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Volumn 11, Issue 2-3, 1998, Pages 89-102

Zinc transcription factors in cellular differentiation and organogenesis

Author keywords

Gene expression; Oogenesis; Organogenesis; Transcription factors; Xenopus laevis; Zinc

Indexed keywords

MESSENGER RNA; RNA POLYMERASE; TRANSCRIPTION FACTOR; ZINC; ZINC FINGER PROTEIN;

EID: 0031879314     PISSN: 0896548X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1520-670x(1998)11:2/3<89::aid-jtra3>3.0.co;2-%23     Document Type: Article
Times cited : (4)

References (100)
  • 1
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee BL, Falchuk KH: The biochemical basis of zinc physiology. Physiol Rev 73:79, 1993.
    • (1993) Physiol Rev , vol.73 , pp. 79
    • Vallee, B.L.1    Falchuk, K.H.2
  • 4
    • 0017870725 scopus 로고
    • Zinc deficiency in murine milk underlies expression of the lethal milk (1m) mutation
    • Piletz JE, Ganschow RE: Zinc deficiency in murine milk underlies expression of the lethal milk (1m) mutation. Science 199:181, 1978.
    • (1978) Science , vol.199 , pp. 181
    • Piletz, J.E.1    Ganschow, R.E.2
  • 5
    • 18144414477 scopus 로고
    • Evidence of a lethal trait, A46, in black pied Danish cattle of Freisian descent
    • Andresen E, Flagstad T, Brummensted E: Evidence of a lethal trait, A46, in black pied Danish cattle of Freisian descent. Nord Veterinaermed 11:473, 1970.
    • (1970) Nord Veterinaermed , vol.11 , pp. 473
    • Andresen, E.1    Flagstad, T.2    Brummensted, E.3
  • 7
    • 0017062639 scopus 로고
    • Hereditary zinc deficiency (Adema disease) in cattle, an animal parallel to acrodermatitis enteropathica
    • Weissman K, Flagsted T: Hereditary zinc deficiency (Adema disease) in cattle, an animal parallel to acrodermatitis enteropathica. Act Derm-Venereol 56:151, 1976.
    • (1976) Act Derm-Venereol , vol.56 , pp. 151
    • Weissman, K.1    Flagsted, T.2
  • 8
    • 73649181547 scopus 로고
    • Zinc metabolism in patients with the syndrome of iron deficiency, hypogonadism and dwarfism
    • Prasad AS, Miale Jr A, Fand Z, Schulert A, Sandstead HH: Zinc metabolism in patients with the syndrome of iron deficiency, hypogonadism and dwarfism. J Lab Clin Med 61:537, 1963.
    • (1963) J Lab Clin Med , vol.61 , pp. 537
    • Prasad, A.S.1    Miale Jr., A.2    Fand, Z.3    Schulert, A.4    Sandstead, H.H.5
  • 9
    • 0016395653 scopus 로고
    • Acrodermatitis enteropathica: A lethal inherited human zinc deficiency disorder
    • Moynahan EJ: Acrodermatitis enteropathica: A lethal inherited human zinc deficiency disorder. Lancet 2:399, 1974.
    • (1974) Lancet , vol.2 , pp. 399
    • Moynahan, E.J.1
  • 10
    • 0002199939 scopus 로고
    • Zinc and reproduction: Effects of deficiency on foetal and postnatal development
    • Mills CF (ed): London: Springer-Verlag
    • Keen CL, Hurley LS: Zinc and reproduction: Effects of deficiency on foetal and postnatal development. In Mills CF (ed): "Zinc in Human Biology." London: Springer-Verlag, 1989, p 183.
    • (1989) Zinc in Human Biology , pp. 183
    • Keen, C.L.1    Hurley, L.S.2
  • 13
    • 0027350998 scopus 로고
    • Zinc in developmental biology: The role of metal dependent transcriptional regulation
    • Prasad AS: New York: Liss
    • Falchuk KH: Zinc in developmental biology: The role of metal dependent transcriptional regulation. In Prasad AS: "Essential and Toxic Trace Elements in Human Health and Disease: An Update." New York: Liss, 1993, p 91.
    • (1993) Essential and Toxic Trace Elements in Human Health and Disease: An Update , pp. 91
    • Falchuk, K.H.1
  • 15
    • 0040215628 scopus 로고
    • Repetitive zinc binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller J, McLachlan AD, Klug A: Repetitive zinc binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J 4:1609, 1985.
    • (1985) EMBO J , vol.4 , pp. 1609
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 16
    • 0027365593 scopus 로고
    • Zinc, iron, and copper contents of Xenopus laevis oocytes and embryos
    • Nomizu T, Falchuk KH, Vallee BL: Zinc, iron, and copper contents of Xenopus laevis oocytes and embryos. Mol Reprod Dev 36:419, 1993.
    • (1993) Mol Reprod Dev , vol.36 , pp. 419
    • Nomizu, T.1    Falchuk, K.H.2    Vallee, B.L.3
  • 19
    • 0029096711 scopus 로고
    • Vitellogenin and lipovitellin: Zinc proteins of Xenopus laevis oocytes
    • Montorzi M, Falchuk KH, Vallee BL: Vitellogenin and lipovitellin: Zinc proteins of Xenopus laevis oocytes. Biochemistry 34:10851, 1995.
    • (1995) Biochemistry , vol.34 , pp. 10851
    • Montorzi, M.1    Falchuk, K.H.2    Vallee, B.L.3
  • 20
    • 0029560868 scopus 로고
    • Zinc uptake and distribution in Xenopus laevis oocytes and embryos
    • Falchuk KH, Montorzi M, Vallee BL: Zinc uptake and distribution in Xenopus laevis oocytes and embryos. Biochemistry 34:16524, 1995.
    • (1995) Biochemistry , vol.34 , pp. 16524
    • Falchuk, K.H.1    Montorzi, M.2    Vallee, B.L.3
  • 21
    • 0023085356 scopus 로고
    • Zinc in DNA replication and transcription
    • Wu FY-H, Wu C-W: Zinc in DNA replication and transcription. Annu Rev Nutr 7:251, 1987.
    • (1987) Annu Rev Nutr , vol.7 , pp. 251
    • Wu, F.Y.-H.1    Wu, C.-W.2
  • 22
    • 0026766977 scopus 로고
    • Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman J: Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins. Ann Rev Biochem 61:897, 1992.
    • (1992) Ann Rev Biochem , vol.61 , pp. 897
    • Coleman, J.1
  • 23
    • 0016434533 scopus 로고
    • Role of zinc in cell division of Euglena gracilis
    • Falchuk KH, Fawcett D, Vallee BL: Role of zinc in cell division of Euglena gracilis. J Cell Sci 17:57, 1975.
    • (1975) J Cell Sci , vol.17 , pp. 57
    • Falchuk, K.H.1    Fawcett, D.2    Vallee, B.L.3
  • 24
    • 0018125013 scopus 로고
    • RNA metabolism, manganese and RNA polymerases of zinc sufficient and zinc-deficient Euglena gracilis
    • Falchuk KH, Hardy C, Ulpino L, Vallee BL: RNA metabolism, manganese and RNA polymerases of zinc sufficient and zinc-deficient Euglena gracilis. Proc Natl Acad Sci USA 75:4175, 1978.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4175
    • Falchuk, K.H.1    Hardy, C.2    Ulpino, L.3    Vallee, B.L.4
  • 25
    • 0022420480 scopus 로고
    • Zinc deficiency and the Euglena gracilis chromatin: Formation of an alpha-amanitin-resistant RNA polymerase II
    • Falchuk KH, Mazus B, Ber E, Ulpino-Lobb L, Vallee BL: Zinc deficiency and the Euglena gracilis chromatin: Formation of an alpha-amanitin-resistant RNA polymerase II. Biochemistry 24:2576, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2576
    • Falchuk, K.H.1    Mazus, B.2    Ber, E.3    Ulpino-Lobb, L.4    Vallee, B.L.5
  • 26
    • 0020481295 scopus 로고
    • Messenger ribonucleic acid function and protein synthesis in zinc deficient E. gracilis
    • Crossley LL, Falchuk KH, Vallee BL: Messenger ribonucleic acid function and protein synthesis in zinc deficient E. gracilis. Biochemistry 21:5359, 1982.
    • (1982) Biochemistry , vol.21 , pp. 5359
    • Crossley, L.L.1    Falchuk, K.H.2    Vallee, B.L.3
  • 27
    • 0021112629 scopus 로고
    • Composition and structure of zinc deficient Euglena gracilis chromatin
    • Stankiewicz A, Falchuk KH, Vallee BL: Composition and structure of zinc deficient Euglena gracilis chromatin. Biochemistry 22:5150, 1983.
    • (1983) Biochemistry , vol.22 , pp. 5150
    • Stankiewicz, A.1    Falchuk, K.H.2    Vallee, B.L.3
  • 28
    • 0021753967 scopus 로고
    • Histone formation, gene expression and zinc deficiency in Euglena gracilis
    • Mazus B, Falchuk KH, Vallee BL: Histone formation, gene expression and zinc deficiency in Euglena gracilis. Biochemistry 23:42, 1984.
    • (1984) Biochemistry , vol.23 , pp. 42
    • Mazus, B.1    Falchuk, K.H.2    Vallee, B.L.3
  • 30
    • 7344242231 scopus 로고
    • Zinc deficiency decreases histone H1* in rat liver
    • Castro CE, Alvares OF, Seval JS: Zinc deficiency decreases histone H1* in rat liver. Nutr Rep Int 34:67, 1986.
    • (1986) Nutr Rep Int , vol.34 , pp. 67
    • Castro, C.E.1    Alvares, O.F.2    Seval, J.S.3
  • 31
    • 0007988013 scopus 로고
    • Zinc deficiency and metabolism of histones and nonhistone proteins in Euglena gracilis
    • Czupryn M, Falchuk KH, Vallee BL: Zinc deficiency and metabolism of histones and nonhistone proteins in Euglena gracilis. Biochemistry 26:8263, 1987.
    • (1987) Biochemistry , vol.26 , pp. 8263
    • Czupryn, M.1    Falchuk, K.H.2    Vallee, B.L.3
  • 32
    • 0021233482 scopus 로고
    • The role of stable complexes that repress and activate eukaryotic genes
    • Brown DD: The role of stable complexes that repress and activate eukaryotic genes. Cell 37:359, 1984.
    • (1984) Cell , vol.37 , pp. 359
    • Brown, D.D.1
  • 33
    • 1842358316 scopus 로고
    • Isolation of a 7S particle from Xenopus laevis oocytes: A 5S RNA-protein complex
    • Picard B, Wegnez M: Isolation of a 7S particle from Xenopus laevis oocytes: A 5S RNA-protein complex. Proc Natl Acad Sci USA 76:241, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 241
    • Picard, B.1    Wegnez, M.2
  • 34
    • 0024811682 scopus 로고
    • Zinc release from Xenopus transcription factor IIIA induced by chemical modifications
    • Shang Z, Liao Y-D, Wu Y-D, Wu C-W: Zinc release from Xenopus transcription factor IIIA induced by chemical modifications. Biochemistry 28:9790, 1989.
    • (1989) Biochemistry , vol.28 , pp. 9790
    • Shang, Z.1    Liao, Y.-D.2    Wu, Y.-D.3    Wu, C.-W.4
  • 35
    • 0000613310 scopus 로고
    • "Zinc fingers": A novel protein motif for nucleic acid recognition
    • Klug A, Rhodes D: "Zinc fingers": A novel protein motif for nucleic acid recognition. Trends Biochem Sci 12:464, 1987.
    • (1987) Trends Biochem Sci , vol.12 , pp. 464
    • Klug, A.1    Rhodes, D.2
  • 36
    • 0021710076 scopus 로고
    • Xenopus 5S gene transcription factor, TFIIIA: Characterization of a cDNA clone and measurement of RNA levels throughout development
    • Ginsberg AM, King BO, Roeder RG: Xenopus 5S gene transcription factor, TFIIIA: Characterization of a cDNA clone and measurement of RNA levels throughout development. Cell 39:479, 1984.
    • (1984) Cell , vol.39 , pp. 479
    • Ginsberg, A.M.1    King, B.O.2    Roeder, R.G.3
  • 37
    • 0022421362 scopus 로고
    • The primary structure of transcription factor TFIIIA has twelve consecutive repeats
    • Brown RS, Sander C, Argos P: The primary structure of transcription factor TFIIIA has twelve consecutive repeats. FEBS Lett 186:271, 1985.
    • (1985) FEBS Lett , vol.186 , pp. 271
    • Brown, R.S.1    Sander, C.2    Argos, P.3
  • 38
    • 0023375317 scopus 로고
    • Metal-dependent folding of single zinc finger from transcription factor IIIA
    • Frankel AD, Berg JM, Pabo CO: Metal-dependent folding of single zinc finger from transcription factor IIIA. Proc Natl Acad Sci USA 84:4841, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4841
    • Frankel, A.D.1    Berg, J.M.2    Pabo, C.O.3
  • 39
    • 0023029134 scopus 로고
    • EXAFS study of the zinc-binding sites in the protein transcription factor IIIA
    • Diakun GP, Fairall L, Klug A: EXAFS study of the zinc-binding sites in the protein transcription factor IIIA. Nature Lond 324:698, 1986.
    • (1986) Nature Lond , vol.324 , pp. 698
    • Diakun, G.P.1    Fairall, L.2    Klug, A.3
  • 40
    • 0023782854 scopus 로고
    • A model for the tertiary structure of the 28 residue DNA-binding motif "zinc finger" common to many eukaryotic transcriptional regulatory proteins
    • Gibson TJ, Postma JP, Brown RS, Argos P: A model for the tertiary structure of the 28 residue DNA-binding motif "zinc finger" common to many eukaryotic transcriptional regulatory proteins. Protein Eng 2:209, 1988.
    • (1988) Protein Eng , vol.2 , pp. 209
    • Gibson, T.J.1    Postma, J.P.2    Brown, R.S.3    Argos, P.4
  • 41
    • 0024341072 scopus 로고
    • Three-dimensional solution structure of a single zinc finger DNA-binding domain
    • Lee MS, Gippert GP, Soman KV, Case DA, Wright PE: Three-dimensional solution structure of a single zinc finger DNA-binding domain. Science Wash DC 245:645, 1989.
    • (1989) Science Wash DC , vol.245 , pp. 645
    • Lee, M.S.1    Gippert, G.P.2    Soman, K.V.3    Case, D.A.4    Wright, P.E.5
  • 43
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich NP, Pabo CO: Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å. Science Wash DC 252:809, 1991.
    • (1991) Science Wash DC , vol.252 , pp. 809
    • Pavletich, N.P.1    Pabo, C.O.2
  • 44
    • 0026558279 scopus 로고
    • Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5S RNA gene
    • Liao X, Clemens KR, Tennant PE, Wright JM, Gottesfeld M: Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5S RNA gene. J Mol Biol 223:857, 1992.
    • (1992) J Mol Biol , vol.223 , pp. 857
    • Liao, X.1    Clemens, K.R.2    Tennant, P.E.3    Wright, J.M.4    Gottesfeld, M.5
  • 45
    • 0027423758 scopus 로고
    • Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers
    • Pavletich NP, Pabo CO: Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers. Science Wash DC 261:1701, 1993.
    • (1993) Science Wash DC , vol.261 , pp. 1701
    • Pavletich, N.P.1    Pabo, C.O.2
  • 46
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor super-family
    • Evans RM: The steroid and thyroid hormone receptor super-family. Science Wash DC 240:889, 1988.
    • (1988) Science Wash DC , vol.240 , pp. 889
    • Evans, R.M.1
  • 48
    • 0023649571 scopus 로고
    • Colocalization of DNA-binding and transcriptional activation functions in the human glucocorticoid receptor
    • Hollenberg SM, Gigure V, Segui P, Evans RM: Colocalization of DNA-binding and transcriptional activation functions in the human glucocorticoid receptor. Cell 49:39, 1987.
    • (1987) Cell , vol.49 , pp. 39
    • Hollenberg, S.M.1    Gigure, V.2    Segui, P.3    Evans, R.M.4
  • 49
    • 0023769378 scopus 로고
    • The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
    • Freedman LP, Luisi BF, Korszun ZR, Basavappa R, Sigler PB, Yamamoto KR: The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature Lond 334:543, 1988.
    • (1988) Nature Lond , vol.334 , pp. 543
    • Freedman, L.P.1    Luisi, B.F.2    Korszun, Z.R.3    Basavappa, R.4    Sigler, P.B.5    Yamamoto, K.R.6
  • 52
    • 0025082229 scopus 로고
    • Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor
    • Pan T, Freedman LP, Coleman JE: Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor. Biochemistry 29:9218, 1990.
    • (1990) Biochemistry , vol.29 , pp. 9218
    • Pan, T.1    Freedman, L.P.2    Coleman, J.E.3
  • 53
    • 0024064789 scopus 로고
    • Metal binding "finger" structures in the glucocorticoid receptor defined by site directed mutagenesis
    • Severne Y, Wieland S, Schaffner W, Rusconi S: Metal binding "finger" structures in the glucocorticoid receptor defined by site directed mutagenesis. EMBO J 8:2503, 1988.
    • (1988) EMBO J , vol.8 , pp. 2503
    • Severne, Y.1    Wieland, S.2    Schaffner, W.3    Rusconi, S.4
  • 55
    • 0023664574 scopus 로고
    • The binding activity of estrogen receptor to DNA and heat shock protein is dependent on receptor-bound metal
    • Sabbah M, Redeuilh G, Secco C, Baulilieu E-E: The binding activity of estrogen receptor to DNA and heat shock protein is dependent on receptor-bound metal. J Biol Chem 262:8631, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 8631
    • Sabbah, M.1    Redeuilh, G.2    Secco, C.3    Baulilieu, E.-E.4
  • 56
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • Schwabe JWR, Neuhaus D, Rhodes D: Solution structure of the DNA-binding domain of the oestrogen receptor. Nature Lond 348:458, 1990.
    • (1990) Nature Lond , vol.348 , pp. 458
    • Jwr, S.1    Neuhaus, D.2    Rhodes, D.3
  • 57
    • 0021924399 scopus 로고
    • Specific DNA binding of GAL4, a positive regulatory protein of yeast
    • Giniger E, Varnum SM, Ptashne M: Specific DNA binding of GAL4, a positive regulatory protein of yeast. Cell 40:767, 1985.
    • (1985) Cell , vol.40 , pp. 767
    • Giniger, E.1    Varnum, S.M.2    Ptashne, M.3
  • 58
    • 0022622235 scopus 로고
    • Separation of DNA binding from the transcription-activation function of a eukaryotic regulatory protein
    • Keegan LG, Gill G, Ptashne M: Separation of DNA binding from the transcription-activation function of a eukaryotic regulatory protein. Science Wash DC 231:699, 1986.
    • (1986) Science Wash DC , vol.231 , pp. 699
    • Keegan, L.G.1    Gill, G.2    Ptashne, M.3
  • 59
    • 0023274870 scopus 로고
    • Genetic evidence that zinc is an essential co-factor in the DNA binding domain of GAL4 protein
    • Johnston M: Genetic evidence that zinc is an essential co-factor in the DNA binding domain of GAL4 protein. Nature Lond 328:353, 1987.
    • (1987) Nature Lond , vol.328 , pp. 353
    • Johnston, M.1
  • 60
    • 0004454148 scopus 로고
    • Structure and function of the Zn(II) binding site within the DNA-binding domain of the GAL4 transcription factor
    • Pan T, Coleman JE: Structure and function of the Zn(II) binding site within the DNA-binding domain of the GAL4 transcription factor. Proc Natl Acad Sci USA 86:3145, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3145
    • Pan, T.1    Coleman, J.E.2
  • 64
    • 0023990358 scopus 로고
    • Tat protein from human immunodeficiency virus forms a metal-linked dimer
    • Frankel AD, Chen L, Cotter RJ, Pabo CO: Tat protein from human immunodeficiency virus forms a metal-linked dimer. Science Wash DC 240:70, 1988.
    • (1988) Science Wash DC , vol.240 , pp. 70
    • Frankel, A.D.1    Chen, L.2    Cotter, R.J.3    Pabo, C.O.4
  • 65
    • 0023681468 scopus 로고
    • Dimerization of the tat protein from human immuno-deficiency virus: A cysteine rich peptide mimics the normal metal-linked dimer interface
    • Frankel AD, Chen L, Cotter RJ, Pabo CO: Dimerization of the tat protein from human immuno-deficiency virus: A cysteine rich peptide mimics the normal metal-linked dimer interface. Proc Natl Acad Sci USA 85:6297, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6297
    • Frankel, A.D.1    Chen, L.2    Cotter, R.J.3    Pabo, C.O.4
  • 67
    • 0028457594 scopus 로고
    • Zinc mining for protein domains
    • Schwabe JWR, Klug A: Zinc mining for protein domains. Struct Biol 1:345, 1994.
    • (1994) Struct Biol , vol.1 , pp. 345
    • Schwabe, J.W.R.1    Klug, A.2
  • 68
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • Kadonaga JT, Carner KR, Masiarz FR, Tjian R: Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell 51:1079, 1987.
    • (1987) Cell , vol.51 , pp. 1079
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 69
    • 0025127160 scopus 로고
    • Role of zinc (II) ions in the structure of the three-finger DNA binding domain of the SP1 transcription factor
    • Kuwahara J, Coleman JE: Role of zinc (II) ions in the structure of the three-finger DNA binding domain of the SP1 transcription factor. Biochemistry 29:8627, 1990.
    • (1990) Biochemistry , vol.29 , pp. 8627
    • Kuwahara, J.1    Coleman, J.E.2
  • 70
    • 0027953395 scopus 로고
    • Relationship between zinc content and DNA-binding activity of the DNA-binding motif of the transcription factor ALCR in Aspergillus nidulans
    • Sequeval D, Felenbok B: Relationship between zinc content and DNA-binding activity of the DNA-binding motif of the transcription factor ALCR in Aspergillus nidulans. Mol Gen Genet 242:33, 1994.
    • (1994) Mol Gen Genet , vol.242 , pp. 33
    • Sequeval, D.1    Felenbok, B.2
  • 72
    • 0025324406 scopus 로고
    • LAC9 DNA binding domain coordinates two zinc atoms per monomer and contacts DNA as a dimer
    • Halvorsen YC, Nandabaln K, Dickson RC: LAC9 DNA binding domain coordinates two zinc atoms per monomer and contacts DNA as a dimer. J Biol Chem 265:13283, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 13283
    • Halvorsen, Y.C.1    Nandabaln, K.2    Dickson, R.C.3
  • 73
    • 0028028333 scopus 로고
    • The DNA-binding domain of the yeast Saccharomyces cervisìae CYP1 (HAP1) transcription factor possesses two zinc ions which are complexed in a zinc cluster
    • Timmerman JE, Guiard B, Shechter E, Delsuc MA, Lallemand JY, Gervais M: The DNA-binding domain of the yeast Saccharomyces cervisìae CYP1 (HAP1) transcription factor possesses two zinc ions which are complexed in a zinc cluster. Eur J Biochem 225:593, 1994.
    • (1994) Eur J Biochem , vol.225 , pp. 593
    • Timmerman, J.E.1    Guiard, B.2    Shechter, E.3    Delsuc, M.A.4    Lallemand, J.Y.5    Gervais, M.6
  • 74
    • 0026074971 scopus 로고
    • The LIM region of a presumptive Caenorhabditis elegans transcription factor is an iron-sulfur and zinc containing metallodomain
    • Li PM, Reichert J, Freyd G, Horvitz HR, Walsh CT: The LIM region of a presumptive Caenorhabditis elegans transcription factor is an iron-sulfur and zinc containing metallodomain. Proc Natl Acad Sci USA. 88:9210, 1991.
    • (1991) Proc Natl Acad Sci USA. , vol.88 , pp. 9210
    • Li, P.M.1    Reichert, J.2    Freyd, G.3    Horvitz, H.R.4    Walsh, C.T.5
  • 76
    • 0024095812 scopus 로고
    • The yeast regulatory protein ADR1 binds in a zinc dependent manner to the upstream activating sequence of ADH2
    • Eisen A, Taylor WE, Blumberg H, Young ET: The yeast regulatory protein ADR1 binds in a zinc dependent manner to the upstream activating sequence of ADH2. Cell Biol 8:4552, 1988.
    • (1988) Cell Biol , vol.8 , pp. 4552
    • Eisen, A.1    Taylor, W.E.2    Blumberg, H.3    Young, E.T.4
  • 77
    • 0021242605 scopus 로고
    • Zinc potentiation of androgen receptor binding to nuclei in vitro
    • Colvard DS, Wilson EM: Zinc potentiation of androgen receptor binding to nuclei in vitro. Biochemistry 23:3471, 1984.
    • (1984) Biochemistry , vol.23 , pp. 3471
    • Colvard, D.S.1    Wilson, E.M.2
  • 78
    • 0025974171 scopus 로고
    • 2+ to bind a regulatory MRE element of the mouse gene encoding metallothionein-1
    • 2+ to bind a regulatory MRE element of the mouse gene encoding metallothionein-1. Gene 97:295, 1991.
    • (1991) Gene , vol.97 , pp. 295
    • Seguin, C.A.1
  • 79
    • 0025025391 scopus 로고
    • Zinc dependent binding of a lover nuclear factor to metal response element MRE-a of the mouse metallothionein gene and variant sequences
    • Searle PF: Zinc dependent binding of a lover nuclear factor to metal response element MRE-a of the mouse metallothionein gene and variant sequences. Nucleic Acid Res 18:4683, 1990.
    • (1990) Nucleic Acid Res , vol.18 , pp. 4683
    • Searle, P.F.1
  • 80
    • 0023502883 scopus 로고
    • RNA polymerase II transcription factors H4TF-1 and H4TF-2 require metal to bind specific DNA sequences
    • Dailey L, Boseman-Roberts S, Heintz N: RNA polymerase II transcription factors H4TF-1 and H4TF-2 require metal to bind specific DNA sequences. Mol Cell Biol 7:4582, 1987.
    • (1987) Mol Cell Biol , vol.7 , pp. 4582
    • Dailey, L.1    Boseman-Roberts, S.2    Heintz, N.3
  • 81
    • 0022476213 scopus 로고
    • Distinct transcription factors bind specifically to two regions of the human histone 4 promotor
    • Dailey L, Hanly SM, Roeder RG, Hinotz N: Distinct transcription factors bind specifically to two regions of the human histone 4 promotor. Proc Natl Acad Sci USA 83:7241, 1986.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7241
    • Dailey, L.1    Hanly, S.M.2    Roeder, R.G.3    Hinotz, N.4
  • 82
    • 0028856133 scopus 로고
    • Scratch, a pan-neural gene encoding a zinc finger protein related to snail, promotes neuronal development
    • Roark M, Sturtevant MA, Emery J, Vaessin H, Grell E, Bier E: Scratch, a pan-neural gene encoding a zinc finger protein related to snail, promotes neuronal development. Genes Dev 9:2384, 1995.
    • (1995) Genes Dev , vol.9 , pp. 2384
    • Roark, M.1    Sturtevant, M.A.2    Emery, J.3    Vaessin, H.4    Grell, E.5    Bier, E.6
  • 83
    • 0026440781 scopus 로고
    • Castor encodes a novel zinc finger protein required for the development of a subset of CNS neurons in Drosophila
    • Mellerick DM, Kassis JA, Zhang SD, Odenwald WF: Castor encodes a novel zinc finger protein required for the development of a subset of CNS neurons in Drosophila. Neuron 9:789, 1992.
    • (1992) Neuron , vol.9 , pp. 789
    • Mellerick, D.M.1    Kassis, J.A.2    Zhang, S.D.3    Odenwald, W.F.4
  • 84
    • 0028107659 scopus 로고
    • Spalt encodes an evolutionary conserved zinc finger protein of novel structure which provides homeotic gene function in the head and tail region of the Drosophila embryo
    • Kuhnlein RP, Frommer G, Friedrich M, Gonzalez-Gaitan M, Weber A, Wagner-Bernholz JF, Gehring WJ, Jackle H, Schuh R: Spalt encodes an evolutionary conserved zinc finger protein of novel structure which provides homeotic gene function in the head and tail region of the Drosophila embryo. EMBO J 13:168, 1994.
    • (1994) EMBO J , vol.13 , pp. 168
    • Kuhnlein, R.P.1    Frommer, G.2    Friedrich, M.3    Gonzalez-Gaitan, M.4    Weber, A.5    Wagner-Bernholz, J.F.6    Gehring, W.J.7    Jackle, H.8    Schuh, R.9
  • 85
    • 0027484361 scopus 로고
    • Perinatal lethality and defects in hindbrain development in mice homozygous for a targeted mutation of the zinc finger gene Krox20
    • Swiatek PJ, Gridely T: Perinatal lethality and defects in hindbrain development in mice homozygous for a targeted mutation of the zinc finger gene Krox20. Genes Dev 7:2071, 1993.
    • (1993) Genes Dev , vol.7 , pp. 2071
    • Swiatek, P.J.1    Gridely, T.2
  • 87
    • 0027988403 scopus 로고
    • Kiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons
    • Bernard O, Ganiatisas S, Kannourakis G, Dringer R: Kiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons. Cell Growth Differ 5:1159, 1994.
    • (1994) Cell Growth Differ , vol.5 , pp. 1159
    • Bernard, O.1    Ganiatisas, S.2    Kannourakis, G.3    Dringer, R.4
  • 88
    • 0028072256 scopus 로고
    • Cloning and structure of a chicken zinc finger cDNA: Restricted expression in developing neural crest cells
    • Schutz B, Niessing J: Cloning and structure of a chicken zinc finger cDNA: Restricted expression in developing neural crest cells. Gene 148:227, 1994.
    • (1994) Gene , vol.148 , pp. 227
    • Schutz, B.1    Niessing, J.2
  • 89
    • 0027960488 scopus 로고
    • A novel zinc finger protein, zic, is involved in neurogenesis, especially in the cell lineage of cerebellar granule cells
    • Aruga J, Yokota N, Hashimoto M, Furuichi T, Fukuda M, Mikoshiba K: A novel zinc finger protein, zic, is involved in neurogenesis, especially in the cell lineage of cerebellar granule cells. J Neurochem 63:1880, 1994.
    • (1994) J Neurochem , vol.63 , pp. 1880
    • Aruga, J.1    Yokota, N.2    Hashimoto, M.3    Furuichi, T.4    Fukuda, M.5    Mikoshiba, K.6
  • 90
    • 0028835366 scopus 로고
    • Expression of zfh-4, a new member of the zinc finger-homeodomain family, in developing brain and muscles
    • Kostich WA, Sanes JR: Expression of zfh-4, a new member of the zinc finger-homeodomain family, in developing brain and muscles. Dev Dyn 202:145, 1995.
    • (1995) Dev Dyn , vol.202 , pp. 145
    • Kostich, W.A.1    Sanes, J.R.2
  • 91
    • 0025766749 scopus 로고
    • The ovo gene of Drosophila encodes a zinc finger protein required for female germ line development
    • Mevel-Ninio M, Terracol R, Kafatos FC: The ovo gene of Drosophila encodes a zinc finger protein required for female germ line development. EMBO J 10:2259, 1991.
    • (1991) EMBO J , vol.10 , pp. 2259
    • Mevel-Ninio, M.1    Terracol, R.2    Kafatos, F.C.3
  • 92
    • 0028801328 scopus 로고
    • Overexpression of the zinc finger protein MZI inhibits hematopoietic development from embryonic stem cells: Correlation with negative regulation of CD34 and c-myc promoter activity
    • Perrotti D, Melotti P, Skorski T, Casella I, Peschle C, Calabretta B: Overexpression of the zinc finger protein MZI inhibits hematopoietic development from embryonic stem cells: Correlation with negative regulation of CD34 and c-myc promoter activity. Mol Cell Biol 15:6075, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 6075
    • Perrotti, D.1    Melotti, P.2    Skorski, T.3    Casella, I.4    Peschle, C.5    Calabretta, B.6
  • 93
    • 0027476673 scopus 로고
    • The zinc finger transcription factor Egr-1 is essential for and restricts differentiation along the macrophage lineage
    • Nguyen HQ, Hoffman-Liebermann B, Liebermann DA: The zinc finger transcription factor Egr-1 is essential for and restricts differentiation along the macrophage lineage. Cell 72:197, 1993.
    • (1993) Cell , vol.72 , pp. 197
    • Nguyen, H.Q.1    Hoffman-Liebermann, B.2    Liebermann, D.A.3
  • 94
    • 0023857156 scopus 로고
    • Disruption of a putative Cys-zinc interaction eliminates the biological activity of the Krüppel finger protein
    • Redemann N, Gaul U, Jackle H: Disruption of a putative Cys-zinc interaction eliminates the biological activity of the Krüppel finger protein. Nature Lond 332:90, 1988.
    • (1988) Nature Lond , vol.332 , pp. 90
    • Redemann, N.1    Gaul, U.2    Jackle, H.3
  • 96
    • 0242437395 scopus 로고
    • Xfn: An embryonic gene coding a multifingered protein in Xenopus
    • Ruiz A, Altaba I, Perry-Okeefe H, Melton DA: Xfn: An embryonic gene coding a multifingered protein in Xenopus. EMBO J 6:3065, 1987.
    • (1987) EMBO J , vol.6 , pp. 3065
    • Ruiz, A.1    Altaba, I.2    Perry-Okeefe, H.3    Melton, D.A.4
  • 97
    • 0024549823 scopus 로고
    • Mesoderm induction and mesoderm-inducing factors in early amphibian development
    • Smith JC: Mesoderm induction and mesoderm-inducing factors in early amphibian development. Development 105:665, 1989.
    • (1989) Development , vol.105 , pp. 665
    • Smith, J.C.1
  • 98
    • 0026326820 scopus 로고
    • Pattern formation during animal development
    • Melton DA: Pattern formation during animal development. Science 252:234, 1991.
    • (1991) Science , vol.252 , pp. 234
    • Melton, D.A.1
  • 99
    • 0026652654 scopus 로고
    • The role of growth factors in embryonic induction in Xenopus laevis
    • Dawid IB, Taira M, Good PJ, Rebagliati MR: The role of growth factors in embryonic induction in Xenopus laevis. Mol Reprod Dev 32:136, 1992.
    • (1992) Mol Reprod Dev , vol.32 , pp. 136
    • Dawid, I.B.1    Taira, M.2    Good, P.J.3    Rebagliati, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.