-
1
-
-
0028606077
-
Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
-
Neet KE, Timm DE (1994) Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci 3:2167-2174.
-
(1994)
Protein Sci
, vol.3
, pp. 2167-2174
-
-
Neet, K.E.1
Timm, D.E.2
-
2
-
-
0029088389
-
Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES
-
Zondlo J, Fisher KE, Lin Z, Ducote KR, Eisenstein E (1995) Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES. Biochemistry 34:10334-10339.
-
(1995)
Biochemistry
, vol.34
, pp. 10334-10339
-
-
Zondlo, J.1
Fisher, K.E.2
Lin, Z.3
Ducote, K.R.4
Eisenstein, E.5
-
3
-
-
0031563834
-
The structural stability of the co-chaperonin GroES
-
Boudker O, Todd MJ, Freire E (1997) The structural stability of the co-chaperonin GroES. J Mol Biol 272:770-779.
-
(1997)
J Mol Biol
, vol.272
, pp. 770-779
-
-
Boudker, O.1
Todd, M.J.2
Freire, E.3
-
4
-
-
0033588259
-
Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model
-
Higurashi T, Nosaka K, Mizobata T, Nagai J, Kawata Y (1999) Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. J Mol Biol 291:703-713.
-
(1999)
J Mol Biol
, vol.291
, pp. 703-713
-
-
Higurashi, T.1
Nosaka, K.2
Mizobata, T.3
Nagai, J.4
Kawata, Y.5
-
5
-
-
0030067634
-
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
-
Hunt JF, Weaver AJ, Landry SJ, Gierasch L, 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
-
-
0030870719
-
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
-
Xu Z, Horwich AL, Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-750.
-
(1997)
Nature
, vol.388
, pp. 741-750
-
-
Xu, Z.1
Horwich, A.L.2
Sigler, P.B.3
-
7
-
-
0141527459
-
Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering
-
Higurashi T, Hiragi Y, Ichimura K, Seki Y, Soda K, Mizobata T, Kawata Y (2003) Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering. J Mol Biol 333:605-620.
-
(2003)
J Mol Biol
, vol.333
, pp. 605-620
-
-
Higurashi, T.1
Hiragi, Y.2
Ichimura, K.3
Seki, Y.4
Soda, K.5
Mizobata, T.6
Kawata, Y.7
-
8
-
-
0034489321
-
Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant
-
Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P (2000) Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Protein Sci 9:2109-2117.
-
(2000)
Protein Sci
, vol.9
, pp. 2109-2117
-
-
Guidry, J.J.1
Moczygemba, C.K.2
Steede, N.K.3
Landry, S.J.4
Wittung-Stafshede, P.5
-
9
-
-
8544231377
-
Structural stability of oligomeric chaperonin 10: The role of two β-strands at the N and C termini in structural stabilization
-
Sakane I, Ikeda M, Matsumoto C, Higurashi T, Inoue K, Hongo K, Mizobata T, Kawata Y (2004) Structural stability of oligomeric chaperonin 10: the role of two β-strands at the N and C termini in structural stabilization. J Mol Biol 344:1123-1133.
-
(2004)
J Mol Biol
, vol.344
, pp. 1123-1133
-
-
Sakane, I.1
Ikeda, M.2
Matsumoto, C.3
Higurashi, T.4
Inoue, K.5
Hongo, K.6
Mizobata, T.7
Kawata, Y.8
-
10
-
-
27644534843
-
Role of the unique peptide tail in hyperthermostable Aquifex aeolicus cochaperonin protein 10
-
Luke K, Apiyo D, Wittung-Stafshede P (2005) Role of the unique peptide tail in hyperthermostable Aquifex aeolicus cochaperonin protein 10. Biochemistry 44:14385-14395.
-
(2005)
Biochemistry
, vol.44
, pp. 14385-14395
-
-
Luke, K.1
Apiyo, D.2
Wittung-Stafshede, P.3
-
11
-
-
0029665047
-
2-macroglobulin molecules with atomic force microscope
-
2-macroglobulin molecules with atomic force microscope. FEBS Lett 385:29-33.
-
(1996)
FEBS Lett
, vol.385
, pp. 29-33
-
-
Mitsui, K.1
Hara, M.2
Ikai, A.3
-
12
-
-
0346668262
-
Force mode atomic force microscopy as a tool for protein folding studies
-
Best RB, Brockwell DJ, Toca-Herrera JL, Blake AW, Smith DA, Radford SE, Clarke J (2003) Force mode atomic force microscopy as a tool for protein folding studies. Anal Chim Acta 479:87-105.
-
(2003)
Anal Chim Acta
, vol.479
, pp. 87-105
-
-
Best, R.B.1
Brockwell, D.J.2
Toca-Herrera, J.L.3
Blake, A.W.4
Smith, D.A.5
Radford, S.E.6
Clarke, J.7
-
13
-
-
33846940059
-
Mechanical unfolding of proteins: Insights into biology, structure and folding
-
Forman JR, Clarke J (2007) Mechanical unfolding of proteins: insights into biology, structure and folding. Curr Opin Struct Biol 17:58-66.
-
(2007)
Curr Opin Struct Biol
, vol.17
, pp. 58-66
-
-
Forman, J.R.1
Clarke, J.2
-
14
-
-
33947098544
-
Structural stability of covalently linked GroES heptamer: Advantages in the formation of oligomeric structure
-
Sakane I, Hongo K, Motojima F, Murayama S, Mizobata T, Kawata Y (2007) Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure. J Mol Biol 367:1171-1185.
-
(2007)
J Mol Biol
, vol.367
, pp. 1171-1185
-
-
Sakane, I.1
Hongo, K.2
Motojima, F.3
Murayama, S.4
Mizobata, T.5
Kawata, Y.6
-
15
-
-
0035341202
-
Mediatorless biosensor for H2O2 based on recombinant forms of horseradish peroxidase directly adsorbed on polycrystalline gold
-
Ferapontova EE, Grigorenko VG, Egorov AM, Börchers T, Ruzgas T, Gorton L (2001) Mediatorless biosensor for H2O2 based on recombinant forms of horseradish peroxidase directly adsorbed on polycrystalline gold. Biosens Bioelectron 16:147-157.
-
(2001)
Biosens Bioelectron
, vol.16
, pp. 147-157
-
-
Ferapontova, E.E.1
Grigorenko, V.G.2
Egorov, A.M.3
Börchers, T.4
Ruzgas, T.5
Gorton, L.6
-
16
-
-
0031011695
-
Reversible unfolding of individual titin immunoglobulin domains by AFM
-
Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-1112.
-
(1997)
Science
, vol.276
, pp. 1109-1112
-
-
Rief, M.1
Gautel, M.2
Oesterhelt, F.3
Fernandez, J.M.4
Gaub, H.E.5
-
19
-
-
0034602693
-
Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme
-
Yang G, Cecconi C, Baase WA, Vetter IR, Breyer WA, Haack JA, Matthews BW, Dahlquist FW, Bustamante C (2000) Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proc Natl Acad Sci USA 97:139-144.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 139-144
-
-
Yang, G.1
Cecconi, C.2
Baase, W.A.3
Vetter, I.R.4
Breyer, W.A.5
Haack, J.A.6
Matthews, B.W.7
Dahlquist, F.W.8
Bustamante, C.9
-
20
-
-
10044290957
-
Reversible mechanical unfolding of single ubiquitin molecules
-
Chyan CL, Lin FC, Peng H, Yuan JM, Chang CH, Lin SH, Yang G (2004) Reversible mechanical unfolding of single ubiquitin molecules. Biophys J 87:3995-4006.
-
(2004)
Biophys J
, vol.87
, pp. 3995-4006
-
-
Chyan, C.L.1
Lin, F.C.2
Peng, H.3
Yuan, J.M.4
Chang, C.H.5
Lin, S.H.6
Yang, G.7
-
21
-
-
0033616713
-
Mechanical and chemical unfolding of a single protein: A comparison
-
Carrion-Vazquez M, Oberhauser AF, Fowler SB, Marszalek PE, Broedel SE, Clarke J, Fernandez JM (1999) Mechanical and chemical unfolding of a single protein: a comparison. Proc Natl Acad Sci USA 96:3694-3699.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 3694-3699
-
-
Carrion-Vazquez, M.1
Oberhauser, A.F.2
Fowler, S.B.3
Marszalek, P.E.4
Broedel, S.E.5
Clarke, J.6
Fernandez, J.M.7
-
22
-
-
0033582763
-
Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
-
Rief M, Pascual J, Saraste M, Gaub HE (1999) Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J Mol Biol 286:553-561.
-
(1999)
J Mol Biol
, vol.286
, pp. 553-561
-
-
Rief, M.1
Pascual, J.2
Saraste, M.3
Gaub, H.E.4
-
23
-
-
0034804341
-
Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
-
Best RB, Li B, Steward A, Daggett V, Clarke J (2001) Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys J 81:2344-2356.
-
(2001)
Biophys J
, vol.81
, pp. 2344-2356
-
-
Best, R.B.1
Li, B.2
Steward, A.3
Daggett, V.4
Clarke, J.5
-
24
-
-
33751418948
-
Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability
-
Luke K, Wittung-Stafshede P (2006) Folding and assembly pathways of co-chaperonin proteins 10: origin of bacterial thermostability. Arch Biochem Biophys 456:8-18.
-
(2006)
Arch Biochem Biophys
, vol.456
, pp. 8-18
-
-
Luke, K.1
Wittung-Stafshede, P.2
-
25
-
-
0036389817
-
Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering
-
Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J (2002) Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J Mol Biol 322:841-849.
-
(2002)
J Mol Biol
, vol.322
, pp. 841-849
-
-
Fowler, S.B.1
Best, R.B.2
Toca Herrera, J.L.3
Rutherford, T.J.4
Steward, A.5
Paci, E.6
Karplus, M.7
Clarke, J.8
-
26
-
-
0042508740
-
The mechanical stability of ubiquitin is linkage dependent
-
Carrion-Vazquez M, Li H, Lu H, Marszalek PE, Oberhauser AF, Fernandez JM (2003) The mechanical stability of ubiquitin is linkage dependent. Nat Struct Biol 10:738-743.
-
(2003)
Nat Struct Biol
, vol.10
, pp. 738-743
-
-
Carrion-Vazquez, M.1
Li, H.2
Lu, H.3
Marszalek, P.E.4
Oberhauser, A.F.5
Fernandez, J.M.6
-
27
-
-
33749263567
-
Kinetic folding and assembly mechanisms differ for two homologous heptamers
-
Luke K, Perham M, Wittung-Stafshede P (2006) Kinetic folding and assembly mechanisms differ for two homologous heptamers. J Mol Biol 363:729-742.
-
(2006)
J Mol Biol
, vol.363
, pp. 729-742
-
-
Luke, K.1
Perham, M.2
Wittung-Stafshede, P.3
-
28
-
-
0026640258
-
Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP
-
Mizobata T, Akiyama Y, Ito K, Yumoto N, Kawata Y (1992) Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP J Biol Chem 267:17773-17779.
-
(1992)
J Biol Chem
, vol.267
, pp. 17773-17779
-
-
Mizobata, T.1
Akiyama, Y.2
Ito, K.3
Yumoto, N.4
Kawata, Y.5
|