-
1
-
-
0027316898
-
To fold or not to fold
-
Agard D. A. To fold or not to fold. Science. 260:1993;1903-1904.
-
(1993)
Science
, vol.260
, pp. 1903-1904
-
-
Agard, D.A.1
-
2
-
-
0023777735
-
Tightly regulated tac promoter vectors useful for the expression of unfused and fused protiens inEscherichia coli
-
Amann E., Ochs B., Abel K. J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused protiens inEscherichia coli. Gene. 69:1988;301-315.
-
(1988)
Gene
, vol.69
, pp. 301-315
-
-
Amann, E.1
Ochs, B.2
Abel, K.J.3
-
4
-
-
0030995661
-
Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions
-
Behlke J., Ristau O., Schönfeld H.-J. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry. 36:1997;5149-5136.
-
(1997)
Biochemistry
, vol.36
, pp. 5149-5136
-
-
Behlke, J.1
Ristau, O.2
Schönfeld, H.-J.3
-
5
-
-
0031946770
-
How chaperones fold proteins
-
Beißinger M., Buchner J. How chaperones fold proteins. Biol. Chem. 379:1998;245-259.
-
(1998)
Biol. Chem.
, vol.379
, pp. 245-259
-
-
Beißinger, M.1
Buchner, J.2
-
6
-
-
0030595346
-
Probing the structural role of an αβ loop of maltose-binding protein by mutagenesis: Heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies
-
Betton J.-M., Boscus D., Missiakas D., Raina S., Hofnung M. Probing the structural role of an αβ loop of maltose-binding protein by mutagenesis: heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J. Mol. Biol. 262:1996;140-150.
-
(1996)
J. Mol. Biol.
, vol.262
, pp. 140-150
-
-
Betton, J.-M.1
Boscus, D.2
Missiakas, D.3
Raina, S.4
Hofnung, M.5
-
7
-
-
0027943510
-
The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
-
Braig K., Otwinowski Z., Hegde R., Boisvert D. C., Joachimiak A., Horwich A. L., Sigler P. B. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature. 371:1994;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
-
8
-
-
0025727072
-
GroE facilitates refolding of citrate synthase by suppressing aggregation
-
Buchner J., Schmidt M., Fuchs M., Jaenicke R., Rudolph R., Schmid F. X., Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30:1991;1586-1591.
-
(1991)
Biochemistry
, vol.30
, pp. 1586-1591
-
-
Buchner, J.1
Schmidt, M.2
Fuchs, M.3
Jaenicke, R.4
Rudolph, R.5
Schmid, F.X.6
Kiefhaber, T.7
-
9
-
-
0029016593
-
The origins and consequences of asymmetry in the chaperonin reaction cycle
-
Burston S. G., Ranson N. A., Clarke A. R. The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249:1995;138-152.
-
(1995)
J. Mol. Biol.
, vol.249
, pp. 138-152
-
-
Burston, S.G.1
Ranson, N.A.2
Clarke, A.R.3
-
10
-
-
0029823985
-
Release of both native and non-native proteins from a cis -only GroEL ternary complex
-
Burston S. G., Weissman J. S., Farr G. W., Fenton W. A., Horwich A. L. Release of both native and non-native proteins from a cis -only GroEL ternary complex. Nature. 383:1996;96-99.
-
(1996)
Nature
, vol.383
, pp. 96-99
-
-
Burston, S.G.1
Weissman, J.S.2
Farr, G.W.3
Fenton, W.A.4
Horwich, A.L.5
-
11
-
-
0028027055
-
Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
-
Chen S., Roseman A. M., Hunter A. S., Wood S. P., Burston S. G., Ranson N. A., Clarke A. R., Saibil H. R. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature. 371:1994;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
-
13
-
-
0030334841
-
2complexes in molecular chaperone activity
-
2complexes in molecular chaperone activity. Fold. Des. 1:1996;265-273.
-
(1996)
Fold. Des.
, vol.1
, pp. 265-273
-
-
Corrales, F.J.1
Fersht, A.R.2
-
14
-
-
0031297406
-
Structural and mechanistic consequences of polypeptide binding by GroEL
-
Coyle J. E., Jaeger J., Groß M., Robinson C., Radford S. E. Structural and mechanistic consequences of polypeptide binding by GroEL. Fold. Des. 2:1997;93-104.
-
(1997)
Fold. Des.
, vol.2
, pp. 93-104
-
-
Coyle, J.E.1
Jaeger, J.2
Groß, M.3
Robinson, C.4
Radford, S.E.5
-
15
-
-
0026416056
-
Molecular chaperones-unfolding protein folding
-
Creighton T. E. Molecular chaperones-unfolding protein folding. Nature. 352:1991;17-18.
-
(1991)
Nature
, vol.352
, pp. 17-18
-
-
Creighton, T.E.1
-
16
-
-
0032531727
-
Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10
-
Dubaquié Y., Looser R., Fünfschilling U., Jenö P., Rospert S. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J. 17:1998;5868-5878.
-
(1998)
EMBO J.
, vol.17
, pp. 5868-5878
-
-
Dubaquié, Y.1
Looser, R.2
Fünfschilling, U.3
Jenö, P.4
Rospert, S.5
-
17
-
-
0029112696
-
Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes
-
Engel A., Hayer-Hartl M. K., Goldie K. N., Pfeifer G., Hegerl R., Müller S., da Silva A. C. R., Baumeister W., Hartl F.-U. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science. 269:1995;832-836.
-
(1995)
Science
, vol.269
, pp. 832-836
-
-
Engel, A.1
Hayer-Hartl, M.K.2
Goldie, K.N.3
Pfeifer, G.4
Hegerl, R.5
Müller, S.6
Da Silva, A.C.R.7
Baumeister, W.8
Hartl, F.-U.9
-
18
-
-
0030750584
-
In vivo observation of polypeptide flux through the bacterial chaperonin system
-
Ewalt K. L., Hendrick J. P., Houry W. A., Hartl F.-U. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500.
-
(1997)
Cell
, vol.90
, pp. 491-500
-
-
Ewalt, K.L.1
Hendrick, J.P.2
Houry, W.A.3
Hartl, F.-U.4
-
19
-
-
0024554107
-
The GroES and GroEL heat shock gene products are essential for bacterial growth at all temperatures
-
Fayet O., Ziegelhoffer T., Georgopoulos C. The GroES and GroEL heat shock gene products are essential for bacterial growth at all temperatures. J. Bacteriol. 171:1989;1379-1385.
-
(1989)
J. Bacteriol.
, vol.171
, pp. 1379-1385
-
-
Fayet, O.1
Ziegelhoffer, T.2
Georgopoulos, C.3
-
20
-
-
0031574908
-
GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein
-
Fedorov A. N., Baldwin T. O. GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein. J. Mol. Biol. 268:1997;712-723.
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 712-723
-
-
Fedorov, A.N.1
Baldwin, T.O.2
-
21
-
-
0020484108
-
Correspondence analysis of aligned images of biological particles
-
Frank J., van Heel M. Correspondence analysis of aligned images of biological particles. J. Mol. Biol. 161:1982;134-137.
-
(1982)
J. Mol. Biol.
, vol.161
, pp. 134-137
-
-
Frank, J.1
Van Heel, M.2
-
22
-
-
0031004530
-
Protein folding: How the mechanism of GroEL action is defined by kinetics
-
Frieden C., Clark C. Protein folding: how the mechanism of GroEL action is defined by kinetics. Proc. Natl Acad. Sci. USA. 94:1997;5535-5538.
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 5535-5538
-
-
Frieden, C.1
Clark, C.2
-
25
-
-
0029157195
-
Asymmetrical interacion of GroEL and GroES in the ATPase cycle of assisted protein folding
-
Hayer-Hartl M. K., Martin J., Hartl F.-U. Asymmetrical interacion of GroEL and GroES in the ATPase cycle of assisted protein folding. Science. 269:1995;836-841.
-
(1995)
Science
, vol.269
, pp. 836-841
-
-
Hayer-Hartl, M.K.1
Martin, J.2
Hartl, F.-U.3
-
26
-
-
0029858706
-
Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
-
Hayer-Hartl M. K., Weber F., Hartl F.-U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15:1996;6111-6121.
-
(1996)
EMBO J.
, vol.15
, pp. 6111-6121
-
-
Hayer-Hartl, M.K.1
Weber, F.2
Hartl, F.-U.3
-
27
-
-
0029879294
-
The EM program package: A platform for image processing in biological electron microscopy
-
Hegerl R. The EM program package: a platform for image processing in biological electron microscopy. J. Struct. Biol. 161:1996;30-34.
-
(1996)
J. Struct. Biol.
, vol.161
, pp. 30-34
-
-
Hegerl, R.1
-
28
-
-
0030569019
-
Interaction of GroEL with conformational states of horse cytochrome c
-
Hoshino M., Kawata Y., Goto Y. Interaction of GroEL with conformational states of horse cytochrome c. J. Mol. Biol. 262:1996;575-587.
-
(1996)
J. Mol. Biol.
, vol.262
, pp. 575-587
-
-
Hoshino, M.1
Kawata, Y.2
Goto, Y.3
-
29
-
-
0030067634
-
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
-
Hunt J. F., Weaver A. J., Landry S. J., Gierasch L., Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;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
-
30
-
-
0027419011
-
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
-
Jackson G. S., Staniforth R. A., Halsall D. J., Atkinson T., Holbrook J. J., Clarke A. R., Burston S. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
-
(1993)
Biochemistry
, vol.32
, pp. 2554-2563
-
-
Jackson, G.S.1
Staniforth, R.A.2
Halsall, D.J.3
Atkinson, T.4
Holbrook, J.J.5
Clarke, A.R.6
Burston, S.7
-
31
-
-
0032562652
-
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
-
Kad N. M., Ranson N. A., Cliff M. J., Clarke A. R. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. J. Mol. Biol. 278:1998;267-278.
-
(1998)
J. Mol. Biol.
, vol.278
, pp. 267-278
-
-
Kad, N.M.1
Ranson, N.A.2
Cliff, M.J.3
Clarke, A.R.4
-
32
-
-
0027092285
-
Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
-
Langer T., Pfeifer G., Martin J., Baumeister W., Hartl F.-U. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11:1992;4757-4765.
-
(1992)
EMBO J.
, vol.11
, pp. 4757-4765
-
-
Langer, T.1
Pfeifer, G.2
Martin, J.3
Baumeister, W.4
Hartl, F.-U.5
-
33
-
-
0029875225
-
Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL
-
Lin Z., Eisenstein E. Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL. Proc. Natl Acad. Sci. USA. 93:1996;1977-1981.
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 1977-1981
-
-
Lin, Z.1
Eisenstein, E.2
-
34
-
-
0028340341
-
The formation of symmetrical GroEL-GroES complexes in the presence of ATP
-
Llorca O., Marco S., Carrascosa J. L., Valpuesta J. M. The formation of symmetrical GroEL-GroES complexes in the presence of ATP. FEBS Letters. 345:1994;181-186.
-
(1994)
FEBS Letters
, vol.345
, pp. 181-186
-
-
Llorca, O.1
Marco, S.2
Carrascosa, J.L.3
Valpuesta, J.M.4
-
35
-
-
0030902005
-
Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings
-
Llorca O., Marco S., Carrascosa J. L., Valpuesta J. M. Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings. FEBS Letters. 405:1997;195-199.
-
(1997)
FEBS Letters
, vol.405
, pp. 195-199
-
-
Llorca, O.1
Marco, S.2
Carrascosa, J.L.3
Valpuesta, J.M.4
-
36
-
-
0032483997
-
GroEL under heat-shock
-
Llorca O., Galan A., Carrascosa J. L., Muga A., Valpuesta J. M. GroEL under heat-shock. J. Biol. Chem. 273:1998;32587-32594.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 32587-32594
-
-
Llorca, O.1
Galan, A.2
Carrascosa, J.L.3
Muga, A.4
Valpuesta, J.M.5
-
37
-
-
0031007938
-
Chaperonin-mediated folding of green fluorescent protein
-
Makino Y., Amada K., Taguchi H., Yoshida M. Chaperonin-mediated folding of green fluorescent protein. J. Biol. Chem. 272:1997;12468-12474.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 12468-12474
-
-
Makino, Y.1
Amada, K.2
Taguchi, H.3
Yoshida, M.4
-
38
-
-
0031030690
-
The effect of macromolecular crowding on chaperonin-mediated protein folding
-
Martin J., Hartl F.-U. The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc. Natl Acad. Sci. USA. 94:1997;1107-1112.
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 1107-1112
-
-
Martin, J.1
Hartl, F.-U.2
-
39
-
-
0030045870
-
Protein folding in the central cavity of the GroEL-GroES chaperonin complex
-
Mayhew M., da Silva A. C. R., Martin J., Erdjument-Bromage H., Tempst P., Hartl F.-U. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature. 379:1996;420-426.
-
(1996)
Nature
, vol.379
, pp. 420-426
-
-
Mayhew, M.1
Da Silva, A.C.R.2
Martin, J.3
Erdjument-Bromage, H.4
Tempst, P.5
Hartl, F.-U.6
-
40
-
-
0021062151
-
Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
-
Miller D. M. III, Olson J. S., Pflugrath J. W., Quiocho R. A. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258:1983;13665-13672.
-
(1983)
J. Biol. Chem.
, vol.258
, pp. 13665-13672
-
-
Miller D.M. III1
Olson, J.S.2
Pflugrath, J.W.3
Quiocho, R.A.4
-
41
-
-
0017104628
-
Fluorescence of proteins in 6-M guanidine hydrochloride. A method for the quantitative determination of tryptophan
-
Pajot P. Fluorescence of proteins in 6-M guanidine hydrochloride. A method for the quantitative determination of tryptophan. Eur. J. Biochem. 63:1976;263-269.
-
(1976)
Eur. J. Biochem.
, vol.63
, pp. 263-269
-
-
Pajot, P.1
-
42
-
-
0028258634
-
Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES
-
Peralta D., Hartman D. J., Hoogenraad N. J., Hoj P. B. Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. FEBS Letters. 339:1994;45-49.
-
(1994)
FEBS Letters
, vol.339
, pp. 45-49
-
-
Peralta, D.1
Hartman, D.J.2
Hoogenraad, N.J.3
Hoj, P.B.4
-
43
-
-
0031588017
-
Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
-
Perrett S., Zahn R., Stenberg G., Fersht A. R. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. J. Mol. Biol. 269:1997;892-901.
-
(1997)
J. Mol. Biol.
, vol.269
, pp. 892-901
-
-
Perrett, S.1
Zahn, R.2
Stenberg, G.3
Fersht, A.R.4
-
44
-
-
0030835654
-
GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II
-
Persson M., Carlsson U., Bergenhem N. GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II. FEBS Letters. 411:1997;43-47.
-
(1997)
FEBS Letters
, vol.411
, pp. 43-47
-
-
Persson, M.1
Carlsson, U.2
Bergenhem, N.3
-
45
-
-
0021266784
-
Lon gene product of Escherichia coli is a heat-shock protein
-
Phillips T. A., VanBogelen R. A., Neidhardt F. C. Lon gene product of Escherichia coli is a heat-shock protein. J. Bacteriol. 159:1984;283-287.
-
(1984)
J. Bacteriol.
, vol.159
, pp. 283-287
-
-
Phillips, T.A.1
Vanbogelen, R.A.2
Neidhardt, F.C.3
-
46
-
-
0031764460
-
Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein
-
Raffy S., Sassoon N., Hofnung M., Betton J.-M. Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein. Protein Sci. 7:1998;2136-2142.
-
(1998)
Protein Sci.
, vol.7
, pp. 2136-2142
-
-
Raffy, S.1
Sassoon, N.2
Hofnung, M.3
Betton, J.-M.4
-
47
-
-
0029087065
-
Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
-
Ranson N. A., Dunster N. J., Burston S. G., Clarke A. R. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 250:1995;581-586.
-
(1995)
J. Mol. Biol.
, vol.250
, pp. 581-586
-
-
Ranson, N.A.1
Dunster, N.J.2
Burston, S.G.3
Clarke, A.R.4
-
48
-
-
0031557387
-
Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
-
Ranson N. A., Burston S. G., Clarke A. R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266:1997;656-664.
-
(1997)
J. Mol. Biol.
, vol.266
, pp. 656-664
-
-
Ranson, N.A.1
Burston, S.G.2
Clarke, A.R.3
-
50
-
-
0030592538
-
The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
-
Roseman A., Chen S., White H., Braig K., Saibil H. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
-
(1996)
Cell
, vol.87
, pp. 241-251
-
-
Roseman, A.1
Chen, S.2
White, H.3
Braig, K.4
Saibil, H.5
-
51
-
-
0030804446
-
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
-
Rye H. S., Burston S. G., Fenton W. A., Beechem J. M., Xu Z., Sigler P. B., Horwich A. L. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature. 388:1997;792-798.
-
(1997)
Nature
, vol.388
, 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
-
52
-
-
0029945635
-
Semper: Distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system
-
Saxton W. O. Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system. J. Struct. Biol. 116:1996;230-236.
-
(1996)
J. Struct. Biol.
, vol.116
, pp. 230-236
-
-
Saxton, W.O.1
-
53
-
-
0028290816
-
On the role of GroES in the chaperonin-assisted folding reaction. Three case studies
-
Schmidt M., Buchner J., Todd M. J., Lorimer G. H., Viitanen P. V. On the role of GroES in the chaperonin-assisted folding reaction. Three case studies. J. Biol. Chem. 269:1994a;10304-10311.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 10304-10311
-
-
Schmidt, M.1
Buchner, J.2
Todd, M.J.3
Lorimer, G.H.4
Viitanen, P.V.5
-
54
-
-
0027968020
-
Correlation between the stability of GroEL-protein ligand complex and the release mechanism
-
Schmidt M., Bücheler U., Kaluza B., Buchner J. Correlation between the stability of GroEL-protein ligand complex and the release mechanism. J. Biol. Chem. 45:1994b;27964-27972.
-
(1994)
J. Biol. Chem.
, vol.45
, pp. 27964-27972
-
-
Schmidt, M.1
Bücheler, U.2
Kaluza, B.3
Buchner, J.4
-
55
-
-
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. H., Buchner J. Symmetric complexes of GroE chaperonins as part of the functional cycle. Science. 271:1994c;656-659.
-
(1994)
Science
, vol.271
, pp. 656-659
-
-
Schmidt, M.1
Rutkat, K.2
Rachel, R.3
Pfeifer, G.4
Jaenicke, R.5
Viitanen, P.6
Lorimer, G.H.7
Buchner, J.8
-
56
-
-
0026493924
-
Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
-
Sharff A. J., Rodseth L. E., Spurlino J. C., Quiocho F. A. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry. 31:1992;10657-10663.
-
(1992)
Biochemistry
, vol.31
, pp. 10657-10663
-
-
Sharff, A.J.1
Rodseth, L.E.2
Spurlino, J.C.3
Quiocho, F.A.4
-
57
-
-
0031684079
-
Structure and function in GroEL-mediated protein folding
-
Sigler P. B., Xu Z., Rye H. S., Burston S. G., Fenton W. A., Horwich A. L. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67:1998;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
-
58
-
-
0029157314
-
Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding
-
Smith K. E., Fisher M. T. Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding. J. Biol. Chem. 270:1995;21517-21523.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 21517-21523
-
-
Smith, K.E.1
Fisher, M.T.2
-
59
-
-
0030994081
-
How GroES regulates binding of non-native protein to GroEL
-
Sparrer H., Buchner J. How GroES regulates binding of non-native protein to GroEL. J. Biol. Chem. 272:1997;14080-14086.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 14080-14086
-
-
Sparrer, H.1
Buchner, J.2
-
60
-
-
0029975103
-
Dynamics of the GroEL-protein complex: Effects of nucleotides and folding mutants
-
Sparrer H., Lilie H., Buchner J. Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants. J. Mol. Biol. 258:1996;74-87.
-
(1996)
J. Mol. Biol.
, vol.258
, pp. 74-87
-
-
Sparrer, H.1
Lilie, H.2
Buchner, J.3
-
61
-
-
0031037687
-
Catalysis of protein folding by symmetric chaperone complexes
-
Sparrer H., Rutkat K., Buchner J. Catalysis of protein folding by symmetric chaperone complexes. Proc. Natl Acad. Sci. USA. 94:1997;1096-1100.
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 1096-1100
-
-
Sparrer, H.1
Rutkat, K.2
Buchner, J.3
-
62
-
-
0025754301
-
The 2.3-Å resolution structure of the maltose- Or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
-
Spurlino J. C., Lu G.-Y., Quiocho F. A. The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266:1991;5202-5219.
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 5202-5219
-
-
Spurlino, J.C.1
Lu, G.-Y.2
Quiocho, F.A.3
-
63
-
-
0028855745
-
Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin
-
Taguchi H., Yoshida M. Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin. FEBS Letters. 359:1995;195-198.
-
(1995)
FEBS Letters
, vol.359
, pp. 195-198
-
-
Taguchi, H.1
Yoshida, M.2
-
64
-
-
0028031345
-
Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
-
Todd M. J., Viitanen P. V., Lorimer G. H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science. 265:1994;659-666.
-
(1994)
Science
, vol.265
, pp. 659-666
-
-
Todd, M.J.1
Viitanen, P.V.2
Lorimer, G.H.3
-
65
-
-
0030006212
-
Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
-
Todd M. J., Lorimer G. L., Thirumalai D. Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc. Natl Acad. Sci. USA. 93:1996;4030-4035.
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 4030-4035
-
-
Todd, M.J.1
Lorimer, G.L.2
Thirumalai, D.3
-
67
-
-
0025940841
-
Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
-
Viitanen P. V., Donaldson G. K., Lorimer G. H., Lubben T. H., Gatenby A. A. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry. 30:1991;9716-9723.
-
(1991)
Biochemistry
, vol.30
, pp. 9716-9723
-
-
Viitanen, P.V.1
Donaldson, G.K.2
Lorimer, G.H.3
Lubben, T.H.4
Gatenby, A.A.5
-
68
-
-
0029837424
-
A thermodynamic coupling mechanism for GroEL-mediated unfolding
-
Walter S., Lorimer G. H., Schmid F. X. A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc. Natl Acad. Sci. USA. 93:1996;9425-9430.
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 9425-9430
-
-
Walter, S.1
Lorimer, G.H.2
Schmid, F.X.3
-
69
-
-
0027933369
-
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonative forms
-
Weissman J. S., Kashi Y., Fenton W. A., Horwich A. L. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonative forms. Cell. 78:1994;693-702.
-
(1994)
Cell
, vol.78
, pp. 693-702
-
-
Weissman, J.S.1
Kashi, Y.2
Fenton, W.A.3
Horwich, A.L.4
-
70
-
-
0028785583
-
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
-
Weissman J. S., Hohl C. M., Kovalenko O., Kashi Y., Chen S., Braig K., Saibil H. R., Fenton W. A., Horwich A. L. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell. 83:1995;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
-
71
-
-
0030056969
-
Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
-
Weissman J. S., Rye H. W., Fenton W. A., Beechem J. M., Horwich A. L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 84:1996;481-490.
-
(1996)
Cell
, vol.84
, pp. 481-490
-
-
Weissman, J.S.1
Rye, H.W.2
Fenton, W.A.3
Beechem, J.M.4
Horwich, A.L.5
-
73
-
-
0029004759
-
Nested cooperativity in the ATPase activity in the oligomeric chaperonin GroEL
-
Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity in the oligomeric chaperonin GroEL. Biochemistry. 34:1995;9716-9723.
-
(1995)
Biochemistry
, vol.34
, pp. 9716-9723
-
-
Yifrach, O.1
Horovitz, A.2
-
74
-
-
0029995319
-
Allosteric control by ATP of non-folded protein binding to GroEL
-
Yifrach O., Horovitz A. Allosteric control by ATP of non-folded protein binding to GroEL. J. Mol. Biol. 255:1996;356-361.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 356-361
-
-
Yifrach, O.1
Horovitz, A.2
-
75
-
-
0028025404
-
Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase
-
Zahn R., Plückthun A. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase. J. Mol. Biol. 242:1994;165-174.
-
(1994)
J. Mol. Biol.
, vol.242
, pp. 165-174
-
-
Zahn, R.1
Plückthun, A.2
-
76
-
-
0030576536
-
Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity
-
Zahn R., Perrett S., Fersht A. R. Conformational states bound by the molecular chaperones GroEL and SecB: a hidden unfolding (annealing) activity. J. Mol. Biol. 261:1996;43-61.
-
(1996)
J. Mol. Biol.
, vol.261
, pp. 43-61
-
-
Zahn, R.1
Perrett, S.2
Fersht, A.R.3
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