-
1
-
-
0029664944
-
The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
-
Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nature Struct. Biol. 3:1996;170-177
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 170-177
-
-
Boisvert, D.C.1
Wang, J.2
Otwinowski, Z.3
Horwich, A.L.4
Sigler, P.B.5
-
2
-
-
0024291318
-
Unfolding free energy changes determined by the linear extrapolation method 2. Incorporation of Δg N-U values in a thermodynamic cycle
-
Bolen D.W., Santoro M.M. Unfolding free energy changes determined by the linear extrapolation method 2. Incorporation of ΔG N-U values in a thermodynamic cycle. Biochemistry. 27:1988;8069-8074
-
(1988)
Biochemistry
, vol.27
, pp. 8069-8074
-
-
Bolen, D.W.1
Santoro, M.M.2
-
3
-
-
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
-
4
-
-
0028885711
-
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
-
Braig K., Adams P.D., Brünger A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2:1995;1083-1094
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 1083-1094
-
-
Braig, K.1
Adams, P.D.2
Brünger, A.T.3
-
5
-
-
0016711868
-
Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
-
Brandts J.F., Halvorson H.R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry. 14:1975;4953-4963
-
(1975)
Biochemistry
, vol.14
, pp. 4953-4963
-
-
Brandts, J.F.1
Halvorson, H.R.2
Brennan, M.3
-
7
-
-
0027155577
-
Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
-
Clarke J., Fersht A.R. Engineered disulfide bonds as probes of the folding pathway of barnase increasing the stability of proteins against the rate of denaturation. Biochemistry. 32:1993;4322-4329
-
(1993)
Biochemistry
, vol.32
, pp. 4322-4329
-
-
Clarke, J.1
Fersht, A.R.2
-
8
-
-
0142229698
-
MSTARA and MSTARI: Interactive PC algorithms for simple, model independent evaluation of sedimentation equilibrium data
-
Cölfen H., Harding S.E. MSTARA and MSTARI Interactive PC algorithms for simple, model independent evaluation of sedimentation equilibrium data. Eur. Biophys. J. 25:1997;333-346
-
(1997)
Eur. Biophys. J.
, vol.25
, pp. 333-346
-
-
Cölfen, H.1
Harding, S.E.2
-
9
-
-
0004243192
-
-
Berlin, Heidelberg, NewYork, London, Paris, Tokyo: Springer-Verlag
-
Demchenko A. Ultraviolet Spectroscopy of Proteins. 1986;Springer-Verlag, Berlin, Heidelberg, NewYork, London, Paris, Tokyo
-
(1986)
Ultraviolet Spectroscopy of Proteins
-
-
Demchenko, A.1
-
10
-
-
0024278597
-
Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn
-
Dyson H.J., Rance M., Houghten R.A., Lerner R.A., Wright P.E. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 201:1988;161-200
-
(1988)
J. Mol. Biol.
, vol.201
, pp. 161-200
-
-
Dyson, H.J.1
Rance, M.2
Houghten, R.A.3
Lerner, R.A.4
Wright, P.E.5
-
11
-
-
0027958069
-
The use of fluorescence methods to monitor unfolding transitions in proteins
-
Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys.J. 66:1994;482-501
-
(1994)
Biophys.J.
, vol.66
, pp. 482-501
-
-
Eftink, M.R.1
-
12
-
-
0024554107
-
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
-
Fayet O., Ziegelhoffer T., Georgopoulos C. The groES and groEL heat shock gene products of Escherichia coli 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
-
13
-
-
0030910349
-
GroEL-mediated protein folding
-
Fenton W.A., Horwich A.L. GroEL-mediated protein folding. Protein Sci. 6:1997;743-760
-
(1997)
Protein Sci.
, vol.6
, pp. 743-760
-
-
Fenton, W.A.1
Horwich, A.L.2
-
14
-
-
0027163998
-
Protein folding and stability: The pathway of folding of barnase
-
Fersht A.R. Protein folding and stability the pathway of folding of barnase. FEBS Letters. 325:1993;5-16
-
(1993)
FEBS Letters
, vol.325
, pp. 5-16
-
-
Fersht, A.R.1
-
15
-
-
0008221693
-
The Optima XL-A: A new analytical ultracentrifuge with a novel precision absorption optical system
-
S.E. Harding, A.J. Rowe, & J.C. Horton. Cambridge: Royal Soc. Chem
-
Giebeler R. The Optima XL-A A new analytical ultracentrifuge with a novel precision absorption optical system. Harding S.E., Rowe A.J., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1992;16-25 Royal Soc. Chem, Cambridge
-
(1992)
Analytical Ultracentrifugation in Biochemistry and Polymer Science
, pp. 16-25
-
-
Giebeler, R.1
-
16
-
-
0024448151
-
Calculation of protein extinction coefficients from amino acid sequence data
-
Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326
-
(1989)
Anal. Biochem.
, vol.182
, pp. 319-326
-
-
Gill, S.C.1
Von Hippel, P.H.2
-
17
-
-
0028841921
-
Residual structure in urea-denatured chaperonin GroEL
-
Gorovits B.M., Seale J.W., Horowitz P.M. Residual structure in urea-denatured chaperonin GroEL. Biochemistry. 34:1995;13928-13933
-
(1995)
Biochemistry
, vol.34
, pp. 13928-13933
-
-
Gorovits, B.M.1
Seale, J.W.2
Horowitz, P.M.3
-
18
-
-
33947343329
-
The preparation of acetate and phosphate buffer solutions of known pH and ionic strength
-
Green A.A. The preparation of acetate and phosphate buffer solutions of known pH and ionic strength. J. Am. Chem. Soc. 55:1933;2331
-
(1933)
J. Am. Chem. Soc.
, vol.55
, pp. 2331
-
-
Green, A.A.1
-
19
-
-
0027457691
-
A comment on: The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): Evidence for the presence of a single tryptophan, by N. C. Price, S. M. Kelly, S. Wood and A. auf der Mauer (1991
-
Hayer-Hartl M.K., Hartl F.-U. A comment on: The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan, by N. C. Price, S. M. Kelly, S. Wood and A. auf der Mauer (1991. FEBS Letters. 320:1993;83-84
-
(1993)
FEBS Letters
, vol.320
, pp. 83-84
-
-
Hayer-Hartl, M.K.1
Hartl, F.-U.2
-
20
-
-
0028000829
-
Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein
-
Kim D., Kim C., Park C. Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein. J. Mol. Biol. 240:1994;385-395
-
(1994)
J. Mol. Biol.
, vol.240
, pp. 385-395
-
-
Kim, D.1
Kim, C.2
Park, C.3
-
21
-
-
0025698613
-
Transient folding intermediates characterized by protein engineering
-
Matouschek A., Kellis J.J., Serrano L., Bycroft M., Fersht A.R. Transient folding intermediates characterized by protein engineering. Nature. 346:1990;440-445
-
(1990)
Nature
, vol.346
, pp. 440-445
-
-
Matouschek, A.1
Kellis, J.J.2
Serrano, L.3
Bycroft, M.4
Fersht, A.R.5
-
22
-
-
0028023363
-
Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding
-
Mendoza J.A., Demeler B., Horowitz P.M. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. J. Biol. Chem. 269:1994;2447-2451
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 2447-2451
-
-
Mendoza, J.A.1
Demeler, B.2
Horowitz, P.M.3
-
23
-
-
0027395167
-
The unfolding and attempted refolding of the bacterial chaperone groEL (cpn60)
-
Price N.C., Kelly S.M., Thomson G.J., Coggins J.R., Wood S., auf der Mauer A. The unfolding and attempted refolding of the bacterial chaperone groEL (cpn60). Biochim. Biophys. Acta. 1161:1993;52-58
-
(1993)
Biochim. Biophys. Acta
, vol.1161
, pp. 52-58
-
-
Price, N.C.1
Kelly, S.M.2
Thomson, G.J.3
Coggins, J.R.4
Wood, S.5
Auf Der Mauer, A.6
-
24
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method 1. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants
-
Santoro M.M., Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method 1. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
25
-
-
0001340839
-
Kinetics of unfolding and refolding of single-domain proteins
-
T.E. Creighton. New York: W. H. Freeman and Company
-
Schmid F.X. Kinetics of unfolding and refolding of single-domain proteins. Creighton T.E. Protein Folding. 1992;197-241 W. H. Freeman and Company, New York
-
(1992)
Protein Folding
, pp. 197-241
-
-
Schmid, F.X.1
-
27
-
-
0029142612
-
Refolding and reassembly of active chaperonin GroEL after denaturation
-
Ybarra J., Horowitz P.M. Refolding and reassembly of active chaperonin GroEL after denaturation. J. Biol. Chem. 270:1995;22113-22115
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 22113-22115
-
-
Ybarra, J.1
Horowitz, P.M.2
-
28
-
-
0030461621
-
Chaperone function and structure of the polypeptide binding domains of GroEL
-
Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., Fersht A.R. Chaperone function and structure of the polypeptide binding domains of GroEL. Proc. Natl Acad. Sci. USA. 93:1996;15024-15029
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 15024-15029
-
-
Zahn, R.1
Buckle, A.M.2
Perrett, S.3
Johnson, C.M.4
Corrales, F.J.5
Golbik, R.6
Fersht, A.R.7
-
29
-
-
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
-
30
-
-
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
-
31
-
-
0030061845
-
Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
-
Zahn R., Perrett S., Stenberg G., Fersht A.R. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science. 271:1996;642-645
-
(1996)
Science
, vol.271
, pp. 642-645
-
-
Zahn, R.1
Perrett, S.2
Stenberg, G.3
Fersht, A.R.4
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