-
1
-
-
0037686252
-
The present view of the mechanism of protein folding
-
V. Daggett, and A.R. Fersht The present view of the mechanism of protein folding Nature Rev. Mol. Cell. Biol. 4 2003 497 502
-
(2003)
Nature Rev. Mol. Cell. Biol.
, vol.4
, pp. 497-502
-
-
Daggett, V.1
Fersht, A.R.2
-
2
-
-
0037221599
-
Is there a unifying mechanism for protein folding?
-
V. Daggett, and A.R. Fersht Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28 2003 18 25
-
(2003)
Trends Biochem. Sci.
, vol.28
, pp. 18-25
-
-
Daggett, V.1
Fersht, A.R.2
-
3
-
-
0037526102
-
Crystal structure of tRNA(m1G37)methyltransferase: Insights into tRNA recognition
-
H.J. Ahn, H.W. Kim, H.J. Yoon, B.I. Lee, S.W. Suh, and J.K. Yang Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition EMBO J. 22 2003 2593 2603
-
(2003)
EMBO J.
, vol.22
, pp. 2593-2603
-
-
Ahn, H.J.1
Kim, H.W.2
Yoon, H.J.3
Lee, B.I.4
Suh, S.W.5
Yang, J.K.6
-
4
-
-
0142216637
-
Insights into catalysis by a knotted TrmD tRNA methyltransferase
-
P.A. Elkins, J.M. Watts, M. Zalacain, A. van Thiel, P.R. Vitazka, and M. Redlak Insights into catalysis by a knotted TrmD tRNA methyltransferase J. Mol. Biol. 333 2003 931 949
-
(2003)
J. Mol. Biol.
, vol.333
, pp. 931-949
-
-
Elkins, P.A.1
Watts, J.M.2
Zalacain, M.3
Van Thiel, A.4
Vitazka, P.R.5
Redlak, M.6
-
5
-
-
0141704142
-
Functional assignment based on structural analysis: Crystal structure of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA methyltransferase with a deep trefoil knot
-
F. Forouhar, J. Shen, R. Xiao, T.B. Acton, G.T. Montelione, and L. Tong Functional assignment based on structural analysis: crystal structure of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA methyltransferase with a deep trefoil knot Proteins: Struct. Funct. Genet. 53 2003 329 332
-
(2003)
Proteins: Struct. Funct. Genet.
, vol.53
, pp. 329-332
-
-
Forouhar, F.1
Shen, J.2
Xiao, R.3
Acton, T.B.4
Montelione, G.T.5
Tong, L.6
-
6
-
-
0037375572
-
Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): A cofactor bound at a site formed by a knot
-
K. Lim, H. Zhang, A. Tempczyk, W. Krajewski, N. Bonander, and J. Toedt Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): a cofactor bound at a site formed by a knot Proteins: Struct. Funct. Genet. 51 2003 56 67
-
(2003)
Proteins: Struct. Funct. Genet.
, vol.51
, pp. 56-67
-
-
Lim, K.1
Zhang, H.2
Tempczyk, A.3
Krajewski, W.4
Bonander, N.5
Toedt, J.6
-
7
-
-
0036774065
-
The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot
-
G. Michel, V. Sauve, R. Larocque, Y. Li, A. Matte, and M. Cygler The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot Structure 10 2002 1303 1315
-
(2002)
Structure
, vol.10
, pp. 1303-1315
-
-
Michel, G.1
Sauve, V.2
Larocque, R.3
Li, Y.4
Matte, A.5
Cygler, M.6
-
8
-
-
0035997122
-
An enzyme with a deep trefoil knot for the active-site architecture
-
O. Nureki, M. Shirouzu, K. Hashimoto, R. Ishitani, T. Terada, and M. Tamakoshi An enzyme with a deep trefoil knot for the active-site architecture Acta Crystallog. sect. D 58 2002 1129 1137
-
(2002)
Acta Crystallog. Sect. D
, vol.58
, pp. 1129-1137
-
-
Nureki, O.1
Shirouzu, M.2
Hashimoto, K.3
Ishitani, R.4
Terada, T.5
Tamakoshi, M.6
-
9
-
-
1842607227
-
Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme
-
O. Nureki, K. Watanabe, S. Fukai, R. Ishii, Y. Endo, H. Hori, and S. Yokoyama Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme Structure 12 2004 593 602
-
(2004)
Structure
, vol.12
, pp. 593-602
-
-
Nureki, O.1
Watanabe, K.2
Fukai, S.3
Ishii, R.4
Endo, Y.5
Hori, H.6
Yokoyama, S.7
-
10
-
-
0037297693
-
Deep trefoil knot implicated in RNA binding found in an archaebacterial protein
-
T.I. Zarembinski, Y. Kim, K. Peterson, D. Christendat, A. Dharamsi, and C.H. Arrowsmith Deep trefoil knot implicated in RNA binding found in an archaebacterial protein Proteins: Struct. Funct. Genet. 50 2003 177 183
-
(2003)
Proteins: Struct. Funct. Genet.
, vol.50
, pp. 177-183
-
-
Zarembinski, T.I.1
Kim, Y.2
Peterson, K.3
Christendat, D.4
Dharamsi, A.5
Arrowsmith, C.H.6
-
11
-
-
0029105847
-
Topological features of protein structures - Knots and links
-
C.Z. Liang, and K. Mislow Topological features of protein structures - knots and links J. Am. Chem. Soc. 117 1995 4201 4213
-
(1995)
J. Am. Chem. Soc.
, vol.117
, pp. 4201-4213
-
-
Liang, C.Z.1
Mislow, K.2
-
13
-
-
0028421135
-
Are there knots in proteins?
-
M.L. Mansfield Are there knots in proteins? Nature Struct. Biol. 1 1994 213 214
-
(1994)
Nature Struct. Biol.
, vol.1
, pp. 213-214
-
-
Mansfield, M.L.1
-
16
-
-
0034710671
-
A deeply knotted protein structure and how it might fold
-
W.R. Taylor A deeply knotted protein structure and how it might fold Nature 406 2000 916 919
-
(2000)
Nature
, vol.406
, pp. 916-919
-
-
Taylor, W.R.1
-
17
-
-
0037413604
-
Protein knots: A tangled problem
-
W.R. Taylor, and K. Lin Protein knots: a tangled problem Nature 421 2003 25
-
(2003)
Nature
, vol.421
, pp. 25
-
-
Taylor, W.R.1
Lin, K.2
-
18
-
-
0029926820
-
S-Adenosylmethionine and methylation
-
P.K. Chiang, R.K. Gordon, J. Tal, G.C. Zeng, B.P. Doctor, K. Pardhasaradhi, and P.P. McCann S-Adenosylmethionine and methylation FASEB J. 10 1996 471 480
-
(1996)
FASEB J.
, vol.10
, pp. 471-480
-
-
Chiang, P.K.1
Gordon, R.K.2
Tal, J.3
Zeng, G.C.4
Doctor, B.P.5
Pardhasaradhi, K.6
McCann, P.P.7
-
19
-
-
0036132209
-
SPOUT: A class of methyltransferases that includes SpoU and TrmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases
-
V. Anantharaman, E.V. Koonin, and L. Aravind SPOUT: a class of methyltransferases that includes SpoU and TrmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases J. Mol. Microbiol. Biotechnol. 4 2002 71 75
-
(2002)
J. Mol. Microbiol. Biotechnol.
, vol.4
, pp. 71-75
-
-
Anantharaman, V.1
Koonin, E.V.2
Aravind, L.3
-
20
-
-
0002394256
-
Influence of chain knotting on the rate of folding
-
A.V. Finkelstein, and A. Badretdinov Influence of chain knotting on the rate of folding Fold. Des. 3 1997 67 68
-
(1997)
Fold. Des.
, vol.3
, pp. 67-68
-
-
Finkelstein, A.V.1
Badretdinov, A.2
-
21
-
-
0028606077
-
Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
-
K.E. Neet, and D.E. Timm Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation Protein Sci. 3 1994 2167 2174
-
(1994)
Protein Sci.
, vol.3
, pp. 2167-2174
-
-
Neet, K.E.1
Timm, D.E.2
-
22
-
-
0030925611
-
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor
-
L.M. Gloss, and C.R. Matthews Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor Biochemistry 36 1997 5612 5623
-
(1997)
Biochemistry
, vol.36
, pp. 5612-5623
-
-
Gloss, L.M.1
Matthews, C.R.2
-
23
-
-
0036084703
-
Equilibrium denaturation studies of the Escherichia coli factor for inversion stimulation: Implications for in vivo function
-
S.A. Hobart, S. Ilin, D.F. Moriarty, R. Osuna, and W. Colon Equilibrium denaturation studies of the Escherichia coli factor for inversion stimulation: implications for in vivo function Protein Sci. 11 2002 1671 1680
-
(2002)
Protein Sci.
, vol.11
, pp. 1671-1680
-
-
Hobart, S.A.1
Ilin, S.2
Moriarty, D.F.3
Osuna, R.4
Colon, W.5
-
24
-
-
0037137182
-
From two-state to three-state: The effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism
-
S.A. Hobart, D.W. Meinhold, R. Osuna, and W. Colon From two-state to three-state: the effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism Biochemistry 41 2002 13744 13754
-
(2002)
Biochemistry
, vol.41
, pp. 13744-13754
-
-
Hobart, S.A.1
Meinhold, D.W.2
Osuna, R.3
Colon, W.4
-
25
-
-
0000022693
-
Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions
-
Y.C. Park, and H. Bedouelle Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions J. Biol. Chem. 273 1998 18052 18059
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 18052-18059
-
-
Park, Y.C.1
Bedouelle, H.2
-
26
-
-
0022555885
-
Determination and analysis of urea and guanidine hydrochloride denaturation curves
-
C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
-
(1986)
Methods Enzymol.
, vol.131
, pp. 266-280
-
-
Pace, C.N.1
-
27
-
-
0031808804
-
Chemical denaturation: Potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption
-
J.L. Soulages Chemical denaturation: potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption Biophys. J. 75 1998 484 492
-
(1998)
Biophys. J.
, vol.75
, pp. 484-492
-
-
Soulages, J.L.1
-
28
-
-
0028820703
-
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
-
J.K. Myers, C.N. Pace, and J.M. Scholtz Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding Protein Sci. 4 1995 2138 2148
-
(1995)
Protein Sci.
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
30
-
-
0029620316
-
Modeling unfolded states of peptides and proteins
-
T.P. Creamer, R. Srinivasan, and G.D. Rose Modeling unfolded states of peptides and proteins Biochemistry 34 1995 16245 16250
-
(1995)
Biochemistry
, vol.34
, pp. 16245-16250
-
-
Creamer, T.P.1
Srinivasan, R.2
Rose, G.D.3
-
31
-
-
0030933329
-
Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility
-
T.P. Creamer, R. Srinivasan, and G.D. Rose Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility Biochemistry 36 1997 2832 2835
-
(1997)
Biochemistry
, vol.36
, pp. 2832-2835
-
-
Creamer, T.P.1
Srinivasan, R.2
Rose, G.D.3
-
32
-
-
0014718113
-
Protein denaturation. Part C. Theoretical models for the mechanism of denaturation
-
C. Tanford Protein denaturation. Part C. Theoretical models for the mechanism of denaturation Advan. Protein Chem. 24 1970 1 95
-
(1970)
Advan. Protein Chem.
, vol.24
, pp. 1-95
-
-
Tanford, C.1
-
33
-
-
0027162959
-
Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits
-
A.C. Clark, J.F. Sinclair, and T.O. Baldwin Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits J. Biol. Chem. 268 1993 10773 10779
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 10773-10779
-
-
Clark, A.C.1
Sinclair, J.F.2
Baldwin, T.O.3
-
35
-
-
0030711517
-
Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
-
J.K. Grimsley, J.M. Scholtz, C.N. Pace, and J.R. Wild Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate Biochemistry 36 1997 14366 14374
-
(1997)
Biochemistry
, vol.36
, pp. 14366-14374
-
-
Grimsley, J.K.1
Scholtz, J.M.2
Pace, C.N.3
Wild, J.R.4
-
36
-
-
0034633885
-
Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate
-
J.A. Hornby, J.K. Luo, J.M. Stevens, L.A. Wallace, W. Kaplan, R.N. Armstrong, and H.W. Dirr Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate Biochemistry 39 2000 12336 12344
-
(2000)
Biochemistry
, vol.39
, pp. 12336-12344
-
-
Hornby, J.A.1
Luo, J.K.2
Stevens, J.M.3
Wallace, L.A.4
Kaplan, W.5
Armstrong, R.N.6
Dirr, H.W.7
-
37
-
-
0036076144
-
Folding and stability of the ligand-binding domain of the glucocorticoid receptor
-
S.H. McLaughlin, and S.E. Jackson Folding and stability of the ligand-binding domain of the glucocorticoid receptor Protein Sci. 11 2002 1926 1936
-
(2002)
Protein Sci.
, vol.11
, pp. 1926-1936
-
-
McLaughlin, S.H.1
Jackson, S.E.2
-
38
-
-
0034718450
-
A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI
-
G. Spudich, and S. Marqusee A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI Biochemistry 39 2000 11677 11683
-
(2000)
Biochemistry
, vol.39
, pp. 11677-11683
-
-
Spudich, G.1
Marqusee, S.2
-
39
-
-
4143107222
-
Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
-
K. Gunasekaran, C.J. Tsai, and R. Nussinov Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers J. Mol. Biol. 341 2004 1327 1341
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 1327-1341
-
-
Gunasekaran, K.1
Tsai, C.J.2
Nussinov, R.3
-
40
-
-
0019872622
-
Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
-
K. Gekko, and S.N. Timasheff Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures Biochemistry 20 1981 4667 4676
-
(1981)
Biochemistry
, vol.20
, pp. 4667-4676
-
-
Gekko, K.1
Timasheff, S.N.2
-
41
-
-
0031815749
-
How do small single-domain proteins fold?
-
S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 81 91
-
(1998)
Fold. Des.
, vol.3
, pp. 81-91
-
-
Jackson, S.E.1
-
42
-
-
0024448151
-
Calculation of protein extinction coefficients from amino acid sequence data
-
S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
-
(1989)
Anal. Biochem.
, vol.182
, pp. 319-326
-
-
Gill, S.C.1
Von Hippel, P.H.2
-
43
-
-
33947482089
-
Dithiothreitol, a new protective reagent for SH groups
-
W.W. Cleland Dithiothreitol, a new protective reagent for SH groups Biochemistry 35 1964 480 482
-
(1964)
Biochemistry
, vol.35
, pp. 480-482
-
-
Cleland, W.W.1
-
44
-
-
0002343673
-
Measuring the conformational stability of a protein
-
T.E. Creighton Oxford University Press Oxford
-
C.N. Pace, B.A. Shirley, and J.A. Thomson Measuring the conformational stability of a protein T.E. Creighton Protein Structure. A Practical Approach 1990 Oxford University Press Oxford 311 330
-
(1990)
Protein Structure. a Practical Approach
, pp. 311-330
-
-
Pace, C.N.1
Shirley, B.A.2
Thomson, J.A.3
-
45
-
-
0000722070
-
Spectral methods of characterizing protein conformation and conformational changes
-
T.E. Creighton Oxford University Press Oxford
-
F.X. Schmid Spectral methods of characterizing protein conformation and conformational changes T.E. Creighton Protein Structure. A Practical Approach 1990 Oxford University Press Oxford 251 285
-
(1990)
Protein Structure. a Practical Approach
, pp. 251-285
-
-
Schmid, F.X.1
-
46
-
-
0001528720
-
Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
-
R. Fraczkiewicz, and W. Braun Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Comput. Chem. 19 1998 319 333
-
(1998)
J. Comput. Chem.
, vol.19
, pp. 319-333
-
-
Fraczkiewicz, R.1
Braun, W.2
|