메뉴 건너뛰기




Volumn 31, Issue 5, 2009, Pages 500-511

Classification of sequence signatures: A guide to Hox protein function

Author keywords

Development; Evolution; Homedomain; Hox; Transcription

Indexed keywords

HOX PROTEIN; PEPTIDE DERIVATIVE; TRANSCRIPTION FACTOR; HOMEODOMAIN PROTEIN; NUCLEAR PROTEIN;

EID: 66449088024     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.200800229     Document Type: Review
Times cited : (52)

References (67)
  • 1
    • 0021451768 scopus 로고
    • A homologous protein-coding sequence in Drosophila homeotic genes and its conservation in other metazoans
    • McGinnis, W., Garber, R. L., Wirz, J., Kuroiwa, A. and Gehring, W. J., A homologous protein-coding sequence in Drosophila homeotic genes and its conservation in other metazoans. Cell 1984. 37: 403-408.
    • (1984) Cell , vol.37 , pp. 403-408
    • McGinnis, W.1    Garber, R.L.2    Wirz, J.3    Kuroiwa, A.4    Gehring, W.J.5
  • 2
    • 0021255982 scopus 로고
    • A conserved DNA sequence in homoeotic genes of the Drosophila Antennapedia and bithorax complexes
    • McGinnis, W., Levine, M. S., Hafen, E., Kuroiwa, A. and Gehring, W. J., A conserved DNA sequence in homoeotic genes of the Drosophila Antennapedia and bithorax complexes. Nature 1984. 308: 428-433.
    • (1984) Nature , vol.308 , pp. 428-433
    • McGinnis, W.1    Levine, M.S.2    Hafen, E.3    Kuroiwa, A.4    Gehring, W.J.5
  • 3
    • 0344902715 scopus 로고
    • Structural relationships among genes that control development: Sequence homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of Drosophila
    • Scott, M. P. and Weiner, A. J., Structural relationships among genes that control development: Sequence homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of Drosophila. Proc Natl Acad Sci USA 1984. 81: 4115-4119.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4115-4119
    • Scott, M.P.1    Weiner, A.J.2
  • 4
    • 39149110563 scopus 로고    scopus 로고
    • The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans
    • King, N., Westbrook, M. J., Young, S. L., Kuo, A., Abedin, M., Fairclough, S., et al. The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans. Nature 2008. 451: 783-788.
    • (2008) Nature , vol.451 , pp. 783-788
    • King, N.1    Westbrook, M.J.2    Young, S.L.3    Kuo, A.4    Abedin, M.5    Fairclough, S.6
  • 5
    • 34447300950 scopus 로고    scopus 로고
    • Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization
    • Putnam, N. H., Srivastava, M., Hellsten, U., Dirks, B., Chapman, J., Terry, A., et al. Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization. Science 2007. 317: 86-94.
    • (2007) Science , vol.317 , pp. 86-94
    • Putnam, N.H.1    Srivastava, M.2    Hellsten, U.3    Dirks, B.4    Chapman, J.5    Terry, A.6
  • 6
    • 24344489338 scopus 로고    scopus 로고
    • The evolution of homeobox genes: Implications for the study of brain development
    • Holland, P. W. and Takahashi, T., The evolution of homeobox genes: Implications for the study of brain development. Brain Res Bull 2005. 66: 484-490.
    • (2005) Brain Res Bull , vol.66 , pp. 484-490
    • Holland, P.W.1    Takahashi, T.2
  • 7
    • 0018240421 scopus 로고
    • A gene complex controlling segmentation in Drosophila
    • Lewis, E. B., A gene complex controlling segmentation in Drosophila. Nature 1978. 276: 565-570.
    • (1978) Nature , vol.276 , pp. 565-570
    • Lewis, E.B.1
  • 8
    • 33646481487 scopus 로고    scopus 로고
    • Axial patterning and diversification in the cnidaria predate the Hox system
    • Kamm, K., Schierwater, B., Jakob, W., Dellaporta, S. L. and Miller, D. J., Axial patterning and diversification in the cnidaria predate the Hox system. Curr Biol 2006. 16: 920-926.
    • (2006) Curr Biol , vol.16 , pp. 920-926
    • Kamm, K.1    Schierwater, B.2    Jakob, W.3    Dellaporta, S.L.4    Miller, D.J.5
  • 10
    • 28844477866 scopus 로고    scopus 로고
    • The genesis and evolution of homeobox gene clusters
    • Garcia-Fernandez, J., The genesis and evolution of homeobox gene clusters. Nat Rev Genet 2005. 6: 881-892.
    • (2005) Nat Rev Genet , vol.6 , pp. 881-892
    • Garcia-Fernandez, J.1
  • 11
    • 0026504525 scopus 로고
    • Homeobox genes and axial patterning
    • McGinnis, W. and Krumlauf, R., Homeobox genes and axial patterning. Cell 1992. 68: 283-302.
    • (1992) Cell , vol.68 , pp. 283-302
    • McGinnis, W.1    Krumlauf, R.2
  • 12
    • 28944438404 scopus 로고    scopus 로고
    • Modulating Hox gene functions during animal body patterning
    • Pearson, J. C., Lemons, D. and McGinnis, W., Modulating Hox gene functions during animal body patterning. Nat Rev Genet 2005. 6: 893-904.
    • (2005) Nat Rev Genet , vol.6 , pp. 893-904
    • Pearson, J.C.1    Lemons, D.2    McGinnis, W.3
  • 13
    • 0242297821 scopus 로고    scopus 로고
    • Beyond homeosis-HOX function in morphogenesis and organogenesis
    • Hombria, J. C. and Lovegrove, B., Beyond homeosis-HOX function in morphogenesis and organogenesis. Differentiation 2003. 71: 461-476.
    • (2003) Differentiation , vol.71 , pp. 461-476
    • Hombria, J.C.1    Lovegrove, B.2
  • 14
    • 6044243723 scopus 로고    scopus 로고
    • Direct integration of Hox and segmentation gene inputs during Drosophila development
    • Gebelein, B., McKay, D. J. and Mann, R. S., Direct integration of Hox and segmentation gene inputs during Drosophila development. Nature 2004. 431: 653-659.
    • (2004) Nature , vol.431 , pp. 653-659
    • Gebelein, B.1    McKay, D.J.2    Mann, R.S.3
  • 15
    • 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, L. M., Grimes, H. L., Cook, T. A. and Gebelein, B., Hox and senseless antagonism functions as a molecular switch to regulate EGF secretion in the Drosophila PNS. Dev Cell 2008. 15: 298-308.
    • (2008) Dev 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
  • 16
    • 0029898760 scopus 로고    scopus 로고
    • Extra specificity from extradenticle: The partnership between HOX and PBX/EXD homeodomain proteins
    • Mann, R. S. and Chan, S.-K., Extra specificity from extradenticle: The partnership between HOX and PBX/EXD homeodomain proteins. Trends Genet 1996. 12: 258-262.
    • (1996) Trends Genet , vol.12 , pp. 258-262
    • Mann, R.S.1    Chan, S.-K.2
  • 17
    • 0031718145 scopus 로고    scopus 로고
    • Hox proteins meet more partners
    • Mann, R. S. and Affolter, M., Hox proteins meet more partners. Curr Opin Genet Dev 1998. 8: 423-429.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 423-429
    • Mann, R.S.1    Affolter, M.2
  • 18
    • 23644434573 scopus 로고    scopus 로고
    • Getting a molecular grasp on Hox contextual activity
    • Merabet, S., Pradel, J. and Graba, Y., Getting a molecular grasp on Hox contextual activity. Trends Genet 2005. 21: 477-480.
    • (2005) Trends Genet , vol.21 , pp. 477-480
    • Merabet, S.1    Pradel, J.2    Graba, Y.3
  • 19
    • 0031127044 scopus 로고    scopus 로고
    • Hox genes in evolution: Protein surfaces and paralog groups
    • Sharkey, M., Graba, Y. and Scott, M. P., Hox genes in evolution: protein surfaces and paralog groups. Trends Genet 1997. 13: 145-151.
    • (1997) Trends Genet , vol.13 , pp. 145-151
    • Sharkey, M.1    Graba, Y.2    Scott, M.P.3
  • 21
    • 1642513707 scopus 로고    scopus 로고
    • Homeodomain to hexapeptide or PBC-interaction-domain distance: Size apparently matters
    • In der Rieden, P. M., Mainguy, G. Woltering, J. M. and Durston, A. J., Homeodomain to hexapeptide or PBC-interaction-domain distance: size apparently matters. Trends Genet 2004. 20: 76-79.
    • (2004) Trends Genet , vol.20 , pp. 76-79
    • In der Rieden, P.M.1    Mainguy, G.2    Woltering, J.M.3    Durston, A.J.4
  • 22
    • 0030417483 scopus 로고    scopus 로고
    • Homeodomain-type DNA recognition
    • Billeter, M., Homeodomain-type DNA recognition. Prog Biophys Mol Biol 1996. 66: 211-225.
    • (1996) Prog Biophys Mol Biol , vol.66 , pp. 211-225
    • Billeter, M.1
  • 23
    • 0027936793 scopus 로고
    • The degree of variation in DNA sequence recognition among four Drosophila homeotic proteins
    • Ekker, S. C., Jackson, D. G., Von Kessler, D. P., Sun, B. I., Young, K. E., et al. The degree of variation in DNA sequence recognition among four Drosophila homeotic proteins. EMBO J 1994. 13: 3551-3560.
    • (1994) EMBO J , vol.13 , pp. 3551-3560
    • Ekker, S.C.1    Jackson, D.G.2    Von Kessler, D.P.3    Sun, B.I.4    Young, K.E.5
  • 24
    • 45449111373 scopus 로고    scopus 로고
    • Analysis of homeodomain specificities allows the family-wide prediction of preferred recognition sites
    • Noyes, M. B., Christensen, R. G., Wakabayashi, A., Stormo, G. D., Brodsky, M. H., et al. Analysis of homeodomain specificities allows the family-wide prediction of preferred recognition sites. Cell 2008. 133: 1277-1289.
    • (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
  • 25
    • 45449115390 scopus 로고    scopus 로고
    • Variation in homeodomain DNA binding revealed by high-resolution analysis of sequence preferences
    • Berger, M. F., Badis, G., Gehrke, A. R., Talukder, S., Philippakis, A. A., Alleyne, T. M., et al. Variation in homeodomain DNA binding revealed by high-resolution analysis of sequence preferences. Cell 2008. 133: 1266-1276.
    • (2008) Cell , vol.133 , pp. 1266-1276
    • Berger, M.F.1    Badis, G.2    Gehrke, A.R.3    Talukder, S.4    Philippakis, A.A.5    Alleyne, T.M.6
  • 26
    • 51649088949 scopus 로고    scopus 로고
    • Cross-regulatory protein-protein interactions between Hox and Pax transcription factors
    • Plaza, S., Prince, F., Adachi, Y., Punzo, C., Cribbs, D. L., et al. Cross-regulatory protein-protein interactions between Hox and Pax transcription factors. Proc Natl Acad Sci USA 2008. 105: 13439-13444.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13439-13444
    • Plaza, S.1    Prince, F.2    Adachi, Y.3    Punzo, C.4    Cribbs, D.L.5
  • 27
    • 0027288479 scopus 로고
    • Ectopic expression and function of the Antp and Scr homeotic genes: The N terminus of the homeodomain is critical to functional specificity
    • Zeng, W., Andrew, D. J., Mathies, L. D., Horner, M. A. and Scott, M. P., Ectopic expression and function of the Antp and Scr homeotic genes: The N terminus of the homeodomain is critical to functional specificity. Development 1993. 118: 339-352.
    • (1993) Development , vol.118 , pp. 339-352
    • Zeng, W.1    Andrew, D.J.2    Mathies, L.D.3    Horner, M.A.4    Scott, M.P.5
  • 29
    • 0026718999 scopus 로고
    • Mapping functional specificity in the Dfd and Ubx homeo domains
    • Lin, L. and McGinnis, W., Mapping functional specificity in the Dfd and Ubx homeo domains. Genes Dev 1992. 6: 1071-1081.
    • (1992) Genes Dev , vol.6 , pp. 1071-1081
    • Lin, L.1    McGinnis, W.2
  • 30
    • 0034635969 scopus 로고    scopus 로고
    • Distinct hox protein sequences determine specificity in different tissues
    • Chauvet, S., Merabet, S., Bilder, D., Scott, M. P., Pradel, J., et al. Distinct hox protein sequences determine specificity in different tissues. Proc Natl Acad Sci USA 2000. 97: 4064-4069.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4064-4069
    • Chauvet, S.1    Merabet, S.2    Bilder, D.3    Scott, M.P.4    Pradel, J.5
  • 32
    • 0042161874 scopus 로고    scopus 로고
    • Structure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posterior
    • LaRonde-LeBlanc, N. A. and Wolberger, C., Structure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posterior. Genes Dev 2003. 17: 2060-2072.
    • (2003) Genes Dev , vol.17 , pp. 2060-2072
    • LaRonde-LeBlanc, N.A.1    Wolberger, C.2
  • 33
    • 0028146174 scopus 로고
    • Functional differences between HOX proteins conferred by two residues in the homeodomain N-terminal arm
    • Phelan, M. L., Sadoul, R. and Featherstone, M. S., Functional differences between HOX proteins conferred by two residues in the homeodomain N-terminal arm. Mol Cell Biol 1994. 14: 5066-5075.
    • (1994) Mol Cell Biol , vol.14 , pp. 5066-5075
    • Phelan, M.L.1    Sadoul, R.2    Featherstone, M.S.3
  • 34
    • 35548931586 scopus 로고    scopus 로고
    • Functional specificity of a Hox protein mediated by the recognition of minor groove structure
    • Joshi, R., Passner, J. M., Rohs, R., Jain, R., Sosinsky, A., Jacob, V., et al. Functional specificity of a Hox protein mediated by the recognition of minor groove structure. Cell 2007. 131: 530-543.
    • (2007) Cell , vol.131 , pp. 530-543
    • Joshi, R.1    Passner, J.M.2    Rohs, R.3    Jain, R.4    Sosinsky, A.5    Jacob, V.6
  • 35
    • 0036976764 scopus 로고    scopus 로고
    • Interchange of DNA-binding modes in the deformed and ultrabithorax homeodomains: A structural role for the N-terminal arm
    • Frazee, R. W., Taylor, J. A. and Tullius, T. D., Interchange of DNA-binding modes in the deformed and ultrabithorax homeodomains: a structural role for the N-terminal arm. J Mol Biol 2002. 323: 665-683.
    • (2002) J Mol Biol , vol.323 , pp. 665-683
    • Frazee, R.W.1    Taylor, J.A.2    Tullius, T.D.3
  • 36
    • 0037096841 scopus 로고    scopus 로고
    • Changing homeodomain residues 2 and 3 of Hoxa1 alters its activity in a cell-type and enhancer dependent manner
    • Remacle, S., Shaw-Jackson, C., Matis, C., Lampe, X., Picard, J., et al. Changing homeodomain residues 2 and 3 of Hoxa1 alters its activity in a cell-type and enhancer dependent manner. Nucleic Acids Res 2002. 30: 2663-2668.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2663-2668
    • Remacle, S.1    Shaw-Jackson, C.2    Matis, C.3    Lampe, X.4    Picard, J.5
  • 37
    • 0035808470 scopus 로고    scopus 로고
    • A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA binding, transactivation, and transforming activities
    • Kataoka, K., Yoshitomo-Nakagawa, K., Shioda, S. and Nishizawa, M., A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA binding, transactivation, and transforming activities. J Biol Chem 2001. 276: 819-826.
    • (2001) J Biol Chem , vol.276 , pp. 819-826
    • Kataoka, K.1    Yoshitomo-Nakagawa, K.2    Shioda, S.3    Nishizawa, M.4
  • 38
    • 0033958662 scopus 로고    scopus 로고
    • Smad1 domains interacting with Hoxc-8 induce osteoblast differentiation
    • Yang, X., Ji, X., Shi, X. and Cao, X., Smad1 domains interacting with Hoxc-8 induce osteoblast differentiation. J Biol Chem 2000. 275: 1065-1072.
    • (2000) J Biol Chem , vol.275 , pp. 1065-1072
    • Yang, X.1    Ji, X.2    Shi, X.3    Cao, X.4
  • 39
    • 0029788292 scopus 로고    scopus 로고
    • Homeodomain interaction with the beta subunit of the general transcription factor TFIIE
    • Zhu, A. and Kuziora, M. A., Homeodomain interaction with the beta subunit of the general transcription factor TFIIE. J Biol Chem 1996. 271: 20993-20996.
    • (1996) J Biol Chem , vol.271 , pp. 20993-20996
    • Zhu, A.1    Kuziora, M.A.2
  • 40
    • 4544348050 scopus 로고    scopus 로고
    • HOXB6 protein is bound to CREB-binding protein and represses globin expression in a DNA binding-dependent, PBX interaction-independent process
    • Shen, W., Chrobak, D., Krishnan, K., Lawrence, H. J. and Largman, C., HOXB6 protein is bound to CREB-binding protein and represses globin expression in a DNA binding-dependent, PBX interaction-independent process. J Biol Chem 2004. 279: 39895-39904.
    • (2004) J Biol Chem , vol.279 , pp. 39895-39904
    • Shen, W.1    Chrobak, D.2    Krishnan, K.3    Lawrence, H.J.4    Largman, C.5
  • 41
    • 0029811475 scopus 로고    scopus 로고
    • HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation
    • Zappavigna, V., Falciola, L., Citterich, M. H., Mavilio, F. and Bianchi, M. E., HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation. EMBO J 1996. 15: 4981-4991.
    • (1996) EMBO J , vol.15 , pp. 4981-4991
    • Zappavigna, V.1    Falciola, L.2    Citterich, M.H.3    Mavilio, F.4    Bianchi, M.E.5
  • 42
    • 0043031450 scopus 로고    scopus 로고
    • Hox proteins functionally cooperate with the GC box-binding protein system through distinct domains
    • Suzuki, M., Ueno, N. and Kuroiwa, A., Hox proteins functionally cooperate with the GC box-binding protein system through distinct domains. J Biol Chem 2003. 278: 30148-30156.
    • (2003) J Biol Chem , vol.278 , pp. 30148-30156
    • Suzuki, M.1    Ueno, N.2    Kuroiwa, A.3
  • 43
    • 1442305333 scopus 로고    scopus 로고
    • The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions
    • Luo, L., Yang, X., Takihara, Y., Knoetgen, H. and Kessel, M., The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions. Nature 2004. 427: 749-753.
    • (2004) Nature , vol.427 , pp. 749-753
    • Luo, L.1    Yang, X.2    Takihara, Y.3    Knoetgen, H.4    Kessel, M.5
  • 44
    • 0027966927 scopus 로고
    • The DNA binding specificity of Ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein
    • Chan, S. K., Jaffe, L., Capovilla,M., Botas, J. and Mann, R. S., The DNA binding specificity of Ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein. Cell 1994. 78: 603-615.
    • (1994) Cell , vol.78 , pp. 603-615
    • Chan, S.K.1    Jaffe, L.2    Capovilla, M.3    Botas, J.4    Mann, R.S.5
  • 45
    • 0028350269 scopus 로고
    • Specificity of HOX protein function depends on DNA-protein and protein-protein interactions, both mediated by the homeo domain
    • Zappavigna, V., Sartori, D. and Mavilio, F., Specificity of HOX protein function depends on DNA-protein and protein-protein interactions, both mediated by the homeo domain. Genes Dev 1994. 8: 732-744.
    • (1994) Genes Dev , vol.8 , pp. 732-744
    • Zappavigna, V.1    Sartori, D.2    Mavilio, F.3
  • 46
    • 0034796574 scopus 로고    scopus 로고
    • The HOX homeodomain proteins block CBP histone acetyltransferase activity
    • Shen, W. F., Krishnan, K., Lawrence, H. J. and Largman, C., The HOX homeodomain proteins block CBP histone acetyltransferase activity. Mol Cell Biol 2001. 21: 7509-7522.
    • (2001) Mol Cell Biol , vol.21 , pp. 7509-7522
    • Shen, W.F.1    Krishnan, K.2    Lawrence, H.J.3    Largman, C.4
  • 47
    • 0033536061 scopus 로고    scopus 로고
    • Activity regulation of Hox proteins, a mechanism for altering functional specificity in development and evolution
    • Li, X. and McGinnis, W., Activity regulation of Hox proteins, a mechanism for altering functional specificity in development and evolution. Proc Natl Acad Sci USA 1999. 96: 6802-6807.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6802-6807
    • Li, X.1    McGinnis, W.2
  • 48
    • 0033521623 scopus 로고    scopus 로고
    • Activity regulation of a Hox protein and a role for the homeodomain in inhibiting transcriptional activation
    • Li, X., Murre, C. and McGinnis, W., Activity regulation of a Hox protein and a role for the homeodomain in inhibiting transcriptional activation. EMBO J 1999. 18: 198-211.
    • (1999) EMBO J , vol.18 , pp. 198-211
    • Li, X.1    Murre, C.2    McGinnis, W.3
  • 49
    • 0027191867 scopus 로고
    • The segment identity functions of Ultrabithorax are contained within its homeo domain and carboxy-terminal sequences
    • Chan, S. K. and Mann, R. S., The segment identity functions of Ultrabithorax are contained within its homeo domain and carboxy-terminal sequences. Genes Dev 1993. 7: 796-811.
    • (1993) Genes Dev , vol.7 , pp. 796-811
    • Chan, S.K.1    Mann, R.S.2
  • 50
    • 0030802426 scopus 로고    scopus 로고
    • Residues flanking the HOX YPWM motif contribute to cooperative interactions with PBX
    • Shanmugam, K., Featherstone, M. S. and Saragovi, H. U., Residues flanking the HOX YPWM motif contribute to cooperative interactions with PBX. J Biol Chem 1997. 272: 19081-19087.
    • (1997) J Biol Chem , vol.272 , pp. 19081-19087
    • Shanmugam, K.1    Featherstone, M.S.2    Saragovi, H.U.3
  • 51
    • 0029939199 scopus 로고    scopus 로고
    • Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus
    • Chang, C. P., Brocchieri, L., Shen, W. F., Largman, C. and Cleary, M. L., Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus. Mol Cell Biol 1996. 16: 1734-1745.
    • (1996) Mol Cell Biol , vol.16 , pp. 1734-1745
    • Chang, C.P.1    Brocchieri, L.2    Shen, W.F.3    Largman, C.4    Cleary, M.L.5
  • 52
    • 0028175730 scopus 로고
    • Functional differences between Ultrabithorax protein isoforms in Drosophila melanogaster: Evidence from elimination, substitution and ectopic expression of specific isoforms
    • Subramaniam, V., Bomze, H. M. and Lopez, A. J., Functional differences between Ultrabithorax protein isoforms in Drosophila melanogaster: Evidence from elimination, substitution and ectopic expression of specific isoforms. Genetics 1994. 136: 979-991.
    • (1994) Genetics , vol.136 , pp. 979-991
    • Subramaniam, V.1    Bomze, H.M.2    Lopez, A.J.3
  • 53
    • 0036774750 scopus 로고    scopus 로고
    • Specificity of distalless repression and limb primordia development by abdominal hox proteins
    • Gebelein, B., Culi, J., Ryoo, H. D., Zhang, W. and Mann, R. S., Specificity of distalless repression and limb primordia development by abdominal hox proteins. Dev Cell 2002. 3: 487-498.
    • (2002) Dev Cell , vol.3 , pp. 487-498
    • Gebelein, B.1    Culi, J.2    Ryoo, H.D.3    Zhang, W.4    Mann, R.S.5
  • 54
    • 4544285896 scopus 로고    scopus 로고
    • Loss of function but no gain of function caused by amino acid substitutions in the hexapeptide of Hoxa1 in vivo
    • Remacle, S., Abbas, L., De Backer, O., Pacico, N., Gavalas, A., Picard, J. J., et al. Loss of function but no gain of function caused by amino acid substitutions in the hexapeptide of Hoxa1 in vivo. Mol Cell Biol 2004. 24: 8567-8575.
    • (2004) Mol Cell Biol , vol.24 , pp. 8567-8575
    • Remacle, S.1    Abbas, L.2    De Backer, O.3    Pacico, N.4    Gavalas, A.5    Picard, J.J.6
  • 55
    • 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. and Ramirez-Solis, R., 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. Dev Biol 2003. 264: 77-90.
    • (2003) Dev Biol , vol.264 , pp. 77-90
    • Medina-Martinez, O.1    Ramirez-Solis, R.2
  • 56
    • 29644440598 scopus 로고    scopus 로고
    • Evolutionarily conserved domains required for activation and repression functions of the Drosophila Hox protein Ultrabithorax
    • Tour, E., Hittinger, C. T. and McGinnis, W., Evolutionarily conserved domains required for activation and repression functions of the Drosophila Hox protein Ultrabithorax. Development 2005. 132: 5271-5281.
    • (2005) Development , vol.132 , pp. 5271-5281
    • Tour, E.1    Hittinger, C.T.2    McGinnis, W.3
  • 57
    • 0029917042 scopus 로고    scopus 로고
    • Functional dissection of the mouse Hox-a5 gene
    • Zhao, J. J. G., Lazzarini, R. A. and Pick, L., Functional dissection of the mouse Hox-a5 gene. EMBO J 1996. 15: 1313-1322.
    • (1996) EMBO J , vol.15 , pp. 1313-1322
    • Zhao, J.J.G.1    Lazzarini, R.A.2    Pick, L.3
  • 58
    • 36448980363 scopus 로고    scopus 로고
    • A unique Extradenticle recruitment mode in the Drosophila Hox protein Ultrabithorax
    • Merabet, S., Saadaoui, M., Sambrani, N., Hudry, B., Pradel, J., Graba, Y., et al. A unique Extradenticle recruitment mode in the Drosophila Hox protein Ultrabithorax. Proc Natl Acad Sci USA 2007. 104: 16946-16951.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16946-16951
    • Merabet, S.1    Saadaoui, M.2    Sambrani, N.3    Hudry, B.4    Pradel, J.5    Graba, Y.6
  • 59
    • 0036337125 scopus 로고    scopus 로고
    • Hox repression of a target gene: Extradenticle-independent, additive action through multiple monomer binding sites
    • Galant, R., Walsh, C. M. and Carroll, S. B., Hox repression of a target gene: Extradenticle-independent, additive action through multiple monomer binding sites. Development 2002. 129: 3115-3126.
    • (2002) Development , vol.129 , pp. 3115-3126
    • Galant, R.1    Walsh, C.M.2    Carroll, S.B.3
  • 60
    • 0037148774 scopus 로고    scopus 로고
    • Evolution of a transcriptional repression domain in an insect Hox protein
    • Galant, R. and Carroll, S. B., Evolution of a transcriptional repression domain in an insect Hox protein. Nature 2002. 415: 910-913.
    • (2002) Nature , vol.415 , pp. 910-913
    • Galant, R.1    Carroll, S.B.2
  • 61
    • 0037148839 scopus 로고    scopus 로고
    • Hox protein mutation and macroevolution of the insect body plan
    • Ronshaugen, M., McGinnis, N. and McGinnis, W., Hox protein mutation and macroevolution of the insect body plan. Nature 2002. 415: 914-917.
    • (2002) Nature , vol.415 , pp. 914-917
    • Ronshaugen, M.1    McGinnis, N.2    McGinnis, W.3
  • 62
    • 0035908952 scopus 로고    scopus 로고
    • Drosophila fushi tarazu. A gene on the border of homeotic function
    • Lohr, U., Yussa, M. and Pick, L., Drosophila fushi tarazu. A gene on the border of homeotic function. Curr Biol 2001. 11: 1403-1412.
    • (2001) Curr Biol , vol.11 , pp. 1403-1412
    • Lohr, U.1    Yussa, M.2    Pick, L.3
  • 63
    • 17144415299 scopus 로고    scopus 로고
    • Cofactor-interaction motifs and the cooption of a homeotic Hox protein into the segmentation pathway of Drosophila melanogaster
    • Lohr, U. and Pick, L., Cofactor-interaction motifs and the cooption of a homeotic Hox protein into the segmentation pathway of Drosophila melanogaster. Curr Biol 2005. 15: 643-649.
    • (2005) Curr Biol , vol.15 , pp. 643-649
    • Lohr, U.1    Pick, L.2
  • 64
    • 0029894663 scopus 로고    scopus 로고
    • Repression by HoxA7 is mediated by the homeodomain and the modulatory action of its N-terminal-arm residues
    • Schnabel, C. A. and Abate-Shen, C., Repression by HoxA7 is mediated by the homeodomain and the modulatory action of its N-terminal-arm residues. MolCellBiol 1996. 16: 2678-2688.
    • (1996) MolCellBiol , vol.16 , pp. 2678-2688
    • Schnabel, C.A.1    Abate-Shen, C.2
  • 65
    • 0033582545 scopus 로고    scopus 로고
    • Structure of a HoxB1-Pbx1 heterodimer bound to DNA: Role of the hexapeptide and a fourth homeodomain helix in complex formation
    • Piper, D. E., Batchelor, A. H., Chang, C. P., Cleary, M. L. and Wolberger, C., Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation. Cell 1999. 96: 587-597.
    • (1999) Cell , vol.96 , pp. 587-597
    • Piper, D.E.1    Batchelor, A.H.2    Chang, C.P.3    Cleary, M.L.4    Wolberger, C.5
  • 66
    • 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., Berenger, H., Pradel, J., et al. The hexapeptide and linker regions of the AbdA Hox protein regulate its activating and repressive functions. Dev Cell 2003. 4: 761-768.
    • (2003) Dev Cell , vol.4 , pp. 761-768
    • Merabet, S.1    Kambris, Z.2    Capovilla, M.3    Berenger, H.4    Pradel, J.5
  • 67
    • 34548530884 scopus 로고    scopus 로고
    • Comprehensive analysis of animal TALE homeobox genes: New conserved motifs and cases of accelerated evolution
    • Mukherjee, K. and Burglin, T. R., Comprehensive analysis of animal TALE homeobox genes: New conserved motifs and cases of accelerated evolution. J Mol Evol 2007. 65: 137-153.
    • (2007) J Mol Evol , vol.65 , pp. 137-153
    • Mukherjee, K.1    Burglin, T.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.