-
1
-
-
0027214204
-
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
-
Horwich, A. L., and Low, K. B., Fenton, W. A., Hirshfield, I. N., and Furtak, K. (1993) Folding In vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74, 909-917
-
(1993)
Cell
, vol.74
, pp. 909-917
-
-
Horwich, A.L.1
Low, K.B.2
Fenton, W.A.3
Hirshfield, I.N.4
Furtak, K.5
-
2
-
-
22744447508
-
Proteome-wide analysis of chaperonin-dependent protein folding in escherichia coli
-
Kerner, M. J., and Naylor, D. J., Ishihama, Y., Maier, T., Chang, H. C., and Stines, A. P., Georgopoulos, C., Frishman, D., Hayer-Hartl, M., Mann, M., and Hartl, F. U. (2005) Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122, 209-220
-
(2005)
Cell
, vol.122
, pp. 209-220
-
-
Kerner, M.J.1
Naylor, D.J.2
Ishihama, Y.3
Maier, T.4
Chang, H.C.5
Stines, A.P.6
Georgopoulos, C.7
Frishman, D.8
Hayer-Hartl, M.9
Mann, M.10
Hartl, F.U.11
-
3
-
-
77951974784
-
A systematic survey of in vivo obligate chaperonin-dependent substrates
-
Fujiwara, K., Ishihama, Y., Nakahigashi, K., Soga, T., and Taguchi H. (2010) A systematic survey of In vivo obligate chaperonin-dependent substrates. EMBO J. 29, 1552-1564
-
(2010)
EMBO J.
, vol.29
, pp. 1552-1564
-
-
Fujiwara, K.1
Ishihama, Y.2
Nakahigashi, K.3
Soga, T.4
Taguchi, H.5
-
4
-
-
0027943510
-
The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
-
Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., and Horwich, A. L., and Sigler, P. B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578-586
-
(1994)
Nature
, vol.371
, pp. 578-586
-
-
Braig, K.1
Otwinowski, Z.2
Hegde, R.3
Boisvert, D.C.4
Joachimiak, A.5
Horwich, A.L.6
Sigler, P.B.7
-
5
-
-
0030067634
-
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
-
Hunt, J. F., and 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. Nature 379, 37-45
-
(1996)
Nature
, vol.379
, pp. 37-45
-
-
Hunt, J.F.1
Weaver, A.J.2
Landry, S.J.3
Gierasch, L.4
Deisenhofer, J.5
-
6
-
-
0030056969
-
Characterization of the active intermediate of a GroEL-groes-mediated protein folding reaction
-
Weissman, J. S., and Rye, H. S., Fenton, W. A., Beechem, J. M., and Horwich, A. L. (1996) Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490
-
(1996)
Cell
, vol.84
, pp. 481-490
-
-
Weissman, J.S.1
Rye, H.S.2
Fenton, W.A.3
Beechem, J.M.4
Horwich, A.L.5
-
7
-
-
0031684079
-
Structure and function in GroEL-mediated protein folding
-
Sigler, P. B., Xu, Z., Rye, H. S., and Burston, S. G., Fenton, W. A., and Horwich, A. L. (1998) Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581-608
-
(1998)
Annu. Rev. Biochem.
, vol.67
, pp. 581-608
-
-
Sigler, P.B.1
Xu, Z.2
Rye, H.S.3
Burston, S.G.4
Fenton, W.A.5
Horwich, A.L.6
-
8
-
-
56249135270
-
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
-
Apetri, A. C., and Horwich, A. L. (2008) Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc. Natl. Acad. Sci. U.S.A. 105, 17351-17355
-
(2008)
Proc. Natl. Acad. Sci. U.S.A.
, vol.105
, pp. 17351-17355
-
-
Apetri, A.C.1
Horwich, A.L.2
-
9
-
-
68649123756
-
The GroEL/GroES cis cavity as a passive anti-aggregation device
-
Horwich, A. L., and Apetri, A. C., and Fenton, W. A. (2009) The GroEL/GroES cis cavity as a passive anti-aggregation device. FEBS Lett. 583, 2654-2662
-
(2009)
FEBS Lett.
, vol.583
, pp. 2654-2662
-
-
Horwich, A.L.1
Apetri, A.C.2
Fenton, W.A.3
-
10
-
-
33646897305
-
Structural features of the GroEL-groes nano-cage required for rapid folding of encapsulated protein
-
Tang, Y. C., and Chang, H. C., Roeben, A., Wischnewski, D., Wischnewski, N., and Kerner, M. J., Hartl, F. U., and Hayer-Hartl, M. (2006) Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 125, 903-914
-
(2006)
Cell
, vol.125
, pp. 903-914
-
-
Tang, Y.C.1
Chang, H.C.2
Roeben, A.3
Wischnewski, D.4
Wischnewski, N.5
Kerner, M.J.6
Hartl, F.U.7
Hayer-Hartl, M.8
-
11
-
-
84904254570
-
Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level
-
Gupta, A. J., Haldar, S., Miličić, G., Hartl, F. U., and Hayer-Hartl, M. (2014) Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level. J. Mol. Biol. 426, 2739-2754
-
(2014)
J. Mol. Biol.
, vol.426
, pp. 2739-2754
-
-
Gupta, A.J.1
Haldar, S.2
Miličić, G.3
Hartl, F.U.4
Hayer-Hartl, M.5
-
12
-
-
84878840158
-
Visualizing GroEL/ES in the act of encapsulating a folding protein
-
Chen, D.-H., Madan, D., Weaver, J., Lin, Z., Schröder, G. F., Chiu, W., and Rye, H. S. (2013) Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell 153, 1354-1365
-
(2013)
Cell
, vol.153
, pp. 1354-1365
-
-
Chen, D.-H.1
Madan, D.2
Weaver, J.3
Lin, Z.4
Schröder, G.F.5
Chiu, W.6
Rye, H.S.7
-
13
-
-
43749113194
-
Hydrophilic residues 526KNDAAD531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity
-
Machida, K., Kono-Okada, A., Hongo, K., Mizobata, T., and Kawata, Y. (2008) Hydrophilic residues 526KNDAAD531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity. J. Biol. Chem. 283, 6886-6896
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 6886-6896
-
-
Machida, K.1
Kono-Okada, A.2
Hongo, K.3
Mizobata, T.4
Kawata, Y.5
-
14
-
-
0028027055
-
Location of a folding protein and shape changes in GroEL-groes complexes imaged by cryo-electron microscopy
-
Chen, S., and Roseman, A. M., Hunter, A. S., Wood, S. P., and Burston, S. G., Ranson, N. A., Clarke, A. R., and Saibil, H. R. (1994) Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 371, 261-264
-
(1994)
Nature
, vol.371
, pp. 261-264
-
-
Chen, S.1
Roseman, A.M.2
Hunter, A.S.3
Wood, S.P.4
Burston, S.G.5
Ranson, N.A.6
Clarke, A.R.7
Saibil, H.R.8
-
15
-
-
0029643911
-
Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
-
Thiyagarajan, P., and Henderson, S. J., and Joachimiak, A. (1996) Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure 4, 79-88
-
(1996)
Structure
, vol.4
, pp. 79-88
-
-
Thiyagarajan, P.1
Henderson, S.J.2
Joachimiak, A.3
-
16
-
-
53049103895
-
Revisiting the GroEL-groes reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant
-
Koike-Takeshita, A., Yoshida, M., and Taguchi, H. (2008) Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant. J. Biol. Chem. 283, 23774-23781
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 23774-23781
-
-
Koike-Takeshita, A.1
Yoshida, M.2
Taguchi, H.3
-
17
-
-
53049090990
-
Football- and bullet-shaped GroEL-groes complexes coexist during the reaction cycle
-
Sameshima, T., Ueno, T., Iizuka, R., Ishii, N., Terada, N., Okabe, K., and Funatsu, T. (2008) Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle. J. Biol. Chem. 283, 23765-23773
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 23765-23773
-
-
Sameshima, T.1
Ueno, T.2
Iizuka, R.3
Ishii, N.4
Terada, N.5
Okabe, K.6
Funatsu, T.7
-
18
-
-
84887433399
-
Symmetric GroEL:Groes2 complexes are the protein-folding functional form of the chaperonin nanomachine
-
Yang, D., Ye, X., and Lorimer, G. H. (2013) Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine. Proc. Natl. Acad. Sci. U.S.A. 110, E4298-E4305
-
(2013)
Proc. Natl. Acad. Sci. U.S.A.
, vol.110
, pp. E4298-E4305
-
-
Yang, D.1
Ye, X.2
Lorimer, G.H.3
-
19
-
-
0033619703
-
Functional communications between the apical and equatorial domains of GroEL through the intermediate domain
-
Kawata, Y., Kawagoe, M., Hongo, K., Miyazaki, T., Higurashi, T., Mizobata, T., and Nagai, J. (1999) Functional communications between the apical and equatorial domains of GroEL through the intermediate domain. Biochemistry 38, 15731-15740
-
(1999)
Biochemistry
, vol.38
, pp. 15731-15740
-
-
Kawata, Y.1
Kawagoe, M.2
Hongo, K.3
Miyazaki, T.4
Higurashi, T.5
Mizobata, T.6
Nagai, J.7
-
20
-
-
0029843044
-
Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain
-
Doering, D. S., and Matsudaira, P. (1996) Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 35, 12677-12685
-
(1996)
Biochemistry
, vol.35
, pp. 12677-12685
-
-
Doering, D.S.1
Matsudaira, P.2
-
21
-
-
0028785583
-
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
-
Weissman, J. S., and Hohl, C. M., Kovalenko, O., Kashi, Y., Chen, S., Braig, K., Saibil, H. R., Fenton, W. A., and Horwich, A. L. (1995) Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83, 577-587
-
(1995)
Cell
, vol.83
, pp. 577-587
-
-
Weissman, J.S.1
Hohl, C.M.2
Kovalenko, O.3
Kashi, Y.4
Chen, S.5
Braig, K.6
Saibil, H.R.7
Fenton, W.A.8
Horwich, A.L.9
-
22
-
-
76849111130
-
Chaperonin-encapsulation of proteins for NMR
-
Tanaka, S., Kawata, Y., Otting, G., Dixon, N. E., Matsuzaki, K., and Hoshino, M. (2010) Chaperonin-encapsulation of proteins for NMR. Biochim. Biophys. Acta 1804, 866-871
-
(2010)
Biochim. Biophys. Acta
, vol.1804
, pp. 866-871
-
-
Tanaka, S.1
Kawata, Y.2
Otting, G.3
Dixon, N.E.4
Matsuzaki, K.5
Hoshino, M.6
-
23
-
-
84899874019
-
Evaluation of the stability of an SR398/GroES chaperonin complex
-
Ishino, S., Kawata, Y., Ikegami, T., Matsuzaki, K., and Hoshino, M. (2014) Evaluation of the stability of an SR398/GroES chaperonin complex. J. Biochem. 155, 295-300
-
(2014)
J. Biochem.
, vol.155
, pp. 295-300
-
-
Ishino, S.1
Kawata, Y.2
Ikegami, T.3
Matsuzaki, K.4
Hoshino, M.5
-
24
-
-
0038035969
-
Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: Hexokinase treatment revealed the exclusive role of ATP
-
Motojima, F., and Yoshida, M. (2003) Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP. J. Biol. Chem. 278, 26648-26654
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 26648-26654
-
-
Motojima, F.1
Yoshida, M.2
-
25
-
-
2442482377
-
GroEL mediates protein folding with a two successive timer mechanism
-
Ueno, T., Taguchi, H., Tadakuma, H., Yoshida, M., and Funatsu, T. (2004) GroEL mediates protein folding with a two successive timer mechanism. Mol. Cell 14, 423-434
-
(2004)
Mol. Cell
, vol.14
, pp. 423-434
-
-
Ueno, T.1
Taguchi, H.2
Tadakuma, H.3
Yoshida, M.4
Funatsu, T.5
-
26
-
-
53049084967
-
Effect of the C-terminal truncation on the functional cycle of chap-eronin GroEL: Implication that the C-terminal region facilitates the transition from the folding-arrested to the folding-competent state
-
Suzuki, M., Ueno, T., Iizuka, R., Miura, T., Zako, T., Akahori, R., Miyake, T., Shimamoto, N., Aoki, M., Tanii, T., Ohdomari, I., and Funatsu, T. (2008) Effect of the C-terminal truncation on the functional cycle of chap-eronin GroEL: implication that the C-terminal region facilitates the transition from the folding-arrested to the folding-competent state. J. Biol. Chem. 283, 23931-23939
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 23931-23939
-
-
Suzuki, M.1
Ueno, T.2
Iizuka, R.3
Miura, T.4
Zako, T.5
Akahori, R.6
Miyake, T.7
Shimamoto, N.8
Aoki, M.9
Tanii, T.10
Ohdomari, I.11
Funatsu, T.12
-
27
-
-
0034719432
-
Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding
-
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
-
(2000)
Biochem. Biophys. Res. Commun.
, vol.267
, pp. 842-849
-
-
Motojima, F.1
Makio, T.2
Aoki, K.3
Makino, Y.4
Kuwajima, K.5
Yoshida, M.6
-
28
-
-
49649089314
-
Determination of the number of active GroES subunits in the fused hep-tamer GroES required for interactions with GroEL
-
Nojima, T., Murayama, S., Yoshida, M., and Motojima, F. (2008) Determination of the number of active GroES subunits in the fused hep-tamer GroES required for interactions with GroEL. J. Biol. Chem. 283, 18385-18392
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 18385-18392
-
-
Nojima, T.1
Murayama, S.2
Yoshida, M.3
Motojima, F.4
-
29
-
-
84907826095
-
Asp-52 in combination with asp-398 playsacritical rolein ATP hydrolysisofchaperonin GroEL
-
Koike-Takeshita, A., Mitsuoka, K., and Taguchi, H. (2014) Asp-52 in combination with Asp-398 playsacritical rolein ATP hydrolysisofchaperonin GroEL. J. Biol. Chem. 289, 30005-30011
-
(2014)
J. Biol. Chem.
, vol.289
, pp. 30005-30011
-
-
Koike-Takeshita, A.1
Mitsuoka, K.2
Taguchi, H.3
-
30
-
-
84907822084
-
Crystal structure of a symmetric football-shaped GroEL:Groes2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings
-
Koike-Takeshita, A., Arakawa, T., Taguchi, H., and Shimamura, T. (2014) Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings. J. Mol. Biol. 426, 3634-3641
-
(2014)
J. Mol. Biol.
, vol.426
, pp. 3634-3641
-
-
Koike-Takeshita, A.1
Arakawa, T.2
Taguchi, H.3
Shimamura, T.4
-
31
-
-
8544241796
-
BeFx stops the chaperonin cycle of GroEL-groes and generates a complex with double folding chambers
-
Taguchi, H., Tsukuda, K., Motojima, F., Koike-Takeshita, A., and Yoshida, M. (2004) BeFx stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers. J. Biol. Chem.279, 45737-45743
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 45737-45743
-
-
Taguchi, H.1
Tsukuda, K.2
Motojima, F.3
Koike-Takeshita, A.4
Yoshida, M.5
-
32
-
-
84907228012
-
Formation and structures of GroEL:Groes2 chaperonin footballs, the protein-folding functional form
-
Fei, X., Ye, X., LaRonde, N. A., and Lorimer, G. H. (2014) Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form. Proc. Natl. Acad. Sci. U.S.A. 111, 12775-12780
-
(2014)
Proc. Natl. Acad. Sci. U.S.A.
, vol.111
, pp. 12775-12780
-
-
Fei, X.1
Ye, X.2
Laronde, N.A.3
Lorimer, G.H.4
-
33
-
-
84905982956
-
The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein
-
Weaver, J., and Rye, H. S. (2014) The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein. J. Biol. Chem. 289, 23219-23232
-
(2014)
J. Biol. Chem.
, vol.289
, pp. 23219-23232
-
-
Weaver, J.1
Rye, H.S.2
-
34
-
-
34248349952
-
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
-
Farr, G. W., and Fenton, W. A., and Horwich, A. L. (2007) Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proc. Natl. Acad. Sci. U.S.A. 104, 5342-5347
-
(2007)
Proc. Natl. Acad. Sci. U.S.A.
, vol.104
, pp. 5342-5347
-
-
Farr, G.W.1
Fenton, W.A.2
Horwich, A.L.3
-
35
-
-
0027525938
-
The strongly conserved carboxyl-terminus glycine-methi-onine motif of the escherichia coli GroEL chaperonin is dispensable
-
McLennan, N. F., and Girshovich, A. S., Lissin, N. M., Charters, Y., and Masters, M. (1993) The strongly conserved carboxyl-terminus glycine-methi-onine motif of the Escherichia coli GroEL chaperonin is dispensable. Mol. Microbiol. 7, 49-58
-
(1993)
Mol. Microbiol.
, vol.7
, pp. 49-58
-
-
McLennan, N.F.1
Girshovich, A.S.2
Lissin, N.M.3
Charters, Y.4
Masters, M.5
-
36
-
-
0028062818
-
The tail of a chap-eronin: The C-terminal region of escherichia coli GroEL protein
-
McLennan, N. F., McAteer, S., and Masters, M. (1994) The tail of a chap-eronin: the C-terminal region of Escherichia coli GroEL protein. Mol. Microbiol. 14, 309-321
-
(1994)
Mol. Microbiol.
, vol.14
, pp. 309-321
-
-
McLennan, N.F.1
McAteer, S.2
Masters, M.3
-
37
-
-
0028151691
-
A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic pheno-type in escherichia coli K-12
-
Burnett, B. P., and Horwich, A. L., and Low, K. B. (1994) A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic pheno-type in Escherichia coli K-12. J. Bacteriol. 176, 6980-6985
-
(1994)
J. Bacteriol.
, vol.176
, pp. 6980-6985
-
-
Burnett, B.P.1
Horwich, A.L.2
Low, K.B.3
-
38
-
-
78649692077
-
Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside
-
Motojima, F., and Yoshida, M. (2010) Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside. EMBO J. 29, 4008-4019
-
(2010)
EMBO J.
, vol.29
, pp. 4008-4019
-
-
Motojima, F.1
Yoshida, M.2
|