메뉴 건너뛰기




Volumn 155, Issue 2, 2006, Pages 130-139

Experimental identification of homodimerizing B-ZIP families in Homo sapiens

Author keywords

ATF6; B ZIP; Dimerization specificity; Leucine zipper; NFIL3; Oasis; XBP

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HETERODIMER; HOMODIMER; PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR BASIC REGION LEUCINE ZIPPER; UNCLASSIFIED DRUG;

EID: 33747786692     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.02.018     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 2242475745 scopus 로고    scopus 로고
    • A heterodimerizing leucine zipper coiled coil system for examining the specificity of a position interactions: amino acids I, V, L, N, A, and K
    • Acharya A., Ruvinov S.B., Gal J., Moll J.R., and Vinson C. A heterodimerizing leucine zipper coiled coil system for examining the specificity of a position interactions: amino acids I, V, L, N, A, and K. Biochemistry 41 (2002) 14122-14131
    • (2002) Biochemistry , vol.41 , pp. 14122-14131
    • Acharya, A.1    Ruvinov, S.B.2    Gal, J.3    Moll, J.R.4    Vinson, C.5
  • 2
    • 0024331502 scopus 로고
    • Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP
    • Agre P., Johnson P.F., and McKnight S.L. Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP. Science 246 (1989) 922-926
    • (1989) Science , vol.246 , pp. 922-926
    • Agre, P.1    Johnson, P.F.2    McKnight, S.L.3
  • 3
    • 0031883280 scopus 로고    scopus 로고
    • A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of c-fos
    • Ahn S., Olive M., Aggarwal S., Krylov D., Ginty D.D., and Vinson C. A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of c-fos. Mol. Cell. Biol. 18 (1998) 967-977
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 967-977
    • Ahn, S.1    Olive, M.2    Aggarwal, S.3    Krylov, D.4    Ginty, D.D.5    Vinson, C.6
  • 4
    • 0026845838 scopus 로고
    • Structure of the leucine zipper
    • Alber T. Structure of the leucine zipper. Curr. Opin. Genet. Dev. 2 (1992) 205-210
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 205-210
    • Alber, T.1
  • 5
    • 0014620599 scopus 로고
    • Human pituitary growth hormone. Physicochemical investigations of the native and reduced-alkylated protein
    • Bewley T.A., Brovetto-Cruz J., and Li C.H. Human pituitary growth hormone. Physicochemical investigations of the native and reduced-alkylated protein. Biochemistry 8 (1969) 4701-4708
    • (1969) Biochemistry , vol.8 , pp. 4701-4708
    • Bewley, T.A.1    Brovetto-Cruz, J.2    Li, C.H.3
  • 6
    • 0025272940 scopus 로고
    • A-helical coiled coils and bundles: how to design an α-helical protein
    • Cohen C., and Parry D. A-helical coiled coils and bundles: how to design an α-helical protein. Protein 7 (1990) 1-14
    • (1990) Protein , vol.7 , pp. 1-14
    • Cohen, C.1    Parry, D.2
  • 7
    • 3042699706 scopus 로고    scopus 로고
    • Dimerization specificity of all 67 B-ZIP motifs in Arabidopsis thaliana: a comparison to Homo sapiens B-ZIP motifs
    • Deppmann C.D., Acharya A., Rishi V., Wobbes B., Smeekens S., Taparowsky E.J., and Vinson C. Dimerization specificity of all 67 B-ZIP motifs in Arabidopsis thaliana: a comparison to Homo sapiens B-ZIP motifs. Nucleic Acids Res. 32 (2004) 3435-3445
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3435-3445
    • Deppmann, C.D.1    Acharya, A.2    Rishi, V.3    Wobbes, B.4    Smeekens, S.5    Taparowsky, E.J.6    Vinson, C.7
  • 8
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos- c-Jun bound to DNA
    • Glover J.N., and Harrison S.C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos- c-Jun bound to DNA. Nature 373 (1995) 257-261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2
  • 10
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz I. Functional inactivation of genes by dominant negative mutations. Nature 329 (1987) 219-222
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 11
    • 0029174419 scopus 로고
    • Transcription factors 1: bZIP proteins
    • Hurst H.C. Transcription factors 1: bZIP proteins. Protein Profile 2 (1995) 101-168
    • (1995) Protein Profile , vol.2 , pp. 101-168
    • Hurst, H.C.1
  • 12
    • 0024205841 scopus 로고
    • The role of the leucine zipper in the fos-jun interaction
    • Kouzarides T., and Ziff E. The role of the leucine zipper in the fos-jun interaction. Nature 336 (1988) 646-651
    • (1988) Nature , vol.336 , pp. 646-651
    • Kouzarides, T.1    Ziff, E.2
  • 13
    • 0032546758 scopus 로고    scopus 로고
    • Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids
    • Krylov D., Barchi J., and Vinson C. Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids. J. Mol. Biol. 279 (1998) 959-972
    • (1998) J. Mol. Biol. , vol.279 , pp. 959-972
    • Krylov, D.1    Barchi, J.2    Vinson, C.3
  • 15
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions
    • Krylov D., Mikhailenko I., and Vinson C. A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 13 (1994) 2849-2861
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 16
    • 0028786167 scopus 로고
    • Extending dimerization interfaces: the bZIP basic region can form a coiled coil
    • Krylov D., Olive M., and Vinson C. Extending dimerization interfaces: the bZIP basic region can form a coiled coil. EMBO J. 14 (1995) 5329-5337
    • (1995) EMBO J. , vol.14 , pp. 5329-5337
    • Krylov, D.1    Olive, M.2    Vinson, C.3
  • 17
    • 0024295767 scopus 로고
    • The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
    • Landschultz W.H., Johnson P.F., and McKnight S.L. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science 240 (1988) 1759-1764
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschultz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 19
    • 0034602397 scopus 로고    scopus 로고
    • Attractive interhelical electrostatic interactions in the proline- and acidic-rich region (PAR) leucine zipper subfamily preclude heterodimerization with other basic leucine zipper subfamilies
    • Moll J.R., Olive M., and Vinson C. Attractive interhelical electrostatic interactions in the proline- and acidic-rich region (PAR) leucine zipper subfamily preclude heterodimerization with other basic leucine zipper subfamilies. J. Biol. Chem. 275 (2000) 34826-34832
    • (2000) J. Biol. Chem. , vol.275 , pp. 34826-34832
    • Moll, J.R.1    Olive, M.2    Vinson, C.3
  • 20
    • 0037595546 scopus 로고    scopus 로고
    • Comprehensive identification of human bZIP interactions with coiled-coil arrays
    • Newman J.R., and Keating A.E. Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 300 (2003) 2097-2101
    • (2003) Science , vol.300 , pp. 2097-2101
    • Newman, J.R.1    Keating, A.E.2
  • 21
    • 0025182484 scopus 로고
    • Design of DNA binding peptides based on the leucine zipper motif
    • O'Neil K.T., Hoess R.H., and DeGrado W.F. Design of DNA binding peptides based on the leucine zipper motif. Science 243 (1990) 774-778
    • (1990) Science , vol.243 , pp. 774-778
    • O'Neil, K.T.1    Hoess, R.H.2    DeGrado, W.F.3
  • 22
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil
    • O'Shea E.K., Klemm J.D., Kim P.S., and Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil. Science 254 (1991) 539-544
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 23
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea E.K., Rutkowski R., and Kim P.S. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell 68 (1992) 699-708
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 24
    • 0030802419 scopus 로고    scopus 로고
    • A dominant negative to activation protein-1 (AP1) that abolishes DNA binding and inhibits oncogenesis
    • Olive M., Krylov D., Echlin D.R., Gardner K., Taparowsky E., and Vinson C. A dominant negative to activation protein-1 (AP1) that abolishes DNA binding and inhibits oncogenesis. J. Biol. Chem. 272 (1997) 18586-18594
    • (1997) J. Biol. Chem. , vol.272 , pp. 18586-18594
    • Olive, M.1    Krylov, D.2    Echlin, D.R.3    Gardner, K.4    Taparowsky, E.5    Vinson, C.6
  • 25
    • 20244385977 scopus 로고    scopus 로고
    • A high-throughput fluorescence-anisotropy screen that identifies small molecule inhibitors of the DNA binding of B-ZIP transcription factors
    • Rishi V., Potter T., Laudeman J., Reinhart R., Silvers T., Selby M., Stevenson T., Krosky P., Stephen A.G., Acharya A., et al. A high-throughput fluorescence-anisotropy screen that identifies small molecule inhibitors of the DNA binding of B-ZIP transcription factors. Anal. Biochem. 340 (2005) 259-271
    • (2005) Anal. Biochem. , vol.340 , pp. 259-271
    • Rishi, V.1    Potter, T.2    Laudeman, J.3    Reinhart, R.4    Silvers, T.5    Selby, M.6    Stevenson, T.7    Krosky, P.8    Stephen, A.G.9    Acharya, A.10
  • 26
    • 0025071850 scopus 로고
    • Evidence of changes in protease sensitivity and subunit exchange rate on DNA binding by C/EBP
    • Shuman J.D., Vinson C.R., and McKnight S.L. Evidence of changes in protease sensitivity and subunit exchange rate on DNA binding by C/EBP. Science 249 (1990) 771-774
    • (1990) Science , vol.249 , pp. 771-774
    • Shuman, J.D.1    Vinson, C.R.2    McKnight, S.L.3
  • 27
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., and Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189 (1986) 113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 28
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson K.S., Vinson C.R., and Freire E. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry 32 (1993) 5491-5496
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 30
    • 0027176792 scopus 로고
    • Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design
    • Vinson C.R., Hai T., and Boyd S.M. Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design. Genes Dev. 7 (1993) 1047-1058
    • (1993) Genes Dev. , vol.7 , pp. 1047-1058
    • Vinson, C.R.1    Hai, T.2    Boyd, S.M.3
  • 31
    • 0024370748 scopus 로고
    • Scissors-grip model for DNA recognition by a family of leucine zipper proteins
    • Vinson C.R., Sigler P.B., and McKnight S.L. Scissors-grip model for DNA recognition by a family of leucine zipper proteins. Science 246 (1989) 911-916
    • (1989) Science , vol.246 , pp. 911-916
    • Vinson, C.R.1    Sigler, P.B.2    McKnight, S.L.3
  • 32
    • 0030929788 scopus 로고    scopus 로고
    • Buried asparagines determine the dimerization specificities of leucine zipper mutants
    • Zeng X., Herndon A.M., and Hu J.C. Buried asparagines determine the dimerization specificities of leucine zipper mutants. Proc. Natl. Acad. Sci. USA 94 (1997) 3673-3678
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3673-3678
    • Zeng, X.1    Herndon, A.M.2    Hu, J.C.3
  • 33
    • 0027949381 scopus 로고
    • The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
    • Zhou N.E., Kay C.M., and Hodges R.S. The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7 (1994) 1365-1372
    • (1994) Protein Eng. , vol.7 , pp. 1365-1372
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.