-
1
-
-
36949033246
-
Two families of chaperonin. Physiology and mechanism
-
Horwich, A. L., Fenton, W. A., Chapman, E., and Farr, G. W. (2007) Two families of chaperonin. Physiology and mechanism. Annu. Rev. Cell Dev. Biol. 23, 115-145
-
(2007)
Annu. Rev. Cell Dev. Biol.
, vol.23
, pp. 115-145
-
-
Horwich, A.L.1
Fenton, W.A.2
Chapman, E.3
Farr, G.W.4
-
2
-
-
79960652801
-
Molecular chaperones in protein folding and proteostasis
-
Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332
-
(2011)
Nature
, vol.475
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
3
-
-
33646907087
-
GroEL-GroESProteinmediated protein folding
-
Horwich, A. L., Farr, G. W., and Fenton, W. A. (2006) GroEL-GroESProteinmediated protein folding. Chem. Rev. 106, 1917-1930
-
(2006)
Chem. Rev.
, vol.106
, pp. 1917-1930
-
-
Horwich, A.L.1
Farr, G.W.2
Fenton, W.A.3
-
4
-
-
70350020881
-
Chaperonin-mediated protein folding. Using a central cavity to kinetically assist polypeptide chain folding
-
Horwich, A. L., and Fenton, W. A. (2009) Chaperonin-mediated protein folding. Using a central cavity to kinetically assist polypeptide chain folding. Q. Rev. Biophys. 42, 83-116
-
(2009)
Q. Rev. Biophys.
, vol.42
, pp. 83-116
-
-
Horwich, A.L.1
Fenton, W.A.2
-
5
-
-
0033597834
-
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
-
Sakikawa, C., Taguchi, H., Makino, Y., and Yoshida, M. (1999) On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274, 21251-21256
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 21251-21256
-
-
Sakikawa, C.1
Taguchi, H.2
Makino, Y.3
Yoshida, M.4
-
6
-
-
0030804446
-
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
-
DOI 10.1038/42047
-
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. Nature 388, 792-798 (Pubitemid 27375160)
-
(1997)
Nature
, vol.388
, Issue.6644
, pp. 792-798
-
-
Rye, H.S.1
Burston, S.G.2
Fenton, W.A.3
Beechem, J.M.4
Xu, Z.5
Sigler, P.B.6
Horwich, A.L.7
-
7
-
-
0033617129
-
GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
-
DOI 10.1016/S0092-8674(00)80742-4
-
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. Cell 97, 325-338 (Pubitemid 29214589)
-
(1999)
Cell
, vol.97
, Issue.3
, pp. 325-338
-
-
Rye, H.S.1
Roseman, A.M.2
Chen, S.3
Furtak, K.4
Fenton, W.A.5
Saibil, H.R.6
Horwich, A.L.7
-
8
-
-
0028071381
-
Symmetric complexes of GroE chaperonins as part of the functional cycle
-
Schmidt, M., Rutkat, K., Rachel, R., Pfeifer, G., Jaenicke, R., Viitanen, P., Lorimer, G., and Buchner, J. (1994) Symmetric complexes of GroE chaperonins as part of the functional cycle. Science 265, 656-659 (Pubitemid 24268275)
-
(1994)
Science
, vol.265
, Issue.5172
, pp. 656-659
-
-
Schmidt, M.1
Rutkat, K.2
Rachel, R.3
Rfeifer, G.4
Jaenicke, R.5
Viitanen, P.6
Lorimer, G.7
Buchner, J.8
-
9
-
-
0038933540
-
Catalysis, commitment and encapsulation during GroE-mediated folding
-
DOI 10.1006/jmbi.1999.2780
-
Beissinger, M., Rutkat, K., and Buchner, J. (1999) Catalysis, commitment and encapsulation during GroE-mediated folding. J. Mol. Biol. 289, 1075-1092 (Pubitemid 29306671)
-
(1999)
Journal of Molecular Biology
, vol.289
, Issue.4
, pp. 1075-1092
-
-
Beissinger, M.1
Rutkat, K.2
Buchner, J.3
-
10
-
-
0030049296
-
Biochemical characterization of symmetric GroEL-GroES complexes: Evidence for a role in protein folding
-
DOI 10.1074/jbc.271.1.68
-
Llorca, O., Carrascosa, J. L., and Valpuesta, J. M. (1996) Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding. J. Biol. Chem. 271, 68-76 (Pubitemid 26026560)
-
(1996)
Journal of Biological Chemistry
, vol.271
, Issue.1
, pp. 68-76
-
-
Llorca, O.1
Carrascosa, J.L.2
Valpuesta, J.M.3
-
11
-
-
0028169935
-
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
-
Azem, A., Kessel, M., and Goloubinoff, P. (1994) Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. Science 265, 653-656
-
(1994)
Science
, vol.265
, pp. 653-656
-
-
Azem, A.1
Kessel, M.2
Goloubinoff, P.3
-
13
-
-
69249146124
-
Probing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP
-
Nojima, T., and Yoshida, M. (2009) Probing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP. J. Biol. Chem. 284, 22834-22839
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 22834-22839
-
-
Nojima, T.1
Yoshida, M.2
-
14
-
-
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
-
16
-
-
77954904803
-
Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides
-
Sameshima, T., Iizuka, R., Ueno, T., Wada, J., Aoki, M., Shimamoto, N., Ohdomari, I., Tanii, T., and Funatsu T. (2010) Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides. J. Biol. Chem. 285, 23159-231564
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 23159-231564
-
-
Sameshima, T.1
Iizuka, R.2
Ueno, T.3
Wada, J.4
Aoki, M.5
Shimamoto, N.6
Ohdomari, I.7
Tanii, T.8
Funatsu, T.9
-
17
-
-
0031037687
-
Catalysis of protein folding by symmetric chaperone complexes
-
DOI 10.1073/pnas.94.4.1096
-
Sparrer, H., Rutkat, K., and Buchner, J. (1997) Catalysis of protein folding by symmetric chaperone complexes. Proc. Natl. Acad. Sci. U.S.A. 94, 1096-1100 (Pubitemid 27087810)
-
(1997)
Proceedings of the National Academy of Sciences of the United States of America
, vol.94
, Issue.4
, pp. 1096-1100
-
-
Sparrer, H.1
Rutkat, K.2
Buchner, J.3
-
18
-
-
0038035969
-
Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: Hexokinase treatment revealed the exclusive role of ATP
-
DOI 10.1074/jbc.M300806200
-
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 (Pubitemid 36876810)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.29
, pp. 26648-26654
-
-
Motojima, F.1
Yoshida, M.2
-
19
-
-
8544241796
-
x stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers
-
DOI 10.1074/jbc.M406795200
-
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 (Pubitemid 39491564)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.44
, pp. 45737-45743
-
-
Taguchi, H.1
Tsukuda, K.2
Motojima, F.3
Koike-Takeshita, A.4
Yoshida, M.5
-
20
-
-
33644868758
-
Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL
-
Koike-Takeshita, A., Shimamura, T., Yokoyama, K., Yoshida, M., and Taguchi, H. (2006) Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL. J. Biol. Chem. 281, 962-967
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 962-967
-
-
Koike-Takeshita, A.1
Shimamura, T.2
Yokoyama, K.3
Yoshida, M.4
Taguchi, H.5
-
21
-
-
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
-
22
-
-
0027443971
-
Force-generating domain of myosin motor
-
DOI 10.1006/bbrc.1993.2422
-
Itakura, S., Yamakawa, H., Toyoshima, Y. Y., Ishijima, A., Kojima, T., Harada, Y., Yanagida, T., Wakabayashi, T., and Sutoh, K. (1993) Force-generating domain of myosin motor. Biochem. Biophys. Res. Commun. 196, 1504-1510 (Pubitemid 23347619)
-
(1993)
Biochemical and Biophysical Research Communications
, vol.196
, Issue.3
, pp. 1504-1510
-
-
Itakura, S.1
Yamakawa, H.2
Toyoshima, Y.Y.3
Ishijima, A.4
Kojima, T.5
Harada, Y.6
Yanagida, T.7
Wakabayashi, T.8
Sutoh, K.9
-
23
-
-
0033536619
-
Single molecular observation of the interaction of GroEL with substrate proteins
-
DOI 10.1006/jmbi.1999.3129
-
Yamasaki, R., Hoshino, M., Wazawa, T., Ishii, Y., Yanagida, T., Kawata, Y., Higurashi, T., Sakai, K., Nagai, J., and Goto, Y. (1999) Single molecular observation of the interaction of GroEL with substrate proteins. J. Mol. Biol. 292, 965-972 (Pubitemid 29481710)
-
(1999)
Journal of Molecular Biology
, vol.292
, Issue.5
, pp. 965-972
-
-
Yamasaki, R.1
Hoshino, M.2
Wazawa, T.3
Ishii, Y.4
Yanagida, T.5
Kawata, Y.6
Higurashi, T.7
Sakai, K.8
Nagai, J.9
Goto, Y.10
-
24
-
-
0029903725
-
GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps
-
DOI 10.1074/jbc.271.45.28229
-
Murai, N., Makino, Y., and Yoshida, M. (1996) GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps. J. Biol. Chem. 271, 28229-28234 (Pubitemid 26374634)
-
(1996)
Journal of Biological Chemistry
, vol.271
, Issue.45
, pp. 28229-28234
-
-
Murai, N.1
Makino, Y.2
Yoshida, M.3
-
25
-
-
0034719432
-
Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding
-
DOI 10.1006/bbrc.1999.2020
-
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 (Pubitemid 30099411)
-
(2000)
Biochemical and Biophysical Research Communications
, vol.267
, Issue.3
, pp. 842-849
-
-
Motojima, F.1
Makio, T.2
Aoki, K.3
Makino, Y.4
Kuwajima, K.5
Yoshida, M.6
-
26
-
-
0028921834
-
Improved green fluorescence
-
Heim, R., Cubitt, A., B., and Tsien, R., Y. (1995) Improved green fluorescence. Nature 373, 663-664
-
(1995)
Nature
, vol.373
, pp. 663-664
-
-
Heim, R.1
Cubitt, A.B.2
Tsien, R.Y.3
-
27
-
-
0033598941
-
The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
-
Chen, L., and Sigler, P. B. (1999) The crystal structure of a GroEL/peptide complex. Plasticity as a basis for substrate diversity. Cell 99, 757-768 (Pubitemid 30017646)
-
(1999)
Cell
, vol.99
, Issue.7
, pp. 757-768
-
-
Chen, L.1
Sigler, P.B.2
-
28
-
-
63249121483
-
GroEL recognizes an amphipathic helix and binds to the hydrophobic side
-
Li, Y., Gao, X., and Chen, L. (2009) GroEL recognizes an amphipathic helix and binds to the hydrophobic side. J. Biol. Chem. 284, 4324-4331
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 4324-4331
-
-
Li, Y.1
Gao, X.2
Chen, L.3
-
29
-
-
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
-
30
-
-
84864852123
-
Flexibility of GroES mobile loop is required for efficient chaperonin function
-
Nojima, T., Ikegami, T., Taguchi, H., and Yoshida, M. (2012) Flexibility of GroES mobile loop is required for efficient chaperonin function. J. Mol. Biol. 422, 291-299
-
(2012)
J. Mol. Biol.
, vol.422
, pp. 291-299
-
-
Nojima, T.1
Ikegami, T.2
Taguchi, H.3
Yoshida, M.4
-
31
-
-
0034876666
-
Single-molecule observation of protein - Protein interactions in the chaperonin system
-
DOI 10.1038/nbt0901-861
-
Taguchi, H., Ueno, T., Tadakuma, H., Yoshida, M., and Funatsu, T. (2001) Single-molecule observation of protein-protein interactions in the chaperonin system. Nat. Biotechnol. 19, 861-865 (Pubitemid 32816757)
-
(2001)
Nature Biotechnology
, vol.19
, Issue.9
, pp. 861-865
-
-
Taguchi, H.1
Ueno, T.2
Tadakuma, H.3
Yoshida, M.4
Funatsu, T.5
-
32
-
-
0031560940
-
Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy
-
DOI 10.1006/bbrc.1997.6732
-
Tokunaga, M., Kitamura, K., Saito, K., Iwane, A. H., and Yanagida, T. (1997) Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy. Biochem. Biophys. Res. Commun. 235, 47-53 (Pubitemid 27302682)
-
(1997)
Biochemical and Biophysical Research Communications
, vol.235
, Issue.1
, pp. 47-53
-
-
Tokunaga, M.1
Kitamura, K.2
Saito, K.3
Iwane, A.H.4
Yanagida, T.5
-
33
-
-
2442482377
-
GroEL mediates protein folding with a two successive timer mechanism
-
DOI 10.1016/S1097-2765(04)00261-8, PII S1097276504002618
-
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 (Pubitemid 38648796)
-
(2004)
Molecular Cell
, vol.14
, Issue.4
, pp. 423-434
-
-
Ueno, T.1
Taguchi, H.2
Tadakuma, H.3
Yoshida, M.4
Funatsu, T.5
-
34
-
-
0028945654
-
Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
-
Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., and Yanagida, T. (1995) Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374, 555-559
-
(1995)
Nature
, vol.374
, pp. 555-559
-
-
Funatsu, T.1
Harada, Y.2
Tokunaga, M.3
Saito, K.4
Yanagida, T.5
-
35
-
-
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
-
36
-
-
53049084967
-
Effect of the C-terminal truncation on the functional cycle of chaperonin 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 chaperonin 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
-
37
-
-
73249133356
-
Direct observation of ultrafast folding and denatured state dynamics in single protein molecules
-
Neuweiler, H., Johnson, C. M., and Fersht, A. R. (2009) Direct observation of ultrafast folding and denatured state dynamics in single protein molecules. Proc. Natl. Acad. Sci. U.S.A. 106, 18569-18574
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 18569-18574
-
-
Neuweiler, H.1
Johnson, C.M.2
Fersht, A.R.3
-
38
-
-
0037452963
-
Watching proteins fold one molecule at a time
-
DOI 10.1073/pnas.2628068100
-
Rhoades, E., Gussakovsky, E., and Haran, G. (2003) Watching proteins fold one molecule at a time. Proc. Natl. Acad. Sci. U.S.A. 100, 3197-3202 (Pubitemid 36356560)
-
(2003)
Proceedings of the National Academy of Sciences of the United States of America
, vol.100
, Issue.6
, pp. 3197-3202
-
-
Rhoades, E.1
Gussakovsky, E.2
Haran, G.3
-
39
-
-
27944505136
-
Allosteric regulation of chaperonins
-
DOI 10.1016/j.sbi.2005.10.001, PII S0959440X05001880, Catalysis and Regulation/Proteins
-
Horovitz, A., and Willison, K. R. (2005) Allosteric regulation of chaperonins. Curr. Opin. Struct. Biol. 15, 646-651 (Pubitemid 41668520)
-
(2005)
Current Opinion in Structural Biology
, vol.15
, Issue.6
, pp. 646-651
-
-
Horovitz, A.1
Willison, K.R.2
-
40
-
-
56249100422
-
Setting the chaperonin timer. The effects of K+ and substrate protein on ATP hydrolysis
-
Grason, J. P., Gresham, J. S., Widjaja, L., Wehri, S. C., and Lorimer, G. H. (2008) Setting the chaperonin timer. The effects of K+ and substrate protein on ATP hydrolysis. Proc. Natl. Acad. Sci. U.S.A. 105, 17334-17338
-
(2008)
Proc. Natl. Acad. Sci. U.S.A.
, vol.105
, pp. 17334-17338
-
-
Grason, J.P.1
Gresham, J.S.2
Widjaja, L.3
Wehri, S.C.4
Lorimer, G.H.5
-
41
-
-
57649114084
-
Triggering protein folding within the GroEL-GroES complex
-
Madan, D., Lin, Z., and Rye, H. S. (2008) Triggering protein folding within the GroEL-GroES complex. J. Biol. Chem. 283, 32003-32013
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 32003-32013
-
-
Madan, D.1
Lin, Z.2
Rye, H.S.3
-
42
-
-
0032714370
-
A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL
-
DOI 10.1006/jmbi.1999.3138
-
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 (Pubitemid 29512064)
-
(1999)
Journal of Molecular Biology
, vol.293
, Issue.3
, pp. 667-684
-
-
Cliff, M.J.1
Kad, N.M.2
Hay, N.3
Lund, P.A.4
Webb, M.R.5
Burston, S.G.6
Clarke, A.R.7
|