-
1
-
-
0028230082
-
Dissociation of enzyme oligomers: A mechanism for allosteric regulation
-
Traut, T. W. 1994. Dissociation of enzyme oligomers: a mechanism for allosteric regulation. Crit. Rev. Biochem. Mol. Biol. 29:125-163.
-
(1994)
Crit. Rev. Biochem. Mol. Biol.
, vol.29
, pp. 125-163
-
-
Traut, T.W.1
-
2
-
-
0024356301
-
Rapid measurement of binding constants and heats of binding using a new titration calorimeter
-
Wiseman, T., S. Williston, J. F. Brandts, and L. N. Lin. 1989. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:131-137.
-
(1989)
Anal. Biochem.
, vol.179
, pp. 131-137
-
-
Wiseman, T.1
Williston, S.2
Brandts, J.F.3
Lin, L.N.4
-
3
-
-
3242726206
-
Characterization of protein-protein interactions by isothermal titration calorimetry
-
Velazquez-Campoy, A., S. A. Leavitt, and E. Freire. 2004. Characterization of protein-protein interactions by isothermal titration calorimetry. Methods Mol. Biol. 261:35-54.
-
(2004)
Methods Mol. Biol.
, vol.261
, pp. 35-54
-
-
Velazquez-Campoy, A.1
Leavitt, S.A.2
Freire, E.3
-
4
-
-
0028102938
-
Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations
-
Burrows, S. D., M. L. Doyle, K. P. Murphy, S. G. Franklin, J. R. White, I. Brooks, D. E. McNulty, M. O. Scott, J. R. Knutson, D. Porter, P. R. Young, and P. Hensley. 1994. Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations. Biochemistry. 33:12741-12745.
-
(1994)
Biochemistry
, vol.33
, pp. 12741-12745
-
-
Burrows, S.D.1
Doyle, M.L.2
Murphy, K.P.3
Franklin, S.G.4
White, J.R.5
Brooks, I.6
McNulty, D.E.7
Scott, M.O.8
Knutson, J.R.9
Porter, D.10
Young, P.R.11
Hensley, P.12
-
5
-
-
0029783312
-
Energetics of cyclodextrin-induced dissociation of insulin
-
Lovatt, M., A. Cooper, and P. Camilleri. 1996. Energetics of cyclodextrin-induced dissociation of insulin. Eur. Biophys. J. 24:354-357.
-
(1996)
Eur. Biophys. J.
, vol.24
, pp. 354-357
-
-
Lovatt, M.1
Cooper, A.2
Camilleri, P.3
-
6
-
-
0027427329
-
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES
-
Martin, J., S. Geromanos, P. Tempst, and F. U. Hartl. 1993. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES. Nature. 366:279-282.
-
(1993)
Nature
, vol.366
, pp. 279-282
-
-
Martin, J.1
Geromanos, S.2
Tempst, P.3
Hartl, F.U.4
-
7
-
-
0028815428
-
GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides
-
Todd, M. J., O. Boudkin, E. Freire, and G. H. Lorimer. 1995. GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides. FEBS Lett. 359:123-125.
-
(1995)
FEBS Lett.
, vol.359
, pp. 123-125
-
-
Todd, M.J.1
Boudkin, O.2
Freire, E.3
Lorimer, G.H.4
-
8
-
-
0029823985
-
Release of both native and non-native proteins from a cis-only GroEL ternary complex
-
Burston, S. G., J. S. Weissman, G. W. Farr, W. A. Fenton, and A. L. Horwich. 1996. Release of both native and non-native proteins from a cis-only GroEL ternary complex. Nature. 383:96-99.
-
(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
-
9
-
-
0033617534
-
Chaperonin function: Folding by forced unfolding
-
Shtilerman, M., G. H. Lorimer, and S. W. Englander. 1999. Chaperonin function: folding by forced unfolding. Science. 284:822-825.
-
(1999)
Science
, vol.284
, pp. 822-825
-
-
Shtilerman, M.1
Lorimer, G.H.2
Englander, S.W.3
-
10
-
-
0030067634
-
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
-
Hunt, J. F., A. J. Weaver, S. J. Landry, L. Gierasch, and J. Deisenhofer. 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
-
11
-
-
0030809754
-
Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10
-
Landry, S. J., N. K. Steede, and K. Maskos. 1997. Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10. Biochemistry. 36:10975-10986.
-
(1997)
Biochemistry
, vol.36
, pp. 10975-10986
-
-
Landry, S.J.1
Steede, N.K.2
Maskos, K.3
-
12
-
-
0029088389
-
Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES
-
Zondlo, J., K. E. Fisher, Z. Lin, K. R. Ducote, and E. Eisenstein. 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
-
13
-
-
0034489321
-
Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant
-
Guidry, J. J., C. K. Moczygemba, N. K. Steede, S. J. Landry, and P. Wittung-Stafshede. 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
-
14
-
-
0036399456
-
Low stability for monomeric human chaperonin protein 10: Interprotein interactions contribute majority of oligomer stability
-
Guidry, J. J., and P. Wittung-Stafshede. 2002. Low stability for monomeric human chaperonin protein 10: interprotein interactions contribute majority of oligomer stability. Arch. Biochem. Biophys. 405:280-282.
-
(2002)
Arch. Biochem. Biophys.
, vol.405
, pp. 280-282
-
-
Guidry, J.J.1
Wittung-Stafshede, P.2
-
15
-
-
0033588259
-
Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model
-
Higurashi, T., K. Nosaka, T. Mizobata, J. Nagai, and Y. Kawata. 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
-
16
-
-
1642422340
-
First characterization of co-chaperonin protein 10 from hyper-thermophilic Aquifex aeolicus
-
Guidry, J., and P. Wittung-Stafshede. 2004. First characterization of co-chaperonin protein 10 from hyper-thermophilic Aquifex aeolicus. Biochem. Biophys. Res. Commun. 317:176-180.
-
(2004)
Biochem. Biophys. Res. Commun.
, vol.317
, pp. 176-180
-
-
Guidry, J.1
Wittung-Stafshede, P.2
-
18
-
-
0031473847
-
SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
-
Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:2714-2723.
-
(1997)
Electrophoresis
, vol.18
, pp. 2714-2723
-
-
Guex, N.1
Peitsch, M.C.2
-
19
-
-
0042622380
-
SWISS-MODEL: An automated protein homology-modeling server
-
Schwede, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31:3381-3385.
-
(2003)
Nucleic Acids Res.
, vol.31
, pp. 3381-3385
-
-
Schwede, T.1
Kopp, J.2
Guex, N.3
Peitsch, M.C.4
-
20
-
-
11344283815
-
Crystal structure of the co-chaperonin Cpn10 from Thermus thermophilus HB8
-
Numoto, N., A. Kita, and K. Miki. 2005. Crystal structure of the co-chaperonin Cpn10 from Thermus thermophilus HB8. Proteins. 58: 498-500.
-
(2005)
Proteins
, vol.58
, pp. 498-500
-
-
Numoto, N.1
Kita, A.2
Miki, K.3
-
21
-
-
4143134164
-
Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
-
Shimamura, T., A. Koike-Takeshita, K. Yokoyama, R. Masui, N. Murai, M. Yoshida, H. Taguchi, and S. Iwata. 2004. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure (Cambridge.). 12:1471-1480.
-
(2004)
Structure (Cambridge.)
, vol.12
, pp. 1471-1480
-
-
Shimamura, T.1
Koike-Takeshita, A.2
Yokoyama, K.3
Masui, R.4
Murai, N.5
Yoshida, M.6
Taguchi, H.7
Iwata, S.8
-
22
-
-
0031563834
-
The structural stability of the co-chaperonin GroES
-
Boudker, O., M. J. Todd, and E. Freire. 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
-
23
-
-
13544250497
-
Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes
-
Abraham, T., R. N. Lewis, R. S. Hodges, and R. N. McElhaney. 2005. Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes. Biochemistry. 44:2103-2112.
-
(2005)
Biochemistry
, vol.44
, pp. 2103-2112
-
-
Abraham, T.1
Lewis, R.N.2
Hodges, R.S.3
McElhaney, R.N.4
-
24
-
-
0017884417
-
The hydrophobic effect and the organization of living matter
-
Tanford, C. 1978. The hydrophobic effect and the organization of living matter. Science. 200:1012-1018.
-
(1978)
Science
, vol.200
, pp. 1012-1018
-
-
Tanford, C.1
-
25
-
-
2942589210
-
Order changes within receptor systems upon ligand binding: Receptor tightening/oligomerisation and the interpretation of binding parameters
-
Williams, D. H., D. P. O'Brien, A. M. Sandercock, and E. Stephens. 2004. Order changes within receptor systems upon ligand binding: receptor tightening/oligomerisation and the interpretation of binding parameters. J. Mol. Biol. 340:373-383.
-
(2004)
J. Mol. Biol.
, vol.340
, pp. 373-383
-
-
Williams, D.H.1
O'Brien, D.P.2
Sandercock, A.M.3
Stephens, E.4
-
26
-
-
0032588346
-
Characterization of the dimer interface of transcription factor NFκB p50 homodimer
-
Sengchanthalangsy, L. L., S. Datta, D. B. Huang, E. Anderson, E. H. Braswell, and G. Ghosh. 1999. Characterization of the dimer interface of transcription factor NFκB p50 homodimer. J. Mol. Biol. 289:1029-1040.
-
(1999)
J. Mol. Biol.
, vol.289
, pp. 1029-1040
-
-
Sengchanthalangsy, L.L.1
Datta, S.2
Huang, D.B.3
Anderson, E.4
Braswell, E.H.5
Ghosh, G.6
-
27
-
-
0029080864
-
Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
-
Gomez, J., and E. Freire. 1995. Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252:337-350.
-
(1995)
J. Mol. Biol.
, vol.252
, pp. 337-350
-
-
Gomez, J.1
Freire, E.2
-
28
-
-
0029114703
-
The heat capacity of proteins
-
Gomez, J., V. J. Hilser, D. Xie, and E. Freire. 1995. The heat capacity of proteins. Proteins. 22:404-412.
-
(1995)
Proteins
, vol.22
, pp. 404-412
-
-
Gomez, J.1
Hilser, V.J.2
Xie, D.3
Freire, E.4
-
29
-
-
0030580089
-
Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors
-
Hilser, V. J., and E. Freire. 1996. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J. Mol. Biol. 262:756-772.
-
(1996)
J. Mol. Biol.
, vol.262
, pp. 756-772
-
-
Hilser, V.J.1
Freire, E.2
-
30
-
-
0029957505
-
The enthalpy change in protein folding and binding: Refinement of parameters for structure-based calculations
-
Hilser, V. J., J. Gomez, and E. Freire. 1996. The enthalpy change in protein folding and binding: refinement of parameters for structure-based calculations. Proteins. 26:123-133.
-
(1996)
Proteins
, vol.26
, pp. 123-133
-
-
Hilser, V.J.1
Gomez, J.2
Freire, E.3
-
31
-
-
0030905238
-
Structure-based thermodynamic analysis of HIV-1 protease inhibitors
-
Bardi, J. S., I. Luque, and E. Freire. 1997. Structure-based thermodynamic analysis of HIV-1 protease inhibitors. Biochemistry. 36: 6588-6596.
-
(1997)
Biochemistry
, vol.36
, pp. 6588-6596
-
-
Bardi, J.S.1
Luque, I.2
Freire, E.3
-
32
-
-
0028859431
-
Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures. Implications for its diverse biological activities
-
Fossati, G., P. Lucietto, P. Giuliani, A. R. Coates, S. Harding, H. Colfen, G. Legname, E. Chan, A. Zaliani, and P. Mascagni. 1995. Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures. Implications for its diverse biological activities. J. Biol. Chem. 270:26159-26167.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 26159-26167
-
-
Fossati, G.1
Lucietto, P.2
Giuliani, P.3
Coates, A.R.4
Harding, S.5
Colfen, H.6
Legname, G.7
Chan, E.8
Zaliani, A.9
Mascagni, P.10
|