-
1
-
-
79960652801
-
Molecular chaperones in protein folding and proteostasis
-
Hartl, F.U., Bracher, A., Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332 (2011).
-
(2011)
Nature
, vol.475
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
2
-
-
0032924953
-
Hsp90 & Co.: A holding for folding
-
Buchner, J. Hsp90 & Co.: a holding for folding. Trends Biochem. Sci. 24, 136-141 (1999).
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 136-141
-
-
Buchner, J.1
-
3
-
-
84874473589
-
Allostery in the Hsp70 chaperone proteins
-
Zuiderweg, E.R.P. et al. Allostery in the Hsp70 chaperone proteins. Top. Curr. Chem. 328, 99-153 (2013).
-
(2013)
Top. Curr. Chem.
, vol.328
, pp. 99-153
-
-
Zuiderweg, E.R.P.1
-
4
-
-
84878901297
-
Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
-
Priya, S., Sharma, S.K., Goloubinoff, P. Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. FEBS Lett. 587, 1981-1987 (2013).
-
(2013)
FEBS Lett.
, vol.587
, pp. 1981-1987
-
-
Priya, S.1
Sharma, S.K.2
Goloubinoff, P.3
-
5
-
-
84886412961
-
Chaperone machines for protein folding, unfolding and disaggregation
-
Saibil, H. Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Mol. Cell Biol. 14, 630-642 (2013).
-
(2013)
Nat. Rev. Mol. Cell Biol.
, vol.14
, pp. 630-642
-
-
Saibil, H.1
-
6
-
-
70350020881
-
Chaperonin-mediated protein folding: Using a central cavity to kinetically assist polypeptide chain folding
-
Horwich, A.L., Fenton, W.A. Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Q. Rev. Biophys. 42, 83-116 (2009).
-
(2009)
Q. Rev. Biophys.
, vol.42
, pp. 83-116
-
-
Horwich, A.L.1
Fenton, W.A.2
-
7
-
-
0027391629
-
Small heat shock proteins are molecular chaperones
-
Jakob, U., Gaestel, M., Engel, K., Buchner, J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520 (1993).
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 1517-1520
-
-
Jakob, U.1
Gaestel, M.2
Engel, K.3
Buchner, J.4
-
8
-
-
75749153007
-
Protein refolding by pH-triggered chaperone binding and release
-
Tapley, T.L., Franzmann, T.M., Chakraborty, S., Jakob, U., Bardwell, J.C.A. Protein refolding by pH-triggered chaperone binding and release. Proc. Natl. Acad. Sci. USA 107, 1071-1076 (2010).
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 1071-1076
-
-
Tapley, T.L.1
Franzmann, T.M.2
Chakraborty, S.3
Jakob, U.4
Bardwell, J.C.A.5
-
9
-
-
77953027489
-
Structure and function of the molecular chaperone Trigger Factor
-
Hoffmann, A., Bukau, B., Kramer, G. Structure and function of the molecular chaperone Trigger Factor. Biochim. Biophys. Acta 1803, 650-661 (2010).
-
(2010)
Biochim. Biophys. Acta
, vol.1803
, pp. 650-661
-
-
Hoffmann, A.1
Bukau, B.2
Kramer, G.3
-
10
-
-
79952363991
-
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy
-
Quan, S. et al. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat. Struct. Mol. Biol. 18, 262-269 (2011).
-
(2011)
Nat. Struct. Mol. Biol.
, vol.18
, pp. 262-269
-
-
Quan, S.1
-
11
-
-
84920516331
-
HdeB functions as an acid-protective chaperone in bacteria
-
Dahl, J.-U. et al. HdeB functions as an acid-protective chaperone in bacteria. J. Biol. Chem. 290, 65-75 (2015).
-
(2015)
J. Biol. Chem.
, vol.290
, pp. 65-75
-
-
Dahl, J.-U.1
-
12
-
-
67650685558
-
An integrated network approach identifies the isobutanol response network of Escherichia coli
-
Brynildsen, M.P., Liao, J.C. An integrated network approach identifies the isobutanol response network of Escherichia coli. Mol. Syst. Biol. 5, 277 (2009).
-
(2009)
Mol. Syst. Biol.
, vol.5
, pp. 277
-
-
Brynildsen, M.P.1
Liao, J.C.2
-
13
-
-
77749245785
-
Functional genomic study of exogenous n-butanol stress in Escherichia coli
-
Rutherford, B.J. et al. Functional genomic study of exogenous n-butanol stress in Escherichia coli. Appl. Environ. Microbiol. 76, 1935-1945 (2010).
-
(2010)
Appl. Environ. Microbiol.
, vol.76
, pp. 1935-1945
-
-
Rutherford, B.J.1
-
14
-
-
84898766164
-
Super Spy variants implicate flexibility in chaperone action
-
Quan, S. et al. Super Spy variants implicate flexibility in chaperone action. eLife 3, e01584 (2014).
-
(2014)
ELife
, vol.3
, pp. e01584
-
-
Quan, S.1
-
15
-
-
0033548553
-
Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
-
Ferguson, N., Capaldi, A.P., James, R., Kleanthous, C., Radford, S.E. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J. Mol. Biol. 286, 1597-1608 (1999).
-
(1999)
J. Mol. Biol.
, vol.286
, pp. 1597-1608
-
-
Ferguson, N.1
Capaldi, A.P.2
James, R.3
Kleanthous, C.4
Radford, S.E.5
-
16
-
-
0035170463
-
Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate
-
Capaldi, A.P., Shastry, M.C.R., Kleanthous, C., Roder, H., Radford, S.E. Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate. Nat. Struct. Biol. 8, 68-72 (2001).
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 68-72
-
-
Capaldi, A.P.1
Shastry, M.C.R.2
Kleanthous, C.3
Roder, H.4
Radford, S.E.5
-
17
-
-
0036183221
-
Im7 folding mechanism: Misfolding on a path to the native state
-
Capaldi, A.P., Kleanthous, C., Radford, S.E. Im7 folding mechanism: misfolding on a path to the native state. Nat. Struct. Biol. 9, 209-216 (2002).
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 209-216
-
-
Capaldi, A.P.1
Kleanthous, C.2
Radford, S.E.3
-
18
-
-
0037423705
-
Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: Similarities and differences in the folding of homologous proteins
-
Friel, C.T., Capaldi, A.P., Radford, S.E. Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293-305 (2003).
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 293-305
-
-
Friel, C.T.1
Capaldi, A.P.2
Radford, S.E.3
-
19
-
-
69749123006
-
Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7
-
Knowling, S.E., Figueiredo, A.M., Whittaker, S.B.M., Moore, G.R., Radford, S.E. Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7. J. Mol. Biol. 392, 1074-1086 (2009).
-
(2009)
J. Mol. Biol.
, vol.392
, pp. 1074-1086
-
-
Knowling, S.E.1
Figueiredo, A.M.2
Whittaker, S.B.M.3
Moore, G.R.4
Radford, S.E.5
-
20
-
-
62049084565
-
The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints
-
Friel, C.T., Smith, D.A., Vendruscolo, M., Gsponer, J., Radford, S.E. The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints. Nat. Struct. Mol. Biol. 16, 318-324 (2009).
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 318-324
-
-
Friel, C.T.1
Smith, D.A.2
Vendruscolo, M.3
Gsponer, J.4
Radford, S.E.5
-
21
-
-
4143080376
-
Trapping the on-pathway folding intermediate of Im7 at equilibrium
-
Spence, G.R., Capaldi, A.P., Radford, S.E. Trapping the on-pathway folding intermediate of Im7 at equilibrium. J. Mol. Biol. 341, 215-226 (2004).
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 215-226
-
-
Spence, G.R.1
Capaldi, A.P.2
Radford, S.E.3
-
22
-
-
30444450687
-
Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7
-
Gsponer, J. et al. Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proc. Natl. Acad. Sci. USA 103, 99-104 (2006).
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 99-104
-
-
Gsponer, J.1
-
23
-
-
33846577660
-
NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7
-
Whittaker, S.B.M., Spence, G.R., Günter Grossmann, J., Radford, S.E., Moore, G.R. NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. J. Mol. Biol. 366, 1001-1015 (2007).
-
(2007)
J. Mol. Biol.
, vol.366
, pp. 1001-1015
-
-
Whittaker, S.B.M.1
Spence, G.R.2
Günter Grossmann, J.3
Radford, S.E.4
Moore, G.R.5
-
24
-
-
84856430482
-
Conformational properties of the unfolded state of Im7 in nondenaturing conditions
-
Pashley, C.L. et al. Conformational properties of the unfolded state of Im7 in nondenaturing conditions. J. Mol. Biol. 416, 300-318 (2012).
-
(2012)
J. Mol. Biol.
, vol.416
, pp. 300-318
-
-
Pashley, C.L.1
-
25
-
-
84864462749
-
Conformational selection or induced fit A critical appraisal of the kinetic mechanism
-
Vogt, A.D., Di Cera, E. Conformational selection or induced fit A critical appraisal of the kinetic mechanism. Biochemistry 51, 5894-5902 (2012).
-
(2012)
Biochemistry
, vol.51
, pp. 5894-5902
-
-
Vogt, A.D.1
Di Cera, E.2
-
26
-
-
84898953700
-
Distinguishing induced fit from conformational selection
-
Gianni, S., Dogan, J., Jemth, P. Distinguishing induced fit from conformational selection. Biophys. Chem. 189, 33-39 (2014).
-
(2014)
Biophys. Chem.
, vol.189
, pp. 33-39
-
-
Gianni, S.1
Dogan, J.2
Jemth, P.3
-
27
-
-
60549105802
-
Global kinetic explorer: A new computer program for dynamic simulation and fitting of kinetic data
-
Johnson, K.A., Simpson, Z.B., Blom, T. Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 387, 20-29 (2009).
-
(2009)
Anal. Biochem.
, vol.387
, pp. 20-29
-
-
Johnson, K.A.1
Simpson, Z.B.2
Blom, T.3
-
28
-
-
33144467755
-
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
-
Jahn, T.R., Parker, M.J., Homans, S.W., Radford, S.E. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat. Struct. Mol. Biol. 13, 195-201 (2006).
-
(2006)
Nat. Struct. Mol. Biol.
, vol.13
, pp. 195-201
-
-
Jahn, T.R.1
Parker, M.J.2
Homans, S.W.3
Radford, S.E.4
-
29
-
-
84869439957
-
A pre-steady state kinetic analysis of the Y60W mutant of trans-3-chloroacrylic acid dehalogenase: Implications for the mechanism of the wild-type enzyme
-
Huddleston, J.P., Schroeder, G.K., Johnson, K.A., Whitman, C.P. A pre-steady state kinetic analysis of the Y60W mutant of trans-3-chloroacrylic acid dehalogenase: implications for the mechanism of the wild-type enzyme. Biochemistry 51, 9420-9435 (2012).
-
(2012)
Biochemistry
, vol.51
, pp. 9420-9435
-
-
Huddleston, J.P.1
Schroeder, G.K.2
Johnson, K.A.3
Whitman, C.P.4
-
30
-
-
84855697030
-
Reaction of cis-3-chloroacrylic acid dehalogenase with an allene substrate 2,3-butadienoate: Hydration via an enamine
-
Schroeder, G.K. et al. Reaction of cis-3-chloroacrylic acid dehalogenase with an allene substrate, 2,3-butadienoate: hydration via an enamine. J. Am. Chem. Soc. 134, 293-304 (2012).
-
(2012)
J. Am. Chem. Soc.
, vol.134
, pp. 293-304
-
-
Schroeder, G.K.1
-
31
-
-
0027179284
-
Refolding of barnase in the presence of GroE
-
Gray, T.E., Fersht, A.R. Refolding of barnase in the presence of GroE. J. Mol. Biol. 232, 1197-1207 (1993).
-
(1993)
J. Mol. Biol.
, vol.232
, pp. 1197-1207
-
-
Gray, T.E.1
Fersht, A.R.2
-
32
-
-
0029019467
-
The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding
-
Corrales, F.J., Fersht, A.R. The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding. Proc. Natl. Acad. Sci. USA 92, 5326-5330 (1995).
-
(1995)
Proc. Natl. Acad. Sci. USA
, vol.92
, pp. 5326-5330
-
-
Corrales, F.J.1
Fersht, A.R.2
-
33
-
-
84937468654
-
Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR
-
Libich, D.S., Tugarinov, V., Clore, G.M. Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Proc. Natl. Acad. Sci. USA 112, 8817-8823 (2015).
-
(2015)
Proc. Natl. Acad. Sci. USA
, vol.112
, pp. 8817-8823
-
-
Libich, D.S.1
Tugarinov, V.2
Clore, G.M.3
-
34
-
-
0032924105
-
Chaperone-mediated protein folding
-
Fink, A.L. Chaperone-mediated protein folding. Physiol. Rev. 79, 425-449 (1999).
-
(1999)
Physiol. Rev.
, vol.79
, pp. 425-449
-
-
Fink, A.L.1
-
35
-
-
0034329452
-
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
-
Young, J.C., Hartl, F.U. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19, 5930-5940 (2000).
-
(2000)
EMBO J.
, vol.19
, pp. 5930-5940
-
-
Young, J.C.1
Hartl, F.U.2
-
36
-
-
17044387386
-
Hsp70 chaperones: Cellular functions and molecular mechanism
-
Mayer, M.P., Bukau, B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684 (2005).
-
(2005)
Cell. Mol. Life Sci.
, vol.62
, pp. 670-684
-
-
Mayer, M.P.1
Bukau, B.2
-
37
-
-
33750000616
-
Folding on the chaperone: Yield enhancement through loose binding
-
Jewett, A.I., Shea, J.E. Folding on the chaperone: yield enhancement through loose binding. J. Mol. Biol. 363, 945-957 (2006).
-
(2006)
J. Mol. Biol.
, vol.363
, pp. 945-957
-
-
Jewett, A.I.1
Shea, J.E.2
|