichtarge, O.3    Bertuch, A.A.4
  • 41
    • 77952356281 scopus 로고    scopus 로고
    • Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors
    • Rodriguez GJ, Yao R, Lichtarge O, Wensel TG. 2010. Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors. Proc. Natl. Acad. Sci. U. S. A. 107:7787- 7792. http://dx.doi.org/10.1073/pnas.0914877107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 7787-7792
    • Rodriguez, G.J.1    Yao, R.2    Lichtarge, O.3    Wensel, T.G.4
  • 42
    • 78649662343 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes
    • Mitchell DA, Mitchell G, Ling Y, Budde C, Deschenes RJ. 2010. Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes. J. Biol. Chem. 285:38104-38114. http://dx.doi.org/10.1074/jbc.M110.169102.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38104-38114
    • Mitchell, D.A.1    Mitchell, G.2    Ling, Y.3    Budde, C.4    Deschenes, R.J.5
  • 43
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins: purification and identification
    • Wan J, Roth AF, Bailey AO, Davis NG. 2007. Palmitoylated proteins: purification and identification. Nat. Protoc. 2:1573-1584. http://dx.doi.org/10.1038/nprot.2007.225.
    • (2007) Nat. Protoc. , vol.2 , pp. 1573-1584
    • Wan, J.1    Roth, A.F.2    Bailey, A.O.3    Davis, N.G.4
  • 45
    • 0027992519 scopus 로고
    • Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe, Isolation of multiple genes conferring resistance
    • Turi TG, Webster P, Rose JK. 1994. Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance. J. Biol. Chem. 269:24229-24236.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24229-24236
    • Turi, T.G.1    Webster, P.2    Rose, J.K.3
  • 46
    • 41649086103 scopus 로고    scopus 로고
    • The actomyosin ring recruits early secretory compartments to the division site in fission yeast
    • Vjestica A, Tang XZ, Oliferenko S. 2008. The actomyosin ring recruits early secretory compartments to the division site in fission yeast. Mol. Biol. Cell 19:1125-1138. http://dx.doi.org/10.1091/mbc.E07-07-0663.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 1125-1138
    • Vjestica, A.1    Tang, X.Z.2    Oliferenko, S.3
  • 48
    • 0346668323 scopus 로고    scopus 로고
    • Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins
    • Zhao L, Lobo S, Dong X, Ault AD, Deschenes RJ. 2002. Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J. Biol. Chem. 277: 49352-49359. http://dx.doi.org/10.1074/jbc.M209760200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49352-49359
    • Zhao, L.1    Lobo, S.2    Dong, X.3    Ault, A.D.4    Deschenes, R.J.5
  • 49
    • 33646830442 scopus 로고    scopus 로고
    • Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins
    • Ohno Y, Kihara A, Sano T, Igarashi Y. 2006. Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins. Biochim. Biophys. Acta 1761:474-483. http://dx.doi.org/10.1016/j.bbalip.2006.03.010.
    • (2006) Biochim. Biophys. Acta. , vol.1761 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 52
    • 79954481319 scopus 로고    scopus 로고
    • Busy traveling Ras
    • Cheng CM, Chang EC. 2011. Busy traveling Ras. Cell Cycle 10:1180- 1181. http://dx.doi.org/10.4161/cc.10.8.15259.
    • (2011) Cell Cycle , vol.10 , pp. 1180-1181
    • Cheng, C.M.1    Chang, E.C.2
  • 54
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock JF, Magee AI, Childs JE, Marshall CJ. 1989. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57:1167-1177. http://dx.doi.org/10.1016/0092-8674(89)90054-8.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 55
    • 0024376173 scopus 로고
    • ras oncogenes in human cancer: a review
    • Bos JL. 1989. ras oncogenes in human cancer: a review. Cancer Res. 49:4682-4689.
    • (1989) Cancer Res , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 58
    • 0030044330 scopus 로고    scopus 로고
    • MCF10AT: a model for the evolution of cancer from proliferative breast disease
    • Dawson PJ, Wolman SR, Tait L, Heppner GH, Miller FR. 1996. MCF10AT: a model for the evolution of cancer from proliferative breast disease. Am. J. Pathol. 148:313-319.
    • (1996) Am. J. Pathol. , vol.148 , pp. 313-319
    • Dawson, P.J.1    Wolman, S.R.2    Tait, L.3    Heppner, G.H.4    Miller, F.R.5
  • 59
    • 0037603113 scopus 로고    scopus 로고
    • Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in threedimensional basement membrane cultures
    • Debnath J, Muthuswamy SK, Brugge JS. 2003. Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in threedimensional basement membrane cultures. Methods 30:256-268. http: //dx.doi.org/10.1016/S1046-2023(03)00032-X.
    • (2003) Methods , vol.30 , pp. 256-268
    • Debnath, J.1    Muthuswamy, S.K.2    Brugge, J.S.3
  • 60
    • 84867267220 scopus 로고    scopus 로고
    • The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate
    • Mitchell DA, Hamel LD, Ishizuka K, Mitchell G, Schaefer LM, Deschenes RJ. 2012. The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate. J. Biol. Chem. 287:34337-34348. http://dx.doi.org/10.1074/jbc.M112.379297.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34337-34348
    • Mitchell, D.A.1    Hamel, L.D.2    Ishizuka, K.3    Mitchell, G.4    Schaefer, L.M.5    Deschenes, R.J.6
  • 62
    • 0035839062 scopus 로고    scopus 로고
    • Molecular evidence for the early colonization of land by fungi and plants
    • Heckman DS, Geiser DM, Eidell BR, Stauffer RL, Kardos NL, Hedges SB. 2001. Molecular evidence for the early colonization of land by fungi and plants. Science 293:1129-1133. http://dx.doi.org/10.1126/science.1061457.
    • (2001) Science , vol.293 , pp. 1129-1133
    • Heckman, D.S.1    Geiser, D.M.2    Eidell, B.R.3    Stauffer, R.L.4    Kardos, N.L.5    Hedges, S.B.6
  • 63
    • 0032031584 scopus 로고    scopus 로고
    • Pseudo-enzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo
    • Bano MC, Jackson CS, Magee AI. 1998. Pseudo-enzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo. Biochem. J. 330:723-731.
    • (1998) Biochem. J. , vol.330 , pp. 723-731
    • Bano, M.C.1    Jackson, C.S.2    Magee, A.I.3
  • 64
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: policing protein stability and traffic
    • Linder ME, Deschenes RJ. 2007. Palmitoylation: policing protein stability and traffic. Nat. Rev. Mol. Cell Biol. 8:74-84. http://dx.doi.org/10.1038 /nrm2084.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 65
    • 0000534698 scopus 로고
    • Involvement of ras in sexual differentiation but not in growth control in fission yeast
    • Nadin-Davis SA, Nasim A, Beach D. 1986. Involvement of ras in sexual differentiation but not in growth control in fission yeast.EMBOJ. 5:2963- 2971.
    • (1986) EMBOJ , vol.5 , pp. 2963-2971
    • Nadin-Davis, S.A.1    Nasim, A.2    Beach, D.3
  • 66
    • 0022554044 scopus 로고
    • Role of a ras homolog in the life cycle of Schizosaccharomyces pombe
    • Fukui Y, Kozasa T, Kaziro Y, Takeda T, Yamamoto M. 1986. Role of a ras homolog in the life cycle of Schizosaccharomyces pombe. Cell 44:329- 336. http://dx.doi.org/10.1016/0092-8674(86)90767-1.
    • (1986) Cell , vol.44 , pp. 329-336
    • Fukui, Y.1    Kozasa, T.2    Kaziro, Y.3    Takeda, T.4    Yamamoto, M.5
  • 67
    • 10244225308 scopus 로고    scopus 로고
    • TMRPres2D: high quality visual representation of transmembrane protein models
    • Spyropoulos IC, Liakopoulos TD, Bagos PG, Hamodrakas SJ. 2004. TMRPres2D: high quality visual representation of transmembrane protein models. Bioinformatics 20:3258-3260. http://dx.doi.org/10.1093 /bioinformatics/bth358.
    • (2004) Bioinformatics , vol.20 , pp. 3258-3260
    • Spyropoulos, I.C.1    Liakopoulos, T.D.2    Bagos, P.G.3    Hamodrakas, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.