메뉴 건너뛰기




Volumn 65, Issue 9, 2008, Pages 1390-1402

The BAG proteins: A ubiquitous family of chaperone regulators

Author keywords

Arabidopsis; BAG domain; BAG protein; Programmed cell death; Stress

Indexed keywords

BCL 2 ASSOCIATED ATHANOGENE PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70; ISOPROTEIN; MUTANT PROTEIN; REGULATOR PROTEIN; UBIQUITIN;

EID: 43049155955     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-7535-2     Document Type: Review
Times cited : (236)

References (89)
  • 1
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity
    • Takayama, S., Sato, T., Krajewski, S., Kochel, K., Irie, S., Millan, J. A. and Reed, J. C. (1995) Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity. Cell 80, 279-284.
    • (1995) Cell , vol.80 , pp. 279-284
    • Takayama, S.1    Sato, T.2    Krajewski, S.3    Kochel, K.4    Irie, S.5    Millan, J.A.6    Reed, J.C.7
  • 3
    • 0029614713 scopus 로고
    • A protein that interacts with members of the nuclear hormone receptor family: Identification and cDNA cloning
    • Zeiner, M. and Gehring, U. (1995) A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning. Proc. Natl. Acad. Sci. USA 92, 11465-11469.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11465-11469
    • Zeiner, M.1    Gehring, U.2
  • 4
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama, S. and Reed, J. C. (2001) Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell Biol. 3, E237-241.
    • (2001) Nat. Cell Biol , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 6
    • 33745841283 scopus 로고    scopus 로고
    • Identification and functional characterization of the BAG protein family in Arabidopsis thaliana
    • Doukhanina, E. V., Chen, S., van der Zalm, E., Godzik, A., Reed, J. and Dickman, M. B. (2006) Identification and functional characterization of the BAG protein family in Arabidopsis thaliana. J. Biol. Chem. 281, 18793-18801.
    • (2006) J. Biol. Chem , vol.281 , pp. 18793-18801
    • Doukhanina, E.V.1    Chen, S.2    van der Zalm, E.3    Godzik, A.4    Reed, J.5    Dickman, M.B.6
  • 8
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann, H., Scheufler, C., Schneider, C., Hohfeld, J., Hartl, F. U. and Moarefi, I. (2001) Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291, 1553-1557.
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 10
    • 0032572715 scopus 로고    scopus 로고
    • Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells
    • Yang, X., Chernenko, G., Hao, Y., Ding, Z., Pater, M. M., Pater, A. and Tang, S. C. (1998) Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells. Oncogene 17, 981-989.
    • (1998) Oncogene , vol.17 , pp. 981-989
    • Yang, X.1    Chernenko, G.2    Hao, Y.3    Ding, Z.4    Pater, M.M.5    Pater, A.6    Tang, S.C.7
  • 12
    • 0032749421 scopus 로고    scopus 로고
    • High level expression of differentially localized BAG-1 isoforms in some oestrogen receptor-positive human breast cancers
    • Brimmell, M., Burns, J. S., Munson, P., McDonald, L., O'Hare, M. J., Lakhani, S. R. and Packham, G. (1999) High level expression of differentially localized BAG-1 isoforms in some oestrogen receptor-positive human breast cancers. Br. J. Cancer 81, 1042-1051.
    • (1999) Br. J. Cancer , vol.81 , pp. 1042-1051
    • Brimmell, M.1    Burns, J.S.2    Munson, P.3    McDonald, L.4    O'Hare, M.J.5    Lakhani, S.R.6    Packham, G.7
  • 13
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • Alberti, S., Demand, J., Esser, C., Emmerich, N., Schild, H. and Hohfeld, J. (2002) Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J. Biol. Chem. 277, 45920-45927.
    • (2002) J. Biol. Chem , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 14
    • 0031466639 scopus 로고    scopus 로고
    • Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation
    • Packham, G., Brimmell, M. and Cleveland, J. L. (1997) Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation. Biochem. J. 328, 807-813.
    • (1997) Biochem. J , vol.328 , pp. 807-813
    • Packham, G.1    Brimmell, M.2    Cleveland, J.L.3
  • 15
    • 0033621089 scopus 로고    scopus 로고
    • The hsp70-associating protein Hap46 binds to DNA and stimulates transcription
    • Zeiner, M., Niyaz, Y. and Gehring, U. (1999) The hsp70-associating protein Hap46 binds to DNA and stimulates transcription. Proc. Natl. Acad. Sci. USA 96, 10194-10199.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10194-10199
    • Zeiner, M.1    Niyaz, Y.2    Gehring, U.3
  • 16
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M. P. and Bukau, B. (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 17
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 18
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: Lessons from the yeast model
    • Chernoff, Y. O. (2007) Stress and prions: lessons from the yeast model. FEBS Lett. 581, 3695-3701.
    • (2007) FEBS Lett , vol.581 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 19
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock conjugate Hsc70 in the mammalian cell: The characterization of the antiapoptotic protein BAG-1 provides novel insights
    • Hohfeld, J. (1998) Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the antiapoptotic protein BAG-1 provides novel insights. Biol. Chem. 379, 269-274.
    • (1998) Biol. Chem , vol.379 , pp. 269-274
    • Hohfeld, J.1
  • 20
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Hohfeld, J. and Jentsch, S. (1997) GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216.
    • (1997) EMBO J , vol.16 , pp. 6209-6216
    • Hohfeld, J.1    Jentsch, S.2
  • 21
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hohfeld, J., Minami, Y. and Hartl, F. U. (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 22
    • 0030671388 scopus 로고    scopus 로고
    • Proteins interacting with the molecular chaperone hsp70/hsc70: Physical associations and effects on refolding activity
    • Gebauer, M., Zeiner, M. and Gehring, U. (1997) Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 417, 109-113.
    • (1997) FEBS Lett , vol.417 , pp. 109-113
    • Gebauer, M.1    Zeiner, M.2    Gehring, U.3
  • 23
    • 0030766734 scopus 로고    scopus 로고
    • Mammalian protein RAP46: An interaction partner and modulator of 70 kDa heat shock proteins
    • Zeiner, M., Gebauer, M. and Gehring, U. (1997) Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16, 5483-5490.
    • (1997) EMBO J , vol.16 , pp. 5483-5490
    • Zeiner, M.1    Gebauer, M.2    Gehring, U.3
  • 25
    • 0039598518 scopus 로고    scopus 로고
    • Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function
    • Luders, J., Demand, J., Papp, O. and Hohfeld, J. (2000) Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function. J. Biol. Chem. 275, 14817-14823.
    • (2000) J. Biol. Chem , vol.275 , pp. 14817-14823
    • Luders, J.1    Demand, J.2    Papp, O.3    Hohfeld, J.4
  • 26
    • 0032525309 scopus 로고    scopus 로고
    • p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: Suppression by BAG-1
    • Matsuzawa, S., Takayama, S., Froesch, B. A., Zapata, J. M. and Reed, J. C. (1998) p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1. EMBO J. 17, 2736-2747.
    • (1998) EMBO J , vol.17 , pp. 2736-2747
    • Matsuzawa, S.1    Takayama, S.2    Froesch, B.A.3    Zapata, J.M.4    Reed, J.C.5
  • 27
    • 0032496242 scopus 로고    scopus 로고
    • BAG-1L protein enhances androgen receptor function
    • Froesch, B. A., Takayama, S. and Reed, J. C. (1998) BAG-1L protein enhances androgen receptor function. J. Biol. Chem. 273, 11660-11666.
    • (1998) J. Biol. Chem , vol.273 , pp. 11660-11666
    • Froesch, B.A.1    Takayama, S.2    Reed, J.C.3
  • 28
    • 0032486380 scopus 로고    scopus 로고
    • RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis
    • Kullmann, M., Schneikert, J., Moll, J., Heck, S., Zeiner, M., Gehring, U. and Cato, A. C. (1998) RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis. J. Biol. Chem. 273, 14620-14625.
    • (1998) J. Biol. Chem , vol.273 , pp. 14620-14625
    • Kullmann, M.1    Schneikert, J.2    Moll, J.3    Heck, S.4    Zeiner, M.5    Gehring, U.6    Cato, A.C.7
  • 29
    • 0032479430 scopus 로고    scopus 로고
    • Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells
    • Liu, R., Takayama, S., Zheng, Y., Froesch, B., Chen, G. Q., Zhang, X., Reed, J. C. and Zhang, X. K. (1998) Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells. J. Biol. Chem. 273, 16985-16992.
    • (1998) J. Biol. Chem , vol.273 , pp. 16985-16992
    • Liu, R.1    Takayama, S.2    Zheng, Y.3    Froesch, B.4    Chen, G.Q.5    Zhang, X.6    Reed, J.C.7    Zhang, X.K.8
  • 30
    • 0029937303 scopus 로고    scopus 로고
    • Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
    • Wang, H. G., Takayama, S., Rapp, U. R. and Reed, J. C. (1996) Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1. Proc. Natl. Acad. Sci. USA 93, 7063-7068.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7063-7068
    • Wang, H.G.1    Takayama, S.2    Rapp, U.R.3    Reed, J.C.4
  • 31
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
    • Song, J., Takeda, M. and Morimoto, R. I. (2001) Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell Biol. 3, 276-282.
    • (2001) Nat. Cell Biol , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 32
    • 0025029382 scopus 로고
    • seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye
    • Carthew, R. W. and Rubin, G. M. (1990) seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye. Cell 63, 561-577.
    • (1990) Cell , vol.63 , pp. 561-577
    • Carthew, R.W.1    Rubin, G.M.2
  • 33
    • 9244251506 scopus 로고    scopus 로고
    • Amson, R. B., Nemani, M., Roperch, J.-P., Israeli, D., Bougueleret, L., Le Gall, I., Medhioub, M., Linares-Cruz, G., Lethrosne, F., Pasturaud, P., Piouffre, L., Prieur, S., Susini, L., Alvaro, V., Millasseau, P., Guidicelli, C., Bui, H., Massart, C., Cazes, L., Dufour, F., Bruzzoni-Giovanelli, H., Owadi, H., Hennion, C., Charpak, G., Dausset, J., Calvo, F., Oren, M., Cohen, D. and Telerman, A. (1996) Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis: activation of the vertebrate homologue of the Drosophila seven in absentia gene. Proc. Natl. Acad. Sci. USA 93, 3953-3957.
    • Amson, R. B., Nemani, M., Roperch, J.-P., Israeli, D., Bougueleret, L., Le Gall, I., Medhioub, M., Linares-Cruz, G., Lethrosne, F., Pasturaud, P., Piouffre, L., Prieur, S., Susini, L., Alvaro, V., Millasseau, P., Guidicelli, C., Bui, H., Massart, C., Cazes, L., Dufour, F., Bruzzoni-Giovanelli, H., Owadi, H., Hennion, C., Charpak, G., Dausset, J., Calvo, F., Oren, M., Cohen, D. and Telerman, A. (1996) Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis: activation of the vertebrate homologue of the Drosophila seven in absentia gene. Proc. Natl. Acad. Sci. USA 93, 3953-3957.
  • 36
    • 34248657576 scopus 로고    scopus 로고
    • Signalling molecules essential for neuronal survival and differentiation
    • Frebel, K. and Wiese, S. (2006) Signalling molecules essential for neuronal survival and differentiation. Biochem. Soc. Trans. 34, 1287-1290.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 1287-1290
    • Frebel, K.1    Wiese, S.2
  • 37
    • 34347204851 scopus 로고    scopus 로고
    • Frebel, K., Wiese, S., Funk, N., Puhringer, D. and Sendtner, M. (2007) Differential modulation of neurite growth by the S- and the L-forms of bag1, a co-chaperone of Hsp70. Neurodegener. Dis. 4, 261-269.
    • Frebel, K., Wiese, S., Funk, N., Puhringer, D. and Sendtner, M. (2007) Differential modulation of neurite growth by the S- and the L-forms of bag1, a co-chaperone of Hsp70. Neurodegener. Dis. 4, 261-269.
  • 39
    • 28844443837 scopus 로고    scopus 로고
    • Is this protein ubiquitinated?
    • Kaiser, P. and Tagwerker, C. (2005) Is this protein ubiquitinated? Methods Enzymol. 399, 243-248.
    • (2005) Methods Enzymol , vol.399 , pp. 243-248
    • Kaiser, P.1    Tagwerker, C.2
  • 40
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001) Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 41
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H. and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428.
    • (2002) Physiol. Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 42
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S. and Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 43
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S. and Pyrowolakis, G. (2000) Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342.
    • (2000) Trends Cell Biol , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 44
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • Varshavsky, A. (1997) The ubiquitin system. Trends Biochem. Sci. 22, 383-387.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 45
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand, J., Alberti, S., Patterson, C. and Hohfeld, J. (2001) Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11, 1569-1577.
    • (2001) Curr. Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 46
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L. Y. and Patterson, C. (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell Biol. 19, 4535-4545.
    • (1999) Mol. Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 48
    • 0033534588 scopus 로고    scopus 로고
    • An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators
    • Takayama, S., Xie, Z. and Reed, J. C. (1999) An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J. Biol. Chem. 274, 781-786.
    • (1999) J. Biol. Chem , vol.274 , pp. 781-786
    • Takayama, S.1    Xie, Z.2    Reed, J.C.3
  • 49
    • 4744350841 scopus 로고    scopus 로고
    • Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate
    • Ueda, K., Kosako, H., Fukui, Y. and Hattori, S. (2004) Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate. J. Biol. Chem. 279, 41815-41821.
    • (2004) J. Biol. Chem , vol.279 , pp. 41815-41821
    • Ueda, K.1    Kosako, H.2    Fukui, Y.3    Hattori, S.4
  • 50
    • 0029890991 scopus 로고    scopus 로고
    • Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation
    • Zu, Y. L., Ai, Y., Gilchrist, A., Labadia, M. E., Sha'afi, R. I. and Huang, C. K. (1996) Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation. Blood 87, 5287-5296.
    • (1996) Blood , vol.87 , pp. 5287-5296
    • Zu, Y.L.1    Ai, Y.2    Gilchrist, A.3    Labadia, M.E.4    Sha'afi, R.I.5    Huang, C.K.6
  • 51
    • 28644442088 scopus 로고    scopus 로고
    • BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP
    • Arndt, V., Daniel, C., Nastainczyk, W., Alberti, S. and Hohfeld, J. (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol. Biol. Cell 16, 5891-5900.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5891-5900
    • Arndt, V.1    Daniel, C.2    Nastainczyk, W.3    Alberti, S.4    Hohfeld, J.5
  • 54
    • 0028410481 scopus 로고
    • Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition
    • Lim, W. A. and Richards, F. M. (1994) Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition. Nat. Struct. Biol. 1, 221-225.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 221-225
    • Lim, W.A.1    Richards, F.M.2
  • 55
    • 0042208135 scopus 로고    scopus 로고
    • CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: Accumulation of poly-ubiquitinated Hsp90 client proteins
    • Doong, H., Rizzo, K., Fang, S., Kulpa, V., Weissman, A. M. and Kohn, E. C. (2003) CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins. J. Biol. Chem. 278, 28490-28500.
    • (2003) J. Biol. Chem , vol.278 , pp. 28490-28500
    • Doong, H.1    Rizzo, K.2    Fang, S.3    Kulpa, V.4    Weissman, A.M.5    Kohn, E.C.6
  • 59
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang, Y., Woronicz, J. D., Liu, W. and Goeddel, D. V. (1999) Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 283, 543-546.
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 61
    • 0033587038 scopus 로고    scopus 로고
    • Apoptosis: Silencing the death receptors
    • Tschopp, J., Martinon, F. and Hofmann, K. (1999) Apoptosis: silencing the death receptors. Curr. Biol. 9, R381-384.
    • (1999) Curr. Biol , vol.9
    • Tschopp, J.1    Martinon, F.2    Hofmann, K.3
  • 62
    • 11844259397 scopus 로고    scopus 로고
    • Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: Protection against radiation-induced effects and target structure for natural killer cells
    • Gehrmann, M., Marienhagen, J., Eichholtz-Wirth, H., Fritz, E., Ellwart, J., Jaattela, M., Zilch, T. and Multhoff, G. (2005) Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: protection against radiation-induced effects and target structure for natural killer cells. Cell Death Differ. 12, 38-51.
    • (2005) Cell Death Differ , vol.12 , pp. 38-51
    • Gehrmann, M.1    Marienhagen, J.2    Eichholtz-Wirth, H.3    Fritz, E.4    Ellwart, J.5    Jaattela, M.6    Zilch, T.7    Multhoff, G.8
  • 64
    • 0025261931 scopus 로고
    • A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain
    • Banerji, J., Sands, J., Strominger, J. L. and Spies, T. (1990) A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain. Proc. Natl. Acad. Sci. USA 87, 2374-2378.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2374-2378
    • Banerji, J.1    Sands, J.2    Strominger, J.L.3    Spies, T.4
  • 65
    • 0035850749 scopus 로고    scopus 로고
    • Human Scythe contains a functional nuclear localization sequence and remains in the nucleus during staurosporine-induced apoptosis
    • Manchen, S. T. and Hubberstey, A. V. (2001) Human Scythe contains a functional nuclear localization sequence and remains in the nucleus during staurosporine-induced apoptosis. Biochem. Biophys. Res. Commun. 287, 1075-1082.
    • (2001) Biochem. Biophys. Res. Commun , vol.287 , pp. 1075-1082
    • Manchen, S.T.1    Hubberstey, A.V.2
  • 67
    • 0033570176 scopus 로고    scopus 로고
    • Reaper-induced dissociation of a Scythe-sequestered cytochrome c-releasing activity
    • Thress, K., Evans, E. K. and Kornbluth, S. (1999) Reaper-induced dissociation of a Scythe-sequestered cytochrome c-releasing activity. EMBO J. 18, 5486-5493.
    • (1999) EMBO J , vol.18 , pp. 5486-5493
    • Thress, K.1    Evans, E.K.2    Kornbluth, S.3
  • 68
    • 0032476659 scopus 로고    scopus 로고
    • Scythe: A novel reaper-binding apoptotic regulator
    • Thress, K., Henzel, W., Shillinglaw, W. and Kornbluth, S. (1998) Scythe: a novel reaper-binding apoptotic regulator. EMBO J. 17, 6135-6143.
    • (1998) EMBO J , vol.17 , pp. 6135-6143
    • Thress, K.1    Henzel, W.2    Shillinglaw, W.3    Kornbluth, S.4
  • 69
    • 27944446355 scopus 로고    scopus 로고
    • The reaper-binding protein scythe modulates apoptosis and proliferation during mammalian development
    • Desmots, F., Russell, H. R., Lee, Y., Boyd, K. and McKinnon, P. J. (2005) The reaper-binding protein scythe modulates apoptosis and proliferation during mammalian development. Mol. Cell Biol. 25, 10329-10337.
    • (2005) Mol. Cell Biol , vol.25 , pp. 10329-10337
    • Desmots, F.1    Russell, H.R.2    Lee, Y.3    Boyd, K.4    McKinnon, P.J.5
  • 70
    • 0347320582 scopus 로고    scopus 로고
    • The human small glutamine-rich TPR-containing protein is required for progress through cell division
    • Winnefeld, M., Rommelaere, J. and Cziepluch, C. (2004) The human small glutamine-rich TPR-containing protein is required for progress through cell division. Exp. Cell Res. 293, 43-57.
    • (2004) Exp. Cell Res , vol.293 , pp. 43-57
    • Winnefeld, M.1    Rommelaere, J.2    Cziepluch, C.3
  • 71
    • 33745934813 scopus 로고    scopus 로고
    • Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest
    • Winnefeld, M., Grewenig, A., Schnolzer, M., Spring, H., Knoch, T. A., Gan, E. C., Rommelaere, J. and Cziepluch, C. (2006) Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest. Exp. Cell Res. 312, 2500-2514.
    • (2006) Exp. Cell Res , vol.312 , pp. 2500-2514
    • Winnefeld, M.1    Grewenig, A.2    Schnolzer, M.3    Spring, H.4    Knoch, T.A.5    Gan, E.C.6    Rommelaere, J.7    Cziepluch, C.8
  • 72
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks, C. L. and Gu, W. (2003) Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr. Opin. Cell Biol. 15, 164-171.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 73
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella, E. and Anderson, C. W. (2001) Post-translational modifications and activation of p53 by genotoxic stresses. Eur. J. Biochem. 268, 2764-2772.
    • (2001) Eur. J. Biochem , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 74
    • 34147156192 scopus 로고    scopus 로고
    • HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53
    • Sasaki, T., Gan, E. C., Wakeham, A., Kornbluth, S., Mak, T. W. and Okada, H. (2007) HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53. Genes Dev. 21, 848-861.
    • (2007) Genes Dev , vol.21 , pp. 848-861
    • Sasaki, T.1    Gan, E.C.2    Wakeham, A.3    Kornbluth, S.4    Mak, T.W.5    Okada, H.6
  • 75
    • 0000515691 scopus 로고    scopus 로고
    • HMM-based databases in InterPro
    • Bateman, A. and Haft, D. H. (2002) HMM-based databases in InterPro. Brief Bioinform. 3, 236-245.
    • (2002) Brief Bioinform , vol.3 , pp. 236-245
    • Bateman, A.1    Haft, D.H.2
  • 76
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles: Strategies for structural predictions using sequence information
    • Rychlewski, L., Jaroszewski, L., Li, W. and Godzik, A. (2000) Comparison of sequence profiles: strategies for structural predictions using sequence information. Protein Sci. 9, 232-241.
    • (2000) Protein Sci , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 77
    • 0034809980 scopus 로고    scopus 로고
    • The J-domain proteins of Arabidopsis thaliana: An unexpectedly large and diverse family of chaperones
    • Miernyk, J. A. (2001) The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and diverse family of chaperones. Cell Stress Chaperones 6, 209-218.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 209-218
    • Miernyk, J.A.1
  • 78
    • 0034804135 scopus 로고    scopus 로고
    • Orthologs in Arabidopsis thaliana of the Hsp70 interacting protein Hip
    • Webb, M. A., Cavaletto, J. M., Klanrit, P. and Thompson, G. A. (2001) Orthologs in Arabidopsis thaliana of the Hsp70 interacting protein Hip. Cell Stress Chaperones 6, 247-255.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 247-255
    • Webb, M.A.1    Cavaletto, J.M.2    Klanrit, P.3    Thompson, G.A.4
  • 79
    • 0038796900 scopus 로고    scopus 로고
    • AtCHIP, a U-box-containing E3 ubiquitin ligase, plays a critical role in temperature stress tolerance in Arabidopsis
    • Yan, J., Wang, J., Li, Q., Hwang, J. R., Patterson, C. and Zhang, H. (2003) AtCHIP, a U-box-containing E3 ubiquitin ligase, plays a critical role in temperature stress tolerance in Arabidopsis. Plant Physiol. 132, 861-869.
    • (2003) Plant Physiol , vol.132 , pp. 861-869
    • Yan, J.1    Wang, J.2    Li, Q.3    Hwang, J.R.4    Patterson, C.5    Zhang, H.6
  • 80
    • 0038420750 scopus 로고    scopus 로고
    • The BAG-family proteins in Arabidopsis thaliana
    • Yan, J., He, C. and Zhang, H. (2003) The BAG-family proteins in Arabidopsis thaliana. Plant Sci. 165, 1-7.
    • (2003) Plant Sci , vol.165 , pp. 1-7
    • Yan, J.1    He, C.2    Zhang, H.3
  • 81
    • 0042173040 scopus 로고    scopus 로고
    • BAG-1 prevents stress-induced long-term growth inhibition in breast cancer cells via a chaperone-dependent pathway
    • Townsend, P. A., Cutress, R. I., Sharp, A., Brimmell, M. and Packham, G. (2003) BAG-1 prevents stress-induced long-term growth inhibition in breast cancer cells via a chaperone-dependent pathway. Cancer Res. 63, 4150-4157.
    • (2003) Cancer Res , vol.63 , pp. 4150-4157
    • Townsend, P.A.1    Cutress, R.I.2    Sharp, A.3    Brimmell, M.4    Packham, G.5
  • 82
    • 0347300280 scopus 로고    scopus 로고
    • Plant responses to drought, salinity and extreme temperatures: Towards genetic engineering for stress tolerance
    • Wang, W., Vinocur, B. and Altman, A. (2003) Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance. Planta 218, 1-14.
    • (2003) Planta , vol.218 , pp. 1-14
    • Wang, W.1    Vinocur, B.2    Altman, A.3
  • 84
    • 35548932873 scopus 로고    scopus 로고
    • Plant disease susceptibility conferred by a 'resistance' gene
    • Lorang, J. M., Sweat, T. A. and Wolpert, T. J. (2007) Plant disease susceptibility conferred by a 'resistance' gene. Proc. Natl. Acad. Sci. USA 104, 14861-14866.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14861-14866
    • Lorang, J.M.1    Sweat, T.A.2    Wolpert, T.J.3
  • 85
    • 0032918558 scopus 로고    scopus 로고
    • Plant cis-acting regulatory DNA elements (PLACE) database: 1999
    • Higo, K., Ugawa, Y., Iwamoto, M. and Korenaga, T. (1999) Plant cis-acting regulatory DNA elements (PLACE) database: 1999. Nucleic Acids Res. 27, 297-300.
    • (1999) Nucleic Acids Res , vol.27 , pp. 297-300
    • Higo, K.1    Ugawa, Y.2    Iwamoto, M.3    Korenaga, T.4
  • 86
    • 0034028259 scopus 로고    scopus 로고
    • Molecular responses to dehydration and low temperature: Differences and cross-talk between two stress signaling pathways
    • Shinozaki, K. and Yamaguchi-Shinozaki, K. (2000) Molecular responses to dehydration and low temperature: differences and cross-talk between two stress signaling pathways. Curr. Opin. Plant Biol. 3, 217-223.
    • (2000) Curr. Opin. Plant Biol , vol.3 , pp. 217-223
    • Shinozaki, K.1    Yamaguchi-Shinozaki, K.2
  • 87
    • 0037256419 scopus 로고    scopus 로고
    • Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional activators in abscisic acid signaling
    • Abe, H., Urao, T., Ito, T., Seki, M., Shinozaki, K. and Yamaguchi-Shinozaki, K. (2003) Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional activators in abscisic acid signaling. Plant Cell 15, 63-78.
    • (2003) Plant Cell , vol.15 , pp. 63-78
    • Abe, H.1    Urao, T.2    Ito, T.3    Seki, M.4    Shinozaki, K.5    Yamaguchi-Shinozaki, K.6
  • 88
    • 0037447146 scopus 로고    scopus 로고
    • ICE1: A regulator of cold-induced transcriptome and freezing tolerance in Arabidopsis
    • Chinnusamy, V., Ohta, M., Kanrar, S., Lee, B. H., Hong, X., Agarwal, M. and Zhu, J. K. (2003) ICE1: a regulator of cold-induced transcriptome and freezing tolerance in Arabidopsis. Genes Dev. 17, 1043-1054.
    • (2003) Genes Dev , vol.17 , pp. 1043-1054
    • Chinnusamy, V.1    Ohta, M.2    Kanrar, S.3    Lee, B.H.4    Hong, X.5    Agarwal, M.6    Zhu, J.K.7
  • 89
    • 0035543415 scopus 로고    scopus 로고
    • Involvement of TAAAG elements suggests a role for Dof transcription factors in guard cell-specific gene expression
    • Plesch, G., Ehrhardt, T. and Mueller-Roeber, B. (2001) Involvement of TAAAG elements suggests a role for Dof transcription factors in guard cell-specific gene expression. Plant J. 28, 455-464.
    • (2001) Plant J , vol.28 , pp. 455-464
    • Plesch, G.1    Ehrhardt, T.2    Mueller-Roeber, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.