메뉴 건너뛰기




Volumn 45, Issue 22, 2006, Pages 6917-6929

Hsc70 contacts helix III of the J domain from polyomavirus T antigens: Addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; GADOLINIUM; INTERFACES (MATERIALS); NUCLEAR MAGNETIC RESONANCE; PARAMAGNETIC MATERIALS; TUMORS;

EID: 33744962120     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060411d     Document Type: Article
Times cited : (34)

References (79)
  • 1
    • 0034306996 scopus 로고    scopus 로고
    • The Rb/E2F pathway: Expanding roles and emerging paradigms
    • Harbour, J. W., and Dean, D. C. (2000) The Rb/E2F pathway: expanding roles and emerging paradigms, Genes Dev. 14, 2393-2409.
    • (2000) Genes Dev. , vol.14 , pp. 2393-2409
    • Harbour, J.W.1    Dean, D.C.2
  • 2
    • 0035063183 scopus 로고    scopus 로고
    • The Rb/E2F pathway and cancer
    • Nevins, J. R. (2001) The Rb/E2F pathway and cancer, Hum. Mol. Genet. 10, 699-703.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 699-703
    • Nevins, J.R.1
  • 4
    • 2942722811 scopus 로고    scopus 로고
    • Molecular mechanisms of E2F-dependent activation and pRB-mediated repression
    • Frolov, M. V., and Dyson, N. J. (2004) Molecular mechanisms of E2F-dependent activation and pRB-mediated repression, J. Cell. Sci. 117, 2173-2181.
    • (2004) J. Cell. Sci. , vol.117 , pp. 2173-2181
    • Frolov, M.V.1    Dyson, N.J.2
  • 5
    • 3242761487 scopus 로고    scopus 로고
    • Emergent human pathogen simian virus 40 and its role in cancer
    • Vilchez, R. A., and Butel, J. S. (2004) Emergent human pathogen simian virus 40 and its role in cancer, Clin. Microbiol. Rev. 17, 495-508.
    • (2004) Clin. Microbiol. Rev. , vol.17 , pp. 495-508
    • Vilchez, R.A.1    Butel, J.S.2
  • 6
    • 0031746554 scopus 로고    scopus 로고
    • Polyomavirus T antigens: Molecular chaperones for multiprotein complexes
    • Brodsky, J. L., and Pipas, J. M. (1998) Polyomavirus T antigens: molecular chaperones for multiprotein complexes, J. Virol. 72, 5329-5334.
    • (1998) J. Virol. , vol.72 , pp. 5329-5334
    • Brodsky, J.L.1    Pipas, J.M.2
  • 8
    • 0035863048 scopus 로고    scopus 로고
    • Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen
    • Kim, H. Y., Ahn, B. Y., and Cho, Y. (2001) Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen, EMBO J. 20, 295-304.
    • (2001) EMBO J. , vol.20 , pp. 295-304
    • Kim, H.Y.1    Ahn, B.Y.2    Cho, Y.3
  • 9
    • 0030812552 scopus 로고    scopus 로고
    • The DnaJ domain of polyomavirus large T antigen is required to regulate Rb family tumor suppressor function
    • Sheng, Q., Denis, D., Ratnofsky, M., Roberts, T. M., DeCaprio, J. A., and Schaffhausen, B. (1997) The DnaJ domain of polyomavirus large T antigen is required to regulate Rb family tumor suppressor function, J. Virol. 71, 9410-9416.
    • (1997) J. Virol. , vol.71 , pp. 9410-9416
    • Sheng, Q.1    Denis, D.2    Ratnofsky, M.3    Roberts, T.M.4    DeCaprio, J.A.5    Schaffhausen, B.6
  • 10
    • 0033842443 scopus 로고    scopus 로고
    • The molecular chaperone activity of simian virus 40 large T antigen is required to disrupt Rb-E2F family complexes by an ATP-dependent mechanism
    • Sullivan, C. S., Cantalupo, P., and Pipas, J. M. (2000) The molecular chaperone activity of simian virus 40 large T antigen is required to disrupt Rb-E2F family complexes by an ATP-dependent mechanism, Mol. Cell. Biol. 20, 6233-6243.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6233-6243
    • Sullivan, C.S.1    Cantalupo, P.2    Pipas, J.M.3
  • 12
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of Hsp40 with Hsp70
    • Greene, M. K., Maskos, K., and Landry, S. J. (1998) Role of the J-domain in the cooperation of Hsp40 with Hsp70, Proc. Natl. Acad. Sci. U.S.A. 95, 6108-6113.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6108-6113
    • Greene, M.K.1    Maskos, K.2    Landry, S.J.3
  • 13
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly and translocation
    • Walsh, P., Bursac, D., Law, Y. C., Cyr, D., and Lithgow, T. (2004) The J-protein family: modulating protein assembly, disassembly and translocation, EMBO Rep. 5, 567-571.
    • (2004) EMBO Rep. , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 14
    • 1542638696 scopus 로고    scopus 로고
    • Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles
    • Gruschus, J. M., Han, C. J., Greener, T., Ferretti, J. A., Greene, L. E., and Eisenberg, E. (2004) Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles, Biochemistry 43, 3111-3119.
    • (2004) Biochemistry , vol.43 , pp. 3111-3119
    • Gruschus, J.M.1    Han, C.J.2    Greener, T.3    Ferretti, J.A.4    Greene, L.E.5    Eisenberg, E.6
  • 15
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham, M. E., and Caplan, A. J. (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function, Cell Stress Chaperones 3, 28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 16
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication, J. Biol. Chem. 269, 5446-5451.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 17
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai, J., and Douglas, M. G. (1996) A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding, J. Biol. Chem. 271, 9347-9354.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 18
    • 0034680778 scopus 로고    scopus 로고
    • NMR structure of the N-terminal J domain of polyomavirus T antigens: Implications for DnaJ-like domains and for T antigen mutations
    • Berjanskii, M. V., Riley, M. I., Xie, A., Semenchenko, V., Folk, W. R., and Van Doren, S. R. (2000) NMR structure of the N-terminal J domain of polyomavirus T antigens: implications for DnaJ-like domains and for T antigen mutations, J. Biol. Chem. 275, 36094-36103.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36094-36103
    • Berjanskii, M.V.1    Riley, M.I.2    Xie, A.3    Semenchenko, V.4    Folk, W.R.5    Van Doren, S.R.6
  • 19
    • 0036859957 scopus 로고    scopus 로고
    • Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain
    • Genevaux, P., Schwager, F., Georgopoulos, C., and Kelley, W. L. (2002) Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain, Genetics 162, 1045-1053.
    • (2002) Genetics , vol.162 , pp. 1045-1053
    • Genevaux, P.1    Schwager, F.2    Georgopoulos, C.3    Kelley, W.L.4
  • 20
    • 0037995501 scopus 로고    scopus 로고
    • Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: Correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK
    • Landry, S. J. (2003) Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK, Biochemistry 42, 4926-4936.
    • (2003) Biochemistry , vol.42 , pp. 4926-4936
    • Landry, S.J.1
  • 21
    • 0037133323 scopus 로고    scopus 로고
    • Mutagenesis of a functional chimeric gene in yeast identifies mutations in the simian virus 40 large T antigen J domain
    • Fewell, S. W., Pipas, J. M., and Brodsky, J. L. (2002) Mutagenesis of a functional chimeric gene in yeast identifies mutations in the simian virus 40 large T antigen J domain, Proc. Natl. Acad. Sci. U.S.A. 99, 2002-2007.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2002-2007
    • Fewell, S.W.1    Pipas, J.M.2    Brodsky, J.L.3
  • 22
  • 23
    • 0029879122 scopus 로고    scopus 로고
    • HLA-DR4 and HLA-DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70-kD heat shock proteins
    • Auger, I., Escola, J. M., Gorvel, J. P., and Roudier, J. (1996) HLA-DR4 and HLA-DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70-kD heat shock proteins, Nat. Med. 2, 306-310.
    • (1996) Nat. Med. , vol.2 , pp. 306-310
    • Auger, I.1    Escola, J.M.2    Gorvel, J.P.3    Roudier, J.4
  • 24
    • 0036222543 scopus 로고    scopus 로고
    • Interaction between heat-shock protein 73 and HLA-DRB1 alleles associated or not with rheumatoid arthritis
    • Auger, I., Lepecuchel, L., and Roudier, J. (2002) Interaction between heat-shock protein 73 and HLA-DRB1 alleles associated or not with rheumatoid arthritis, Arthritis Rheum. 46, 929-933.
    • (2002) Arthritis Rheum. , vol.46 , pp. 929-933
    • Auger, I.1    Lepecuchel, L.2    Roudier, J.3
  • 25
    • 0030910370 scopus 로고    scopus 로고
    • A function for the QKRAA amino acid motif: Mediating binding of DnaJ to DnaK. Implications for the association of rheumatoid arthritis with HLA-DR4
    • Auger, I., and Roudier, J. (1997) A function for the QKRAA amino acid motif: mediating binding of DnaJ to DnaK. Implications for the association of rheumatoid arthritis with HLA-DR4, J. Clin. Invest. 99, 1818-1822.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1818-1822
    • Auger, I.1    Roudier, J.2
  • 26
    • 0041734594 scopus 로고    scopus 로고
    • Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
    • Suh, W. C., Lu, C. Z., and Gross, C. A. (1999) Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ, J. Biol. Chem. 274, 30534-30539.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30534-30539
    • Suh, W.C.1    Lu, C.Z.2    Gross, C.A.3
  • 27
    • 4644243721 scopus 로고    scopus 로고
    • Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium tumefaciens identifies amino acid residues critical to its in vivo function, Int
    • Hennessy, F., Boshoff, A., and Blatch, G. L. (2005) Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium tumefaciens identifies amino acid residues critical to its in vivo function, Int. J. Biochem. Cell Biol. 37, 177-191.
    • (2005) J. Biochem. Cell Biol. , vol.37 , pp. 177-191
    • Hennessy, F.1    Boshoff, A.2    Blatch, G.L.3
  • 28
    • 22344447035 scopus 로고    scopus 로고
    • Not all J domains are created equal: Implications for the specificity of Hsp40-Hsp70 interactions
    • Hennessy, F., Nicoll, W. S., Zimmermann, R., Cheetham, M. E., and Blatch, G. L. (2005) Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions, Protein Sci. 14, 1697-1709.
    • (2005) Protein Sci. , vol.14 , pp. 1697-1709
    • Hennessy, F.1    Nicoll, W.S.2    Zimmermann, R.3    Cheetham, M.E.4    Blatch, G.L.5
  • 29
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein-protein complexes
    • Takahashi, H., Nakanishi, T., Kami, K., Arata, Y., and Shimada, I. (2000) A novel NMR method for determining the interfaces of large protein-protein complexes, Nat. Struct. Biol. 7, 220-223.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 30
    • 0037433504 scopus 로고    scopus 로고
    • 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics, J. Am. Chem. Soc. 125, 2902-2912.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 31
    • 25144456011 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions
    • Pellecchia, M. (2005) Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions, Chem. Biol. 72, 961-971.
    • (2005) Chem. Biol. , vol.72 , pp. 961-971
    • Pellecchia, M.1
  • 32
    • 0032493331 scopus 로고    scopus 로고
    • TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe
    • Arumugam, S., Hemme, C. L., Yoshida, N., Suzuki, K., Nagase, H., Berjanskii, M., Wu, B., and Van Doren, S. R. (1998) TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe, Biochemistry 37, 9650-9657.
    • (1998) Biochemistry , vol.37 , pp. 9650-9657
    • Arumugam, S.1    Hemme, C.L.2    Yoshida, N.3    Suzuki, K.4    Nagase, H.5    Berjanskii, M.6    Wu, B.7    Van Doren, S.R.8
  • 34
    • 0033610476 scopus 로고    scopus 로고
    • Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes
    • Matsuo, H., Walters, K. J., Teruya, K., Tanaka, T., Gassner, G. T., Lippard, S. J., Kyogoku, Y., and Wagner, G. (1999) Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes, J. Am. Chem. Soc. 121, 9903-9904.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9903-9904
    • Matsuo, H.1    Walters, K.J.2    Teruya, K.3    Tanaka, T.4    Gassner, G.T.5    Lippard, S.J.6    Kyogoku, Y.7    Wagner, G.8
  • 35
    • 0038723727 scopus 로고    scopus 로고
    • Global orientation of bound MMP-3 and N-TIMP-1 via residual dipolar couplings
    • Arumugam, S., and Van Doren, S. R. (2003) Global orientation of bound MMP-3 and N-TIMP-1 via residual dipolar couplings, Biochemistry 42, 7950-7958.
    • (2003) Biochemistry , vol.42 , pp. 7950-7958
    • Arumugam, S.1    Van Doren, S.R.2
  • 36
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate
    • Pintacuda, G., and Otting, G. (2002) Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate, J. Am. Chem. Soc. 124, 372-373.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 37
    • 1542289014 scopus 로고    scopus 로고
    • NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: Evidence for a two-site binding model
    • Gao, G., Prutzman, K. C., King, M. L., Scheswohl, D. M., DeRose, E. F., London, R. E., Schaller, M. D., and Campbell, S. L. (2004) NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model, J. Biol. Chem. 279, 8441-8451.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8441-8451
    • Gao, G.1    Prutzman, K.C.2    King, M.L.3    Scheswohl, D.M.4    DeRose, E.F.5    London, R.E.6    Schaller, M.D.7    Campbell, S.L.8
  • 38
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge, O., Bourne, H. R., and Cohen, F. E. (1996) An evolutionary trace method defines binding surfaces common to protein families, J. Mol. Biol. 257, 342-358.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 39
    • 0029664921 scopus 로고    scopus 로고
    • Evolutionarily conserved Galphabetagamma binding surfaces support a model of the G protein-receptor complex
    • Lichtarge, O., Bourne, H. R., and Cohen, F. E. (1996) Evolutionarily conserved Galphabetagamma binding surfaces support a model of the G protein-receptor complex, Proc. Natl. Acad. Sci. U.S.A. 93, 7507-7511.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 7507-7511
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 40
    • 0035126520 scopus 로고    scopus 로고
    • Prediction and confirmation of a site critical for effector regulation of RGS domain activity
    • Sowa, M. E., He, W., Slep, K. C., Kercher, M. A., Lichtarge, O., and Wensel, T. G. (2001) Prediction and confirmation of a site critical for effector regulation of RGS domain activity, Nat. Struct. Biol. 8, 234-237.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 234-237
    • Sowa, M.E.1    He, W.2    Slep, K.C.3    Kercher, M.A.4    Lichtarge, O.5    Wensel, T.G.6
  • 41
    • 0036300444 scopus 로고    scopus 로고
    • Structural clusters of evolutionary trace residues are statistically significant and common in proteins
    • Madabushi, S., Yao, H., Marsh, M., Kristensen, D. M., Philippi, A., Sowa, M. E., and Lichtarge, O. (2002) Structural clusters of evolutionary trace residues are statistically significant and common in proteins, J. Mol. Biol. 316, 139-154.
    • (2002) J. Mol. Biol. , vol.316 , pp. 139-154
    • Madabushi, S.1    Yao, H.2    Marsh, M.3    Kristensen, D.M.4    Philippi, A.5    Sowa, M.E.6    Lichtarge, O.7
  • 42
    • 0036468670 scopus 로고    scopus 로고
    • Evolutionary predictions of binding surfaces and interactions
    • Lichtarge, O., and Sowa, M. E. (2002) Evolutionary predictions of binding surfaces and interactions, Curr. Opin. Struct. Biol. 12, 21-27.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 21-27
    • Lichtarge, O.1    Sowa, M.E.2
  • 43
    • 0028360726 scopus 로고
    • Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1
    • Cyr, D. M., and Douglas, M. G. (1994) Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1, J. Biol. Chem. 269, 9798-9804.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9798-9804
    • Cyr, D.M.1    Douglas, M.G.2
  • 44
    • 0033929731 scopus 로고    scopus 로고
    • Species-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40
    • Sullivan, C. S., Tremblay, J. D., Fewell, S. W., Lewis, J. A., Brodsky, J. L., and Pipas, J. M. (2000) Species-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40, Mol. Cell. Biol. 20, 5749-5757.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5749-5757
    • Sullivan, C.S.1    Tremblay, J.D.2    Fewell, S.W.3    Lewis, J.A.4    Brodsky, J.L.5    Pipas, J.M.6
  • 45
    • 0027484169 scopus 로고
    • Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis
    • O'Brien, M. C., and McKay, D. B. (1993) Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis, J. Biol. Chem. 268, 24323-24329.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24323-24329
    • O'Brien, M.C.1    McKay, D.B.2
  • 46
    • 3142677815 scopus 로고    scopus 로고
    • The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains
    • Zhang, Y., and Zuiderweg, E. R. (2004) The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains, Proc. Natl. Acad. Sci. U.S.A. 101, 10272-10277.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10272-10277
    • Zhang, Y.1    Zuiderweg, E.R.2
  • 47
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 48
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard, T. D., and Kneller, D. G. (2000) SPARKY, University of California, San Francisco.
    • (2000) SPARKY
    • Goddard, T.D.1    Kneller, D.G.2
  • 49
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 50
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) An improved assay for nanomole amounts of inorganic phosphate, Anal. Biochem. 100, 95-97.
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 51
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill, R., Dowhan, W., and Wickner, W. (1990) The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins, Cell 60, 271-280.
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 53
    • 0141706377 scopus 로고    scopus 로고
    • NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase
    • Lee, G. I., Ding, Z., Walker, J. C., and Van Doren, S. R. (2003) NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase, Proc. Natl. Acad. Sci. U.S.A. 100, 11261-11266.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11261-11266
    • Lee, G.I.1    Ding, Z.2    Walker, J.C.3    Van Doren, S.R.4
  • 54
    • 0032711731 scopus 로고    scopus 로고
    • Analysis of heregulin symmetry by weighted evolutionary tracing
    • Landgraf, R., Fischer, D., and Eisenberg, D. (1999) Analysis of heregulin symmetry by weighted evolutionary tracing, Protein Eng. 12, 943-951.
    • (1999) Protein Eng. , vol.12 , pp. 943-951
    • Landgraf, R.1    Fischer, D.2    Eisenberg, D.3
  • 55
    • 0036382875 scopus 로고    scopus 로고
    • Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in psec to nsec and μsec to msec
    • Berjanskii, M. V., Riley, M. I., and Van Doren, S. R. (2002) Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in psec to nsec and μsec to msec, J. Mol. Biol. 321, 503-516.
    • (2002) J. Mol. Biol. , vol.321 , pp. 503-516
    • Berjanskii, M.V.1    Riley, M.I.2    Van Doren, S.R.3
  • 56
    • 28944437358 scopus 로고    scopus 로고
    • Structure of the Rb C-terminal domain bound to E2F1-DP1: A mechanism for phosphorylation-induced E2F release
    • Rubin, S. M., Gall, A. L., Zheng, N., and Pavletich, N. P. (2005) Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release, Cell 123, 1093-1106.
    • (2005) Cell , vol.123 , pp. 1093-1106
    • Rubin, S.M.1    Gall, A.L.2    Zheng, N.3    Pavletich, N.P.4
  • 57
    • 0001913048 scopus 로고    scopus 로고
    • Predicting Protein Disorder for N-, C-, and Internal Regions
    • Li, X., Romero, P., Rani, M., Dunker, A. K., and Obradovic, Z. (1999) Predicting Protein Disorder for N-, C-, and Internal Regions, Genome Inf. Ser. 10, 30-40.
    • (1999) Genome Inf. Ser. , vol.10 , pp. 30-40
    • Li, X.1    Romero, P.2    Rani, M.3    Dunker, A.K.4    Obradovic, Z.5
  • 59
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • Romero, P., Obradovic, Z., and Dunker, A. K. (2004) Natively disordered proteins: functions and predictions, Appl. Bioinf. 3, 105-113.
    • (2004) Appl. Bioinf. , vol.3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 60
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, V., Yang, C. F., and Frydman, J. (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment, EMBO J. 18, 85-95.
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 61
    • 0026799491 scopus 로고
    • Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
    • Sadis, S., and Hightower, L. E. (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange, Biochemistry 31, 9406-9412.
    • (1992) Biochemistry , vol.31 , pp. 9406-9412
    • Sadis, S.1    Hightower, L.E.2
  • 62
    • 23944475554 scopus 로고    scopus 로고
    • Switches, catapults, and chaperones: Steady-state kinetic analysis of Hsp70-substrate interactions
    • Chesnokova, L. S., and Witt, S. N. (2005) Switches, catapults, and chaperones: steady-state kinetic analysis of Hsp70-substrate interactions, Biochemistry 44, 11224-11233.
    • (2005) Biochemistry , vol.44 , pp. 11224-11233
    • Chesnokova, L.S.1    Witt, S.N.2
  • 63
    • 0030790668 scopus 로고    scopus 로고
    • Tiny T antigen: An autonomous polyomavirus T antigen amino-terminal domain
    • Riley, M. I., Yoo, W., Mda, N. Y., and Folk, W. R. (1997) Tiny T antigen: an autonomous polyomavirus T antigen amino-terminal domain, J. Virol. 71, 6068-6074.
    • (1997) J. Virol. , vol.71 , pp. 6068-6074
    • Riley, M.I.1    Yoo, W.2    Mda, N.Y.3    Folk, W.R.4
  • 64
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian, Y. Q., Patel, D., Hartl, F.-U., and McGoll, D. J. (1996) Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain, J. Mol. Biol. 260, 224-235.
    • (1996) J. Mol. Biol. , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.-U.3    McGoll, D.J.4
  • 65
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia, M., Szyperski, T., Wall, D., Georgopoulos, C., and Wüthrich, K. (1996) NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone, J. Mol. Biol. 260, 236-250.
    • (1996) J. Mol. Biol. , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 66
    • 0025371625 scopus 로고
    • The amino terminus of polyomavirus middle T antigen is required for transformation
    • Cook, D. N., and Hassell, J. A. (1990) The amino terminus of polyomavirus middle T antigen is required for transformation, J. Virol. 64, 1879-1887.
    • (1990) J. Virol. , vol.64 , pp. 1879-1887
    • Cook, D.N.1    Hassell, J.A.2
  • 67
    • 0029025435 scopus 로고
    • Amino-terminal regions of polyomavirus middle T antigen are required for interactions with protein phosphatase 2A
    • Glenn, G. M., and Eckhart, W. (1995) Amino-terminal regions of polyomavirus middle T antigen are required for interactions with protein phosphatase 2A, J. Virol. 69, 3729-3736.
    • (1995) J. Virol. , vol.69 , pp. 3729-3736
    • Glenn, G.M.1    Eckhart, W.2
  • 68
    • 0029836495 scopus 로고    scopus 로고
    • A novel simian virus 40 early-region domain mediates transactivation of the cyclin a promoter by small-t antigen and is required for transformation in small-t antigen-dependent assay
    • Porras, A., Bennett, J., Howe, A., Tokos, K., Bouck, N., Henglein, B., Sathyamangalam, S., Thimmapaya, B., and Rundell, K. (1996) A novel simian virus 40 early-region domain mediates transactivation of the cyclin A promoter by small-t antigen and is required for transformation in small-t antigen-dependent assay, J. Virol. 70, 6902-6908.
    • (1996) J. Virol. , vol.70 , pp. 6902-6908
    • Porras, A.1    Bennett, J.2    Howe, A.3    Tokos, K.4    Bouck, N.5    Henglein, B.6    Sathyamangalam, S.7    Thimmapaya, B.8    Rundell, K.9
  • 69
    • 3342960406 scopus 로고    scopus 로고
    • Experimentally biased model structure of the Hsc70/auxilin complex: Substrate transfer and interdomain structural change
    • Gruschus, J. M., Greene, L. E., Eisenberg, E., and Ferretti, J. A. (2004) Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural change, Protein Sci. 13, 2029-2044.
    • (2004) Protein Sci. , vol.13 , pp. 2029-2044
    • Gruschus, J.M.1    Greene, L.E.2    Eisenberg, E.3    Ferretti, J.A.4
  • 70
    • 0036382875 scopus 로고    scopus 로고
    • Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in psec to nsec and μsec to msec
    • Berjanskii, M. V., Riley, M. I., and Van Doren, S. R. (2002) Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in psec to nsec and μsec to msec, J. Mol. Biol. 321, 503-516.
    • (2002) J. Mol. Biol. , vol.321 , pp. 503-516
    • Berjanskii, M.V.1    Riley, M.I.2    Van Doren, S.R.3
  • 71
    • 0034023572 scopus 로고    scopus 로고
    • J domain-independent regulation of the Rb family by polyomavirus large T antigen
    • Sheng, Q., Love, T. M., and Schaffhausen, B. (2000) J domain-independent regulation of the Rb family by polyomavirus large T antigen, J. Virol. 74, 5280-5290.
    • (2000) J. Virol. , vol.74 , pp. 5280-5290
    • Sheng, Q.1    Love, T.M.2    Schaffhausen, B.3
  • 73
    • 0029682742 scopus 로고    scopus 로고
    • TAF-like function of SV40 large T antigen
    • Damania, B., and Alwine, J. C. (1996) TAF-like function of SV40 large T antigen, Genes Dev. 10, 1369-1381.
    • (1996) Genes Dev. , vol.10 , pp. 1369-1381
    • Damania, B.1    Alwine, J.C.2
  • 74
    • 0031951664 scopus 로고    scopus 로고
    • Simian virus 40 large T antigen interacts with human TFIIB-related factor and small nuclear RNA-activating protein complex for transcriptional activation of TATA-containing polymerase III promoters
    • Damania, B., Mital, R., and Alwine, J. C. (1998) Simian virus 40 large T antigen interacts with human TFIIB-related factor and small nuclear RNA-activating protein complex for transcriptional activation of TATA-containing polymerase III promoters, Mol. Cell. Biol. 18, 1331-1338.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1331-1338
    • Damania, B.1    Mital, R.2    Alwine, J.C.3
  • 75
    • 0024978377 scopus 로고
    • Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication
    • Alfano, C., and McMacken, R. (1989) Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication, J. Biol. Chem. 264, 10709-10718.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10709-10718
    • Alfano, C.1    McMacken, R.2
  • 76
    • 0024316732 scopus 로고
    • Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz, M., Ang, D., Liberek, K., and Georgopoulos, C. (1989) Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins, EMBO J. 8, 1601-1608.
    • (1989) EMBO J. , vol.8 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4
  • 77
    • 0025875276 scopus 로고
    • Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA
    • Wickner, S., Hoskins, J., and McKenney, K. (1991) Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA, Nature 350, 165-167.
    • (1991) Nature , vol.350 , pp. 165-167
    • Wickner, S.1    Hoskins, J.2    McKenney, K.3
  • 78
    • 0026454375 scopus 로고
    • DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step
    • Wickner, S., Skowyra, D., Hoskins, J., and McKenney, K. (1992) DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step, Proc. Natl. Acad. Sci. U.S.A. 89, 10345-10349.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10345-10349
    • Wickner, S.1    Skowyra, D.2    Hoskins, J.3    McKenney, K.4
  • 79
    • 0037115601 scopus 로고    scopus 로고
    • Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor
    • Lee, C., Chang, J. H., Lee, H. S., and Cho, Y. (2002) Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor, Genes Dev. 16, 3199-3212.
    • (2002) Genes Dev. , vol.16 , pp. 3199-3212
    • Lee, C.1    Chang, J.H.2    Lee, H.S.3    Cho, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.