Crossref
journal-article
Oxford University Press (OUP)
The Journal of Biochemistry (286)
References
28
Referenced
24
-
Fenton, W.A. and Horwich, A.L. (2003) Chaperonin-mediated protein folding: fate of substrate polypeptide. Q. Rev. Biophys.36, 229–256
(
10.1017/S0033583503003883
) -
Bukau, B. and Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell92, 351–366
(
10.1016/S0092-8674(00)80928-9
) - Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D.C., Joachimiak, A., Horwich, A.L., and Sigler, P.B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature371, 578–586
-
Braig, K., Adams, P.D., and Brunger, A.T. (1995) Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat. Struct. Biol.2, 1083–1094
(
10.1038/nsb1295-1083
) -
Bartolucci, C., Lamba, D., Grazulis, S., Manakova, E., and Heumann, H. (2005) Crystal structure of wild-type chaperonin GroEL. J. Mol. Biol.354, 940–951
(
10.1016/j.jmb.2005.09.096
) - Boisvert, D.C., Wang, J., Otwinowski, Z., Horwich, A.L., and Sigler, P.B. (1996) The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP γ S. Nat. Struct. Biol.3, 170–177
-
Wang, J. and Boisvert, D.C. (2003) Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0 Å resolution. J. Mol. Biol.327, 843–855
(
10.1016/S0022-2836(03)00184-0
) -
Xu, Z., Horwich, A.L., and Sigler, P.B. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature388, 741–750
(
10.1038/41944
) -
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. USA94, 12366–12371
(
10.1073/pnas.94.23.12366
) -
Riek, R., Pervushin, K., and Wüthrich, K. (2000) TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem. Sci.25, 462–468
(
10.1016/S0968-0004(00)01665-0
) -
Fiaux, J., Bertelsen, E.B., Horwich, A.L., and Wüthrich, K. (2002) NMR analysis of a 900K GroEL GroES complex. Nature418, 207–211
(
10.1038/nature00860
) -
Riek, R., Wider, G., Pervushin, K., and Wüthrich, K. (1999) Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. Proc. Natl. Acad. Sci. USA96, 4918–4923
(
10.1073/pnas.96.9.4918
) -
Kato, K., Sautès-Fridman, C., Yamada, W., Kobayashi, K., Uchiyama, S., Kim, H., Enokizono, J., Galinha, A., Kobayashi, Y., Fridman, W.H., Arata, Y., and Shimada, I. (2000) Structural basis of the interaction between IgG and Fcγ receptors. J. Mol. Biol.295, 213–224
(
10.1006/jmbi.1999.3351
) -
Kato, K., Gouda, H., Takaha, W., Yoshino, A., Matsunaga, C., and Arata, Y. (1993) 13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G. FEBS Lett.328, 49–54
(
10.1016/0014-5793(93)80963-U
) -
Hochuli, M., Szyperski, T., and Wüthrich, K. (2000) Deuterium isotope effects on the central carbon metabolism of Escherichia coli cells grown on a D2O-containing minimal medium. J. Biomol. NMR17, 33–42
(
10.1023/A:1008329124672
) -
Motojima, F., Makio, T., Aoki, K., Makino, Y., Kuwajima, K., and Yoshida, M. (2000) Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding. Biochem. Biophys. Res. Commun.267, 842–849
(
10.1006/bbrc.1999.2020
) -
Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem.72, 248–254
(
10.1016/0003-2697(76)90527-3
) - Kainosho, M. and Tsuji, T. (1982) Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution. Biochemistry21, 6273–6279
-
Kato, K., Matsunaga, C., Igarashi, T., Kim, H., Odaka, A., Shimada, I., and Arata, Y. (1991) Complete assignment of the methionyl carbonyl carbon resonances in switch variant anti-dansyl antibodies labeled with [1-13C]methionine. Biochemistry30, 270–278
(
10.1021/bi00215a037
) -
Fenton, W.A., Kashi, Y., Furtak, K., and Horwich, A.L. (1994) Residues in chaperonin GroEL required for polypeptide binding and release. Nature371, 614–619
(
10.1038/371614a0
) -
Rye, H.S., Burston, S.G., Fenton, W.A., Beechem, J.M., Xu, Z., Sigler, P.B., and Horwich, A.L. (1997) Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature388, 792–798
(
10.1038/42047
) -
Rye, H.S., Roseman, A.M., Chen, S., Furtak, K., Fenton, W.A., Saibil, H.R., and Horwich, A.L. (1999) GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell97, 325–338
(
10.1016/S0092-8674(00)80742-4
) - Gray, T.E. and Fersht, A.R. (1991) Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett.292, 254–258
- Hunt, J.F., Weaver, A.J., Landry, S.J., Gierasch, L., and Deisenhofer, J. (1996) The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature379, 37–45
-
Fiaux, J., Bertelsen, E.B., Horwich, A.L., and Wüthrich, K. (2004) Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background. J. Biomol. NMR29, 289–297
(
10.1023/B:JNMR.0000032523.00554.38
) -
Cliff, M.J., Kad, N.M., Hay, N., Lund, P.A., Webb, M.R., Burston, S.G., and Clarke, A.R. (1999) A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. J. Mol. Biol.293, 667–684
(
10.1006/jmbi.1999.3138
) -
Ranson, N.A., Farr, G.W., Roseman, A.M., Gowen, B., Fenton, W.A., Horwich, A.L., and Saibil, H.R. (2001) ATP-bound states of GroEL captured by cryo-electron microscopy. Cell107, 869–879
(
10.1016/S0092-8674(01)00617-1
) -
Ranson, N.A., Clare, D.K., Farr, G.W., Houldershaw, D., Horwich, A.L., and Saibil, H.R. (2006) Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat. Struct. Mol. Biol.13, 147–152
(
10.1038/nsmb1046
)
Dates
Type | When |
---|---|
Created | 18 years, 11 months ago (Sept. 9, 2006, 4:19 p.m.) |
Deposited | 7 years, 10 months ago (Oct. 10, 2017, 1:14 p.m.) |
Indexed | 1 year, 3 months ago (May 20, 2024, 4:38 p.m.) |
Issued | 18 years, 10 months ago (Oct. 1, 2006) |
Published | 18 years, 10 months ago (Oct. 1, 2006) |
Published Online | 18 years, 10 months ago (Oct. 1, 2006) |
Published Print | 18 years, 10 months ago (Oct. 1, 2006) |