메뉴 건너뛰기




Volumn 2015, Issue 4, 2015, Pages

Inhibitory activities of short linear motifs underlie hox interactome specificity in vivo

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; HEXAPEPTIDE; HOMEODOMAIN PROTEIN; HOX PROTEIN; HYBRID PROTEIN; RED FLUORESCENT PROTEIN; TRANSCRIPTION FACTOR;

EID: 84928129042     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.06034.001     Document Type: Article
Times cited : (8)

References (76)
  • 2
    • 84893709652 scopus 로고    scopus 로고
    • CRISPR/Cas9 and genome editing in Drosophila
    • Bassett AR, Liu JL. 2014. CRISPR/Cas9 and genome editing in Drosophila. Journal of Genetics and Genomics 41: 7–19. doi: 10.1016/j.jgg.2013.12.004.
    • (2014) Journal of Genetics and Genomics , vol.41 , pp. 7-19
    • Bassett, A.R.1    Liu, J.L.2
  • 5
    • 84877727235 scopus 로고    scopus 로고
    • A versatile platform for creating a comprehensive UAS- ORFeome library in Drosophila
    • Bischof J, Björklund M, Furger E, Schertel C, Taipale J, Basler K. 2013. A versatile platform for creating a comprehensive UAS- ORFeome library in Drosophila. Development 140:2434–2442. doi: 10.1242/dev.088757.
    • (2013) Development , vol.140 , pp. 2434-2442
    • Bischof, J.1    Björklund, M.2    Furger, E.3    Schertel, C.4    Taipale, J.5    Basler, K.6
  • 7
    • 78650391868 scopus 로고    scopus 로고
    • Genetics. Revealing the dark matter of the genome
    • Blaxter M. 2010. Genetics. Revealing the dark matter of the genome. Science 330:1758–1759. doi: 10.1126/science.1200700.
    • (2010) Science , vol.330 , pp. 1758-1759
    • Blaxter, M.1
  • 8
    • 2942702019 scopus 로고    scopus 로고
    • Hox transcription factor ultrabithorax Ib physically and genetically interacts with disconnected interacting protein 1, a double-stranded RNA-binding protein
    • Bondos SE, Catanese DJ Jr, Tan XX, Bicknell A, Li L, Matthews KS. 2004. Hox transcription factor ultrabithorax Ib physically and genetically interacts with disconnected interacting protein 1, a double-stranded RNA-binding protein. The Journal of Biological Chemistry 279:26433–26444. doi: 10.1074/jbc.M312842200.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 26433-26444
    • Bondos, S.E.1    Catanese, D.J.2    Tan, X.X.3    Bicknell, A.4    Li, L.5    Matthews, K.S.6
  • 9
    • 33646903233 scopus 로고    scopus 로고
    • Physical and genetic interactions link hox function with diverse transcription factors and cell signaling proteins
    • Bondos SE, Tan XX, Matthews KS. 2006. Physical and genetic interactions link hox function with diverse transcription factors and cell signaling proteins. Molecular & Cellular Proteomics 5:824–834. doi: 10.1074/mcp.M500256-MCP200.
    • (2006) Molecular & Cellular Proteomics , vol.5 , pp. 824-834
    • Bondos, S.E.1    Tan, X.X.2    Matthews, K.S.3
  • 10
    • 84901585344 scopus 로고    scopus 로고
    • Drosophila melanogaster Hox transcription factors access the RNA polymerase II machinery through direct homeodomain binding to a conserved motif of mediator subunit Med19
    • Boube M, Hudry B, Immarigeon C, Carrier Y, Bernat-Fabre S, Merabet S, Graba Y, Bourbon HM, Cribbs DL. 2014. Drosophila melanogaster Hox transcription factors access the RNA polymerase II machinery through direct homeodomain binding to a conserved motif of mediator subunit Med19. PLOS Genetics 10:e1004303. doi: 10.1371/journal.pgen.1004303.
    • (2014) PLOS Genetics , vol.10
    • Boube, M.1    Hudry, B.2    Immarigeon, C.3    Carrier, Y.4    Bernat-Fabre, S.5    Merabet, S.6    Graba, Y.7    Bourbon, H.M.8    Cribbs, D.L.9
  • 11
    • 80051991355 scopus 로고    scopus 로고
    • Evolution of a derived protein-protein interaction between HoxA11 and Foxo1a in mammals caused by changes in intramolecular regulation
    • Brayer KJ, Lynch VJ, Wagner GP. 2011. Evolution of a derived protein-protein interaction between HoxA11 and Foxo1a in mammals caused by changes in intramolecular regulation. Proceedings of the National Academy of Sciences of USA 108:E414–E420. doi: 10.1073/pnas.1100990108.
    • (2011) Proceedings of the National Academy of Sciences of USA , vol.108 , pp. E414-E420
    • Brayer, K.J.1    Lynch, V.J.2    Wagner, G.P.3
  • 12
    • 0036333329 scopus 로고    scopus 로고
    • Abdominal A specifies one cell type in Drosophila by regulating one principal target gene
    • Brodu V, Elstob PR, Gould AP. 2002. abdominal A specifies one cell type in Drosophila by regulating one principal target gene. Development 129:2957–2963.
    • (2002) Development , vol.129 , pp. 2957-2963
    • Brodu, V.1    Elstob, P.R.2    Gould, A.P.3
  • 14
    • 0029925624 scopus 로고    scopus 로고
    • An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif
    • Chan SK, Pöpperl H, Krumlauf R, Mann RS. 1996. An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif. The EMBO Journal 15: 2476–2487.
    • (1996) The EMBO Journal , vol.15 , pp. 2476-2487
    • Chan, S.K.1    Pöpperl, H.2    Krumlauf, R.3    Mann, R.S.4
  • 15
    • 38949202286 scopus 로고    scopus 로고
    • Common functions of central and posterior Hox genes for the repression of head in the trunk of Drosophila
    • Coiffier D, Charroux B, Kerridge S. 2008. Common functions of central and posterior Hox genes for the repression of head in the trunk of Drosophila. Development 135:291–300. doi: 10.1242/dev.009662.
    • (2008) Development , vol.135 , pp. 291-300
    • Coiffier, D.1    Charroux, B.2    Kerridge, S.3
  • 16
    • 77957332664 scopus 로고    scopus 로고
    • Combinatorial binding leads to diverse regulatory responses: Lmd is a tissue-specific modulator of Mef2 activity
    • Cunha PM, Sandmann T, Gustafson EH, Ciglar L, Eichenlaub MP, Furlong EE. 2010. Combinatorial binding leads to diverse regulatory responses: Lmd is a tissue-specific modulator of Mef2 activity. PLOS Genetics 6:e1001014. doi: 10.1371/journal.pgen.1001014.
    • (2010) PLOS Genetics , vol.6
    • Cunha, P.M.1    Sandmann, T.2    Gustafson, E.H.3    Ciglar, L.4    Eichenlaub, M.P.5    Furlong, E.E.6
  • 17
    • 33750737048 scopus 로고    scopus 로고
    • A simple and efficient method to identify replacements of P-lacZ by P-Gal4 lines allows obtaining Gal4 insertions in the bithorax complex of Drosophila
    • de Navas L, Foronda D, Suzanne M, Sánchez-Herrero E. 2006. A simple and efficient method to identify replacements of P-lacZ by P-Gal4 lines allows obtaining Gal4 insertions in the bithorax complex of Drosophila. Mechanisms of Development 123:860–867. doi: 10.1016/j.mod.2006.07.010.
    • (2006) Mechanisms of Development , vol.123 , pp. 860-867
    • De Navas, L.1    Foronda, D.2    Suzanne, M.3    Sánchez-Herrero, E.4
  • 19
    • 0026098805 scopus 로고
    • The gene teashirt is required for the development of Drosophila embryonic trunk segments and encodes a protein with widely spaced zinc finger motifs
    • Fasano L, Röder L, Coré N, Alexandre E, Vola C, Jacq B, Kerridge S. 1991. The gene teashirt is required for the development of Drosophila embryonic trunk segments and encodes a protein with widely spaced zinc finger motifs. Cell 64:63–79. doi: 10.1016/0092-8674(91)90209-H.
    • (1991) Cell , vol.64 , pp. 63-79
    • Fasano, L.1    Röder, L.2    Coré, N.3    Alexandre, E.4    Vola, C.5    Jacq, B.6    Kerridge, S.7
  • 20
    • 1642553347 scopus 로고    scopus 로고
    • The origins of axial patterning in the metazoa: How old is bilateral symmetry?
    • Finnerty JR. 2003. The origins of axial patterning in the metazoa: how old is bilateral symmetry? The International Journal of Developmental Biology 47:523–529.
    • (2003) The International Journal of Developmental Biology , vol.47 , pp. 523-529
    • Finnerty, J.R.1
  • 22
    • 31644439148 scopus 로고    scopus 로고
    • Requirement of Abdominal-A and Abdominal-B in the developing genitalia of Drosophila breaks the posterior downregulation rule
    • Foronda D, Estrada B, de Navas L, Sánchez-Herrero E. 2005. Requirement of Abdominal-A and Abdominal-B in the developing genitalia of Drosophila breaks the posterior downregulation rule. Development 133:117–127. doi: 10.1242/dev.02173.
    • (2005) Development , vol.133 , pp. 117-127
    • Foronda, D.1    Estrada, B.2    De Navas, L.3    Sánchez-Herrero, E.4
  • 23
    • 0036337125 scopus 로고    scopus 로고
    • Hox repression of a target gene: Extradenticle-independent, additive action through multiple monomer binding sites
    • Galant R, Walsh CM, Carroll SB. 2002. Hox repression of a target gene: extradenticle-independent, additive action through multiple monomer binding sites. Development 3126:3115–3126.
    • (2002) Development , vol.3126 , pp. 3115-3126
    • Galant, R.1    Walsh, C.M.2    Carroll, S.B.3
  • 24
    • 0036774750 scopus 로고    scopus 로고
    • Specificity of distalless repression and limb primordia development by abdominal hox proteins
    • Gebelein B, Culi J, Ryoo HD, Zhang W, Mann RS. 2002. Specificity of distalless repression and limb primordia development by abdominal hox proteins. Developmental Cell 3:487–498.
    • (2002) Developmental Cell , vol.3 , pp. 487-498
    • Gebelein, B.1    Culi, J.2    Ryoo, H.D.3    Zhang, W.4    Mann, R.S.5
  • 25
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein
    • Ghosh I, Hamilton AD, Regan L. 2000. Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein. Journal of the American Chemical Society 122:5658–5659. doi: 10.1021/ja994421w.
    • (2000) Journal of the American Chemical Society , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 29
    • 84907789769 scopus 로고    scopus 로고
    • The intrinsically disordered regions of the Drosophila melanogaster Hox protein ultrabithorax select interacting proteins based on partner topology
    • Hsiao H-C, Gonzalez KL, Catanese DJ Jr, Jordy KE, Matthews KS, Bondos SE. 2014. The intrinsically disordered regions of the Drosophila melanogaster Hox protein ultrabithorax select interacting proteins based on partner topology. PLOS ONE 9:e108217. doi: 10.1371/journal.pone.0108217.
    • (2014) PLOS ONE , vol.9
    • Hsiao, H.-C.1    Gonzalez, K.L.2    Catanese, D.J.3    Jordy, K.E.4    Matthews, K.S.5    Bondos, S.E.6
  • 30
    • 84863702620 scopus 로고    scopus 로고
    • Hox proteins display a common and ancestral ability to diversify their interaction mode with the PBC class cofactors
    • Hudry B, Remacle S, Delfini MC, Rezsohazy R, Graba Y, Merabet S. 2012. Hox proteins display a common and ancestral ability to diversify their interaction mode with the PBC class cofactors. PLOS Biology 10:e1001351. doi: 10.1371/journal.pbio.1001351.
    • (2012) PLOS Biology , vol.10
    • Hudry, B.1    Remacle, S.2    Delfini, M.C.3    Rezsohazy, R.4    Graba, Y.5    Merabet, S.6
  • 32
    • 79251552527 scopus 로고    scopus 로고
    • Visualization of protein interactions in living Drosophila embryos by the bimolecular fluorescence complementation assay
    • Hudry B, Viala S, Graba Y, Merabet S. 2011. Visualization of protein interactions in living Drosophila embryos by the bimolecular fluorescence complementation assay. BMC Biology 9:5. doi: 10.1186/1741-7007-9-5.
    • (2011) BMC Biology , vol.9 , pp. 5
    • Hudry, B.1    Viala, S.2    Graba, Y.3    Merabet, S.4
  • 33
    • 1642513707 scopus 로고    scopus 로고
    • Homeodomain to hexapeptide or PBC-interactiondomain distance: size apparently matters
    • In der Rieden PM, Mainguy G, Woltering JM, Durston AJ. 2004. Homeodomain to hexapeptide or PBC-interactiondomain distance: size apparently matters. Trends in Genetics 20:76–79. doi: 10.1016/j.tig.2003.12.001.
    • (2004) Trends in Genetics , vol.20 , pp. 76-79
    • In Der Rieden, P.M.1    Mainguy, G.2    Woltering, J.M.3    Durston, A.J.4
  • 35
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola TK. 2008. Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annual Review of Biophysics 37:465–487. doi: 10.1146/annurev.biophys.37.032807.125842.
    • (2008) Annual Review of Biophysics , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 36
    • 84869238373 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC): A 5-year update and future perspectives
    • Kodama Y, Hu CD. 2012. Bimolecular fluorescence complementation (BiFC): a 5-year update and future perspectives. Biotechniques 53:285–298. doi: 10.2144/000113943.
    • (2012) Biotechniques , vol.53 , pp. 285-298
    • Kodama, Y.1    Hu, C.D.2
  • 37
    • 34447573973 scopus 로고    scopus 로고
    • Small peptide regulators of actin-based cell morphogenesis encoded by a polycistronic mRNA
    • Kondo T, Hashimoto Y, Kato K, Inagaki S, Hayashi S, Kageyama Y. 2007. Small peptide regulators of actin-based cell morphogenesis encoded by a polycistronic mRNA. Nature Cell Biology 9:660–665. doi: 10.1038/ncb1595.
    • (2007) Nature Cell Biology , vol.9 , pp. 660-665
    • Kondo, T.1    Hashimoto, Y.2    Kato, K.3    Inagaki, S.4    Hayashi, S.5    Kageyama, Y.6
  • 38
    • 84860503075 scopus 로고    scopus 로고
    • HOT regions function as patterned developmental enhancers and have a distinct cis-regulatory signature
    • Kvon EZ, Stampfel G, Yáñez-Cuna JO, Dickson BJ, Stark A. 2012. HOT regions function as patterned developmental enhancers and have a distinct cis-regulatory signature. Genes & Development 26:908–913. doi: 10.1101/gad.188052.112.
    • (2012) Genes & Development , vol.26 , pp. 908-913
    • Kvon, E.Z.1    Stampfel, Yáñez-Cuna, G.2    Dickson, J.O.B.J.3    Stark, A.4
  • 40
    • 84889560325 scopus 로고    scopus 로고
    • Extracting insight from noisy cellular networks
    • Landry CR, Levy ED, Abd Rabbo D, Tarassov K, Michnick SW. 2013. Extracting insight from noisy cellular networks. Cell 155:983–989. doi: 10.1016/j.cell.2013.11.003.
    • (2013) Cell , vol.155 , pp. 983-989
    • Landry, C.R.1    Levy, E.D.2    Abd Rabbo, D.3    Tarassov, K.4    Michnick, S.W.5
  • 44
    • 48549085170 scopus 로고    scopus 로고
    • Hox and senseless antagonism functions as a molecular switch to regulate EGF secretion in the Drosophila PNS
    • Li-kroeger D, Witt LM, Grimes HL, Cook TA, Gebelein B. 2008. Hox and senseless antagonism functions as a molecular switch to regulate EGF secretion in the Drosophila PNS. Developmental Cell 15:298–308. doi: 10. 1016/j.devcel.2008.06.001.
    • (2008) Developmental Cell , vol.15 , pp. 298-308
    • Li-Kroeger, D.1    Witt, L.M.2    Grimes, H.L.3    Cook, T.A.4    Gebelein, B.5
  • 46
    • 84883487014 scopus 로고    scopus 로고
    • Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames
    • Magny EG, Pueyo JI, Pearl FM, Cespedes MA, Niven JE, Bishop SA, Couso JP. 2013. Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames. Science 341:1116–1120. doi: 10.1126/science.1238802.
    • (2013) Science , vol.341 , pp. 1116-1120
    • Magny, E.G.1    Pueyo, J.I.2    Pearl, F.M.3    Cespedes, M.A.4    Niven, J.E.5    Bishop, S.A.6    Couso, J.P.7
  • 47
    • 67749095703 scopus 로고    scopus 로고
    • Hox Specificity unique roles for cofactors and collaborators
    • Mann RS, Lelli KM, Joshi R. 2009. Hox Specificity unique roles for cofactors and collaborators. Current Topics in Developmental Biology 88:63–101. doi: 10.1016/S0070-2153(09)88003-4.
    • (2009) Current Topics in Developmental Biology , vol.88 , pp. 63-101
    • Mann, R.S.1    Lelli, K.M.2    Joshi, R.3
  • 48
    • 18344401779 scopus 로고    scopus 로고
    • In vivo mutagenesis of the Hoxb8 hexapeptide domain leads to dominant homeotic transformations that mimic the loss-of-function mutations in genes of the Hoxb cluster
    • Medina-martinez O, Ramı R. 2003. In vivo mutagenesis of the Hoxb8 hexapeptide domain leads to dominant homeotic transformations that mimic the loss-of-function mutations in genes of the Hoxb cluster. Developmental Biology 264:77–90. doi: 10.1016/j.ydbio.2003.07.020.
    • (2003) Developmental Biology , vol.264 , pp. 77-90
    • Medina-Martinez, O.1    Ramı, R.2
  • 49
    • 84890858140 scopus 로고    scopus 로고
    • Tracking context-specific transcription factors regulating hox activity
    • Merabet S, Dard A. 2014. Tracking context-specific transcription factors regulating hox activity. Developmental Dynamics 243:16–23. doi: 10.1002/dvdy.24002.
    • (2014) Developmental Dynamics , vol.243 , pp. 16-23
    • Merabet, S.1    Dard, A.2
  • 50
    • 79959219860 scopus 로고    scopus 로고
    • On the border of the homeotic function: Re-evaluating the controversial role of cofactor-recruiting motifs: The role of cofactor-recruiting motifs in conferring Hox evolutionary flexibility may critically depend on the protein environment
    • Merabet S, Hudry B. 2011. On the border of the homeotic function: re-evaluating the controversial role of cofactor-recruiting motifs: the role of cofactor-recruiting motifs in conferring Hox evolutionary flexibility may critically depend on the protein environment. Bioessays 33:499–507. doi: 10.1002/bies.201100019.
    • (2011) Bioessays , vol.33 , pp. 499-507
    • Merabet, S.1    Hudry, B.2
  • 51
    • 0037991521 scopus 로고    scopus 로고
    • The hexapeptide and linker regions of the AbdA Hox protein regulate its activating and repressive functions
    • Merabet S, Kambris Z, Capovilla M, Bérenger H, Pradel J, Graba Y. 2003. The hexapeptide and linker regions of the AbdA Hox protein regulate its activating and repressive functions. Developmental Cell 4:761–768. doi: 10.1016/S1534-5807(03)00126-6.
    • (2003) Developmental Cell , vol.4 , pp. 761-768
    • Merabet, S.1    Kambris, Z.2    Capovilla, M.3    Bérenger, H.4    Pradel, J.5    Graba, Y.6
  • 53
    • 66449088024 scopus 로고    scopus 로고
    • Classification of sequence signatures: A guide to Hox protein function
    • Merabet S, Hudry B, Saadaoui M, Graba Y. 2009. Classification of sequence signatures: a guide to Hox protein function. Bioessays 31:500–511. doi: 10.1002/bies.200800229.
    • (2009) Bioessays , vol.31 , pp. 500-511
    • Merabet, S.1    Hudry, B.2    Saadaoui, M.3    Graba, Y.4
  • 56
    • 52649104026 scopus 로고    scopus 로고
    • Monitoring the interference of proteinprotein interactions in vivo by bimolecular fluorescence complementation: The DnaK case
    • Morell M, Czihal P, Hoffmann R, Otvos L, Avilés FX, Ventura S. 2008. Monitoring the interference of proteinprotein interactions in vivo by bimolecular fluorescence complementation: the DnaK case. Proteomics 8: 3433–3442. doi: 10.1002/pmic.200700739.
    • (2008) Proteomics , vol.8 , pp. 3433-3442
    • Morell, M.1    Czihal, P.2    Hoffmann, R.3    Otvos, L.4    Avilés, F.X.5    Ventura, S.6
  • 57
    • 34548530884 scopus 로고    scopus 로고
    • Comprehensive analysis of animal TALE homeobox genes: New conserved motifs and cases of accelerated evolution
    • Mukherjee K, Bürglin TR. 2007. Comprehensive analysis of animal TALE homeobox genes: new conserved motifs and cases of accelerated evolution. Journal of Molecular Evolution 65:137–153. doi: 10.1007/s00239-006-0023-0.
    • (2007) Journal of Molecular Evolution , vol.65 , pp. 137-153
    • Mukherjee, K.1    Bürglin, T.R.2
  • 58
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: Evolutionary interaction switches
    • Neduva V, Russell RB. 2005. Linear motifs: evolutionary interaction switches. FEBS Letters 579:3342–3345. doi: 10.1016/j.febslet.2005.04.005.
    • (2005) FEBS Letters , vol.579 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 59
    • 45449111373 scopus 로고    scopus 로고
    • Analysis of homeodomain specificities allows the family-wide prediction of preferred recognition sites
    • Noyes MB, Christensen RG, Wakabayashi A, Stormo GD, Brodsky MH, Wolfe SA. 2008. Analysis of homeodomain specificities allows the family-wide prediction of preferred recognition sites. Cell 133:1277–1289. doi: 10.1016/j.cell.2008.05.023.
    • (2008) Cell , vol.133 , pp. 1277-1289
    • Noyes, M.B.1    Christensen, R.G.2    Wakabayashi, A.3    Stormo, G.D.4    Brodsky, M.H.5    Wolfe, S.A.6
  • 60
    • 77953637330 scopus 로고    scopus 로고
    • Physical mechanisms of signal integration by WASP family proteins
    • Padrick SB, Rosen MK. 2010. Physical mechanisms of signal integration by WASP family proteins. Annual Review of Biochemistry 79:707–735. doi: 10.1146/annurev.biochem.77.060407.135452.
    • (2010) Annual Review of Biochemistry , vol.79 , pp. 707-735
    • Padrick, S.B.1    Rosen, M.K.2
  • 61
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson T, Gish GD, Nash P. 2001. SH2 domains, interaction modules and cellular wiring. Trends in Cell Biology 11: 504–511. doi: 10.1016/S0962-8924(01)02154-7.
    • (2001) Trends in Cell Biology , vol.11 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 63
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: Modular effectors of cellular regulation
    • Pufall MA, Graves BJ. 2002. Autoinhibitory domains: modular effectors of cellular regulation. Annual Review of Cell and Developmental Biology 18:421–462. doi: 10.1146/annurev.cellbio.18.031502.133614.
    • (2002) Annual Review of Cell and Developmental Biology , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 64
    • 84964313069 scopus 로고    scopus 로고
    • Long non-coding RNAs as a source of new peptides
    • Ruiz-Orera J, Messeguer X, Subirana JA, Alba MM. 2014. Long non-coding RNAs as a source of new peptides. eLife 3:e03523. doi: 10.7554/eLife.03523.
    • (2014) Elife , vol.3
    • Ruiz-Orera, J.1    Messeguer, X.2    Subirana, J.A.3    Alba, M.M.4
  • 67
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • Stein A, Aloy P. 2008. Contextual specificity in peptide-mediated protein interactions. PLOS ONE 3:e2524. doi: 10.1371/journal.pone.0002524.
    • (2008) PLOS ONE , vol.3
    • Stein, A.1    Aloy, P.2
  • 68
    • 77956925998 scopus 로고    scopus 로고
    • Messy biology and the origins of evolutionary innovations
    • Tawfik DS. 2010. Messy biology and the origins of evolutionary innovations. Nature Chemical Biology 6:692–696. doi: 10.1038/nchembio.441.
    • (2010) Nature Chemical Biology , vol.6 , pp. 692-696
    • Tawfik, D.S.1
  • 69
    • 84904469894 scopus 로고    scopus 로고
    • Million peptide motifs for the molecular biologist
    • Tompa P, Davey NE, Gibson TJ, Babu MM. 2014. Million peptide motifs for the molecular biologist. Molecular Cell 55:161–169. doi: 10.1016/j.molcel.2014.05.032.
    • (2014) Molecular Cell , vol.55 , pp. 161-169
    • Tompa, P.1    Davey, N.E.2    Gibson, T.J.3    Babu, M.M.4
  • 71
    • 84876158670 scopus 로고    scopus 로고
    • The switches.ELM resource: A compendium of conditional regulatory interaction interfaces
    • Van Roey K, Dinkel H, Weatheritt RJ, Gibson TJ, Davey NE. 2013. The switches.ELM resource: a compendium of conditional regulatory interaction interfaces. Science Signaling 6:rs7. doi: 10.1126/scisignal.2003345.
    • (2013) Science Signaling , vol.6 , pp. 7
    • Van Roey, K.1    Dinkel, H.2    Weatheritt, R.J.3    Gibson, T.J.4    Davey, N.E.5
  • 73
    • 84902446852 scopus 로고    scopus 로고
    • Short linear motifs: Ubiquitous and functionally diverse protein interaction modules directing cell regulation
    • Van Roey K, Uyar B, Weatheritt RJ, Dinkel H, Seiler M, Budd A, Gibson TJ, Davey NE. 2014. Short linear motifs: Ubiquitous and functionally diverse protein interaction modules directing cell regulation. Chemical Reviews 114: 6733–6778. doi: 10.1021/cr400585q.
    • (2014) Chemical Reviews , vol.114 , pp. 6733-6778
    • Van Roey, K.1    Uyar, B.2    Weatheritt, R.J.3    Dinkel, H.4    Seiler, M.5    Budd, A.6    Gibson, T.J.7    Davey, N.E.8
  • 74
    • 33845698104 scopus 로고    scopus 로고
    • P[acman]: A BAC transgenic platform for targeted insertion of large DNA fragments in D. melanogaster
    • Venken KJ, He Y, Hoskins RA, Bellen HJ. 2006. P[acman]: a BAC transgenic platform for targeted insertion of large DNA fragments in D. melanogaster. Science 314:1747–1751. doi: 10.1126/science.1134426.
    • (2006) Science , vol.314 , pp. 1747-1751
    • Venken, K.J.1    He, Y.2    Hoskins, R.A.3    Bellen, H.J.4
  • 75
    • 35348950692 scopus 로고    scopus 로고
    • Collaboration between Smads and a Hox protein in target gene repression
    • Walsh CM, Carroll SB. 2007. Collaboration between Smads and a Hox protein in target gene repression. Development 134:3585–3592. doi: 10.1242/dev.009522.
    • (2007) Development , vol.134 , pp. 3585-3592
    • Walsh, C.M.1    Carroll, S.B.2
  • 76
    • 34547816223 scopus 로고    scopus 로고
    • The role of Hox genes during vertebrate limb development
    • Zakany J, Duboule D. 2007. The role of Hox genes during vertebrate limb development. Current Opinion in Genetics & Development 17:359–366. doi: 10.1016/j.gde.2007.05.011.
    • (2007) Current Opinion in Genetics & Development , vol.17 , pp. 359-366
    • Zakany, J.1    Duboule, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.