-
1
-
-
0029049321
-
Extremely rapid folding in the absence of intermediates: the cold-shock protein from Bacillus subtilis
-
Schindler T., Herrler M., Marahiel M.A., and Schmid F.X. Extremely rapid folding in the absence of intermediates: the cold-shock protein from Bacillus subtilis. Nature Struct. Biol. 2 (1995) 663-673
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 663-673
-
-
Schindler, T.1
Herrler, M.2
Marahiel, M.A.3
Schmid, F.X.4
-
3
-
-
0037470575
-
Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant
-
Horng J.C., Moroz V., and Raleigh D.P. Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant. J. Mol. Biol. 326 (2003) 1261-1270
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 1261-1270
-
-
Horng, J.C.1
Moroz, V.2
Raleigh, D.P.3
-
4
-
-
0029151158
-
Submillisecond folding of monomeric lambda repressor
-
Huang G.S., and Oas T.G. Submillisecond folding of monomeric lambda repressor. Proc. Natl Acad. Sci. USA 92 (1995) 6878-6882
-
(1995)
Proc. Natl Acad. Sci. USA
, vol.92
, pp. 6878-6882
-
-
Huang, G.S.1
Oas, T.G.2
-
5
-
-
0034610360
-
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
-
Mayor U., Johnson C.M., Daggett V., and Fersht A.R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl Acad. Sci. USA 97 (2000) 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
-
6
-
-
0033624685
-
Fast kinetics and mechanisms in protein folding
-
Eaton W.A., Munoz V., Hagen S.J., Jas G.S., Lapidus L.J., Henry E.R., and Hofrichter J. Fast kinetics and mechanisms in protein folding. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 327-359
-
(2000)
Annu. Rev. Biophys. Biomol. Struct.
, vol.29
, pp. 327-359
-
-
Eaton, W.A.1
Munoz, V.2
Hagen, S.J.3
Jas, G.S.4
Lapidus, L.J.5
Henry, E.R.6
Hofrichter, J.7
-
7
-
-
0016711868
-
Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
-
Brandts J.F., Halvorson H.R., and Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14 (1975) 4953-4963
-
(1975)
Biochemistry
, vol.14
, pp. 4953-4963
-
-
Brandts, J.F.1
Halvorson, H.R.2
Brennan, M.3
-
8
-
-
0000247412
-
Prolyl isomerization and its catalysis in protein folding
-
Pain R.H. (Ed), Oxford University Press, Oxford, UK
-
Balbach J., and Schmid F.X. Prolyl isomerization and its catalysis in protein folding. In: Pain R.H. (Ed). Mechanisms of Protein Folding (2000), Oxford University Press, Oxford, UK 212-237
-
(2000)
Mechanisms of Protein Folding
, pp. 212-237
-
-
Balbach, J.1
Schmid, F.X.2
-
9
-
-
0025299887
-
Occurrence and role of cis peptide bonds in protein structures
-
Stewart D.E., Sarkar A., and Wampler J.E. Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214 (1990) 253-260
-
(1990)
J. Mol. Biol.
, vol.214
, pp. 253-260
-
-
Stewart, D.E.1
Sarkar, A.2
Wampler, J.E.3
-
10
-
-
0001340839
-
Kinetics of unfolding and refolding of single-domain proteins
-
Creighton T.E. (Ed), Freeman, New York
-
Schmid F.X. Kinetics of unfolding and refolding of single-domain proteins. In: Creighton T.E. (Ed). Protein Folding. 1st edit. (1992), Freeman, New York 197-241
-
(1992)
Protein Folding. 1st edit.
, pp. 197-241
-
-
Schmid, F.X.1
-
13
-
-
0028050923
-
Peptidyl-prolyl cis/trans isomerases and their effectors
-
Fischer G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33 (1994) 1415-1436
-
(1994)
Angew. Chem. Int. Ed. Engl.
, vol.33
, pp. 1415-1436
-
-
Fischer, G.1
-
14
-
-
0032926319
-
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
-
Göthel S.F., and Marahiel M.A. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell. Mol. Life Sci. 55 (1999) 423-436
-
(1999)
Cell. Mol. Life Sci.
, vol.55
, pp. 423-436
-
-
Göthel, S.F.1
Marahiel, M.A.2
-
16
-
-
1242292029
-
Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
-
Fischer G., and Aumüller T. Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Pharmacol. 148 (2004) 105-150
-
(2004)
Rev. Physiol. Biochem. Pharmacol.
, vol.148
, pp. 105-150
-
-
Fischer, G.1
Aumüller, T.2
-
17
-
-
2442586718
-
Catalysis of proline-directed protein phosphorylation by peptidyl-prolyl cis/trans isomerases
-
Weiwad M., Werner A., Rucknagel P., Schierhorn A., Kullertz G., and Fischer G. Catalysis of proline-directed protein phosphorylation by peptidyl-prolyl cis/trans isomerases. J. Mol. Biol. 339 (2004) 635-646
-
(2004)
J. Mol. Biol.
, vol.339
, pp. 635-646
-
-
Weiwad, M.1
Werner, A.2
Rucknagel, P.3
Schierhorn, A.4
Kullertz, G.5
Fischer, G.6
-
18
-
-
0028864461
-
Identification of the peptidyl-prolyl cis/trans isomerase bound to the Escherichia coli ribosome as the trigger factor
-
Stoller G., Rücknagel K.P., Nierhaus K., Schmid F.X., Fischer G., and Rahfeld J.-U. Identification of the peptidyl-prolyl cis/trans isomerase bound to the Escherichia coli ribosome as the trigger factor. EMBO J. 14 (1995) 4939-4948
-
(1995)
EMBO J.
, vol.14
, pp. 4939-4948
-
-
Stoller, G.1
Rücknagel, K.P.2
Nierhaus, K.3
Schmid, F.X.4
Fischer, G.5
Rahfeld, J.-U.6
-
19
-
-
0031029046
-
Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
-
Scholz C., Stoller G., Zarnt T., Fischer G., and Schmid F.X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16 (1997) 54-58
-
(1997)
EMBO J.
, vol.16
, pp. 54-58
-
-
Scholz, C.1
Stoller, G.2
Zarnt, T.3
Fischer, G.4
Schmid, F.X.5
-
20
-
-
0030916764
-
The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase
-
Hottenrott S., Schumann T., Plückthun A., Fischer G., and Rahfeld J.U. The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase. J. Biol. Chem. 272 (1997) 15697-15701
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 15697-15701
-
-
Hottenrott, S.1
Schumann, T.2
Plückthun, A.3
Fischer, G.4
Rahfeld, J.U.5
-
21
-
-
30144446085
-
SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities
-
Scholz C., Eckert B., Hagn F., Schaarschmidt P., Balbach J., and Schmid F.X. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities. Biochemistry 45 (2006) 20-33
-
(2006)
Biochemistry
, vol.45
, pp. 20-33
-
-
Scholz, C.1
Eckert, B.2
Hagn, F.3
Schaarschmidt, P.4
Balbach, J.5
Schmid, F.X.6
-
22
-
-
0029809115
-
Isolation and amino acid sequence of a new 22-kDa FKBP- like peptidyl-prolyl cis/trans-isomerase of Escherichia coli - Similarity to Mip-like proteins of pathogenic bacteria
-
Rahfeld J.U., Rucknagel K.P., Stoller G., Horne S.M., Schierhorn A., Young K.D., and Fischer G. Isolation and amino acid sequence of a new 22-kDa FKBP- like peptidyl-prolyl cis/trans-isomerase of Escherichia coli - Similarity to Mip-like proteins of pathogenic bacteria. J. Biol. Chem. 271 (1996) 22130-22138
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 22130-22138
-
-
Rahfeld, J.U.1
Rucknagel, K.P.2
Stoller, G.3
Horne, S.M.4
Schierhorn, A.5
Young, K.D.6
Fischer, G.7
-
23
-
-
13444309317
-
Stabilities and activities of the N- and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli
-
Suzuki Y., Takano K., and Kanaya S. Stabilities and activities of the N- and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli. FEBS J. 272 (2005) 632-642
-
(2005)
FEBS J.
, vol.272
, pp. 632-642
-
-
Suzuki, Y.1
Takano, K.2
Kanaya, S.3
-
24
-
-
0039423955
-
The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines
-
Bothmann H., and Plückthun A. The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines. J. Biol. Chem. 275 (2000) 17100-17105
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 17100-17105
-
-
Bothmann, H.1
Plückthun, A.2
-
25
-
-
0038831330
-
The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
-
Ramm K., and Plückthun A. The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J. Biol. Chem. 275 (2000) 17106-17113
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 17106-17113
-
-
Ramm, K.1
Plückthun, A.2
-
26
-
-
0035816225
-
High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA
-
Ramm K., and Plückthun A. High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. J. Mol. Biol. 310 (2001) 485-498
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 485-498
-
-
Ramm, K.1
Plückthun, A.2
-
27
-
-
0346366809
-
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
-
Saul F.A., Arie J.P., Vulliez-le Norm B., Kahn R., Betton J.M., and Bentley G.A. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335 (2004) 595-608
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 595-608
-
-
Saul, F.A.1
Arie, J.P.2
Vulliez-le Norm, B.3
Kahn, R.4
Betton, J.M.5
Bentley, G.A.6
-
28
-
-
0029131389
-
Phi X174 lysis requires slyD, a host gene which is related to the FKBP family of peptidyl-prolyl cis-trans isomerases
-
Roof W.D., and Young R. Phi X174 lysis requires slyD, a host gene which is related to the FKBP family of peptidyl-prolyl cis-trans isomerases. FEMS Microbiol. Rev. 17 (1995) 213-218
-
(1995)
FEMS Microbiol. Rev.
, vol.17
, pp. 213-218
-
-
Roof, W.D.1
Young, R.2
-
29
-
-
0030960946
-
Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family
-
Roof W.D., Fang H.Q., Young K.D., Sun J., and Young R. Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family. Mol. Microbiol. 25 (1997) 1031-1046
-
(1997)
Mol. Microbiol.
, vol.25
, pp. 1031-1046
-
-
Roof, W.D.1
Fang, H.Q.2
Young, K.D.3
Sun, J.4
Young, R.5
-
30
-
-
0036046111
-
The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174
-
Bernhardt T.G., Roof W.D., and Young R. The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174. Mol. Microbiol. 45 (2002) 99-108
-
(2002)
Mol. Microbiol.
, vol.45
, pp. 99-108
-
-
Bernhardt, T.G.1
Roof, W.D.2
Young, R.3
-
31
-
-
33749624883
-
Interaction of the transmembrane domain of lysis protein E from bacteriophage {phi}X174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD
-
Mendel S., Holbourn J.M., Schouten J.A., and Bugg T.D. Interaction of the transmembrane domain of lysis protein E from bacteriophage {phi}X174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD. Microbiology 152 (2006) 2959-2967
-
(2006)
Microbiology
, vol.152
, pp. 2959-2967
-
-
Mendel, S.1
Holbourn, J.M.2
Schouten, J.A.3
Bugg, T.D.4
-
32
-
-
0028070767
-
slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases
-
Roof W.D., Horne S.M., Young K.D., and Young R. slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases. J. Biol. Chem. 269 (1994) 2902-2910
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 2902-2910
-
-
Roof, W.D.1
Horne, S.M.2
Young, K.D.3
Young, R.4
-
33
-
-
15744391209
-
A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway
-
Zhang J.W., Butland G., Greenblatt J.F., Emili A., and Zamble D.B. A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway. J. Biol. Chem. 280 (2005) 4360-4366
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 4360-4366
-
-
Zhang, J.W.1
Butland, G.2
Greenblatt, J.F.3
Emili, A.4
Zamble, D.B.5
-
34
-
-
0026800935
-
Bacteriophage lysis: mechanism and regulation
-
Young R. Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56 (1992) 430-481
-
(1992)
Microbiol. Rev.
, vol.56
, pp. 430-481
-
-
Young, R.1
-
35
-
-
0027934203
-
An Escherichia coli protein consisting of a domain homologous to FK506- binding proteins (FKBP) and a new metal binding motif
-
Wülfing C., Lombardero J., and Plückthun A. An Escherichia coli protein consisting of a domain homologous to FK506- binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem. 269 (1994) 2895-2901
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 2895-2901
-
-
Wülfing, C.1
Lombardero, J.2
Plückthun, A.3
-
36
-
-
0034681154
-
FK506 binding protein from a thermophilic archaeon, methanococcus thermolithotrophicus, has chaperone-like activity in vitro
-
Furutani M., Ideno A., Iida T., and Maruyama T. FK506 binding protein from a thermophilic archaeon, methanococcus thermolithotrophicus, has chaperone-like activity in vitro. Biochemistry 39 (2000) 453-462
-
(2000)
Biochemistry
, vol.39
, pp. 453-462
-
-
Furutani, M.1
Ideno, A.2
Iida, T.3
Maruyama, T.4
-
37
-
-
0037449135
-
Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities
-
Suzuki R., Nagata K., Yumoto F., Kawakami M., Nemoto N., Furutani M., et al. Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities. J. Mol. Biol. 328 (2003) 1149-1160
-
(2003)
J. Mol. Biol.
, vol.328
, pp. 1149-1160
-
-
Suzuki, R.1
Nagata, K.2
Yumoto, F.3
Kawakami, M.4
Nemoto, N.5
Furutani, M.6
-
38
-
-
0031572824
-
A protease-free assay for peptidyl-prolyl cis/trans isomerases using standard peptide substrates
-
Janowski B., Wöllner S., Schutkowski M., and Fischer G. A protease-free assay for peptidyl-prolyl cis/trans isomerases using standard peptide substrates. Anal. Biochem. 252 (1997) 293-307
-
(1997)
Anal. Biochem.
, vol.252
, pp. 293-307
-
-
Janowski, B.1
Wöllner, S.2
Schutkowski, M.3
Fischer, G.4
-
39
-
-
11844279155
-
Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules
-
Scholz C., Schaarschmidt P., Engel A.M., Andres H., Schmitt U., Faatz E., et al. Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules. J. Mol. Biol. 345 (2005) 1229-1241
-
(2005)
J. Mol. Biol.
, vol.345
, pp. 1229-1241
-
-
Scholz, C.1
Schaarschmidt, P.2
Engel, A.M.3
Andres, H.4
Schmitt, U.5
Faatz, E.6
-
40
-
-
0026760365
-
Enzymatic catalysis of prolyl isomerization in an unfolding protein
-
Mücke M., and Schmid F.X. Enzymatic catalysis of prolyl isomerization in an unfolding protein. Biochemistry 31 (1992) 7848-7854
-
(1992)
Biochemistry
, vol.31
, pp. 7848-7854
-
-
Mücke, M.1
Schmid, F.X.2
-
41
-
-
0028606121
-
Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds
-
Mücke M., and Schmid F.X. Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry 33 (1994) 14608-14619
-
(1994)
Biochemistry
, vol.33
, pp. 14608-14619
-
-
Mücke, M.1
Schmid, F.X.2
-
42
-
-
22144469126
-
Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study
-
Spencer D.S., Xu K., Logan T.M., and Zhou H.X. Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study. J. Mol. Biol. 351 (2005) 219-232
-
(2005)
J. Mol. Biol.
, vol.351
, pp. 219-232
-
-
Spencer, D.S.1
Xu, K.2
Logan, T.M.3
Zhou, H.X.4
-
43
-
-
0030801864
-
Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR
-
Zhang Z., Li W., Logan T.M., Li M., and Marshall A.G. Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR. Protein Sci. 6 (1997) 2203-2217
-
(1997)
Protein Sci.
, vol.6
, pp. 2203-2217
-
-
Zhang, Z.1
Li, W.2
Logan, T.M.3
Li, M.4
Marshall, A.G.5
-
44
-
-
0041743073
-
Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization
-
Russo A.T., Rosgen J., and Bolen D.W. Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization. J. Mol. Biol. 330 (2003) 851-866
-
(2003)
J. Mol. Biol.
, vol.330
, pp. 851-866
-
-
Russo, A.T.1
Rosgen, J.2
Bolen, D.W.3
-
45
-
-
0027522740
-
Equilibrium denaturation of recombinant human FK binding protein in urea
-
Egan D.A., Logan T.M., Liang H., Matayoshi E., Fesik S.W., and Holzman T.F. Equilibrium denaturation of recombinant human FK binding protein in urea. Biochemistry 32 (1993) 1920-1927
-
(1993)
Biochemistry
, vol.32
, pp. 1920-1927
-
-
Egan, D.A.1
Logan, T.M.2
Liang, H.3
Matayoshi, E.4
Fesik, S.W.5
Holzman, T.F.6
-
46
-
-
0025311245
-
Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding
-
Kiefhaber T., Grunert H.P., Hahn U., and Schmid F.X. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry 29 (1990) 6475-6480
-
(1990)
Biochemistry
, vol.29
, pp. 6475-6480
-
-
Kiefhaber, T.1
Grunert, H.P.2
Hahn, U.3
Schmid, F.X.4
-
47
-
-
0029868655
-
Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique
-
Mayr L.M., Odefey C., Schutkowski M., and Schmid F.X. Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry 35 (1996) 5550-5561
-
(1996)
Biochemistry
, vol.35
, pp. 5550-5561
-
-
Mayr, L.M.1
Odefey, C.2
Schutkowski, M.3
Schmid, F.X.4
-
48
-
-
0025868143
-
Determination of kinetic constants for peptidyl prolyl cis- trans isomerases by an improved spectrophotometric assay
-
Kofron J.L., Kuzmic P., Kishore V., Colonbonilla E., and Rich D.H. Determination of kinetic constants for peptidyl prolyl cis- trans isomerases by an improved spectrophotometric assay. Biochemistry 30 (1991) 6127-6134
-
(1991)
Biochemistry
, vol.30
, pp. 6127-6134
-
-
Kofron, J.L.1
Kuzmic, P.2
Kishore, V.3
Colonbonilla, E.4
Rich, D.H.5
-
49
-
-
0025373627
-
Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes
-
Harrison R.K., and Stein R.L. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry 29 (1990) 3813-3816
-
(1990)
Biochemistry
, vol.29
, pp. 3813-3816
-
-
Harrison, R.K.1
Stein, R.L.2
-
50
-
-
11944257991
-
Mechanistic studies of enzymic and nonenzymic prolyl cis- trans isomerization
-
Harrison R.K., and Stein R.L. Mechanistic studies of enzymic and nonenzymic prolyl cis- trans isomerization. J. Am. Chem. Soc. 114 (1992) 3464-3471
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 3464-3471
-
-
Harrison, R.K.1
Stein, R.L.2
-
51
-
-
0025727072
-
GroE facilitates refolding of citrate synthase by suppressing aggregation
-
Buchner J., Schmidt M., Fuchs M., Jaenicke R., Rudolph R., Schmid F.X., and Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30 (1991) 1586-1591
-
(1991)
Biochemistry
, vol.30
, pp. 1586-1591
-
-
Buchner, J.1
Schmidt, M.2
Fuchs, M.3
Jaenicke, R.4
Rudolph, R.5
Schmid, F.X.6
Kiefhaber, T.7
-
52
-
-
0031943566
-
Analysis of chaperone function using citrate synthase as nonnative substrate protein
-
Buchner J., Grallert H., and Jakob U. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 290 (1998) 323-338
-
(1998)
Methods Enzymol.
, vol.290
, pp. 323-338
-
-
Buchner, J.1
Grallert, H.2
Jakob, U.3
-
53
-
-
0023387587
-
Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form
-
Crooke E., and Wickner W. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc. Natl Acad. Sci. USA 84 (1987) 5216-5220
-
(1987)
Proc. Natl Acad. Sci. USA
, vol.84
, pp. 5216-5220
-
-
Crooke, E.1
Wickner, W.2
-
54
-
-
0031554922
-
Modular structure of the trigger factor required for high activity in protein folding
-
Zarnt T., Tradler T., Stoller G., Scholz C., Schmid F.X., and Fischer G. Modular structure of the trigger factor required for high activity in protein folding. J. Mol. Biol. 271 (1997) 827-837
-
(1997)
J. Mol. Biol.
, vol.271
, pp. 827-837
-
-
Zarnt, T.1
Tradler, T.2
Stoller, G.3
Scholz, C.4
Schmid, F.X.5
Fischer, G.6
-
55
-
-
4944246094
-
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
-
Ferbitz L., Maier T., Patzelt H., Bukau B., Deuerling E., and Ban N. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431 (2004) 590-596
-
(2004)
Nature
, vol.431
, pp. 590-596
-
-
Ferbitz, L.1
Maier, T.2
Patzelt, H.3
Bukau, B.4
Deuerling, E.5
Ban, N.6
-
56
-
-
0029765609
-
New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
-
Missiakas D., Betton J.M., and Raina S. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol.Microbiol. 21 (1996) 871-884
-
(1996)
Mol.Microbiol.
, vol.21
, pp. 871-884
-
-
Missiakas, D.1
Betton, J.M.2
Raina, S.3
-
57
-
-
4544245760
-
The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae
-
Ludlam A.V., Moore B.A., and Xu Z. The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae. Proc. Natl Acad. Sci. USA 101 (2004) 13436-13441
-
(2004)
Proc. Natl Acad. Sci. USA
, vol.101
, pp. 13436-13441
-
-
Ludlam, A.V.1
Moore, B.A.2
Xu, Z.3
-
58
-
-
0034862888
-
Crystal structure of Mip, a prolylisomerase from Legionella pneumophila
-
Riboldi-Tunnicliffe A., Konig B., Jessen S., Weiss M.S., Rahfeld J., Hacker J., et al. Crystal structure of Mip, a prolylisomerase from Legionella pneumophila. Nature Struct. Biol. 8 (2001) 779-783
-
(2001)
Nature Struct. Biol.
, vol.8
, pp. 779-783
-
-
Riboldi-Tunnicliffe, A.1
Konig, B.2
Jessen, S.3
Weiss, M.S.4
Rahfeld, J.5
Hacker, J.6
-
59
-
-
0034048647
-
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
-
McCarthy A.A., Haebel P.W., Torronen A., Rybin V., Baker E.N., and Metcalf P. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nature Struct. Biol. 7 (2000) 196-199
-
(2000)
Nature Struct. Biol.
, vol.7
, pp. 196-199
-
-
McCarthy, A.A.1
Haebel, P.W.2
Torronen, A.3
Rybin, V.4
Baker, E.N.5
Metcalf, P.6
-
60
-
-
2942669907
-
Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
-
Heras B., Edeling M.A., Schirra H.J., Raina S., and Martin J.L. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. Proc. Natl Acad. Sci. USA 101 (2004) 8876-8881
-
(2004)
Proc. Natl Acad. Sci. USA
, vol.101
, pp. 8876-8881
-
-
Heras, B.1
Edeling, M.A.2
Schirra, H.J.3
Raina, S.4
Martin, J.L.5
-
61
-
-
30344444015
-
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
-
Tian G., Xiang S., Noiva R., Lennarz W.J., and Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124 (2006) 61-73
-
(2006)
Cell
, vol.124
, pp. 61-73
-
-
Tian, G.1
Xiang, S.2
Noiva, R.3
Lennarz, W.J.4
Schindelin, H.5
-
64
-
-
0024448151
-
Calculation of protein extinction coefficients from amino acid sequence data
-
Gill S.C., and von Hippel P.H. 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
-
65
-
-
0028871804
-
How to measure and predict the molar absorption coefficient of a protein
-
Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
-
(1995)
Protein Sci.
, vol.4
, pp. 2411-2423
-
-
Pace, C.N.1
Vajdos, F.2
Fee, L.3
Grimsley, G.4
Gray, T.5
-
66
-
-
0042121237
-
Multiple sequence alignment with the Clustal series of programs
-
Chenna R., Sugawara H., Koike T., Lopez R., Gibson T.J., Higgins D.G., and Thompson J.D. Multiple sequence alignment with the Clustal series of programs. Nucl. Acids Res. 31 (2003) 3497-3500
-
(2003)
Nucl. Acids Res.
, vol.31
, pp. 3497-3500
-
-
Chenna, R.1
Sugawara, H.2
Koike, T.3
Lopez, R.4
Gibson, T.J.5
Higgins, D.G.6
Thompson, J.D.7
-
67
-
-
0027439390
-
Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
-
Van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., and Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229 (1993) 105-124
-
(1993)
J. Mol. Biol.
, vol.229
, pp. 105-124
-
-
Van Duyne, G.D.1
Standaert, R.F.2
Karplus, P.A.3
Schreiber, S.L.4
Clardy, J.5
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