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Volumn 329, Issue 4, 2003, Pages 631-644

Functional domains of FOXJ2

Author keywords

FHX; Fork head; FOXJ2; Nuclear localization; Transactivation domain

Indexed keywords

AMINO ACID; GLUTAMINE; HISTIDINE; PROLINE; SERINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR FOXJ2; TYROSINE; UNCLASSIFIED DRUG;

EID: 0038054313     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00524-2     Document Type: Article
Times cited : (23)

References (31)
  • 2
    • 17344379513 scopus 로고    scopus 로고
    • Five years on the wings of fork head
    • Kaufmann E., Knochel W. Five years on the wings of fork head. Mech. Dev. 57:1996;3-20.
    • (1996) Mech. Dev. , vol.57 , pp. 3-20
    • Kaufmann, E.1    Knochel, W.2
  • 3
    • 0036387193 scopus 로고    scopus 로고
    • Forkhead transcription factors: Key players in development and metabolism
    • Carlsson P., Mahlapuu M. Forkhead transcription factors: key players in development and metabolism. Dev. Biol. 250:2002;1-23.
    • (2002) Dev. Biol. , vol.250 , pp. 1-23
    • Carlsson, P.1    Mahlapuu, M.2
  • 7
    • 0031918364 scopus 로고    scopus 로고
    • Regulation of gene expression at the beginning of mammalian development and the TEAD family of transcription factors
    • Kaneko K.J., DePamphilis M.L. Regulation of gene expression at the beginning of mammalian development and the TEAD family of transcription factors. Dev. Genet. 22:1998;43-55.
    • (1998) Dev. Genet. , vol.22 , pp. 43-55
    • Kaneko, K.J.1    DePamphilis, M.L.2
  • 8
    • 0032483539 scopus 로고    scopus 로고
    • The human forkhead protein FREAC-2 contains two functionally redundant activation domains and interacts with TBP and TFIIB
    • Hellqvist M., Mahlapuu M., Blixt A., Enerback S., Carlsson P. The human forkhead protein FREAC-2 contains two functionally redundant activation domains and interacts with TBP and TFIIB. J. Biol. Chem. 273:1998;23335-23343.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23335-23343
    • Hellqvist, M.1    Mahlapuu, M.2    Blixt, A.3    Enerback, S.4    Carlsson, P.5
  • 9
    • 0028920898 scopus 로고
    • Analysis of hepatocyte nuclear factor-3 beta protein domains required for transcriptional activation and nuclear targeting
    • Qian X., Costa R.H. Analysis of hepatocyte nuclear factor-3 beta protein domains required for transcriptional activation and nuclear targeting. Nucl. Acids Res. 23:1995;1184-1191.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1184-1191
    • Qian, X.1    Costa, R.H.2
  • 10
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark K.L., Halay E.D., Lai E., Burley S.K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature. 364:1993;412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 11
    • 0034730514 scopus 로고    scopus 로고
    • Creating temperature-sensitive winged helix transcription factors. Amino acids that stabilize the DNA binding domain of HNF3
    • Stevens K., Cirillo L., Zaret K.S. Creating temperature-sensitive winged helix transcription factors. Amino acids that stabilize the DNA binding domain of HNF3. J. Biol. Chem. 275:2000;30471-30477.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30471-30477
    • Stevens, K.1    Cirillo, L.2    Zaret, K.S.3
  • 12
    • 0028046675 scopus 로고
    • Cloning and characterization of seven human forkhead proteins: Binding site specificity and DNA bending
    • Pierrou S., Hellqvist M., Samuelsson L., Enerback S., Carlsson P. Cloning and characterization of seven human forkhead proteins: binding site specificity and DNA bending. Embo J. 13:1994;5002-5012.
    • (1994) Embo J. , vol.13 , pp. 5002-5012
    • Pierrou, S.1    Hellqvist, M.2    Samuelsson, L.3    Enerback, S.4    Carlsson, P.5
  • 13
    • 0037160050 scopus 로고    scopus 로고
    • Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms: Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding
    • Zhang X., Gan L., Pan H., Guo S., He X., Olson S.T., et al. Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms: direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding. J. Biol. Chem. 2002.
    • (2002) J. Biol. Chem
    • Zhang, X.1    Gan, L.2    Pan, H.3    Guo, S.4    He, X.5    Olson, S.T.6
  • 14
    • 0035034038 scopus 로고    scopus 로고
    • Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX
    • Brownawell A.M., Kops G.J., Macara I.G., Burgering B.M. Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. Mol. Cell Biol. 21:2001;3534-3546.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3534-3546
    • Brownawell, A.M.1    Kops, G.J.2    Macara, I.G.3    Burgering, B.M.4
  • 15
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias M.J., Wiesner S., Sudol M. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Letters. 513:2002;30-37.
    • (2002) FEBS Letters , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 16
    • 12644288646 scopus 로고    scopus 로고
    • Products of the grg (Groucho-related gene) family can dimerize through the amino-terminal Q domain
    • Pinto M., Lobe C.G. Products of the grg (Groucho-related gene) family can dimerize through the amino-terminal Q domain. J. Biol. Chem. 271:1996;33026-33031.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33026-33031
    • Pinto, M.1    Lobe, C.G.2
  • 17
    • 0024811686 scopus 로고
    • Synergistic activation by the glutamine-rich domains of human transcription factor Sp1
    • Courey A.J., Holtzman D.A., Jackson S.P., Tjian R. Synergistic activation by the glutamine-rich domains of human transcription factor Sp1. Cell. 59:1989;827-836.
    • (1989) Cell , vol.59 , pp. 827-836
    • Courey, A.J.1    Holtzman, D.A.2    Jackson, S.P.3    Tjian, R.4
  • 18
    • 0024340524 scopus 로고
    • The proline-rich transcriptional activator of CTF/NF-I is distinct from the replication and DNA binding domain
    • Mermod N., O'Neill E.A., Kelly T.J., Tjian R. The proline-rich transcriptional activator of CTF/NF-I is distinct from the replication and DNA binding domain. Cell. 58:1989;741-753.
    • (1989) Cell , vol.58 , pp. 741-753
    • Mermod, N.1    O'Neill, E.A.2    Kelly, T.J.3    Tjian, R.4
  • 19
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara I.G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65:2001;570-594.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 20
    • 0028000121 scopus 로고
    • New member of the winged-helix protein family disrupted in mouse and rat nude mutations
    • Nehls M., Pfeifer D., Schorpp M., Hedrich H., Boehm T. New member of the winged-helix protein family disrupted in mouse and rat nude mutations. Nature. 372:1994;103-107.
    • (1994) Nature , vol.372 , pp. 103-107
    • Nehls, M.1    Pfeifer, D.2    Schorpp, M.3    Hedrich, H.4    Boehm, T.5
  • 21
    • 0026664462 scopus 로고
    • Characterization and chromosomal mapping of the gene encoding the cellular DNA binding protein HTLF
    • Li C., Lusis A.J., Sparkes R., Tran S.M., Gaynor R. Characterization and chromosomal mapping of the gene encoding the cellular DNA binding protein HTLF. Genomics. 13:1992;658-664.
    • (1992) Genomics , vol.13 , pp. 658-664
    • Li, C.1    Lusis, A.J.2    Sparkes, R.3    Tran, S.M.4    Gaynor, R.5
  • 22
    • 0030912117 scopus 로고    scopus 로고
    • Reconstitution of a MEC1-independent checkpoint in yeast by expression of a novel human fork head cDNA
    • Pati D., Keller C., Groudine M., Plon S.E. Reconstitution of a MEC1-independent checkpoint in yeast by expression of a novel human fork head cDNA. Mol. Cell Biol. 17:1997;3037-3046.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 3037-3046
    • Pati, D.1    Keller, C.2    Groudine, M.3    Plon, S.E.4
  • 23
    • 0032146749 scopus 로고    scopus 로고
    • Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1
    • Kudo N., Wolff B., Sekimoto T., Schreiner E.P., Yoneda Y., Yanagida M., et al. Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. Expt. Cell. Res. 242:1998;540-547.
    • (1998) Expt. Cell. Res. , vol.242 , pp. 540-547
    • Kudo, N.1    Wolff, B.2    Sekimoto, T.3    Schreiner, E.P.4    Yoneda, Y.5    Yanagida, M.6
  • 24
    • 0025162339 scopus 로고
    • HNF-3A, a hepatocyte-enriched transcription factor of novel structure is regulated transcriptionally
    • Lai E., Prezioso V.R., Smith E., Litvin O., Costa R.H., Darnell J.E. Jr. HNF-3A, a hepatocyte-enriched transcription factor of novel structure is regulated transcriptionally. Genes Dev. 4:1990;1427-1436.
    • (1990) Genes Dev. , vol.4 , pp. 1427-1436
    • Lai, E.1    Prezioso, V.R.2    Smith, E.3    Litvin, O.4    Costa, R.H.5    Darnell J.E., Jr.6
  • 25
    • 0022348840 scopus 로고
    • Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3′:5′-monophosphate-dependent protein kinase
    • Kishimoto A., Nishiyama K., Nakanishi H., Uratsuji Y., Nomura H., Takeyama Y., Nishizuka Y. Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 260:1985;12492-12499.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12492-12499
    • Kishimoto, A.1    Nishiyama, K.2    Nakanishi, H.3    Uratsuji, Y.4    Nomura, H.5    Takeyama, Y.6    Nishizuka, Y.7
  • 26
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • Pinna L.A., Ruzzene M. How do protein kinases recognize their substrates? Biochim. Biophys. Acta. 1314:1996;191-225.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 28
    • 0004265596 scopus 로고    scopus 로고
    • F.A. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: Wiley
    • Ausubel F.A., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. 1998;Wiley, New York.
    • (1998) Current Protocols in Molecular Biology
  • 30
    • 0038352888 scopus 로고    scopus 로고
    • Analysis of protein-DNA binding at equilibrium
    • Rippe K. Analysis of protein-DNA binding at equilibrium. Futura. 12:1997;20-26.
    • (1997) Futura , vol.12 , pp. 20-26
    • Rippe, K.1
  • 31
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 25:1997;4876-4882.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.