-
1
-
-
0027190754
-
Evaluation of secondary structure of proteins from circular dischroism spectra using an unsupervised learning neural network
-
Andrade MA, Chacon P, Merelo JJ and Moran F (1993) Evaluation of secondary structure of proteins from circular dischroism spectra using an unsupervised learning neural network. Prot Eng 6: 383-390
-
(1993)
Prot Eng
, vol.6
, pp. 383-390
-
-
Andrade, M.A.1
Chacon, P.2
Merelo, J.J.3
Moran, F.4
-
2
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181: 223-230
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
3
-
-
0028286158
-
Effect of divalent cations on the molecular structure of the GroEL oligomer
-
Azem A, Diamant S and Goloubinoff P (1994) Effect of divalent cations on the molecular structure of the GroEL oligomer. Biochemistry 33: 6671-6675
-
(1994)
Biochemistry
, vol.33
, pp. 6671-6675
-
-
Azem, A.1
Diamant, S.2
Goloubinoff, P.3
-
4
-
-
0025988476
-
Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
-
Badcoe IG, Smith CJ, Wood S, Halsall DJ, Holbrook JJ, Lund P and Clarke AR (1991) Binding of a chaperonin to the folding intermediates of lactate dehydrogenase. Biochemistry 30: 9195-9200
-
(1991)
Biochemistry
, vol.30
, pp. 9195-9200
-
-
Badcoe, I.G.1
Smith, C.J.2
Wood, S.3
Halsall, D.J.4
Holbrook, J.J.5
Lund, P.6
Clarke, A.R.7
-
5
-
-
0029664944
-
The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATPgammaS
-
Boisvert DC, Wang J, Otwinowski Z, Horwich AL and Sigler PB (1996) The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATPgammaS. Nat Struct Biol 3: 170-177
-
(1996)
Nat 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
-
6
-
-
0027943510
-
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
-
Braig K, Otwinowski Z, Hedge R, Boisvert DC, Joachimiak A, Horwich AL and Sigler PB (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371: 578-586
-
(1994)
Nature
, vol.371
, pp. 578-586
-
-
Braig, K.1
Otwinowski, Z.2
Hedge, R.3
Boisvert, D.C.4
Joachimiak, A.5
Horwich, A.L.6
Sigler, P.B.7
-
7
-
-
0031046191
-
Model peptide studies demonstrate that amphipathic secondary structure can be recognized by the chaperonin GroEL (Cpn60)
-
Brazil BT, Cleland JL, McDowell RS, Skelton NJ, Paris K and Horowitz PM (1997) Model peptide studies demonstrate that amphipathic secondary structure can be recognized by the chaperonin GroEL (Cpn60). J Biol Chem 272: 5105-5111
-
(1997)
J Biol Chem
, vol.272
, pp. 5105-5111
-
-
Brazil, B.T.1
Cleland, J.L.2
McDowell, R.S.3
Skelton, N.J.4
Paris, K.5
Horowitz, P.M.6
-
8
-
-
0344084999
-
The binding of 4,4′-bis (1-anilino-8-napthalenesulfonic acid) to the GroEl apical domain fragment is cooperative and induces the formation of a folding intermediate with increased hydrophobic surface exposure
-
in press
-
Brazil BT, Buckle AM, Demeler B, Fersht AR and Horowitz PM (1998a) The binding of 4,4′-bis (1-anilino-8-napthalenesulfonic Acid) to the GroEl apical domain fragment is cooperative and induces the formation of a folding intermediate with increased hydrophobic surface exposure. J Mol Biol (in press)
-
(1998)
J Mol Biol
-
-
Brazil, B.T.1
Buckle, A.M.2
Demeler, B.3
Fersht, A.R.4
Horowitz, P.M.5
-
10
-
-
0025727072
-
GroE facilitates refolding of citrate synthase by suppressing aggregation
-
Buchner J, Schmidt M, Fuchs M, Jaenicke R, Schmid FX and Kiefhaber T (1991) GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30: 1586-1591
-
(1991)
Biochemistry
, vol.30
, pp. 1586-1591
-
-
Buchner, J.1
Schmidt, M.2
Fuchs, M.3
Jaenicke, R.4
Schmid, F.X.5
Kiefhaber, T.6
-
11
-
-
0030966765
-
A structural model for GroEL-polypeptide recognition
-
Buckle AM, Zahn R and Fersht AR (1997) A structural model for GroEL-polypeptide recognition. Proc Natl Acad Sci USA 94: 3571-3575
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3571-3575
-
-
Buckle, A.M.1
Zahn, R.2
Fersht, A.R.3
-
12
-
-
0030841343
-
Conformational disease
-
Carrell RW and Lomas DA (1997) Conformational disease. Lancet 350: 134-138
-
(1997)
Lancet
, vol.350
, pp. 134-138
-
-
Carrell, R.W.1
Lomas, D.A.2
-
13
-
-
0002617993
-
A simple model of chaperonin-mediated protein folding
-
Chan HS and Dill KA (1996) A simple model of chaperonin-mediated protein folding. Proteins 24: 345-351
-
(1996)
Proteins
, vol.24
, pp. 345-351
-
-
Chan, H.S.1
Dill, K.A.2
-
16
-
-
0028902882
-
Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL
-
Diamant S, Azem A, Weiss C and Goloubinoff P (1995) Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL. Biochemistry 34: 273-277
-
(1995)
Biochemistry
, vol.34
, pp. 273-277
-
-
Diamant, S.1
Azem, A.2
Weiss, C.3
Goloubinoff, P.4
-
17
-
-
0030888362
-
Thermodynamics of protein unfolding: Questions pertinent to testing the validity of the two-state model
-
Eftink MR and Ionescu R (1997) Thermodynamics of protein unfolding: questions pertinent to testing the validity of the two-state model. Biophys Chem 64: 175-197
-
(1997)
Biophys Chem
, vol.64
, pp. 175-197
-
-
Eftink, M.R.1
Ionescu, R.2
-
19
-
-
0030750584
-
In vivo observation of polypeptide flux through the bacterial chaperonin system
-
Ewalt KL, Hendrick JP, Houry WA and Hartl FU (1997) In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90: 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
-
20
-
-
0024554107
-
The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
-
Fayet O, Zieghelhoffer T and Georgopopulos C (1989) The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bact 171: 1379-1385
-
(1989)
J Bact
, vol.171
, pp. 1379-1385
-
-
Fayet, O.1
Zieghelhoffer, T.2
Georgopopulos, C.3
-
21
-
-
0028113299
-
Residues in chaperonin GroEL required for polypeptide binding and release
-
Fenton WA, Kashi Y, Furtak K and Horwhich AL (1994) Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371: 614-619
-
(1994)
Nature
, vol.371
, pp. 614-619
-
-
Fenton, W.A.1
Kashi, Y.2
Furtak, K.3
Horwhich, A.L.4
-
22
-
-
0025260865
-
The mechanism of protein folding. Implications of in vitro refolding models for de novo folding and translocation in the cell
-
Fisher G and Schmid FX (1990) The mechanism of protein folding. Implications of in vitro refolding models for de novo folding and translocation in the cell. Biochemistry 29: 2205-2215
-
(1990)
Biochemistry
, vol.29
, pp. 2205-2215
-
-
Fisher, G.1
Schmid, F.X.2
-
23
-
-
0026741821
-
Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (Chaperonin-60) and ATP
-
Fisher MT (1992) Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the Presence of GroEL (Chaperonin-60) and ATP. Biochemistry 31: 3955-3963
-
(1992)
Biochemistry
, vol.31
, pp. 3955-3963
-
-
Fisher, M.T.1
-
24
-
-
0027388993
-
Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
-
Gasset M, Baldwin MA, Fletterick RJ and Pruisner SB (1993) Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc Natl Acad Sci 90: 1-5
-
(1993)
Proc Natl Acad Sci
, vol.90
, pp. 1-5
-
-
Gasset, M.1
Baldwin, M.A.2
Fletterick, R.J.3
Pruisner, S.B.4
-
26
-
-
0026584271
-
Protein folding in the cell
-
Gething MJ and Sambrook J (1992) Protein folding in the cell. Nature 355: 33-45
-
(1992)
Nature
, vol.355
, pp. 33-45
-
-
Gething, M.J.1
Sambrook, J.2
-
27
-
-
0028916849
-
Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401
-
Gibbons DL and Horowitz PM (1995) Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401. J Biol Chem 270: 7335-7340
-
(1995)
J Biol Chem
, vol.270
, pp. 7335-7340
-
-
Gibbons, D.L.1
Horowitz, P.M.2
-
28
-
-
0028844404
-
The chaperonin GroEL is destabilized by binding of ADP
-
Gorovits B and Horowitz PM (1995) The chaperonin GroEL is destabilized by binding of ADP. J Biol Chem 270: 28551-28556
-
(1995)
J Biol Chem
, vol.270
, pp. 28551-28556
-
-
Gorovits, B.1
Horowitz, P.M.2
-
29
-
-
0030936011
-
ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces
-
Corovits BM, Ybarra J and Horowitz PM (1997) ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces. J Biol Chem 272: 6842-6845
-
(1997)
J Biol Chem
, vol.272
, pp. 6842-6845
-
-
Corovits, B.M.1
Ybarra, J.2
Horowitz, P.M.3
-
30
-
-
0027179284
-
Refolding of barnase in the presence of GroE
-
Gray TE and Fersht AR (1993) Refolding of barnase in the presence of GroE. J Mol Biol 232: 1197-1207
-
(1993)
J Mol Biol
, vol.232
, pp. 1197-1207
-
-
Gray, T.E.1
Fersht, A.R.2
-
31
-
-
0026779422
-
Interaction of heta-shock protein 70 with p53 translated in vitro: Evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation
-
Hainaut P and Millier J (1992) Interaction of heta-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. EMBO J 11: 3513-3520
-
(1992)
EMBO J
, vol.11
, pp. 3513-3520
-
-
Hainaut, P.1
Millier, J.2
-
32
-
-
0033582587
-
Thermodynamics of model prions and its implications for the problem of prion protein folding
-
Harrison PM, Chan HS, Prusiner SB and Cohen FE (1999) Thermodynamics of model prions and its implications for the problem of prion protein folding. J Mol Biol 286: 593-606
-
(1999)
J Mol Biol
, vol.286
, pp. 593-606
-
-
Harrison, P.M.1
Chan, H.S.2
Prusiner, S.B.3
Cohen, F.E.4
-
33
-
-
0028334547
-
Conformational specificity of the folding of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin
-
Hayer-Hartl MK, Ewbank JJ, Creighton TE and Hartl FU (1994) Conformational specificity of the folding of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin. The EMBO Journal 13: 3192-3202
-
(1994)
The EMBO Journal
, vol.13
, pp. 3192-3202
-
-
Hayer-Hartl, M.K.1
Ewbank, J.J.2
Creighton, T.E.3
Hartl, F.U.4
-
34
-
-
0028899753
-
Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer
-
Horowitz PM, Hua S and Gibbons DL (1995) Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer. J Biol Chem 270: 1535-1542
-
(1995)
J Biol Chem
, vol.270
, pp. 1535-1542
-
-
Horowitz, P.M.1
Hua, S.2
Gibbons, D.L.3
-
35
-
-
0028792612
-
Nature and consequences of GroEL-protein interactions
-
Itzhaki LS, Otzen DE and Fersht AR (1995) Nature and consequences of GroEL-protein interactions. Biochemistry 34: 14581-14587
-
(1995)
Biochemistry
, vol.34
, pp. 14581-14587
-
-
Itzhaki, L.S.1
Otzen, D.E.2
Fersht, A.R.3
-
36
-
-
0027419011
-
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
-
Jackson GS, Staniforth RA, Haisall DJ, Atkinson T, Holbrook JJ, Clarke AR, and Burston SG (1993) Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry 32: 2554-2563
-
(1993)
Biochemistry
, vol.32
, pp. 2554-2563
-
-
Jackson, G.S.1
Staniforth, R.A.2
Haisall, D.J.3
Atkinson, T.4
Holbrook, J.J.5
Clarke, A.R.6
Burston, S.G.7
-
37
-
-
0030754680
-
Protein misassembly in vitro
-
Richards FM, Eisenberg DS, Kim PM and Wetzel R (Eds), Sandiego: Academic Press
-
Jaenicke R and Seckler R (1997) Protein misassembly in vitro. In: Richards FM, Eisenberg DS, Kim PM and Wetzel R (Eds), Advances in Protein Chemistry. Sandiego: Academic Press
-
(1997)
Advances in Protein Chemistry
-
-
Jaenicke, R.1
Seckler, R.2
-
38
-
-
0030582682
-
Dominant forces ion the recognition of a transient folding intermediate of alspha-Lactalbumin by GroEL
-
Katsumata K, Okazaki A, Tsurupa GP and Kuwajima K (1996) Dominant forces ion the recognition of a transient folding intermediate of alspha-Lactalbumin by GroEL. J Mol Biol 264: 643-649
-
(1996)
J Mol Biol
, vol.264
, pp. 643-649
-
-
Katsumata, K.1
Okazaki, A.2
Tsurupa, G.P.3
Kuwajima, K.4
-
39
-
-
0029909034
-
Refolding and reassociation of glycerol dehydrogenase from bacillus stearothermophilus in the absence and presence of GroEL
-
Krauss O and Gore MG (1996) Refolding and reassociation of glycerol dehydrogenase from bacillus stearothermophilus in the absence and presence of GroEL. Eur J Biochem 241: 538-545
-
(1996)
Eur J Biochem
, vol.241
, pp. 538-545
-
-
Krauss, O.1
Gore, M.G.2
-
40
-
-
0024417964
-
The molten-globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima K (1989) The molten-globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Structure, Function and Genetics 6: 87-103
-
(1989)
Proteins: Structure, Function and Genetics
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
41
-
-
0020475449
-
A simple method for displaying the hydrophobia character of a protein
-
Kyte J and Doolittle RF (1982) A simple method for displaying the hydrophobia character of a protein. J Mol Biol 157: 105-132
-
(1982)
J Mol Biol
, vol.157
, pp. 105-132
-
-
Kyte, J.1
Doolittle, R.F.2
-
42
-
-
0025291463
-
The Eschericia coli heta shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor
-
Laminet AA, Ziegelhoffer T, Georgopoulos C and Pluckthun A (1990) The Eschericia coli heta shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. The EMBO Journal 9: 2315-2319
-
(1990)
The EMBO Journal
, vol.9
, pp. 2315-2319
-
-
Laminet, A.A.1
Ziegelhoffer, T.2
Georgopoulos, C.3
Pluckthun, A.4
-
43
-
-
0025840379
-
The chaperonin GroEL binds a polypeptide in an alpha-helical conformation
-
Landry SJ and Gierasch LM (1991) The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry 30: 7359-7362
-
(1991)
Biochemistry
, vol.30
, pp. 7359-7362
-
-
Landry, S.J.1
Gierasch, L.M.2
-
44
-
-
0026693596
-
Pursuit of the molecular structure of amyloid plaque: New technology provides unexpected and critical information
-
Lansbury PT Jr (1992) In pursuit of the molecular structure of amyloid plaque: new technology provides unexpected and critical information. Biochemsitry 31: 6865-6870
-
(1992)
Biochemsitry
, vol.31
, pp. 6865-6870
-
-
Lansbury P.T., Jr.1
-
45
-
-
0032522864
-
Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulfonic acid
-
Li XL, Lei XD, Cai H, Li J, Yang SL, Wang CC and Tsou CL (1998) Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulfonic Acid. Biochem J 331: 505-511
-
(1998)
Biochem J
, vol.331
, pp. 505-511
-
-
Li, X.L.1
Lei, X.D.2
Cai, H.3
Li, J.4
Yang, S.L.5
Wang, C.C.6
Tsou, C.L.7
-
46
-
-
0028838951
-
The hydrophobic nature of GroEL-substrate binding
-
Lin Z, Schwarz FP and Eisenstein E (1995) The Hydrophobic nature of GroEL-substrate binding. J Biol Chem 270: 1011-1014
-
(1995)
J Biol Chem
, vol.270
, pp. 1011-1014
-
-
Lin, Z.1
Schwarz, F.P.2
Eisenstein, E.3
-
47
-
-
0344605026
-
Kinetic and energetic aspects of chaperonin function
-
Ellis RJ (ed.) New York: Academic Press
-
Lund ARCaPA (1996) Kinetic and energetic aspects of chaperonin function. In: Ellis RJ (ed.) The Chaperonins New York: Academic Press
-
(1996)
The Chaperonins
-
-
Lund, A.R.Ca.P.A.1
-
49
-
-
0025820393
-
Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
-
Mendoza JA, Rogers E, Lorimer GH and Horowitz PM (1991) Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J Biol Chem 266: 13044-13049
-
(1991)
J Biol Chem
, vol.266
, pp. 13044-13049
-
-
Mendoza, J.A.1
Rogers, E.2
Lorimer, G.H.3
Horowitz, P.M.4
-
50
-
-
0026640258
-
Effects of the chaperonin GroE on the refolding of tryptophanase from Escerichia coli
-
Mizobata T, Akiyama Y, Ito K, Yumoto N and Kawata Y (1992) Effects of the chaperonin GroE on the refolding of tryptophanase from Escerichia coli. J Biol Chem 267: 1773-1779
-
(1992)
J Biol Chem
, vol.267
, pp. 1773-1779
-
-
Mizobata, T.1
Akiyama, Y.2
Ito, K.3
Yumoto, N.4
Kawata, Y.5
-
51
-
-
0026317333
-
Reconstitution of a heat shock effect in vitro: Influence of GroE on the thermal aggregation of alpha-glucosidase from yeast
-
Neugebauer BH, Rudolph R, Schmidt M and Buchner J (1991) Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast. Biochemistry 30: 11609-11614
-
(1991)
Biochemistry
, vol.30
, pp. 11609-11614
-
-
Neugebauer, B.H.1
Rudolph, R.2
Schmidt, M.3
Buchner, J.4
-
53
-
-
0022969885
-
Speculations on the functions of the major heat shock and glucose-regulated proteins
-
Pelham HRB (1986) Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46: 959-961
-
(1986)
Cell
, vol.46
, pp. 959-961
-
-
Pelham, H.R.B.1
-
54
-
-
0031588017
-
Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
-
Perrett S, Zahn R, Stenberg G and Fersht AR (1997) Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. J Mol Biol 269: 892-901
-
(1997)
J Mol Biol
, vol.269
, pp. 892-901
-
-
Perrett, S.1
Zahn, R.2
Stenberg, G.3
Fersht, A.R.4
-
55
-
-
0030835654
-
GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II
-
Persson M, Carlsson U and Bergenhem N (1997) GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II. FEBS Letters 411: 43-47
-
(1997)
FEBS Letters
, vol.411
, pp. 43-47
-
-
Persson, M.1
Carlsson, U.2
Bergenhem, N.3
-
56
-
-
0025212107
-
Evidence for a molten globule state as a general intermediate in protein folding
-
Ptitsyn OB, Pain RH, Semisotnov GV and Razgulyaev OI (1990) Evidence for a molten globule state as a general intermediate in protein folding. FEBS Letters 262: 20-24
-
(1990)
FEBS Letters
, vol.262
, pp. 20-24
-
-
Ptitsyn, O.B.1
Pain, R.H.2
Semisotnov, G.V.3
Razgulyaev, O.I.4
-
57
-
-
0028342786
-
Amino acid specificity of the Escerichia coli chaperone GroEL (heat shock protein 60)
-
Richarme G and Kohiyama M (1994) Amino acid specificity of the Escerichia coli chaperone GroEL (Heat Shock Protein 60). J Biol Chem 69: 7095-7098
-
(1994)
J Biol Chem
, vol.69
, pp. 7095-7098
-
-
Richarme, G.1
Kohiyama, M.2
-
58
-
-
0030592538
-
The chaperonin ATPase cycle: Mechanism of allosterk switching and movements of substrate-binding domains in GroEL
-
Roseman AM, Chen S, White H, Braig K and Saibil HR (1996) The chaperonin ATPase cycle: mechanism of allosterk switching and movements of substrate-binding domains in GroEL. Cell 87: 241-251
-
(1996)
Cell
, vol.87
, pp. 241-251
-
-
Roseman, A.M.1
Chen, S.2
White, H.3
Braig, K.4
Saibil, H.R.5
-
59
-
-
0026801563
-
Interaction of GroE with an all-B-protein
-
Schmidt M and Buchner J (1992) Interaction of GroE with an all-B-protein. J Biol Chem 267: 16829-16833
-
(1992)
J Biol Chem
, vol.267
, pp. 16829-16833
-
-
Schmidt, M.1
Buchner, J.2
-
60
-
-
0029036303
-
Photoincorporation of 4,4′-Bis(1-anilino-8-napthalenesulfonic acid) into the apical domain of GroEL: Specific information from a nonspecific probe
-
Seale JW, Martinez JL and Horowitz PM (1995) Photoincorporation of 4,4′-Bis(1-anilino-8-napthalenesulfonic Acid) into the apical domain of GroEL: specific information from a nonspecific probe. Biochemistry 34: 7443-7449
-
(1995)
Biochemistry
, vol.34
, pp. 7443-7449
-
-
Seale, J.W.1
Martinez, J.L.2
Horowitz, P.M.3
-
61
-
-
0031918723
-
Photoincorporation of a fluorscent probe into GroEL: Defining the site of interaction
-
Seale JW, Brazil BT and Horowitz PM (1997) Photoincorporation of a fluorscent probe into GroEL: defining the site of interaction. Methods in Enzymology 290: 318-323
-
(1997)
Methods in Enzymology
, vol.290
, pp. 318-323
-
-
Seale, J.W.1
Brazil, B.T.2
Horowitz, P.M.3
-
62
-
-
0029653879
-
Unliganded GroEL at 2.8 A: Structure and functional implications
-
Sigler PB and Horwich AL (1995) Unliganded GroEL at 2.8 A: structure and functional implications. Philos Trans R Soc Lond B Biol Sci 348: 113-119
-
(1995)
Philos Trans R Soc Lond B Biol Sci
, vol.348
, pp. 113-119
-
-
Sigler, P.B.1
Horwich, A.L.2
-
63
-
-
0028231826
-
Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
-
Staniforth RA, Burston SG, Atkinson T and Clarke AR (1994a) Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10. Biochem J 300: 651-658
-
(1994)
Biochem J
, vol.300
, pp. 651-658
-
-
Staniforth, R.A.1
Burston, S.G.2
Atkinson, T.3
Clarke, A.R.4
-
64
-
-
0028232947
-
The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding
-
Staniforth RA, Cortes A, Burston SG, Atkinson T, Holbrook JJ and Clarke AR (1994b) The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding. FEBS Letters 344: 129-135
-
(1994)
FEBS Letters
, vol.344
, pp. 129-135
-
-
Staniforth, R.A.1
Cortes, A.2
Burston, S.G.3
Atkinson, T.4
Holbrook, J.J.5
Clarke, A.R.6
-
65
-
-
0030929819
-
Ligands regulate GroEL thermostability
-
Surin AK, Kotova NV, Kashparov IA, Marchenkov VV, Marchenkova YS and Semisotnov GV (1997) Ligands regulate GroEL thermostability. FEBS Letters 405: 260-262
-
(1997)
FEBS Letters
, vol.405
, pp. 260-262
-
-
Surin, A.K.1
Kotova, N.V.2
Kashparov, I.A.3
Marchenkov, V.V.4
Marchenkova, Y.S.5
Semisotnov, G.V.6
-
66
-
-
0029918182
-
Misfolding the way to disease
-
Taubes G (1996) Misfolding the way to disease (news). Science 271: 1493-1495
-
(1996)
Science
, vol.271
, pp. 1493-1495
-
-
Taubes, G.1
-
67
-
-
0026649584
-
The cytsic fibrosis transmembrane conductance regulator
-
Thomas PJ (1992) The cytsic fibrosis transmembrane conductance regulator. J Biol Chem 267: 5727-5730
-
(1992)
J Biol Chem
, vol.267
, pp. 5727-5730
-
-
Thomas, P.J.1
-
68
-
-
0028856292
-
Defective protein folding as a basis of human disease
-
Thomas PJ, Qu BH and Pedersen PL (1995) Defective protein folding as a basis of human disease. Trends in Bioch Sci 20: 456-459
-
(1995)
Trends in Bioch Sci
, vol.20
, pp. 456-459
-
-
Thomas, P.J.1
Qu, B.H.2
Pedersen, P.L.3
-
69
-
-
0028031345
-
Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
-
Todd MJ, Viitanen PV and Lorimer GH (1994) Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265: 659-666
-
(1994)
Science
, vol.265
, pp. 659-666
-
-
Todd, M.J.1
Viitanen, P.V.2
Lorimer, G.H.3
-
70
-
-
0030006212
-
Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
-
Todd MJ, Lorimer GH and Thirumalai D (1996) Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci 93: 4030-4035
-
(1996)
Proc Natl Acad Sci
, vol.93
, pp. 4030-4035
-
-
Todd, M.J.1
Lorimer, G.H.2
Thirumalai, D.3
-
71
-
-
0031689866
-
Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator
-
Vankeerberghen A, Wei L, Jaspers M, Cassiman JJ, Nilius B and Cuppens H (1998) Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator. Hum Mol Genet 7: 1761-1769
-
(1998)
Hum Mol Genet
, vol.7
, pp. 1761-1769
-
-
Vankeerberghen, A.1
Wei, L.2
Jaspers, M.3
Cassiman, J.J.4
Nilius, B.5
Cuppens, H.6
-
73
-
-
0025940841
-
Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
-
Viitanen PV, Donaldson GK, Lorimer GH, Luben TH and Gatenby AA (1991) Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry 30: 9716-9723
-
(1991)
Biochemistry
, vol.30
, pp. 9716-9723
-
-
Viitanen, P.V.1
Donaldson, G.K.2
Lorimer, G.H.3
Luben, T.H.4
Gatenby, A.A.5
-
74
-
-
0027065105
-
Purified chaperonin 60 (GroEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
-
Viitanen PV, Gatenby AA and Lorimer GH (1992) Purified chaperonin 60 (GroEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sci 1: 363-369
-
(1992)
Protein Sci
, vol.1
, pp. 363-369
-
-
Viitanen, P.V.1
Gatenby, A.A.2
Lorimer, G.H.3
-
75
-
-
0032514615
-
GroEL-GroES-mediated protein folding requires an intact central cavity
-
Wang JD, Michelitsch MD and Weissman JS (1998) GroEL-GroES-mediated protein folding requires an intact central cavity. Proc Natl Acad Sci USA 95: 12163-12168
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 12163-12168
-
-
Wang, J.D.1
Michelitsch, M.D.2
Weissman, J.S.3
-
77
-
-
0029131202
-
A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone
-
White ZW, Fisher KE and Eisenstein E (1995) A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone. J Biol Chem 270: 20404-20409
-
(1995)
J Biol Chem
, vol.270
, pp. 20404-20409
-
-
White, Z.W.1
Fisher, K.E.2
Eisenstein, E.3
-
79
-
-
0030870719
-
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
-
see Comments
-
Xu Z, Horwich AL and Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex [see Comments]. Nature 388: 741-750
-
(1997)
Nature
, vol.388
, pp. 741-750
-
-
Xu, Z.1
Horwich, A.L.2
Sigler, P.B.3
-
80
-
-
0029004759
-
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
-
Yifrach O and Horovitz A (1995) Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34: 5303-5308
-
(1995)
Biochemistry
, vol.34
, pp. 5303-5308
-
-
Yifrach, O.1
Horovitz, A.2
-
81
-
-
0028260023
-
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
-
Zahn R, Spitzfaden C, Ottiger M, Wutrich K and Pluckthun A (1994a) Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 368: 261-265
-
(1994)
Nature
, vol.368
, pp. 261-265
-
-
Zahn, R.1
Spitzfaden, C.2
Ottiger, M.3
Wutrich, K.4
Pluckthun, A.5
-
82
-
-
0028075011
-
Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of B-lactamase precursor
-
Zahn R, Axmann SE, Rucknagel KP, Jaeger E, Laminet AA and Pluckthun A (1994b) Thermodynamic partitioning model for Hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of B-lactamase precursor. J Mol Biol 242: 150-164
-
(1994)
J Mol Biol
, vol.242
, pp. 150-164
-
-
Zahn, R.1
Axmann, S.E.2
Rucknagel, K.P.3
Jaeger, E.4
Laminet, A.A.5
Pluckthun, A.6
-
83
-
-
0028025404
-
Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase
-
Zahn R and Pluckthun A (1994c) Thermodynamic partitioning model for Hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase. J Mol Biol 242: 165-174
-
(1994)
J Mol Biol
, vol.242
, pp. 165-174
-
-
Zahn, R.1
Pluckthun, A.2
-
84
-
-
0030461621
-
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
-
Zahn R, Buckle AM, Perrett S, Johnson CM, Corrales FJ, Golbik R and Fersht AR (1996) Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Proc Natl Acad Sci USA 93: 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
-
85
-
-
0027409438
-
-
Zheng X, Rosenberg LE, Kalousek F and Fenton WA (1993) GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase. 268: 7489-7493
-
(1993)
GroEL, GroES, and ATP-dependent Folding and Spontaneous Assembly of Ornithine Transcarbamylase.
, vol.268
, pp. 7489-7493
-
-
Zheng, X.1
Rosenberg, L.E.2
Kalousek, F.3
Fenton, W.A.4
|