-
1
-
-
2242480182
-
Kinetic analysis of R67 dihydrofolate reductase folding: From the unfolded monomer to the native tetramer
-
Bodenreider, C., Kellershohn, N., Goldberg, M.E., and Mejean, A. 2002. Kinetic analysis of R67 dihydrofolate reductase folding: From the unfolded monomer to the native tetramer. Biochemistry 41: 14988-14999.
-
(2002)
Biochemistry
, vol.41
, pp. 14988-14999
-
-
Bodenreider, C.1
Kellershohn, N.2
Goldberg, M.E.3
Mejean, A.4
-
2
-
-
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., and Horwich, A.L. 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
-
3
-
-
0034718449
-
SecA folds via a dimeric intermediate
-
Doyle, S.M., Braswell, E.H., and Teschke, C.M. 2000. SecA folds via a dimeric intermediate. Biochemistry 39: 11667-11676.
-
(2000)
Biochemistry
, vol.39
, pp. 11667-11676
-
-
Doyle, S.M.1
Braswell, E.H.2
Teschke, C.M.3
-
4
-
-
0032506048
-
Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate
-
Gloss, L.M. and Matthews, C.R. 1998. Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry 37: 15990-15999.
-
(1998)
Biochemistry
, vol.37
, pp. 15990-15999
-
-
Gloss, L.M.1
Matthews, C.R.2
-
5
-
-
0141959709
-
Importance of native-state topology for determining the folding rate of two-state proteins
-
Gromiha, M.M. 2003. Importance of native-state topology for determining the folding rate of two-state proteins. J. Chem. Inf. Comput. Sci. 43: 1481-1485.
-
(2003)
J. Chem. Inf. Comput. Sci.
, vol.43
, pp. 1481-1485
-
-
Gromiha, M.M.1
-
6
-
-
0035967862
-
Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction
-
Gromiha, M.M. and Selvaraj, S. 2001. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction. J. Mol. Biol. 310: 27-32.
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 27-32
-
-
Gromiha, M.M.1
Selvaraj, S.2
-
7
-
-
0034489321
-
Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant
-
Guidry, J., Moczygemba, C., Steede, K., Landry, S., and 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.1
Moczygemba, C.2
Steede, K.3
Landry, S.4
Wittung-Stafshede, P.5
-
8
-
-
0036399456
-
Low stability for monomeric human chaperonin protein 10: Interprotein interactions contribute majority of oligomer stability
-
Guidry, J.J. and Wittung-Stafshede, P. 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
-
9
-
-
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., and 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
-
10
-
-
0042510944
-
Contact order revisited: Influence of protein size on the folding rate
-
Ivankov, D.N., Garbuzynskiy, S.O., Alm, E., Plaxco, K.W., Baker, D., and Finkelstein, A.V. 2003. Contact order revisited: Influence of protein size on the folding rate. Protein Sci. 12: 2057-2062.
-
(2003)
Protein Sci.
, vol.12
, pp. 2057-2062
-
-
Ivankov, D.N.1
Garbuzynskiy, S.O.2
Alm, E.3
Plaxco, K.W.4
Baker, D.5
Finkelstein, A.V.6
-
11
-
-
0031815749
-
How do small single-domain proteins fold?
-
Jackson, S.E. 1998. How do small single-domain proteins fold? Fold. Des. 3: R81-R91.
-
(1998)
Fold. Des.
, vol.3
-
-
Jackson, S.E.1
-
12
-
-
0030028728
-
Principles of protein-protein interactions
-
Jones, S. and Thornton, J.M. 1996. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. 93: 13-20.
-
(1996)
Proc. Natl. Acad. Sci.
, vol.93
, pp. 13-20
-
-
Jones, S.1
Thornton, J.M.2
-
13
-
-
0041624356
-
The largest protein observed to fold by two-state kinetic mechanism does not obey contact-order correlation
-
Jones, K. and Wittung-Stafshede, P. 2003. The largest protein observed to fold by two-state kinetic mechanism does not obey contact-order correlation. J. Am. Chem. Soc. 125: 9606-9607.
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 9606-9607
-
-
Jones, K.1
Wittung-Stafshede, P.2
-
14
-
-
0242330738
-
The importance of explicit chain representation in protein folding models: An examination of lsing-like models
-
Karanicolas, J. and Brooks III, C.L. 2003. The importance of explicit chain representation in protein folding models: An examination of lsing-like models. Proteins 53: 740-747.
-
(2003)
Proteins
, vol.53
, pp. 740-747
-
-
Karanicolas, J.1
Brooks III, C.L.2
-
15
-
-
0042631521
-
Contact order dependent protein folding rates: Kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences
-
Kaya, H. and Chan, H.S. 2003. Contact order dependent protein folding rates: Kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences. Proteins 52: 524-533.
-
(2003)
Proteins
, vol.52
, pp. 524-533
-
-
Kaya, H.1
Chan, H.S.2
-
16
-
-
0030809754
-
Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10
-
Landry, S.J., Steede, N.K., and Maskos, K. 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
-
17
-
-
0345743709
-
Protein topology determines binding mechanism
-
Levy, Y., Wolynes, P.G., and Onuchic, J.N. 2004. Protein topology determines binding mechanism. Proc. Natl. Acad. Sci. 101: 511-516.
-
(2004)
Proc. Natl. Acad. Sci.
, vol.101
, pp. 511-516
-
-
Levy, Y.1
Wolynes, P.G.2
Onuchic, J.N.3
-
18
-
-
0037215268
-
The topomer search model: A simple, quantitative theory of two-state protein folding kinetics
-
Makarov, D.E. and Plaxco, K.W. 2003. The topomer search model: A simple, quantitative theory of two-state protein folding kinetics. Protein Sci. 12: 17-26.
-
(2003)
Protein Sci.
, vol.12
, pp. 17-26
-
-
Makarov, D.E.1
Plaxco, K.W.2
-
19
-
-
0028810468
-
Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase
-
Mann, C.J., Shao, X., and Matthews, C.R. 1995. Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry 34: 14573-14580.
-
(1995)
Biochemistry
, vol.34
, pp. 14573-14580
-
-
Mann, C.J.1
Shao, X.2
Matthews, C.R.3
-
20
-
-
0027427329
-
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES
-
Martin, J., Geromanos, S., Tempst, P., and Hartl, F.U. 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
-
21
-
-
0028325298
-
P22 Arc repressor: Folding kinetics of a single-domain, dimeric protein
-
Milla, M.E. and Sauer, R.T. 1994. P22 Arc repressor: Folding kinetics of a single-domain, dimeric protein. Biochemistry 33: 1125-1133.
-
(1994)
Biochemistry
, vol.33
, pp. 1125-1133
-
-
Milla, M.E.1
Sauer, R.T.2
-
22
-
-
0034708714
-
Heme orientation affects holo-myoglobin folding and unfolding kinetics
-
Moczygemba, C., Guidry, J., and Wittung-Stafshede, P. 2000. Heme orientation affects holo-myoglobin folding and unfolding kinetics. FEBS Lett. 470: 203-206.
-
(2000)
FEBS Lett.
, vol.470
, pp. 203-206
-
-
Moczygemba, C.1
Guidry, J.2
Wittung-Stafshede, P.3
-
23
-
-
0032500678
-
Folding and association of β-galactosidase
-
Nichtl, A., Buchner, J., Jaenicke, R., Rudolph, R., and Scheibel, T. 1998. Folding and association of β-galactosidase. J. Mol. Biol. 282: 1083-1091.
-
(1998)
J. Mol. Biol.
, vol.282
, pp. 1083-1091
-
-
Nichtl, A.1
Buchner, J.2
Jaenicke, R.3
Rudolph, R.4
Scheibel, T.5
-
24
-
-
0032503027
-
The changing nature of the protein folding transition state: Implications for the shape of the free-energy profile for folding
-
Oliveberg, M., Tan, Y.J., Silow, M., and Fersht, A.R. 1998. The changing nature of the protein folding transition state: Implications for the shape of the free-energy profile for folding. J. Mol. Biol. 277: 933-943.
-
(1998)
J. Mol. Biol.
, vol.277
, pp. 933-943
-
-
Oliveberg, M.1
Tan, Y.J.2
Silow, M.3
Fersht, A.R.4
-
25
-
-
0032502839
-
Contact order, transition state placement and the refolding rates of single domain proteins
-
Plaxco, K.W., Simons, K.T., and Baker, D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277: 985-994.
-
(1998)
J. Mol. Biol.
, vol.277
, pp. 985-994
-
-
Plaxco, K.W.1
Simons, K.T.2
Baker, D.3
-
26
-
-
0034687123
-
Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
-
Plaxco, K.W., Simons, K.T., Ruczinski, I., and David, B. 2000. Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics. Biochemistry 39: 11177-11183.
-
(2000)
Biochemistry
, vol.39
, pp. 11177-11183
-
-
Plaxco, K.W.1
Simons, K.T.2
Ruczinski, I.3
David, B.4
-
27
-
-
0033617534
-
Chaperonin function: Folding by forced unfolding
-
Shtilerman, M., Lorimer, G.H., and Englander, S.W. 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
-
28
-
-
0034682561
-
Evidence for partial secondary structure formation in the transition state for arc repressor refolding and dimerization
-
Srivastava, A.K. and Sauer, R.T. 2000. Evidence for partial secondary structure formation in the transition state for arc repressor refolding and dimerization. Biochemistry 39: 8308-8314.
-
(2000)
Biochemistry
, vol.39
, pp. 8308-8314
-
-
Srivastava, A.K.1
Sauer, R.T.2
-
29
-
-
0034570812
-
Preparation of recombinant human Hsp10
-
Steede, N.K., Guidry, J.J., and Landry, S.J. 2000. Preparation of recombinant human Hsp10. Methods Mol. Biol. 140: 145-151.
-
(2000)
Methods Mol. Biol.
, vol.140
, pp. 145-151
-
-
Steede, N.K.1
Guidry, J.J.2
Landry, S.J.3
-
30
-
-
0028815428
-
GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides
-
Todd, M.J., Boudkin, O., Freire, E., and Lorimer, G.H. 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
-
31
-
-
0029966342
-
Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
-
Waldburger, C.D., Jonsson, T., and Sauer, R.T. 1996. Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl. Acad. Sci. 93: 2629-2634.
-
(1996)
Proc. Natl. Acad. Sci.
, vol.93
, pp. 2629-2634
-
-
Waldburger, C.D.1
Jonsson, T.2
Sauer, R.T.3
-
32
-
-
0027241972
-
Refolding of luciferase subunits from urea and assembly of the active heterodimer: Evidence for folding intermediates that precede and follow the dimerization step on the pathway to the active form of the enzyme
-
Ziegler, M.M., Goldberg, M.E., Chaffotte, A.F., and Baldwin, T.O. 1993. Refolding of luciferase subunits from urea and assembly of the active heterodimer: Evidence for folding intermediates that precede and follow the dimerization step on the pathway to the active form of the enzyme. J. Biol. Chem. 268: 10760-10765.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 10760-10765
-
-
Ziegler, M.M.1
Goldberg, M.E.2
Chaffotte, A.F.3
Baldwin, T.O.4
|