-
1
-
-
0000505830
-
Reductive cleavage of disulfide bridges in ribonuclease
-
Sela M., White F.H., Anfinsen C.B. Reductive cleavage of disulfide bridges in ribonuclease. Science 1957, 125:691-692.
-
(1957)
Science
, vol.125
, pp. 691-692
-
-
Sela, M.1
White, F.H.2
Anfinsen, C.B.3
-
2
-
-
0000063331
-
Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease
-
White F.H. Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease. J. Biol. Chem. 1961, 236:1353-1360.
-
(1961)
J. Biol. Chem.
, vol.236
, pp. 1353-1360
-
-
White, F.H.1
-
3
-
-
74249107702
-
Assessment of CASP8 structure predictions for template free targets
-
Ben-David M., Noivirt-Brik O., Paz A., Prilusky J., Sussman J.L., Levy Y. Assessment of CASP8 structure predictions for template free targets. Proteins 2009, 77(Suppl. 9):50-65.
-
(2009)
Proteins
, vol.77
, Issue.SUPPL. 9
, pp. 50-65
-
-
Ben-David, M.1
Noivirt-Brik, O.2
Paz, A.3
Prilusky, J.4
Sussman, J.L.5
Levy, Y.6
-
4
-
-
33846498387
-
Thermodynamics of protein denatured states
-
Bowler B.E. Thermodynamics of protein denatured states. Mol. BioSyst. 2007, 3:88-99.
-
(2007)
Mol. BioSyst.
, vol.3
, pp. 88-99
-
-
Bowler, B.E.1
-
5
-
-
9344227330
-
Native and nonnative conformational preferences in the urea-unfolded state of barstar
-
Bhavesh N.S., Juneja J., Udgaonkar J.B., Hosur R.V. Native and nonnative conformational preferences in the urea-unfolded state of barstar. Protein Sci. 2004, 13:3085-3091.
-
(2004)
Protein Sci.
, vol.13
, pp. 3085-3091
-
-
Bhavesh, N.S.1
Juneja, J.2
Udgaonkar, J.B.3
Hosur, R.V.4
-
6
-
-
27144532135
-
Solution structure of a protein denatured state and folding intermediate
-
Religa T.L., Markson J.S., Mayor U., Freund S.M., Fersht A.R. Solution structure of a protein denatured state and folding intermediate. Nature 2005, 437:1053-1056.
-
(2005)
Nature
, vol.437
, pp. 1053-1056
-
-
Religa, T.L.1
Markson, J.S.2
Mayor, U.3
Freund, S.M.4
Fersht, A.R.5
-
7
-
-
66749176784
-
The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure
-
Shan B., Eliezer D., Raleigh D.P. The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry 2009, 48:4707-4719.
-
(2009)
Biochemistry
, vol.48
, pp. 4707-4719
-
-
Shan, B.1
Eliezer, D.2
Raleigh, D.P.3
-
8
-
-
0141861067
-
Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?
-
Uversky V.N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?. Cell. Mol. Life Sci. 2003, 60:1852-1871.
-
(2003)
Cell. Mol. Life Sci.
, vol.60
, pp. 1852-1871
-
-
Uversky, V.N.1
-
9
-
-
4344716256
-
Random-coil behavior and the dimensions of chemically unfolded proteins
-
Kohn J.E., Millett I.S., Jacob J., Zagrovic B., Dillon T.M., Cingel N., Dothager R.S., Seifert S., Thiyagarajan P., Sosnick T.R., Hasan M.Z., Pande V.S., Ruczinski I., Doniach S., Plaxco K.W. Random-coil behavior and the dimensions of chemically unfolded proteins. Proc. Natl. Acad. Sci. USA 2004, 101:12491-12496.
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 12491-12496
-
-
Kohn, J.E.1
Millett, I.S.2
Jacob, J.3
Zagrovic, B.4
Dillon, T.M.5
Cingel, N.6
Dothager, R.S.7
Seifert, S.8
Thiyagarajan, P.9
Sosnick, T.R.10
Hasan, M.Z.11
Pande, V.S.12
Ruczinski, I.13
Doniach, S.14
Plaxco, K.W.15
-
10
-
-
4344707281
-
Unfolded proteins and protein folding studied by NMR
-
Dyson H.J., Wright P.E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 2004, 104:3607-3622.
-
(2004)
Chem. Rev.
, vol.104
, pp. 3607-3622
-
-
Dyson, H.J.1
Wright, P.E.2
-
11
-
-
33747768414
-
Characterizing residual structure in disordered protein states using nuclear magnetic resonance
-
Eliezer D. Characterizing residual structure in disordered protein states using nuclear magnetic resonance. Methods Mol. Biol. 2007, 350:49-67.
-
(2007)
Methods Mol. Biol.
, vol.350
, pp. 49-67
-
-
Eliezer, D.1
-
12
-
-
0030296877
-
Urea-induced equilibrium unfolding of single tryptophan mutants of yeast phosphoglycerate kinase: Evidence for a stable intermediate
-
Szpikowska B.K., Mas M.T. Urea-induced equilibrium unfolding of single tryptophan mutants of yeast phosphoglycerate kinase: Evidence for a stable intermediate. Arch. Biochem. Biophys. 1996, 335:173-182.
-
(1996)
Arch. Biochem. Biophys.
, vol.335
, pp. 173-182
-
-
Szpikowska, B.K.1
Mas, M.T.2
-
13
-
-
0032880520
-
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein
-
Gualfetti P.J., Iwakura M., Lee J.C., Kihara H., Bilsel O., Zitzewitz J.A., Matthews C.R. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry 1999, 38:13367-13378.
-
(1999)
Biochemistry
, vol.38
, pp. 13367-13378
-
-
Gualfetti, P.J.1
Iwakura, M.2
Lee, J.C.3
Kihara, H.4
Bilsel, O.5
Zitzewitz, J.A.6
Matthews, C.R.7
-
14
-
-
0027772180
-
Urea-induced unfolding of the α subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration
-
Saab-Rincon G., Froebe C.L., Matthews C.R. Urea-induced unfolding of the α subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry 1993, 32:13981-13990.
-
(1993)
Biochemistry
, vol.32
, pp. 13981-13990
-
-
Saab-Rincon, G.1
Froebe, C.L.2
Matthews, C.R.3
-
15
-
-
0030070225
-
Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase
-
Saab-Rincon G., Gualfetti P.J., Matthews C.R. Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. Biochemistry 1996, 35:1988-1994.
-
(1996)
Biochemistry
, vol.35
, pp. 1988-1994
-
-
Saab-Rincon, G.1
Gualfetti, P.J.2
Matthews, C.R.3
-
16
-
-
0032813944
-
The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli
-
Gualfetti P.J., Bilsel O., Matthews C.R. The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Sci. 1999, 8:1623-1635.
-
(1999)
Protein Sci.
, vol.8
, pp. 1623-1635
-
-
Gualfetti, P.J.1
Bilsel, O.2
Matthews, C.R.3
-
17
-
-
0026719686
-
Global analysis of biochemical and biophysical data
-
Beechem J.M. Global analysis of biochemical and biophysical data. Methods Enzymol. 1992, 210:37-54.
-
(1992)
Methods Enzymol.
, vol.210
, pp. 37-54
-
-
Beechem, J.M.1
-
18
-
-
0141816814
-
Role of residual structure in the unfolded state of a thermophilic protein
-
Robic S., Guzman-Casado M., Sanchez-Ruiz J.M., Marqusee S. Role of residual structure in the unfolded state of a thermophilic protein. Proc. Natl. Acad. Sci. USA 2003, 100:11345-11349.
-
(2003)
Proc. Natl. Acad. Sci. USA
, vol.100
, pp. 11345-11349
-
-
Robic, S.1
Guzman-Casado, M.2
Sanchez-Ruiz, J.M.3
Marqusee, S.4
-
19
-
-
0036295079
-
Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H
-
Hollien J., Marqusee S. Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H. J. Mol. Biol. 2002, 316:327-340.
-
(2002)
J. Mol. Biol.
, vol.316
, pp. 327-340
-
-
Hollien, J.1
Marqusee, S.2
-
20
-
-
0026554928
-
Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution
-
Katayanagi K., Miyagawa M., Matsushima M., Ishikawa M., Kanaya S., Nakamura H., Ikehara M., Matsuzaki T., Morikawa K. Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution. J. Mol. Biol. 1992, 223:1029-1052.
-
(1992)
J. Mol. Biol.
, vol.223
, pp. 1029-1052
-
-
Katayanagi, K.1
Miyagawa, M.2
Matsushima, M.3
Ishikawa, M.4
Kanaya, S.5
Nakamura, H.6
Ikehara, M.7
Matsuzaki, T.8
Morikawa, K.9
-
21
-
-
0027246520
-
Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 A resolution
-
Ishikawa K., Okumura M., Katayanagi K., Kimura S., Kanaya S., Nakamura H., Morikawa K. Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 A resolution. J. Mol. Biol. 1993, 230:529-542.
-
(1993)
J. Mol. Biol.
, vol.230
, pp. 529-542
-
-
Ishikawa, K.1
Okumura, M.2
Katayanagi, K.3
Kimura, S.4
Kanaya, S.5
Nakamura, H.6
Morikawa, K.7
-
22
-
-
0028820703
-
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein folding
-
Myers J.K., Pace C.N., Scholtz J.M. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein folding. Protein Sci. 1995, 4:2138-2148.
-
(1995)
Protein Sci.
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
23
-
-
0036147997
-
Contributions of folding cores to the thermostabilities of two ribonucleases H
-
Robic S., Berger J.M., Marqusee S. Contributions of folding cores to the thermostabilities of two ribonucleases H. Protein Sci. 2002, 11:381-389.
-
(2002)
Protein Sci.
, vol.11
, pp. 381-389
-
-
Robic, S.1
Berger, J.M.2
Marqusee, S.3
-
24
-
-
0031663369
-
The green fluorescent protein
-
Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 1998, 67:509-544.
-
(1998)
Annu. Rev. Biochem.
, vol.67
, pp. 509-544
-
-
Tsien, R.Y.1
-
25
-
-
70349321624
-
The discovery and development of the green fluorescent protein, GFP
-
Sanders J.K., Jackson S.E. The discovery and development of the green fluorescent protein, GFP. Chem. Soc. Rev. 2009, 38:2821-2822.
-
(2009)
Chem. Soc. Rev.
, vol.38
, pp. 2821-2822
-
-
Sanders, J.K.1
Jackson, S.E.2
-
26
-
-
8344290520
-
Acid denaturation and refolding of green fluorescent protein
-
Enoki S., Saeki K., Maki K., Kuwajima K. Acid denaturation and refolding of green fluorescent protein. Biochemistry 2004, 43:14238-14248.
-
(2004)
Biochemistry
, vol.43
, pp. 14238-14248
-
-
Enoki, S.1
Saeki, K.2
Maki, K.3
Kuwajima, K.4
-
27
-
-
33746911626
-
The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein
-
Enoki S., Maki K., Inobe T., Takahashi K., Kamagata K., Oroguchi T., Nakatani H., Tomoyori K., Kuwajima K. The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein. J. Mol. Biol. 2006, 361:969-982.
-
(2006)
J. Mol. Biol.
, vol.361
, pp. 969-982
-
-
Enoki, S.1
Maki, K.2
Inobe, T.3
Takahashi, K.4
Kamagata, K.5
Oroguchi, T.6
Nakatani, H.7
Tomoyori, K.8
Kuwajima, K.9
-
28
-
-
33747801406
-
19F NMR studies of the native and denatured states of green fluorescent protein
-
Khan F., Kuprov I., Craggs T.D., Hore P.J., Jackson S.E. 19F NMR studies of the native and denatured states of green fluorescent protein. J. Am. Chem. Soc. 2006, 128:10729-10737.
-
(2006)
J. Am. Chem. Soc.
, vol.128
, pp. 10729-10737
-
-
Khan, F.1
Kuprov, I.2
Craggs, T.D.3
Hore, P.J.4
Jackson, S.E.5
-
29
-
-
70349347502
-
The extremely slow-exchanging core and acid-denatured state of green fluorescent protein
-
Huang J.R., Hsu S.T., Christodoulou J., Jackson S.E. The extremely slow-exchanging core and acid-denatured state of green fluorescent protein. HFSP J. 2008, 2:378-387.
-
(2008)
HFSP J.
, vol.2
, pp. 378-387
-
-
Huang, J.R.1
Hsu, S.T.2
Christodoulou, J.3
Jackson, S.E.4
-
30
-
-
0015920746
-
Stages in the mechanism of self-organization of protein molecules
-
Ptitsyn O.B. Stages in the mechanism of self-organization of protein molecules. Dokl. Akad. Nauk. SSSR 1973, 210:1213-1215.
-
(1973)
Dokl. Akad. Nauk. SSSR
, vol.210
, pp. 1213-1215
-
-
Ptitsyn, O.B.1
-
31
-
-
0021572887
-
Liquid-like state of side chains at the intermediate stage of protein denaturation
-
Ohgushi M., Wada A. Liquid-like state of side chains at the intermediate stage of protein denaturation. Adv. Biophys. 1984, 18:75-90.
-
(1984)
Adv. Biophys.
, vol.18
, pp. 75-90
-
-
Ohgushi, M.1
Wada, A.2
-
32
-
-
0025345415
-
Intermediates in the folding reactions of small proteins
-
Kim P.S., Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 1990, 59:631-660.
-
(1990)
Annu. Rev. Biochem.
, vol.59
, pp. 631-660
-
-
Kim, P.S.1
Baldwin, R.L.2
-
33
-
-
0001579510
-
-
Mechanisms of Protein Folding; Pain, R. H., Ed.; 2nd ed.; Oxford University Press: Oxford
-
Kuwajima, K.; Arai, M. The molten globule state: The physical picture and biological significance. In: Mechanisms of Protein Folding; Pain, R. H., Ed.; 2nd ed.; Oxford University Press: Oxford, 2000; pp 138-174.
-
(2000)
The molten globule state: The physical picture and biological significance
, pp. 138-174
-
-
Kuwajima, K.1
Arai, M.2
-
34
-
-
0030059690
-
The molten globule state of alpha-lactalbumin
-
Kuwajima K. The molten globule state of alpha-lactalbumin. FASEB J. 1996, 10:102-109.
-
(1996)
FASEB J.
, vol.10
, pp. 102-109
-
-
Kuwajima, K.1
-
35
-
-
70350524972
-
The human alpha-lactalbumin molten globule: Comparison of structural preferences at pH 2 and pH 7
-
Rosner H.I., Redfield C. The human alpha-lactalbumin molten globule: Comparison of structural preferences at pH 2 and pH 7. J. Mol. Biol. 2009, 394:351-362.
-
(2009)
J. Mol. Biol.
, vol.394
, pp. 351-362
-
-
Rosner, H.I.1
Redfield, C.2
-
36
-
-
0025186451
-
Structural characterization of a partly folded apomyoglobin intermediate
-
Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science 1990, 249:1544-1548.
-
(1990)
Science
, vol.249
, pp. 1544-1548
-
-
Hughson, F.M.1
Wright, P.E.2
Baldwin, R.L.3
-
39
-
-
0029917563
-
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface
-
Bychkova V.E., Dujsekina A.E., Klenin S.I., Tiktopulo E.I., Uversky V.N., Ptitsyn O.B. Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 1996, 35:6058-6063.
-
(1996)
Biochemistry
, vol.35
, pp. 6058-6063
-
-
Bychkova, V.E.1
Dujsekina, A.E.2
Klenin, S.I.3
Tiktopulo, E.I.4
Uversky, V.N.5
Ptitsyn, O.B.6
-
40
-
-
0029811784
-
Structure of the acid state of Escherichia coli ribonuclease HI
-
Dabora J.M., Pelton J.G., Marqusee S. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry 1996, 35:11951-11958.
-
(1996)
Biochemistry
, vol.35
, pp. 11951-11958
-
-
Dabora, J.M.1
Pelton, J.G.2
Marqusee, S.3
-
41
-
-
0025932041
-
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
-
van der Goot F.G., Gonzalez-Manas J.M., Lakey J.H., Pattus F. A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 1991, 354:408-410.
-
(1991)
Nature
, vol.354
, pp. 408-410
-
-
van der Goot, F.G.1
Gonzalez-Manas, J.M.2
Lakey, J.H.3
Pattus, F.4
-
42
-
-
0022397324
-
Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration
-
Blewitt M.G., Chung L.A., London E. Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration. Biochemistry 1985, 24:5458-5464.
-
(1985)
Biochemistry
, vol.24
, pp. 5458-5464
-
-
Blewitt, M.G.1
Chung, L.A.2
London, E.3
-
43
-
-
0037044842
-
Membrane protein insertion regulated by bringing electrostatic and hydrophobic interactions into play. A case study with the translocation domain of diphtheria toxin
-
Chenal A., Savarin P., Nizard P., Guillain F., Gillet D., Forge V. Membrane protein insertion regulated by bringing electrostatic and hydrophobic interactions into play. A case study with the translocation domain of diphtheria toxin. J. Biol. Chem. 2002, 277:43425-43432.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 43425-43432
-
-
Chenal, A.1
Savarin, P.2
Nizard, P.3
Guillain, F.4
Gillet, D.5
Forge, V.6
-
44
-
-
0035823118
-
Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules
-
Wijesinha-Bettoni R., Dobson C.M., Redfield C. Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules. J. Mol. Biol. 2001, 312:261-273.
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 261-273
-
-
Wijesinha-Bettoni, R.1
Dobson, C.M.2
Redfield, C.3
-
45
-
-
34247859221
-
Equilibrium and kinetics of the folding and unfolding of canine milk lysozyme
-
Nakatani H., Maki K., Saeki K., Aizawa T., Demura M., Kawano K., Tomoda S., Kuwajima K. Equilibrium and kinetics of the folding and unfolding of canine milk lysozyme. Biochemistry 2007, 46:5238-5251.
-
(2007)
Biochemistry
, vol.46
, pp. 5238-5251
-
-
Nakatani, H.1
Maki, K.2
Saeki, K.3
Aizawa, T.4
Demura, M.5
Kawano, K.6
Tomoda, S.7
Kuwajima, K.8
-
46
-
-
0029185844
-
Molten globules
-
Fink A.L. Molten globules. Methods Mol. Biol. 1995, 40:343-360.
-
(1995)
Methods Mol. Biol.
, vol.40
, pp. 343-360
-
-
Fink, A.L.1
-
47
-
-
37149049312
-
X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
-
Putnam C.D., Hammel M., Hura G.L., Tainer J.A. X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 2007, 40:191-285.
-
(2007)
Q. Rev. Biophys.
, vol.40
, pp. 191-285
-
-
Putnam, C.D.1
Hammel, M.2
Hura, G.L.3
Tainer, J.A.4
-
48
-
-
4644302181
-
NMR studies of partially folded molten-globule states
-
Redfield C. NMR studies of partially folded molten-globule states. Methods Mol. Biol. 2004, 278:233-254.
-
(2004)
Methods Mol. Biol.
, vol.278
, pp. 233-254
-
-
Redfield, C.1
-
49
-
-
3342993181
-
Hydrogen exchange methods to study protein folding
-
Krishna M.M., Hoang L., Lin Y., Englander S.W. Hydrogen exchange methods to study protein folding. Methods 2004, 34:51-64.
-
(2004)
Methods
, vol.34
, pp. 51-64
-
-
Krishna, M.M.1
Hoang, L.2
Lin, Y.3
Englander, S.W.4
-
50
-
-
0028061986
-
Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state
-
Dabora J.M., Marqusee S. Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state. Protein Sci. 1994, 3:1401-1408.
-
(1994)
Protein Sci.
, vol.3
, pp. 1401-1408
-
-
Dabora, J.M.1
Marqusee, S.2
-
51
-
-
42149137302
-
Carbonic anhydrases - An overview
-
Supuran C.T. Carbonic anhydrases - An overview. Curr. Pharm. Design 2008, 14:603-614.
-
(2008)
Curr. Pharm. Design
, vol.14
, pp. 603-614
-
-
Supuran, C.T.1
-
52
-
-
0027389744
-
Characterization of folding intermediates of human carbonic anhydrase II: Probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis
-
Martensson L.G., Jonsson B.H., Freskgard P.O., Kihlgren A., Svensson M., Carlsson U. Characterization of folding intermediates of human carbonic anhydrase II: Probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis. Biochemistry 1993, 32:224-231.
-
(1993)
Biochemistry
, vol.32
, pp. 224-231
-
-
Martensson, L.G.1
Jonsson, B.H.2
Freskgard, P.O.3
Kihlgren, A.4
Svensson, M.5
Carlsson, U.6
-
53
-
-
0030972636
-
Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis
-
Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S. Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis. Hum. Mutat. 1997, 9:383-387.
-
(1997)
Hum. Mutat.
, vol.9
, pp. 383-387
-
-
Hu, P.Y.1
Lim, E.J.2
Ciccolella, J.3
Strisciuglio, P.4
Sly, W.S.5
-
54
-
-
4344710278
-
Unfolding a folding disease: Folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II
-
Almstedt K., Lundqvist M., Carlsson J., Karlsson M., Persson B., Jonsson B.H., Carlsson U., Hammarstrom P. Unfolding a folding disease: Folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II. J. Mol. Biol. 2004, 342:619-633.
-
(2004)
J. Mol. Biol.
, vol.342
, pp. 619-633
-
-
Almstedt, K.1
Lundqvist, M.2
Carlsson, J.3
Karlsson, M.4
Persson, B.5
Jonsson, B.H.6
Carlsson, U.7
Hammarstrom, P.8
-
55
-
-
67049119436
-
Small-molecule suppression of misfolding of mutated human carbonic anhydrase II linked to marble brain disease
-
Almstedt K., Rafstedt T., Supuran C.T., Carlsson U., Hammarstrom P. Small-molecule suppression of misfolding of mutated human carbonic anhydrase II linked to marble brain disease. Biochemistry 2009, 48:5358-5364.
-
(2009)
Biochemistry
, vol.48
, pp. 5358-5364
-
-
Almstedt, K.1
Rafstedt, T.2
Supuran, C.T.3
Carlsson, U.4
Hammarstrom, P.5
-
56
-
-
0031033159
-
Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase
-
Webb T., Jackson P.J., Morris G.E. Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase. Biochem. J. 1997, 321(Pt. 1):83-88.
-
(1997)
Biochem. J.
, vol.321
, Issue.PT. 1
, pp. 83-88
-
-
Webb, T.1
Jackson, P.J.2
Morris, G.E.3
-
57
-
-
0037137182
-
From two-state to three-state: The effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation in an altered equilibrium denaturation mechanism
-
Hobart S.A., Meinhold D.W., Osuna R., Colon W. From two-state to three-state: The effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation in an altered equilibrium denaturation mechanism. Biochemistry 2002, 41:13744-13754.
-
(2002)
Biochemistry
, vol.41
, pp. 13744-13754
-
-
Hobart, S.A.1
Meinhold, D.W.2
Osuna, R.3
Colon, W.4
-
58
-
-
0034718450
-
A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI
-
Spudich G., Marqusee S. A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI. Biochemistry 2000, 39:11677-11683.
-
(2000)
Biochemistry
, vol.39
, pp. 11677-11683
-
-
Spudich, G.1
Marqusee, S.2
-
59
-
-
0037540410
-
Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase
-
Sanchez del Pino M.M., Fersht A.R. Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase. Biochemistry 1997, 36:5560-5565.
-
(1997)
Biochemistry
, vol.36
, pp. 5560-5565
-
-
Sanchez del Pino, M.M.1
Fersht, A.R.2
-
60
-
-
0036071577
-
Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: A test of the conservation of folding mechanisms hypothesis in (beta(alpha)) (8) barrels
-
Forsyth W.R., Matthews C.R. Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: A test of the conservation of folding mechanisms hypothesis in (beta(alpha)) (8) barrels. J. Mol. Biol. 2002, 320:1119-1133.
-
(2002)
J. Mol. Biol.
, vol.320
, pp. 1119-1133
-
-
Forsyth, W.R.1
Matthews, C.R.2
-
61
-
-
35548965931
-
Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Go model simulation
-
Gu Z., Rao M.K., Forsyth W.R., Finke J.M., Matthews C.R. Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Go model simulation. J. Mol. Biol. 2007, 374:528-546.
-
(2007)
J. Mol. Biol.
, vol.374
, pp. 528-546
-
-
Gu, Z.1
Rao, M.K.2
Forsyth, W.R.3
Finke, J.M.4
Matthews, C.R.5
-
62
-
-
34547680288
-
Topology and sequence in the folding of a TIM barrel protein: Global analysis highlights partitioning between transient off-pathway and stable on-pathway folding intermediates in the complex folding mechanism of a (βα)8 barrel of unknown function from B. subtilis
-
Forsyth W.R., Bilsel O., Gu Z., Matthews C.R. Topology and sequence in the folding of a TIM barrel protein: Global analysis highlights partitioning between transient off-pathway and stable on-pathway folding intermediates in the complex folding mechanism of a (βα)8 barrel of unknown function from B. subtilis. J. Mol. Biol. 2007, 372:236-253.
-
(2007)
J. Mol. Biol.
, vol.372
, pp. 236-253
-
-
Forsyth, W.R.1
Bilsel, O.2
Gu, Z.3
Matthews, C.R.4
-
63
-
-
34547111529
-
Pressure and denaturants in the unfolding of triosephosphate isomerase: The monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica
-
Vazquez-Perez A.R., Fernandez-Velasco D.A. Pressure and denaturants in the unfolding of triosephosphate isomerase: The monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica. Biochemistry 2007, 46:8624-8633.
-
(2007)
Biochemistry
, vol.46
, pp. 8624-8633
-
-
Vazquez-Perez, A.R.1
Fernandez-Velasco, D.A.2
-
64
-
-
0033060003
-
Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein
-
Zitzewitz J.A., Gualfetti P.J., Perkons I.A., Wasta S.A., Matthews C.R. Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. Protein Sci. 1999, 8:1200-1209.
-
(1999)
Protein Sci.
, vol.8
, pp. 1200-1209
-
-
Zitzewitz, J.A.1
Gualfetti, P.J.2
Perkons, I.A.3
Wasta, S.A.4
Matthews, C.R.5
-
65
-
-
0033520098
-
Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: An amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein
-
Zitzewitz J.A., Matthews C.R. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: An amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry 1999, 38:10205-10214.
-
(1999)
Biochemistry
, vol.38
, pp. 10205-10214
-
-
Zitzewitz, J.A.1
Matthews, C.R.2
-
66
-
-
4143057003
-
Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: Insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry
-
Rojsajjakul T., Wintrode P., Vadrevu R., Robert Matthews C., Smith D.L. Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: Insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry. J. Mol. Biol. 2004, 341:241-253.
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 241-253
-
-
Rojsajjakul, T.1
Wintrode, P.2
Vadrevu, R.3
Robert Matthews, C.4
Smith, D.L.5
-
67
-
-
39649117122
-
NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: Implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein
-
Vadrevu R., Wu Y., Matthews C.R. NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: Implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein. J. Mol. Biol. 2008, 377:294-306.
-
(2008)
J. Mol. Biol.
, vol.377
, pp. 294-306
-
-
Vadrevu, R.1
Wu, Y.2
Matthews, C.R.3
-
68
-
-
0031837168
-
Protein folding: Matching theory and experiment
-
Laurents D.V., Baldwin R.L. Protein folding: Matching theory and experiment. Biophys. J. 1998, 75:428-434.
-
(1998)
Biophys. J.
, vol.75
, pp. 428-434
-
-
Laurents, D.V.1
Baldwin, R.L.2
-
69
-
-
48249156678
-
The search for folding intermediates and the mechanism of protein folding
-
Baldwin R.L. The search for folding intermediates and the mechanism of protein folding. Annu. Rev. Biophys. 2008, 37:1-21.
-
(2008)
Annu. Rev. Biophys.
, vol.37
, pp. 1-21
-
-
Baldwin, R.L.1
-
70
-
-
0015597839
-
Nucleation, rapid folding, and globular intrachain regions in proteins
-
Wetlaufer D.B. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. USA 1973, 70:697-701.
-
(1973)
Proc. Natl. Acad. Sci. USA
, vol.70
, pp. 697-701
-
-
Wetlaufer, D.B.1
-
71
-
-
0037221599
-
Is there a unifying mechanism for protein folding?
-
Daggett V., Fersht A.R. Is there a unifying mechanism for protein folding?. Trends Biochem. Sci. 2003, 28:18-25.
-
(2003)
Trends Biochem. Sci.
, vol.28
, pp. 18-25
-
-
Daggett, V.1
Fersht, A.R.2
-
72
-
-
0020024242
-
Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
-
Kim P.S., Baldwin R.L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 1982, 51:459-489.
-
(1982)
Annu. Rev. Biochem.
, vol.51
, pp. 459-489
-
-
Kim, P.S.1
Baldwin, R.L.2
-
73
-
-
0033871781
-
Protein folding intermediates and pathways studied by hydrogen exchange
-
Englander S.W. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 2000, 29:213-238.
-
(2000)
Annu. Rev. Biophys. Biomol. Struct.
, vol.29
, pp. 213-238
-
-
Englander, S.W.1
-
74
-
-
2542599277
-
Phi-value analysis and the nature of protein-folding transition states
-
Fersht A.R., Sato S. Phi-value analysis and the nature of protein-folding transition states. Proc. Natl. Acad. Sci. USA 2004, 101:7976-7981.
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 7976-7981
-
-
Fersht, A.R.1
Sato, S.2
-
75
-
-
0031919973
-
Evidence for barrier-limited protein folding kinetics on the microsecond time scale
-
Shastry M.C., Roder H. Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nat. Struct. Biol. 1998, 5:385-392.
-
(1998)
Nat. Struct. Biol.
, vol.5
, pp. 385-392
-
-
Shastry, M.C.1
Roder, H.2
-
76
-
-
0031969090
-
A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale
-
Shastry M.C., Luck S.D., Roder H. A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophys. J. 1998, 74:2714-2721.
-
(1998)
Biophys. J.
, vol.74
, pp. 2714-2721
-
-
Shastry, M.C.1
Luck, S.D.2
Roder, H.3
-
77
-
-
0242610902
-
All-atom simulations of protein folding and unfolding
-
Day R., Daggett V. All-atom simulations of protein folding and unfolding. Adv. Protein Chem. 2003, 66:373-403.
-
(2003)
Adv. Protein Chem.
, vol.66
, pp. 373-403
-
-
Day, R.1
Daggett, V.2
-
78
-
-
0027313673
-
Pathways of protein folding
-
Matthews C.R. Pathways of protein folding. Annu. Rev. Biochem. 1993, 62:653-683.
-
(1993)
Annu. Rev. Biochem.
, vol.62
, pp. 653-683
-
-
Matthews, C.R.1
-
79
-
-
0028802181
-
Initial hydrophobic collapse in the folding of barstar
-
Agashe V.R., Shastry M.C., Udgaonkar J.B. Initial hydrophobic collapse in the folding of barstar. Nature 1995, 377:754-757.
-
(1995)
Nature
, vol.377
, pp. 754-757
-
-
Agashe, V.R.1
Shastry, M.C.2
Udgaonkar, J.B.3
-
80
-
-
0028944346
-
Is burst hydrophobic collapse necessary for protein folding?
-
Gutin A.M., Abkevich V.I., Shakhnovich E.I. Is burst hydrophobic collapse necessary for protein folding?. Biochemistry 1995, 34:3066-3076.
-
(1995)
Biochemistry
, vol.34
, pp. 3066-3076
-
-
Gutin, A.M.1
Abkevich, V.I.2
Shakhnovich, E.I.3
-
81
-
-
0025911762
-
How does protein synthesis give rise to the 3D-structure?
-
Ptitsyn O.B. How does protein synthesis give rise to the 3D-structure?. FEBS Lett. 1991, 285:176-181.
-
(1991)
FEBS Lett.
, vol.285
, pp. 176-181
-
-
Ptitsyn, O.B.1
-
82
-
-
0028327236
-
Protein folding dynamics: The diffusion-collision model and experimental data
-
Karplus M., Weaver D.L. Protein folding dynamics: The diffusion-collision model and experimental data. Protein Sci. 1994, 3:650-668.
-
(1994)
Protein Sci.
, vol.3
, pp. 650-668
-
-
Karplus, M.1
Weaver, D.L.2
-
83
-
-
0033080081
-
Is protein folding hierarchic? II. Folding intermediates and transition states
-
Baldwin R.L., Rose G.D. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 1999, 24:77-83.
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 77-83
-
-
Baldwin, R.L.1
Rose, G.D.2
-
84
-
-
0032972986
-
Is protein folding hierarchic? I. Local structure and peptide folding
-
Baldwin R.L., Rose G.D. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem. Sci. 1999, 24:26-33.
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 26-33
-
-
Baldwin, R.L.1
Rose, G.D.2
-
85
-
-
0037686252
-
The present view of the mechanism of protein folding
-
Daggett V., Fersht A. The present view of the mechanism of protein folding. Nat. Rev. Mol. Cell Biol. 2003, 4:497-502.
-
(2003)
Nat. Rev. Mol. Cell Biol.
, vol.4
, pp. 497-502
-
-
Daggett, V.1
Fersht, A.2
-
86
-
-
0031815749
-
How do small single-domain proteins fold?
-
Jackson S.E. How do small single-domain proteins fold?. Fold. Des. 1998, 3:R81-R91.
-
(1998)
Fold. Des.
, vol.3
-
-
Jackson, S.E.1
-
87
-
-
0030322669
-
Protein folding funnels: The nature of the transition state ensemble
-
Onuchic J.N., Socci N.D., Luthey-Schulten Z., Wolynes P.G. Protein folding funnels: The nature of the transition state ensemble. Fold. Des. 1996, 1:441-450.
-
(1996)
Fold. Des.
, vol.1
, pp. 441-450
-
-
Onuchic, J.N.1
Socci, N.D.2
Luthey-Schulten, Z.3
Wolynes, P.G.4
-
88
-
-
0032444334
-
Folding nucleus: Specific or multiple? Insights from lattice models and experiments
-
Shakhnovich EI. Folding nucleus: Specific or multiple? Insights from lattice models and experiments. Fold. Des. 1998, 3:R108-R111.
-
(1998)
Fold. Des.
, vol.3
-
-
Shakhnovich, E.I.1
-
89
-
-
0034685604
-
Topological and energetic factors: What determines the structural details of the transition state ensemble and 'en-route' intermediates for protein folding? An investigation for small globular proteins
-
Clementi C., Nymeyer H., Onuchic J.N. Topological and energetic factors: What determines the structural details of the transition state ensemble and 'en-route' intermediates for protein folding? An investigation for small globular proteins. J. Mol. Biol. 2000, 298:937-953.
-
(2000)
J. Mol. Biol.
, vol.298
, pp. 937-953
-
-
Clementi, C.1
Nymeyer, H.2
Onuchic, J.N.3
-
90
-
-
0035370662
-
Multiple protein folding nuclei and the transition state ensemble in two-state proteins
-
Klimov D.K., Thirumalai D. Multiple protein folding nuclei and the transition state ensemble in two-state proteins. Proteins 2001, 43:465-475.
-
(2001)
Proteins
, vol.43
, pp. 465-475
-
-
Klimov, D.K.1
Thirumalai, D.2
-
91
-
-
1842298212
-
From Levinthal to pathways to funnels
-
Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 1997, 4:10-19.
-
(1997)
Nat. Struct. Biol.
, vol.4
, pp. 10-19
-
-
Dill, K.A.1
Chan, H.S.2
-
92
-
-
0028947257
-
G Funnels, pathways, and the energy landscape of protein folding: A synthesis
-
Bryngelson J.D., Onuchic J.N., Socci N.D., Wolynes P. G Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 1995, 21:167-195.
-
(1995)
Proteins
, vol.21
, pp. 167-195
-
-
Bryngelson, J.D.1
Onuchic, J.N.2
Socci, N.D.3
Wolynes, P.4
-
95
-
-
14044275168
-
Symmetry and frustration in protein energy landscapes: A near degeneracy resolves the Rop dimer-folding mystery
-
Levy Y., Cho S.S., Shen T., Onuchic J.N., Wolynes P.G. Symmetry and frustration in protein energy landscapes: A near degeneracy resolves the Rop dimer-folding mystery. Proc. Natl. Acad. Sci. USA 2005, 102:2373-2378.
-
(2005)
Proc. Natl. Acad. Sci. USA
, vol.102
, pp. 2373-2378
-
-
Levy, Y.1
Cho, S.S.2
Shen, T.3
Onuchic, J.N.4
Wolynes, P.G.5
-
96
-
-
33847306593
-
A unified mechanism for protein folding: Predetermined pathways with optional errors
-
Krishna M.M., Englander S.W. A unified mechanism for protein folding: Predetermined pathways with optional errors. Protein Sci. 2007, 16:449-464.
-
(2007)
Protein Sci.
, vol.16
, pp. 449-464
-
-
Krishna, M.M.1
Englander, S.W.2
-
97
-
-
0037225280
-
Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
-
Sanchez I.E., Kiefhaber T. Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 2003, 325:367-376.
-
(2003)
J. Mol. Biol.
, vol.325
, pp. 367-376
-
-
Sanchez, I.E.1
Kiefhaber, T.2
-
98
-
-
0033535951
-
Intermediates can accelerate protein folding
-
Wagner C., Kiefhaber T. Intermediates can accelerate protein folding. Proc. Natl. Acad. Sci. USA 1999, 96:6716-6721.
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 6716-6721
-
-
Wagner, C.1
Kiefhaber, T.2
-
99
-
-
33846901901
-
Intermediates: Ubiquitous species on folding energy landscapes?
-
Brockwell D.J., Radford S.E. Intermediates: Ubiquitous species on folding energy landscapes?. Curr. Opin. Struct. Biol. 2007, 17:30-37.
-
(2007)
Curr. Opin. Struct. Biol.
, vol.17
, pp. 30-37
-
-
Brockwell, D.J.1
Radford, S.E.2
-
100
-
-
0037456298
-
The complete folding pathway of a protein from nanoseconds to microseconds
-
Mayor U., Guydosh N.R., Johnson C.M., Grossmann J.G., Sato S., Jas G.S., Freund S.M., Alonso D.O., Daggett V., Fersht A.R. The complete folding pathway of a protein from nanoseconds to microseconds. Nature 2003, 421:863-867.
-
(2003)
Nature
, vol.421
, pp. 863-867
-
-
Mayor, U.1
Guydosh, N.R.2
Johnson, C.M.3
Grossmann, J.G.4
Sato, S.5
Jas, G.S.6
Freund, S.M.7
Alonso, D.O.8
Daggett, V.9
Fersht, A.R.10
-
101
-
-
0141457507
-
The kinetic pathway of folding of barnase
-
Khan F., Chuang J.I., Gianni S., Fersht A.R. The kinetic pathway of folding of barnase. J. Mol. Biol. 2003, 333:169-186.
-
(2003)
J. Mol. Biol.
, vol.333
, pp. 169-186
-
-
Khan, F.1
Chuang, J.I.2
Gianni, S.3
Fersht, A.R.4
-
102
-
-
0033580679
-
Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots
-
Otzen D.E., Kristensen O., Proctor M., Oliveberg M. Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots. Biochemistry 1999, 38:6499-6511.
-
(1999)
Biochemistry
, vol.38
, pp. 6499-6511
-
-
Otzen, D.E.1
Kristensen, O.2
Proctor, M.3
Oliveberg, M.4
-
103
-
-
0033550298
-
The cooperativity of burst phase reactions explored
-
Parker M.J., Marqusee S. The cooperativity of burst phase reactions explored. J. Mol. Biol. 1999, 293:1195-1210.
-
(1999)
J. Mol. Biol.
, vol.293
, pp. 1195-1210
-
-
Parker, M.J.1
Marqusee, S.2
-
104
-
-
0027190920
-
Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding
-
Mann C.J., Matthews C.R. Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry 1993, 32:5282-5290.
-
(1993)
Biochemistry
, vol.32
, pp. 5282-5290
-
-
Mann, C.J.1
Matthews, C.R.2
-
105
-
-
0030961780
-
The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
-
Raschke T.M., Marqusee S. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat. Struct. Biol. 1997, 4:298-304.
-
(1997)
Nat. Struct. Biol.
, vol.4
, pp. 298-304
-
-
Raschke, T.M.1
Marqusee, S.2
-
106
-
-
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. 1999, 286:1597-1608.
-
(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
-
107
-
-
0033607209
-
Relationship between the native-state hydrogen exchange and the folding pathways of barnase
-
Chu R.A., Takei J., Barchi J.J., Bai Y. Relationship between the native-state hydrogen exchange and the folding pathways of barnase. Biochemistry 1999, 38:14119-14124.
-
(1999)
Biochemistry
, vol.38
, pp. 14119-14124
-
-
Chu, R.A.1
Takei, J.2
Barchi, J.J.3
Bai, Y.4
-
108
-
-
0034718547
-
Absence of stable intermediates on the folding pathway of barnase
-
Takei J., Chu R.A., Bai Y. Absence of stable intermediates on the folding pathway of barnase. Proc. Natl. Acad. Sci. USA 2000, 97:10796-10801.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 10796-10801
-
-
Takei, J.1
Chu, R.A.2
Bai, Y.3
-
109
-
-
0036303563
-
Lack of definable nucleation sites in the rate-limiting transition state of barnase under native conditions
-
Chu R.A., Bai Y. Lack of definable nucleation sites in the rate-limiting transition state of barnase under native conditions. J. Mol. Biol. 2002, 315:759-770.
-
(2002)
J. Mol. Biol.
, vol.315
, pp. 759-770
-
-
Chu, R.A.1
Bai, Y.2
-
110
-
-
1642307617
-
The folding pathway of barnase: The rate-limiting transition state and a hidden intermediate under native conditions
-
Vu N.D., Feng H., Bai Y. The folding pathway of barnase: The rate-limiting transition state and a hidden intermediate under native conditions. Biochemistry 2004, 43:3346-3356.
-
(2004)
Biochemistry
, vol.43
, pp. 3346-3356
-
-
Vu, N.D.1
Feng, H.2
Bai, Y.3
-
111
-
-
0034687686
-
A kinetically significant intermediate in the folding of barnase
-
Fersht A.R. A kinetically significant intermediate in the folding of barnase. Proc. Natl. Acad. Sci. USA 2000, 97:14121-14126.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 14121-14126
-
-
Fersht, A.R.1
-
112
-
-
0034628913
-
Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
-
Wong K.B., Clarke J., Bond C.J., Neira J.L., Freund S.M., Fersht A.R., Daggett V. Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J. Mol. Biol. 2000, 296:1257-1282.
-
(2000)
J. Mol. Biol.
, vol.296
, pp. 1257-1282
-
-
Wong, K.B.1
Clarke, J.2
Bond, C.J.3
Neira, J.L.4
Freund, S.M.5
Fersht, A.R.6
Daggett, V.7
-
113
-
-
0030844583
-
Ultrafast signals in protein folding and the polypeptide contracted state
-
Sosnick T.R., Shtilerman M.D., Mayne L., Englander S.W. Ultrafast signals in protein folding and the polypeptide contracted state. Proc. Natl. Acad. Sci. USA 1997, 94:8545-8550.
-
(1997)
Proc. Natl. Acad. Sci. USA
, vol.94
, pp. 8545-8550
-
-
Sosnick, T.R.1
Shtilerman, M.D.2
Mayne, L.3
Englander, S.W.4
-
114
-
-
0031697733
-
The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
-
Qi P.X., Sosnick T.R., Englander S.W. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nat. Struct. Biol. 1998, 5:882-884.
-
(1998)
Nat. Struct. Biol.
, vol.5
, pp. 882-884
-
-
Qi, P.X.1
Sosnick, T.R.2
Englander, S.W.3
-
115
-
-
69149110300
-
De Sancho, D. Exploiting the downhill folding regime via experiment
-
Munoz V., Sadqi M., Naganathan A.N. de Sancho, D. Exploiting the downhill folding regime via experiment. HFSP J. 2008, 2:342-353.
-
(2008)
HFSP J.
, vol.2
, pp. 342-353
-
-
Munoz, V.1
Sadqi, M.2
Naganathan, A.N.3
-
116
-
-
0142169165
-
Crystal structures of engrailed homeodomain mutants: Implications for stability and dynamics
-
Stollar E.J., Mayor U., Lovell S.C., Federici L., Freund S.M., Fersht A.R., Luisi B.F. Crystal structures of engrailed homeodomain mutants: Implications for stability and dynamics. J. Biol. Chem. 2003, 278:43699-43708.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 43699-43708
-
-
Stollar, E.J.1
Mayor, U.2
Lovell, S.C.3
Federici, L.4
Freund, S.M.5
Fersht, A.R.6
Luisi, B.F.7
-
117
-
-
0034610360
-
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
-
Mayor U., Johnson C.M., Daggett V., Fersht A.R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl. Acad. Sci. USA 2000, 97:13518-13522.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 13518-13522
-
-
Mayor, U.1
Johnson, C.M.2
Daggett, V.3
Fersht, A.R.4
-
118
-
-
0142185492
-
The denatured state of Engrailed homeodomain under denaturing and native conditions
-
Mayor U., Grossmann J.G., Foster N.W., Freund S.M., Fersht A.R. The denatured state of Engrailed homeodomain under denaturing and native conditions. J. Mol. Biol. 2003, 333:977-991.
-
(2003)
J. Mol. Biol.
, vol.333
, pp. 977-991
-
-
Mayor, U.1
Grossmann, J.G.2
Foster, N.W.3
Freund, S.M.4
Fersht, A.R.5
-
119
-
-
40049106475
-
Fluorescence resonance energy transfer analysis of the folding pathway of Engrailed homeodomain
-
Huang F., Settanni G., Fersht A.R. Fluorescence resonance energy transfer analysis of the folding pathway of Engrailed homeodomain. Protein Eng. Des. Sel. 2008, 21:131-146.
-
(2008)
Protein Eng. Des. Sel.
, vol.21
, pp. 131-146
-
-
Huang, F.1
Settanni, G.2
Fersht, A.R.3
-
120
-
-
0345255608
-
Unifying features in protein-folding mechanisms
-
Gianni S., Guydosh N.R., Khan F., Caldas T.D., Mayor U., White G.W., DeMarco M.L., Daggett V., Fersht A.R. Unifying features in protein-folding mechanisms. Proc. Natl. Acad. Sci. USA 2003, 100:13286-13291.
-
(2003)
Proc. Natl. Acad. Sci. USA
, vol.100
, pp. 13286-13291
-
-
Gianni, S.1
Guydosh, N.R.2
Khan, F.3
Caldas, T.D.4
Mayor, U.5
White, G.W.6
DeMarco, M.L.7
Daggett, V.8
Fersht, A.R.9
-
121
-
-
0031127043
-
Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
-
Munoz V., Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 1997, 41:495-509.
-
(1997)
Biopolymers
, vol.41
, pp. 495-509
-
-
Munoz, V.1
Serrano, L.2
-
122
-
-
0032539590
-
Molten globule unfolding monitored by hydrogen exchange in urea
-
Chamberlain A.K., Marqusee S. Molten globule unfolding monitored by hydrogen exchange in urea. Biochemistry 1998, 37:1736-1742.
-
(1998)
Biochemistry
, vol.37
, pp. 1736-1742
-
-
Chamberlain, A.K.1
Marqusee, S.2
-
123
-
-
0029746061
-
Detection of rare partially folded molecules in equilibrium with the native conformation of RNase H
-
Chamberlain A.K., Handel T.M., Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNase H. Nat. Struct. Biol. 1996, 9:782-787.
-
(1996)
Nat. Struct. Biol.
, vol.9
, pp. 782-787
-
-
Chamberlain, A.K.1
Handel, T.M.2
Marqusee, S.3
-
124
-
-
0347627528
-
Destabilization of the Escherichia coli RNase H kinetic intermediate: Switching between a two-state and three-state folding mechanism
-
Spudich G.M., Miller E.J., Marqusee S. Destabilization of the Escherichia coli RNase H kinetic intermediate: Switching between a two-state and three-state folding mechanism. J. Mol. Biol. 2004, 335:609-618.
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 609-618
-
-
Spudich, G.M.1
Miller, E.J.2
Marqusee, S.3
-
125
-
-
67650667409
-
The folding trajectory of RNase H is dominated by its topology and not local stability: A protein engineering study of variants that fold via two-state and three-state mechanisms
-
Connell K.B., Miller E.J., Marqusee S. The folding trajectory of RNase H is dominated by its topology and not local stability: A protein engineering study of variants that fold via two-state and three-state mechanisms. J. Mol. Biol. 2009, 391:450-460.
-
(2009)
J. Mol. Biol.
, vol.391
, pp. 450-460
-
-
Connell, K.B.1
Miller, E.J.2
Marqusee, S.3
-
126
-
-
67650656650
-
A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble
-
Connell K.B., Horner G.A., Marqusee S. A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble. J. Mol. Biol. 2009, 391:461-470.
-
(2009)
J. Mol. Biol.
, vol.391
, pp. 461-470
-
-
Connell, K.B.1
Horner, G.A.2
Marqusee, S.3
-
127
-
-
0029643523
-
Protein folding intermediates: Native-state hydrogen exchange
-
Bai Y., Sosnick T.R., Mayne L., Englander S.W. Protein folding intermediates: Native-state hydrogen exchange. Science 1995, 269:192-197.
-
(1995)
Science
, vol.269
, pp. 192-197
-
-
Bai, Y.1
Sosnick, T.R.2
Mayne, L.3
Englander, S.W.4
-
130
-
-
0037126070
-
Cytochrome c folding pathway: Kinetic native-state hydrogen exchange
-
Hoang L., Bedard S., Krishna M.M., Lin Y., Englander S.W. Cytochrome c folding pathway: Kinetic native-state hydrogen exchange. Proc. Natl. Acad. Sci. USA 2002, 99:12173-12178.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 12173-12178
-
-
Hoang, L.1
Bedard, S.2
Krishna, M.M.3
Lin, Y.4
Englander, S.W.5
-
131
-
-
0032884925
-
Confirmation of the hierarchical folding of RNase H: A protein engineering study
-
Raschke T.M., Kho J., Marqusee S. Confirmation of the hierarchical folding of RNase H: A protein engineering study. Nat. Struct. Biol. 1999, 6:825-831.
-
(1999)
Nat. Struct. Biol.
, vol.6
, pp. 825-831
-
-
Raschke, T.M.1
Kho, J.2
Marqusee, S.3
-
132
-
-
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. 2004, 341:215-226.
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 215-226
-
-
Spence, G.R.1
Capaldi, A.P.2
Radford, S.E.3
-
133
-
-
6344291152
-
Detection and structure determination of an equilibrium unfolding intermediate of Rd-apocytochrome b562: Native fold with non-native hydrophobic interactions
-
Feng H., Vu N.D., Bai Y. Detection and structure determination of an equilibrium unfolding intermediate of Rd-apocytochrome b562: Native fold with non-native hydrophobic interactions. J. Mol. Biol. 2004, 343:1477-1485.
-
(2004)
J. Mol. Biol.
, vol.343
, pp. 1477-1485
-
-
Feng, H.1
Vu, N.D.2
Bai, Y.3
-
134
-
-
12344311123
-
Detection of a hidden folding intermediate of the third domain of PDZ
-
Feng H., Vu N.D., Bai Y. Detection of a hidden folding intermediate of the third domain of PDZ. J. Mol. Biol. 2005, 346:345-353.
-
(2005)
J. Mol. Biol.
, vol.346
, pp. 345-353
-
-
Feng, H.1
Vu, N.D.2
Bai, Y.3
-
135
-
-
0035170463
-
Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate
-
Capaldi A.P., Shastry M.C., Kleanthous C., Roder H., Radford S.E. Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate. Nat. Struct. Biol. 2001, 8:68-72.
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 68-72
-
-
Capaldi, A.P.1
Shastry, M.C.2
Kleanthous, C.3
Roder, H.4
Radford, S.E.5
-
136
-
-
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. 2002, 9:209-216.
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 209-216
-
-
Capaldi, A.P.1
Kleanthous, C.2
Radford, S.E.3
-
137
-
-
1442351134
-
Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7
-
Gorski S.A., Le Duff C.S., Capaldi A.P., Kalverda A.P., Beddard G.S., Moore G.R., Radford S.E. Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7. J. Mol. Biol. 2004, 337:183-193.
-
(2004)
J. Mol. Biol.
, vol.337
, pp. 183-193
-
-
Gorski, S.A.1
Le Duff, C.S.2
Capaldi, A.P.3
Kalverda, A.P.4
Beddard, G.S.5
Moore, G.R.6
Radford, S.E.7
-
138
-
-
30444450687
-
Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7
-
Gsponer J., Hopearuoho H., Whittaker S.B., Spence G.R., Moore G.R., Paci E., Radford S.E., Vendruscolo M. Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proc. Natl. Acad. Sci. USA 2006, 103:99-104.
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 99-104
-
-
Gsponer, J.1
Hopearuoho, H.2
Whittaker, S.B.3
Spence, G.R.4
Moore, G.R.5
Paci, E.6
Radford, S.E.7
Vendruscolo, M.8
-
139
-
-
33846577660
-
NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7
-
Whittaker S.B., Spence G.R., Gunter 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. 2007, 366:1001-1015.
-
(2007)
J. Mol. Biol.
, vol.366
, pp. 1001-1015
-
-
Whittaker, S.B.1
Spence, G.R.2
Gunter Grossmann, J.3
Radford, S.E.4
Moore, G.R.5
-
140
-
-
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. 2003, 326:293-305.
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 293-305
-
-
Friel, C.T.1
Capaldi, A.P.2
Radford, S.E.3
-
141
-
-
0035965128
-
Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9
-
Gorski S.A., Capaldi A.P., Kleanthous C., Radford S.E. Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9. J. Mol. Biol. 2001, 312:849-863.
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 849-863
-
-
Gorski, S.A.1
Capaldi, A.P.2
Kleanthous, C.3
Radford, S.E.4
-
142
-
-
4143061715
-
Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design
-
Friel C.T., Beddard G.S., Radford S.E. Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design. J. Mol. Biol. 2004, 342:261-273.
-
(2004)
J. Mol. Biol.
, vol.342
, pp. 261-273
-
-
Friel, C.T.1
Beddard, G.S.2
Radford, S.E.3
-
143
-
-
34447261443
-
The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9
-
Morton V.L., Friel C.T., Allen L.R., Paci E., Radford S.E. The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9. J. Mol. Biol. 2007, 371:554-568.
-
(2007)
J. Mol. Biol.
, vol.371
, pp. 554-568
-
-
Morton, V.L.1
Friel, C.T.2
Allen, L.R.3
Paci, E.4
Radford, S.E.5
-
144
-
-
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. 2009, 16:318-324.
-
(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
-
145
-
-
38049140954
-
Consequences of localized frustration for the folding mechanism of the IM7 protein
-
Sutto L., Latzer J., Hegler J.A., Ferreiro D.U., Wolynes P.G. Consequences of localized frustration for the folding mechanism of the IM7 protein. Proc. Natl. Acad. Sci. USA 2007, 104:19825-19830.
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 19825-19830
-
-
Sutto, L.1
Latzer, J.2
Hegler, J.A.3
Ferreiro, D.U.4
Wolynes, P.G.5
-
146
-
-
0033616632
-
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time
-
Bilsel O., Yang L., Zitzewitz J.A., Beechem J.M., Matthews C.R. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry 1999, 38:4177-4187.
-
(1999)
Biochemistry
, vol.38
, pp. 4177-4187
-
-
Bilsel, O.1
Yang, L.2
Zitzewitz, J.A.3
Beechem, J.M.4
Matthews, C.R.5
-
147
-
-
0033579862
-
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels
-
Bilsel O., Zitzewitz J.A., Bowers K.E., Matthews C.R. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry 1999, 38:1018-1029.
-
(1999)
Biochemistry
, vol.38
, pp. 1018-1029
-
-
Bilsel, O.1
Zitzewitz, J.A.2
Bowers, K.E.3
Matthews, C.R.4
-
148
-
-
0028227296
-
Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
-
Itzhaki L.S., Evans P.A., Dobson C.M., Radford S.E. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes. Biochemistry 1994, 33:5212-5220.
-
(1994)
Biochemistry
, vol.33
, pp. 5212-5220
-
-
Itzhaki, L.S.1
Evans, P.A.2
Dobson, C.M.3
Radford, S.E.4
-
149
-
-
0034622508
-
Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles
-
Ionescu R.M., Smith V.F., O'Neill J.C., Matthews C.R. Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry 2000, 39:9540-9550.
-
(2000)
Biochemistry
, vol.39
, pp. 9540-9550
-
-
Ionescu, R.M.1
Smith, V.F.2
O'Neill, J.C.3
Matthews, C.R.4
-
150
-
-
0027315969
-
A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
-
Jennings P.A., Finn B.E., Jones B.E., Matthews C.R. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model. Biochemistry 1993, 32:3783-3789.
-
(1993)
Biochemistry
, vol.32
, pp. 3783-3789
-
-
Jennings, P.A.1
Finn, B.E.2
Jones, B.E.3
Matthews, C.R.4
-
151
-
-
0036289101
-
Highly divergent dihydrofolate reductases conserve complex folding mechanisms
-
Wallace L.A., Matthews C.R. Highly divergent dihydrofolate reductases conserve complex folding mechanisms. J. Mol. Biol. 2002, 315:193-211.
-
(2002)
J. Mol. Biol.
, vol.315
, pp. 193-211
-
-
Wallace, L.A.1
Matthews, C.R.2
-
152
-
-
0026005997
-
Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
-
Kuwajima K., Garvey E.P., Finn B.E., Matthews C.R., Sugai S. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 1991, 30:7693-7703.
-
(1991)
Biochemistry
, vol.30
, pp. 7693-7703
-
-
Kuwajima, K.1
Garvey, E.P.2
Finn, B.E.3
Matthews, C.R.4
Sugai, S.5
-
153
-
-
39149125451
-
Kinetic folding of Haloferax volcanii and Escherichia coli dihydrofolate reductases: Haloadaptation by unfolded state destabilization at high ionic strength
-
Gloss L.M., Topping T.B., Binder A.K., Lohman J.R. Kinetic folding of Haloferax volcanii and Escherichia coli dihydrofolate reductases: Haloadaptation by unfolded state destabilization at high ionic strength. J. Mol. Biol. 2008, 376:1451-1462.
-
(2008)
J. Mol. Biol.
, vol.376
, pp. 1451-1462
-
-
Gloss, L.M.1
Topping, T.B.2
Binder, A.K.3
Lohman, J.R.4
-
154
-
-
0028947956
-
Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
-
Jones B.E., Matthews C.R. Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci. 1995, 4:167-177.
-
(1995)
Protein Sci.
, vol.4
, pp. 167-177
-
-
Jones, B.E.1
Matthews, C.R.2
-
155
-
-
0024784280
-
A hydrophobic cluster forms early in the folding of dihydrofolate reductase
-
Garvey E.P., Swank J., Matthews C.R. A hydrophobic cluster forms early in the folding of dihydrofolate reductase. Proteins 1989, 6:259-266.
-
(1989)
Proteins
, vol.6
, pp. 259-266
-
-
Garvey, E.P.1
Swank, J.2
Matthews, C.R.3
-
156
-
-
0021872251
-
Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase
-
Penner M.H., Frieden C. Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase. J. Biol. Chem. 1985, 260:5366-5369.
-
(1985)
J. Biol. Chem.
, vol.260
, pp. 5366-5369
-
-
Penner, M.H.1
Frieden, C.2
-
158
-
-
73649087901
-
Folding of tetrameric p53: Oligomerization and tumorigenic mutations induce misfolding and loss of function
-
Lubin D.J., Butler J.S., Loh S.N. Folding of tetrameric p53: Oligomerization and tumorigenic mutations induce misfolding and loss of function. J. Mol. Biol. 2010, 395:705-716.
-
(2010)
J. Mol. Biol.
, vol.395
, pp. 705-716
-
-
Lubin, D.J.1
Butler, J.S.2
Loh, S.N.3
-
159
-
-
0038661090
-
Equilibrium folding of the core histones: The H3-H4 tetramer is less stable than the H2A-H2B dimer
-
Banks D.D., Gloss L.M. Equilibrium folding of the core histones: The H3-H4 tetramer is less stable than the H2A-H2B dimer. Biochemistry 2003, 42:6827-6839.
-
(2003)
Biochemistry
, vol.42
, pp. 6827-6839
-
-
Banks, D.D.1
Gloss, L.M.2
-
160
-
-
0030874395
-
Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: Equilibria with high kinetic barriers
-
Lai Z., McCulloch J., Lashuel H.A., Kelly J.W. Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: Equilibria with high kinetic barriers. Biochemistry 1997, 36:10230-10239.
-
(1997)
Biochemistry
, vol.36
, pp. 10230-10239
-
-
Lai, Z.1
McCulloch, J.2
Lashuel, H.A.3
Kelly, J.W.4
-
161
-
-
50049085496
-
Conformational stability and folding mechanisms of dimeric proteins
-
Rumfeldt J.A., Galvagnion C., Vassall K.A., Meiering E.M. Conformational stability and folding mechanisms of dimeric proteins. Prog. Biophys. Mol. Biol. 2008, 98:61-84.
-
(2008)
Prog. Biophys. Mol. Biol.
, vol.98
, pp. 61-84
-
-
Rumfeldt, J.A.1
Galvagnion, C.2
Vassall, K.A.3
Meiering, E.M.4
-
162
-
-
61849169556
-
Practical approaches to protein folding and assembly: Spectroscopic strategies in thermodynamics and kinetics
-
Walters J., Milam S.L., Clark A.C. Practical approaches to protein folding and assembly: Spectroscopic strategies in thermodynamics and kinetics. Methods Enzymol. 2009, 455:1-39.
-
(2009)
Methods Enzymol.
, vol.455
, pp. 1-39
-
-
Walters, J.1
Milam, S.L.2
Clark, A.C.3
-
163
-
-
80053413229
-
Equilibrium and kinetic approaches for studying oligomeric protein folding
-
Gloss L.M. Equilibrium and kinetic approaches for studying oligomeric protein folding. Methods Enzymol. 2009, 466:326-358.
-
(2009)
Methods Enzymol.
, vol.466
, pp. 326-358
-
-
Gloss, L.M.1
-
164
-
-
0036369436
-
Contact system. New concepts on activation mechanisms and bioregulatory functions
-
Yarovaya G.A., Blokhina T.B., Neshkova E.A. Contact system. New concepts on activation mechanisms and bioregulatory functions. Biochemistry (Moscow) 2002, 67:13-24.
-
(2002)
Biochemistry (Moscow)
, vol.67
, pp. 13-24
-
-
Yarovaya, G.A.1
Blokhina, T.B.2
Neshkova, E.A.3
-
165
-
-
33744927154
-
Crystal structure of the factor XI zymogen reveals a pathway for transactivation
-
Papagrigoriou E., McEwan P.A., Walsh P.N., Emsley J. Crystal structure of the factor XI zymogen reveals a pathway for transactivation. Nat. Struct. Mol. Biol. 2006, 13:557-558.
-
(2006)
Nat. Struct. Mol. Biol.
, vol.13
, pp. 557-558
-
-
Papagrigoriou, E.1
McEwan, P.A.2
Walsh, P.N.3
Emsley, J.4
-
166
-
-
0035874505
-
Model for a factor IX activation complex on blood platelets: Dimeric conformation of factor XIa is essential
-
Gailani D., Ho D., Sun M.F., Cheng Q., Walsh P.N. Model for a factor IX activation complex on blood platelets: Dimeric conformation of factor XIa is essential. Blood 2001, 97:3117-3122.
-
(2001)
Blood
, vol.97
, pp. 3117-3122
-
-
Gailani, D.1
Ho, D.2
Sun, M.F.3
Cheng, Q.4
Walsh, P.N.5
-
167
-
-
33847118925
-
Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: Spectroscopic and mutational analysis
-
Riley P.W., Cheng H., Samuel D., Roder H., Walsh P.N. Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: Spectroscopic and mutational analysis. J. Mol. Biol. 2007, 367:558-573.
-
(2007)
J. Mol. Biol.
, vol.367
, pp. 558-573
-
-
Riley, P.W.1
Cheng, H.2
Samuel, D.3
Roder, H.4
Walsh, P.N.5
-
168
-
-
0026606348
-
Expression of human blood coagulation factor XI: Characterization of the defect in factor XI type III deficiency
-
Meijers J.C., Davie E.W., Chung D.W. Expression of human blood coagulation factor XI: Characterization of the defect in factor XI type III deficiency. Blood 1992, 79:1435-1440.
-
(1992)
Blood
, vol.79
, pp. 1435-1440
-
-
Meijers, J.C.1
Davie, E.W.2
Chung, D.W.3
-
169
-
-
0034710671
-
A deeply knotted protein structure and how it might fold
-
Taylor W.R. A deeply knotted protein structure and how it might fold. Nature 2000, 406:916-919.
-
(2000)
Nature
, vol.406
, pp. 916-919
-
-
Taylor, W.R.1
-
170
-
-
33846362515
-
A comparison of the folding of two knotted proteins: YbeA and YibK
-
Mallam A.L., Jackson S.E. A comparison of the folding of two knotted proteins: YbeA and YibK. J. Mol. Biol. 2007, 366:650-665.
-
(2007)
J. Mol. Biol.
, vol.366
, pp. 650-665
-
-
Mallam, A.L.1
Jackson, S.E.2
-
171
-
-
0037375572
-
Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): A cofactor bound at a site formed by a knot
-
Lim K., Zhang H., Tempczyk A., Krajewski W., Bonander N., Toedt J., Howard A., Eisenstein E., Herzberg O. Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): A cofactor bound at a site formed by a knot. Proteins 2003, 51:56-67.
-
(2003)
Proteins
, vol.51
, pp. 56-67
-
-
Lim, K.1
Zhang, H.2
Tempczyk, A.3
Krajewski, W.4
Bonander, N.5
Toedt, J.6
Howard, A.7
Eisenstein, E.8
Herzberg, O.9
-
172
-
-
13844255609
-
Folding studies on a knotted protein
-
Mallam A.L., Jackson S.E. Folding studies on a knotted protein. J. Mol. Biol. 2005, 346:1409-1421.
-
(2005)
J. Mol. Biol.
, vol.346
, pp. 1409-1421
-
-
Mallam, A.L.1
Jackson, S.E.2
-
173
-
-
33745163582
-
Probing nature's knots: The folding pathway of a knotted homodimeric protein
-
Mallam A.L., Jackson S.E. Probing nature's knots: The folding pathway of a knotted homodimeric protein. J. Mol. Biol. 2006, 359:1420-1436.
-
(2006)
J. Mol. Biol.
, vol.359
, pp. 1420-1436
-
-
Mallam, A.L.1
Jackson, S.E.2
-
174
-
-
33846090298
-
Tying the knot that binds
-
Gloss L.M. Tying the knot that binds. Structure 2007, 15:2-4.
-
(2007)
Structure
, vol.15
, pp. 2-4
-
-
Gloss, L.M.1
-
175
-
-
0035812633
-
Rough energy landscapes in protein folding: Dimeric E. coli Trp repressor folds through three parallel channels
-
Gloss L.M., Simler B.R., Matthews C.R. Rough energy landscapes in protein folding: Dimeric E. coli Trp repressor folds through three parallel channels. J. Mol. Biol. 2001, 312:1121-1134.
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 1121-1134
-
-
Gloss, L.M.1
Simler, B.R.2
Matthews, C.R.3
-
176
-
-
33846099591
-
The dimerization of an α/β knotted protein is essential for structure and function
-
Mallam A.L., Jackson S.E. The dimerization of an α/β knotted protein is essential for structure and function. Structure 2007, 15:111-122.
-
(2007)
Structure
, vol.15
, pp. 111-122
-
-
Mallam, A.L.1
Jackson, S.E.2
-
178
-
-
44449146446
-
Knotted fusion proteins reveal unexpected possibilities in protein folding
-
Mallam A.L., Onuoha S.C., Grossmann J.G., Jackson S.E. Knotted fusion proteins reveal unexpected possibilities in protein folding. Mol. Cell 2008, 30:642-648.
-
(2008)
Mol. Cell
, vol.30
, pp. 642-648
-
-
Mallam, A.L.1
Onuoha, S.C.2
Grossmann, J.G.3
Jackson, S.E.4
-
179
-
-
0036108484
-
3D domain swapping: As domains continue to swap
-
Liu Y., Eisenberg D. 3D domain swapping: As domains continue to swap. Protein Sci. 2002, 11:1285-1299.
-
(2002)
Protein Sci.
, vol.11
, pp. 1285-1299
-
-
Liu, Y.1
Eisenberg, D.2
-
180
-
-
4143135385
-
Stability and folding mechanism of mesophilic, thermophilic and hyperthermophilic archael histones: The importance of folding intermediates
-
Topping T.B., Gloss L.M. Stability and folding mechanism of mesophilic, thermophilic and hyperthermophilic archael histones: The importance of folding intermediates. J. Mol. Biol. 2004, 342:247-260.
-
(2004)
J. Mol. Biol.
, vol.342
, pp. 247-260
-
-
Topping, T.B.1
Gloss, L.M.2
-
181
-
-
10044293974
-
Three-state kinetic folding mechanism of the H2A/H2B histone heterodimer: The N-terminal tails affect the transition state between a dimeric intermediate and the native dimer
-
Placek B.J., Gloss L.M. Three-state kinetic folding mechanism of the H2A/H2B histone heterodimer: The N-terminal tails affect the transition state between a dimeric intermediate and the native dimer. J. Mol. Biol. 2005, 345:827-836.
-
(2005)
J. Mol. Biol.
, vol.345
, pp. 827-836
-
-
Placek, B.J.1
Gloss, L.M.2
-
182
-
-
1942537192
-
2 histone tetramer of the core nucleosome
-
2 histone tetramer of the core nucleosome. Protein Sci. 2004, 13:1304-1316.
-
(2004)
Protein Sci.
, vol.13
, pp. 1304-1316
-
-
Banks, D.D.1
Gloss, L.M.2
-
183
-
-
0027162959
-
Folding of the bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits
-
Clark A.C., Sinclair J.F., Baldwin T.O. Folding of the bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits. J. Biol. Chem. 1993, 268:10773-10779.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 10773-10779
-
-
Clark, A.C.1
Sinclair, J.F.2
Baldwin, T.O.3
-
184
-
-
0027178317
-
Contributions of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme
-
Baldwin T.O., Ziegler M.M., Chaffotte A.F., Goldberg M.E. Contributions of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme. J. Biol.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 10766-10772
-
-
Baldwin, T.O.1
Ziegler, M.M.2
Chaffotte, A.F.3
Goldberg, M.E.4
-
185
-
-
0031037666
-
Kinetic mechanism of luciferase subunit folding and assembly
-
Clark A.C., Raso S.W., Sinclair J.F., Ziegler M.M., Chaffotte A.F., Baldwin T.O. Kinetic mechanism of luciferase subunit folding and assembly. Biochemistry 1997, 36:1891-1899.
-
(1997)
Biochemistry
, vol.36
, pp. 1891-1899
-
-
Clark, A.C.1
Raso, S.W.2
Sinclair, J.F.3
Ziegler, M.M.4
Chaffotte, A.F.5
Baldwin, T.O.6
-
186
-
-
0031032079
-
Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap
-
Thoden J.B., Holden H.M., Fisher A.J., Sinclair J.F., Wesenberg G., Baldwin T.O., Rayment I. Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap. Protein Sci. 1997, 6:13-23.
-
(1997)
Protein Sci.
, vol.6
, pp. 13-23
-
-
Thoden, J.B.1
Holden, H.M.2
Fisher, A.J.3
Sinclair, J.F.4
Wesenberg, G.5
Baldwin, T.O.6
Rayment, I.7
-
187
-
-
56949105979
-
Mutational analysis of the stability of the H2A and H2B histone monomers
-
Stump M.R., Gloss L.M. Mutational analysis of the stability of the H2A and H2B histone monomers. J. Mol. Biol. 2008, 384:1369-1383.
-
(2008)
J. Mol. Biol.
, vol.384
, pp. 1369-1383
-
-
Stump, M.R.1
Gloss, L.M.2
-
188
-
-
77955266816
-
Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer
-
Stump M.R., Gloss L.M. Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer. J. Mol. Biol. 2010, 401:518-531.
-
(2010)
J. Mol. Biol.
, vol.401
, pp. 518-531
-
-
Stump, M.R.1
Gloss, L.M.2
-
189
-
-
0032502839
-
Contact order, transition state placement and the refolding rates of single domain proteins
-
Plaxco K.W., Simons K.T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 1998, 277:985-994.
-
(1998)
J. Mol. Biol.
, vol.277
, pp. 985-994
-
-
Plaxco, K.W.1
Simons, K.T.2
Baker, D.3
-
190
-
-
0034687123
-
Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
-
Plaxco K.W., Simons K.T., Ruczinski I., Baker D. Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics. Biochemistry 2000, 39:11177-11183.
-
(2000)
Biochemistry
, vol.39
, pp. 11177-11183
-
-
Plaxco, K.W.1
Simons, K.T.2
Ruczinski, I.3
Baker, D.4
-
191
-
-
0024412506
-
Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease
-
Wlodawer A., Miller M., Jaskolski M., Sathyanarayana B.K., Baldwin E., Weber I.T., Selk L.M., Clawson L., Schneider J., Kent S.B. Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease. Science 1989, 245:616-621.
-
(1989)
Science
, vol.245
, pp. 616-621
-
-
Wlodawer, A.1
Miller, M.2
Jaskolski, M.3
Sathyanarayana, B.K.4
Baldwin, E.5
Weber, I.T.6
Selk, L.M.7
Clawson, L.8
Schneider, J.9
Kent, S.B.10
-
192
-
-
62649160354
-
The folding free-energy surface of HIV-1 protease: Insights into the thermodynamic basis for resistance to inhibitors
-
Noel A.F., Bilsel O., Kundu A., Wu Y., Zitzewitz J.A., Matthews C.R. The folding free-energy surface of HIV-1 protease: Insights into the thermodynamic basis for resistance to inhibitors. J. Mol. Biol. 2009, 387:1002-1016.
-
(2009)
J. Mol. Biol.
, vol.387
, pp. 1002-1016
-
-
Noel, A.F.1
Bilsel, O.2
Kundu, A.3
Wu, Y.4
Zitzewitz, J.A.5
Matthews, C.R.6
-
193
-
-
0026711256
-
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase
-
Parge H.E., Hallewell R.A., Tainer J.A. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. USA 1992, 89:6109-6113.
-
(1992)
Proc. Natl. Acad. Sci. USA
, vol.89
, pp. 6109-6113
-
-
Parge, H.E.1
Hallewell, R.A.2
Tainer, J.A.3
-
194
-
-
33751071644
-
Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase
-
Svensson A.K., Bilsel O., Kondrashkina E., Zitzewitz J.A., Matthews C.R. Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase. J. Mol. Biol. 2006, 364:1084-1102.
-
(2006)
J. Mol. Biol.
, vol.364
, pp. 1084-1102
-
-
Svensson, A.K.1
Bilsel, O.2
Kondrashkina, E.3
Zitzewitz, J.A.4
Matthews, C.R.5
-
195
-
-
46749117136
-
Molecular and cellular aspects of protein misfolding and disease
-
Herczenik E., Gebbink M.F. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 2008, 22:2115-2133.
-
(2008)
FASEB J.
, vol.22
, pp. 2115-2133
-
-
Herczenik, E.1
Gebbink, M.F.2
-
196
-
-
68649110959
-
Bridging the gap: From protein misfolding to protein misfolding diseases
-
Luheshi L.M., Dobson C.M. Bridging the gap: From protein misfolding to protein misfolding diseases. FEBS Lett. 2009, 583:2581-2586.
-
(2009)
FEBS Lett.
, vol.583
, pp. 2581-2586
-
-
Luheshi, L.M.1
Dobson, C.M.2
-
198
-
-
70349305183
-
Inhibitors of protein aggregation and toxicity
-
Amijee H., Madine J., Middleton D.A., Doig A.J. Inhibitors of protein aggregation and toxicity. Biochem. Soc. Trans. 2009, 37:692-696.
-
(2009)
Biochem. Soc. Trans.
, vol.37
, pp. 692-696
-
-
Amijee, H.1
Madine, J.2
Middleton, D.A.3
Doig, A.J.4
-
199
-
-
59649105575
-
Pathogenesis of and therapeutic strategies to ameliorate the transthyretin amyloidoses
-
Sekijima Y., Kelly J.W., Ikeda S. Pathogenesis of and therapeutic strategies to ameliorate the transthyretin amyloidoses. Curr. Pharm. Des. 2008, 14:3219-3230.
-
(2008)
Curr. Pharm. Des.
, vol.14
, pp. 3219-3230
-
-
Sekijima, Y.1
Kelly, J.W.2
Ikeda, S.3
-
200
-
-
68649113747
-
The role of molecular chaperones in human misfolding diseases
-
Broadley S.A., Hartl F.U. The role of molecular chaperones in human misfolding diseases. FEBS Lett. 2009, 583:2647-2653.
-
(2009)
FEBS Lett.
, vol.583
, pp. 2647-2653
-
-
Broadley, S.A.1
Hartl, F.U.2
-
201
-
-
0024297340
-
Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
-
Hyde C.C., Ahmed S.A., Padlan E.A., Miles E.W., Davies D.R. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 1988, 263:17857-17871.
-
(1988)
J. Biol. Chem.
, vol.263
, pp. 17857-17871
-
-
Hyde, C.C.1
Ahmed, S.A.2
Padlan, E.A.3
Miles, E.W.4
Davies, D.R.5
-
202
-
-
0034562065
-
Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein
-
Battistutta R., Negro A., Zanotti G. Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein. Proteins 2000, 41:429-437.
-
(2000)
Proteins
, vol.41
, pp. 429-437
-
-
Battistutta, R.1
Negro, A.2
Zanotti, G.3
-
203
-
-
0031015737
-
Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
-
Sawaya M.R., Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence. Biochemistry 1997, 36:586-603.
-
(1997)
Biochemistry
, vol.36
, pp. 586-603
-
-
Sawaya, M.R.1
Kraut, J.2
-
204
-
-
0029924193
-
NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this Archaeal protein is a histone
-
Starich M.R., Sandman K., Reeve J.N., Summers M.F. NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this Archaeal protein is a histone. J. Mol. Biol. 1996, 255:187-203.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 187-203
-
-
Starich, M.R.1
Sandman, K.2
Reeve, J.N.3
Summers, M.F.4
-
205
-
-
35648937607
-
Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation
-
Samuel D., Cheng H., Riley P.W., Canutescu A.A., Nagaswami C., Weisel J.W., Bu Z., Walsh P.N., Roder H. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proc. Natl. Acad. Sci. USA 2007, 104:15693-15698.
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 15693-15698
-
-
Samuel, D.1
Cheng, H.2
Riley, P.W.3
Canutescu, A.A.4
Nagaswami, C.5
Weisel, J.W.6
Bu, Z.7
Walsh, P.N.8
Roder, H.9
-
206
-
-
28844466085
-
Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin
-
Nishimura C., Dyson H.J., Wright P.E. Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin. J. Mol. Biol. 2006, 355:139-156.
-
(2006)
J. Mol. Biol.
, vol.355
, pp. 139-156
-
-
Nishimura, C.1
Dyson, H.J.2
Wright, P.E.3
-
207
-
-
0345862223
-
Folding mechanism of FIS, the intertwined, dimeric factor for inversion stimulation
-
Topping T.B., Hoch D.A., Gloss L.M. Folding mechanism of FIS, the intertwined, dimeric factor for inversion stimulation. J. Mol. Biol. 2004, 335:1065-1081.
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 1065-1081
-
-
Topping, T.B.1
Hoch, D.A.2
Gloss, L.M.3
-
208
-
-
0030627747
-
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
-
Munson M., Anderson K.S., Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Fold. Des. 1997, 2:77-87.
-
(1997)
Fold. Des.
, vol.2
, pp. 77-87
-
-
Munson, M.1
Anderson, K.S.2
Regan, L.3
-
209
-
-
40049098125
-
Conservation of mechanism, variation of rate: Folding kinetics of three homologous four-helix bundle proteins
-
Dalal S., Canet D., Kaiser S.E., Dobson C.M., Regan L. Conservation of mechanism, variation of rate: Folding kinetics of three homologous four-helix bundle proteins. Protein Eng. Des. Sel. 2008, 21:197-206.
-
(2008)
Protein Eng. Des. Sel.
, vol.21
, pp. 197-206
-
-
Dalal, S.1
Canet, D.2
Kaiser, S.E.3
Dobson, C.M.4
Regan, L.5
-
210
-
-
0030925611
-
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor
-
Gloss L.M., Matthews C.R. Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry 1997, 36:5612-5623.
-
(1997)
Biochemistry
, vol.36
, pp. 5612-5623
-
-
Gloss, L.M.1
Matthews, C.R.2
-
211
-
-
0037126728
-
Interleukin-1 beta folding between pH 5 and 7: Experimental evidence for three-state folding behavior and robust transition state positions late in folding
-
Finke J.M., Jennings P.A. Interleukin-1 beta folding between pH 5 and 7: Experimental evidence for three-state folding behavior and robust transition state positions late in folding. Biochemistry 2002, 41:15056-15067.
-
(2002)
Biochemistry
, vol.41
, pp. 15056-15067
-
-
Finke, J.M.1
Jennings, P.A.2
-
212
-
-
54449086396
-
Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?
-
Capraro D.T., Roy M., Onuchic J.N., Jennings P.A. Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?. Proc. Natl. Acad. Sci. USA 2008, 105:14844-14848.
-
(2008)
Proc. Natl. Acad. Sci. USA
, vol.105
, pp. 14844-14848
-
-
Capraro, D.T.1
Roy, M.2
Onuchic, J.N.3
Jennings, P.A.4
-
213
-
-
0029929965
-
Intrinsic tryptophans of CRABPI as probes of structure and folding
-
Clark P.L., Liu Z.P., Zhang J., Gierasch L.M. Intrinsic tryptophans of CRABPI as probes of structure and folding. Protein Sci. 1996, 5:1108-1117.
-
(1996)
Protein Sci.
, vol.5
, pp. 1108-1117
-
-
Clark, P.L.1
Liu, Z.P.2
Zhang, J.3
Gierasch, L.M.4
-
214
-
-
0035874143
-
Folding of intracellular retinol and retinoic acid binding proteins
-
Burns L.L., Ropson I.J. Folding of intracellular retinol and retinoic acid binding proteins. Proteins 2001, 43:292-302.
-
(2001)
Proteins
, vol.43
, pp. 292-302
-
-
Burns, L.L.1
Ropson, I.J.2
-
215
-
-
0034620582
-
Beta-sheet proteins with nearly identical structures have different folding intermediates
-
Dalessio P.M., Ropson I.J. Beta-sheet proteins with nearly identical structures have different folding intermediates. Biochemistry 2000, 39:860-871.
-
(2000)
Biochemistry
, vol.39
, pp. 860-871
-
-
Dalessio, P.M.1
Ropson, I.J.2
-
216
-
-
66149164339
-
Comparison of the folding mechanism of highly homologous proteins in the lipid-binding protein family
-
Ropson I.J., Boyer J.A., Schaeffer B.A., Dalessio P.M. Comparison of the folding mechanism of highly homologous proteins in the lipid-binding protein family. Proteins 2009, 75:799-806.
-
(2009)
Proteins
, vol.75
, pp. 799-806
-
-
Ropson, I.J.1
Boyer, J.A.2
Schaeffer, B.A.3
Dalessio, P.M.4
-
217
-
-
0034984382
-
Mapping the folding pathway of an immunoglobulin domain: Structural detail from Phi value analysis and movement of the transition state
-
Fowler S.B., Clarke J. Mapping the folding pathway of an immunoglobulin domain: Structural detail from Phi value analysis and movement of the transition state. Structure 2001, 9:355-366.
-
(2001)
Structure
, vol.9
, pp. 355-366
-
-
Fowler, S.B.1
Clarke, J.2
-
218
-
-
73149121172
-
Folding and assembly kinetics of procaspase-3
-
Milam S.L., Clark A.C. Folding and assembly kinetics of procaspase-3. Protein Sci. 2009, 18:2500-2517.
-
(2009)
Protein Sci.
, vol.18
, pp. 2500-2517
-
-
Milam, S.L.1
Clark, A.C.2
-
219
-
-
0033554860
-
Folding and assembly of dimeric human glutathione transferase A1-1
-
Wallace L.A., Dirr H.W. Folding and assembly of dimeric human glutathione transferase A1-1. Biochemistry 1999, 38:16686-16694.
-
(1999)
Biochemistry
, vol.38
, pp. 16686-16694
-
-
Wallace, L.A.1
Dirr, H.W.2
-
220
-
-
0026751786
-
The folding of hen lysozyme involves partially structured intermediates and multiple pathways
-
Radford S.E., Dobson C.M., Evans P.A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 1992, 358:302-307.
-
(1992)
Nature
, vol.358
, pp. 302-307
-
-
Radford, S.E.1
Dobson, C.M.2
Evans, P.A.3
-
221
-
-
0027770910
-
Detection of transient protein folding populations by mass spectrometry
-
Miranker A., Robinson C.V., Radford S.E., Aplin R.T., Dobson C.M. Detection of transient protein folding populations by mass spectrometry. Science 1993, 262:896-900.
-
(1993)
Science
, vol.262
, pp. 896-900
-
-
Miranker, A.1
Robinson, C.V.2
Radford, S.E.3
Aplin, R.T.4
Dobson, C.M.5
-
222
-
-
0035942316
-
Folding mechanism of ketosteroid isomerase from Comamonas testosteroni
-
Kim D.H., Jang D.S., Nam G.H., Choi K.Y. Folding mechanism of ketosteroid isomerase from Comamonas testosteroni. Biochemistry 2001, 40:5011-5017.
-
(2001)
Biochemistry
, vol.40
, pp. 5011-5017
-
-
Kim, D.H.1
Jang, D.S.2
Nam, G.H.3
Choi, K.Y.4
-
223
-
-
0035082463
-
Roles of dimerization in folding and stability of ketosteroid isomerase from Pseudomonas putida biotype B
-
Kim D.H., Nam G.H., Jang D.S., Yun S., Choi G., Lee H.C., Choi K.Y. Roles of dimerization in folding and stability of ketosteroid isomerase from Pseudomonas putida biotype B. Protein Sci. 2001, 10:741-752.
-
(2001)
Protein Sci.
, vol.10
, pp. 741-752
-
-
Kim, D.H.1
Nam, G.H.2
Jang, D.S.3
Yun, S.4
Choi, G.5
Lee, H.C.6
Choi, K.Y.7
-
224
-
-
0842324785
-
The nucleosome: From genomic organization to genomic regulation
-
Khorasanizadeh S. The nucleosome: From genomic organization to genomic regulation. Cell 2004, 116:259-272.
-
(2004)
Cell
, vol.116
, pp. 259-272
-
-
Khorasanizadeh, S.1
-
225
-
-
33744937937
-
Early events in protein folding explored by rapid mixing methods
-
Roder H., Maki K., Cheng H. Early events in protein folding explored by rapid mixing methods. Chem. Rev. 2006, 106:1836-1861.
-
(2006)
Chem. Rev.
, vol.106
, pp. 1836-1861
-
-
Roder, H.1
Maki, K.2
Cheng, H.3
|