-
1
-
-
0030830073
-
A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
-
Andersen C.L., Matthey-Dupraz A., Missiakas D., and Raina S. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol. Microbiol. 26 (1997) 121-132
-
(1997)
Mol. Microbiol.
, vol.26
, pp. 121-132
-
-
Andersen, C.L.1
Matthey-Dupraz, A.2
Missiakas, D.3
Raina, S.4
-
2
-
-
0033597878
-
Oxidative protein folding is driven by the electron transport system
-
Bader M., Muse W., Ballou D.P., Gassner C., and Bardwell J.C. Oxidative protein folding is driven by the electron transport system. Cell 98 (1999) 217-227
-
(1999)
Cell
, vol.98
, pp. 217-227
-
-
Bader, M.1
Muse, W.2
Ballou, D.P.3
Gassner, C.4
Bardwell, J.C.5
-
3
-
-
0035794534
-
Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA
-
Bader M.W., Hiniker A., Regeimbal J., Goldstone D., Haebel P.W., Riemer J., et al. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. Embo J. 20 (2001) 1555-1562
-
(2001)
Embo J.
, vol.20
, pp. 1555-1562
-
-
Bader, M.W.1
Hiniker, A.2
Regeimbal, J.3
Goldstone, D.4
Haebel, P.W.5
Riemer, J.6
-
4
-
-
0034714289
-
Disulfide bonds are generated by quinone reduction
-
Bader M.W., Xie T., Yu C.A., and Bardwell J.C. Disulfide bonds are generated by quinone reduction. J. Biol. Chem. 275 (2000) 26082-26088
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 26082-26088
-
-
Bader, M.W.1
Xie, T.2
Yu, C.A.3
Bardwell, J.C.4
-
5
-
-
0027475212
-
A pathway for disulfide bond formation in vivo
-
Bardwell J.C., Lee J.O., Jander G., Martin N., Belin D., and Beckwith J. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 1038-1042
-
(1993)
Proc. Natl. Acad. Sci. U.S.A.
, vol.90
, pp. 1038-1042
-
-
Bardwell, J.C.1
Lee, J.O.2
Jander, G.3
Martin, N.4
Belin, D.5
Beckwith, J.6
-
6
-
-
0026091179
-
Identification of a protein required for disulfide bond formation in vivo
-
Bardwell J.C., McGovern K., and Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 67 (1991) 581-589
-
(1991)
Cell
, vol.67
, pp. 581-589
-
-
Bardwell, J.C.1
McGovern, K.2
Beckwith, J.3
-
7
-
-
15744375548
-
The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase DsbC
-
Berkmen M., Boyd D., and Beckwith J. The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase DsbC. J. Biol. Chem. 280 (2005) 11387-11394
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 11387-11394
-
-
Berkmen, M.1
Boyd, D.2
Beckwith, J.3
-
8
-
-
0033583239
-
In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
-
Bessette P.H., Cotto J.J., Gilbert H.F., and Georgiou G. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J. Biol. Chem. 274 (1999) 7784-7792
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 7784-7792
-
-
Bessette, P.H.1
Cotto, J.J.2
Gilbert, H.F.3
Georgiou, G.4
-
9
-
-
0024066065
-
The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
-
Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., et al. The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. Embo J. 7 (1988) 2593-2599
-
(1988)
Embo J.
, vol.7
, pp. 2593-2599
-
-
Bode, W.1
Engh, R.2
Musil, D.3
Thiele, U.4
Huber, R.5
Karshikov, A.6
-
10
-
-
0033767925
-
Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
-
Carmel-Harel O., and Storz G. Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54 (2000) 439-461
-
(2000)
Annu. Rev. Microbiol.
, vol.54
, pp. 439-461
-
-
Carmel-Harel, O.1
Storz, G.2
-
11
-
-
0033538564
-
Chaperone activity of DsbC
-
Chen J., Song J.L., Zhang S., Wang Y., Cui D.F., and Wang C.C. Chaperone activity of DsbC. J. Biol. Chem. 274 (1999) 19601-19605
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 19601-19605
-
-
Chen, J.1
Song, J.L.2
Zhang, S.3
Wang, Y.4
Cui, D.F.5
Wang, C.C.6
-
12
-
-
0027155577
-
Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
-
Clarke J., and Fersht A.R. Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation. Biochemistry 32 (1993) 4322-4329
-
(1993)
Biochemistry
, vol.32
, pp. 4322-4329
-
-
Clarke, J.1
Fersht, A.R.2
-
13
-
-
22244473019
-
The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant
-
Collet J.F., Peisach D., Bardwell J.C., and Xu Z. The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant. Protein Sci. 14 (2005) 1863-1869
-
(2005)
Protein Sci.
, vol.14
, pp. 1863-1869
-
-
Collet, J.F.1
Peisach, D.2
Bardwell, J.C.3
Xu, Z.4
-
15
-
-
0034612337
-
Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex
-
Couprie J., Vinci F., Dugave C., Qu E., and Moutiez M. Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex. Biochemistry 39 (2000) 6732-6742
-
(2000)
Biochemistry
, vol.39
, pp. 6732-6742
-
-
Couprie, J.1
Vinci, F.2
Dugave, C.3
Qu, E.4
Moutiez, M.5
-
16
-
-
0027446271
-
Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
-
Dailey F.E., and Berg H.C. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 1043-1047
-
(1993)
Proc. Natl. Acad. Sci. U.S.A.
, vol.90
, pp. 1043-1047
-
-
Dailey, F.E.1
Berg, H.C.2
-
17
-
-
0020855355
-
Hydrogen exchange and structural dynamics of proteins and nucleic acids
-
Englander S.W., and Kallenbach N.R. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quart. Rev. Biophys. 16 (1983) 521-655
-
(1983)
Quart. Rev. Biophys.
, vol.16
, pp. 521-655
-
-
Englander, S.W.1
Kallenbach, N.R.2
-
18
-
-
0028965483
-
Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12
-
Fong S.T., Camakaris J., and Lee B.T. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol. Microbiol. 15 (1995) 1127-1137
-
(1995)
Mol. Microbiol.
, vol.15
, pp. 1127-1137
-
-
Fong, S.T.1
Camakaris, J.2
Lee, B.T.3
-
19
-
-
0037018912
-
Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD
-
Goulding C.W., Sawaya M.R., Parseghian A., Lim V., Eisenberg D., and Missiakas D. Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD. Biochemistry 41 (2002) 6920-6927
-
(2002)
Biochemistry
, vol.41
, pp. 6920-6927
-
-
Goulding, C.W.1
Sawaya, M.R.2
Parseghian, A.3
Lim, V.4
Eisenberg, D.5
Missiakas, D.6
-
20
-
-
0042815104
-
Mechanism of the electron transfer catalyst DsbB from Escherichia coli
-
Grauschopf U., Fritz A., and Glockshuber R. Mechanism of the electron transfer catalyst DsbB from Escherichia coli. Embo J. 22 (2003) 3503-3513
-
(2003)
Embo J.
, vol.22
, pp. 3503-3513
-
-
Grauschopf, U.1
Fritz, A.2
Glockshuber, R.3
-
21
-
-
0032526690
-
Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization
-
Guddat L.W., Bardwell J.C., and Martin J.L. Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization. Structure 6 (1998) 757-767
-
(1998)
Structure
, vol.6
, pp. 757-767
-
-
Guddat, L.W.1
Bardwell, J.C.2
Martin, J.L.3
-
22
-
-
0031010755
-
The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding
-
Guddat L.W., Bardwell J.C., Zander T., and Martin J.L. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Sci. 6 (1997) 1148-1156
-
(1997)
Protein Sci.
, vol.6
, pp. 1148-1156
-
-
Guddat, L.W.1
Bardwell, J.C.2
Zander, T.3
Martin, J.L.4
-
23
-
-
0037119945
-
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDalpha complex
-
Haebel P.W., Goldstone D., Katzen F., Beckwith J., and Metcalf P. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDalpha complex. Embo J. 21 (2002) 4774-4784
-
(2002)
Embo J.
, vol.21
, pp. 4774-4784
-
-
Haebel, P.W.1
Goldstone, D.2
Katzen, F.3
Beckwith, J.4
Metcalf, P.5
-
24
-
-
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. U.S.A. 101 (2004) 8876-8881
-
(2004)
Proc. Natl. Acad. Sci. U.S.A.
, vol.101
, pp. 8876-8881
-
-
Heras, B.1
Edeling, M.A.2
Schirra, H.J.3
Raina, S.4
Martin, J.L.5
-
25
-
-
1842477219
-
In vivo substrate specificity of periplasmic disulfide oxidoreductases
-
Hiniker A., and Bardwell J.C. In vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. 279 (2004) 12967-12973
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 12967-12973
-
-
Hiniker, A.1
Bardwell, J.C.2
-
26
-
-
26644437700
-
Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC
-
Hiniker A., Collet J.F., and Bardwell J.C. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem. 280 (2005) 33785-33791
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 33785-33791
-
-
Hiniker, A.1
Collet, J.F.2
Bardwell, J.C.3
-
27
-
-
0026698060
-
Oxidized redox state of glutathione in the endoplasmic reticulum
-
Hwang C., Sinskey A.J., and Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257 (1992) 1496-1502
-
(1992)
Science
, vol.257
, pp. 1496-1502
-
-
Hwang, C.1
Sinskey, A.J.2
Lodish, H.F.3
-
28
-
-
0037013828
-
Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade
-
Inaba K., and Ito K. Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. Embo J. 21 (2002) 2646-2654
-
(2002)
Embo J.
, vol.21
, pp. 2646-2654
-
-
Inaba, K.1
Ito, K.2
-
29
-
-
25444431826
-
Reactivities of quinone-free DsbB from Escherichia coli
-
Inaba K., Takahashi Y.H., and Ito K. Reactivities of quinone-free DsbB from Escherichia coli. J. Biol. Chem. 280 (2005) 33035-33044
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 33035-33044
-
-
Inaba, K.1
Takahashi, Y.H.2
Ito, K.3
-
30
-
-
0028154918
-
Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
-
Jander G., Martin N.L., and Beckwith J. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. Embo J. 13 (1994) 5121-5127
-
(1994)
Embo J.
, vol.13
, pp. 5121-5127
-
-
Jander, G.1
Martin, N.L.2
Beckwith, J.3
-
31
-
-
0030787850
-
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
-
Joly J.C., and Swartz J.R. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36 (1997) 10067-10072
-
(1997)
Biochemistry
, vol.36
, pp. 10067-10072
-
-
Joly, J.C.1
Swartz, J.R.2
-
32
-
-
0034718489
-
Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli
-
Kadokura H., Bader M., Tian H., Bardwell J.C., and Beckwith J. Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 10884-10889
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 10884-10889
-
-
Kadokura, H.1
Bader, M.2
Tian, H.3
Bardwell, J.C.4
Beckwith, J.5
-
34
-
-
1642556877
-
Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding
-
Kadokura H., Tian H., Zander T., Bardwell J.C., and Beckwith J. Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding. Science 303 (2004) 534-537
-
(2004)
Science
, vol.303
, pp. 534-537
-
-
Kadokura, H.1
Tian, H.2
Zander, T.3
Bardwell, J.C.4
Beckwith, J.5
-
35
-
-
0026567097
-
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
-
Kamitani S., Akiyama Y., and Ito K. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. Embo J. 11 (1992) 57-62
-
(1992)
Embo J.
, vol.11
, pp. 57-62
-
-
Kamitani, S.1
Akiyama, Y.2
Ito, K.3
-
36
-
-
0034703766
-
Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
-
Katzen F., and Beckwith J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103 (2000) 769-779
-
(2000)
Cell
, vol.103
, pp. 769-779
-
-
Katzen, F.1
Beckwith, J.2
-
37
-
-
0037716929
-
Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)
-
Kim J.H., Kim S.J., Jeong D.G., Son J.H., and Ryu S.E. Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1). FEBS Lett. 543 (2003) 164-169
-
(2003)
FEBS Lett.
, vol.543
, pp. 164-169
-
-
Kim, J.H.1
Kim, S.J.2
Jeong, D.G.3
Son, J.H.4
Ryu, S.E.5
-
39
-
-
14044257165
-
Protein thiol modifications visualized in vivo
-
Leichert L.I., and Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol. 2 (2004) e333
-
(2004)
PLoS Biol.
, vol.2
-
-
Leichert, L.I.1
Jakob, U.2
-
40
-
-
0035847099
-
Disulfide-dependent folding and export of Escherichia coli DsbC
-
Liu X., and Wang C.C. Disulfide-dependent folding and export of Escherichia coli DsbC. J. Biol. Chem. 276 (2001) 1146-1151
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 1146-1151
-
-
Liu, X.1
Wang, C.C.2
-
41
-
-
0027373949
-
Crystal structure of the DsbA protein required for disulphide bond formation in vivo
-
Martin J.L., Bardwell J.C., and Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365 (1993) 464-468
-
(1993)
Nature
, vol.365
, pp. 464-468
-
-
Martin, J.L.1
Bardwell, J.C.2
Kuriyan, J.3
-
42
-
-
1242284596
-
An engineered pathway for the formation of protein disulfide bonds
-
Masip L., Pan J.L., Haldar S., Penner-Hahn J.E., DeLisa M.P., Georgiou G., et al. An engineered pathway for the formation of protein disulfide bonds. Science 303 (2004) 1185-1189
-
(2004)
Science
, vol.303
, pp. 1185-1189
-
-
Masip, L.1
Pan, J.L.2
Haldar, S.3
Penner-Hahn, J.E.4
DeLisa, M.P.5
Georgiou, G.6
-
43
-
-
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. Nat. Struct. Biol. 7 (2000) 196-199
-
(2000)
Nat. 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
-
44
-
-
0027787823
-
The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
-
Mecsas J., Rouviere P.E., Erickson J.W., Donohue T.J., and Gross C.A. The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes Dev. 7 (1993) 2618-2628
-
(1993)
Genes Dev.
, vol.7
, pp. 2618-2628
-
-
Mecsas, J.1
Rouviere, P.E.2
Erickson, J.W.3
Donohue, T.J.4
Gross, C.A.5
-
45
-
-
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
-
46
-
-
0027291239
-
Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
-
Missiakas D., Georgopoulos C., and Raina S. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 7084-7088
-
(1993)
Proc. Natl. Acad. Sci. U.S.A.
, vol.90
, pp. 7084-7088
-
-
Missiakas, D.1
Georgopoulos, C.2
Raina, S.3
-
47
-
-
0028979629
-
Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
-
Missiakas D., Schwager F., and Raina S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. Embo J. 14 (1995) 3415-3424
-
(1995)
Embo J.
, vol.14
, pp. 3415-3424
-
-
Missiakas, D.1
Schwager, F.2
Raina, S.3
-
48
-
-
0032943018
-
On the non-respect of the thermodynamic cycle by DsbA variants
-
Moutiez M., Burova T.V., Haertle T., and Quemeneur E. On the non-respect of the thermodynamic cycle by DsbA variants. Protein Sci. 8 (1999) 106-112
-
(1999)
Protein Sci.
, vol.8
, pp. 106-112
-
-
Moutiez, M.1
Burova, T.V.2
Haertle, T.3
Quemeneur, E.4
-
49
-
-
0028360184
-
Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
-
Nelson J.W., and Creighton T.E. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33 (1994) 5974-5983
-
(1994)
Biochemistry
, vol.33
, pp. 5974-5983
-
-
Nelson, J.W.1
Creighton, T.E.2
-
50
-
-
0023661636
-
Protein engineering of subtilisin BPN′: Enhanced stabilization through the introduction of two cysteines to form a disulfide bond
-
Pantoliano M.W., Ladner R.C., Bryan P.N., Rollence M.L., Wood J.F., and Poulos T.L. Protein engineering of subtilisin BPN′: Enhanced stabilization through the introduction of two cysteines to form a disulfide bond. Biochemistry 26 (1987) 2077-2082
-
(1987)
Biochemistry
, vol.26
, pp. 2077-2082
-
-
Pantoliano, M.W.1
Ladner, R.C.2
Bryan, P.N.3
Rollence, M.L.4
Wood, J.F.5
Poulos, T.L.6
-
51
-
-
0037031882
-
DsbB catalyzes disulfide bond formation de novo
-
Regeimbal J., and Bardwell J.C. DsbB catalyzes disulfide bond formation de novo. J. Biol. Chem. 277 (2002) 32706-32713
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 32706-32713
-
-
Regeimbal, J.1
Bardwell, J.C.2
-
52
-
-
0345133346
-
Disulfide bond formation involves a quinhydrone-type charge-transfer complex
-
Regeimbal J., Gleiter S., Trumpower B.L., Yu C.A., Diwakar M., Ballou D.P., et al. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 13779-13784
-
(2003)
Proc. Natl. Acad. Sci. U.S.A.
, vol.100
, pp. 13779-13784
-
-
Regeimbal, J.1
Gleiter, S.2
Trumpower, B.L.3
Yu, C.A.4
Diwakar, M.5
Ballou, D.P.6
-
53
-
-
0030668672
-
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
-
Rietsch A., Bessette P., Georgiou G., and Beckwith J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179 (1997) 6602-6608
-
(1997)
J. Bacteriol.
, vol.179
, pp. 6602-6608
-
-
Rietsch, A.1
Bessette, P.2
Georgiou, G.3
Beckwith, J.4
-
54
-
-
2442607486
-
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD
-
Rozhkova A., Stirnimann C.U., Frei P., Grauschopf U., Brunisholz R., Grutter M.G., et al. Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. Embo J. 23 (2004) 1709-1719
-
(2004)
Embo J.
, vol.23
, pp. 1709-1719
-
-
Rozhkova, A.1
Stirnimann, C.U.2
Frei, P.3
Grauschopf, U.4
Brunisholz, R.5
Grutter, M.G.6
-
55
-
-
0032485920
-
Structure of reduced DsbA from Escherichia coli in solution
-
Schirra H.J., Renner C., Czisch M., Huber-Wunderlich M., Holak T.A., and Glockshuber R. Structure of reduced DsbA from Escherichia coli in solution. Biochemistry 37 (1998) 6263-6276
-
(1998)
Biochemistry
, vol.37
, pp. 6263-6276
-
-
Schirra, H.J.1
Renner, C.2
Czisch, M.3
Huber-Wunderlich, M.4
Holak, T.A.5
Glockshuber, R.6
-
56
-
-
3042709650
-
Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways
-
Segatori L., Paukstelis P.J., Gilbert H.F., and Georgiou G. Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 10018-10023
-
(2004)
Proc. Natl. Acad. Sci. U.S.A.
, vol.101
, pp. 10018-10023
-
-
Segatori, L.1
Paukstelis, P.J.2
Gilbert, H.F.3
Georgiou, G.4
-
57
-
-
22444432755
-
The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases
-
Sevier C.S., Kadokura H., Tam V.C., Beckwith J., Fass D., and Kaiser C.A. The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Sci. 14 (2005) 1630-1642
-
(2005)
Protein Sci.
, vol.14
, pp. 1630-1642
-
-
Sevier, C.S.1
Kadokura, H.2
Tam, V.C.3
Beckwith, J.4
Fass, D.5
Kaiser, C.A.6
-
58
-
-
0036842559
-
Formation and transfer of disulphide bonds in living cells
-
Sevier C.S., and Kaiser C.A. Formation and transfer of disulphide bonds in living cells. Nat. Rev. Mol. Cell Biol. 3 (2002) 836-847
-
(2002)
Nat. Rev. Mol. Cell Biol.
, vol.3
, pp. 836-847
-
-
Sevier, C.S.1
Kaiser, C.A.2
-
59
-
-
0034607656
-
DsbG, a protein disulfide isomerase with chaperone activity
-
Shao F., Bader M.W., Jakob U., and Bardwell J.C. DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 275 (2000) 13349-13352
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 13349-13352
-
-
Shao, F.1
Bader, M.W.2
Jakob, U.3
Bardwell, J.C.4
-
60
-
-
0030220763
-
Engineering enzymes for stability
-
Shaw A., and Bott R. Engineering enzymes for stability. Curr. Opin. Struct. Biol. 6 (1996) 546-550
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 546-550
-
-
Shaw, A.1
Bott, R.2
-
61
-
-
0028215226
-
Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
-
Shevchik V.E., Condemine G., and Robert-Baudouy J. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. Embo J. 13 (1994) 2007-2012
-
(1994)
Embo J.
, vol.13
, pp. 2007-2012
-
-
Shevchik, V.E.1
Condemine, G.2
Robert-Baudouy, J.3
-
62
-
-
0032900848
-
Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+
-
Stafford S.J., Humphreys D.P., and Lund P.A. Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+. FEMS Microbiol. Lett. 174 (1999) 179-184
-
(1999)
FEMS Microbiol. Lett.
, vol.174
, pp. 179-184
-
-
Stafford, S.J.1
Humphreys, D.P.2
Lund, P.A.3
-
63
-
-
0033230589
-
Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
-
Stewart E.J., Katzen F., and Beckwith J. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. Embo J. 18 (1999) 5963-5971
-
(1999)
Embo J.
, vol.18
, pp. 5963-5971
-
-
Stewart, E.J.1
Katzen, F.2
Beckwith, J.3
-
64
-
-
21744448514
-
Structural basis and kinetics of DsbD-dependent cytochrome c maturation
-
Stirnimann C.U., Rozhkova A., Grauschopf U., Grutter M.G., Glockshuber R., and Capitani G. Structural basis and kinetics of DsbD-dependent cytochrome c maturation. Structure (Cambridge) 13 (2005) 985-993
-
(2005)
Structure (Cambridge)
, vol.13
, pp. 985-993
-
-
Stirnimann, C.U.1
Rozhkova, A.2
Grauschopf, U.3
Grutter, M.G.4
Glockshuber, R.5
Capitani, G.6
-
65
-
-
0034725691
-
The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC
-
Sun X.X., and Wang C.C. The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC. J. Biol. Chem. 275 (2000) 22743-22749
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 22743-22749
-
-
Sun, X.X.1
Wang, C.C.2
-
66
-
-
8744256714
-
Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli
-
Takahashi Y.H., Inaba K., and Ito K. Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. J. Biol. Chem. 279 (2004) 47057-47065
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 47057-47065
-
-
Takahashi, Y.H.1
Inaba, K.2
Ito, K.3
-
67
-
-
14544306637
-
Mutational analysis of the disulfide catalysts DsbA and DsbB
-
Tan J., Lu Y., and Bardwell J.C. Mutational analysis of the disulfide catalysts DsbA and DsbB. J. Bacteriol. 187 (2005) 1504-1510
-
(2005)
J. Bacteriol.
, vol.187
, pp. 1504-1510
-
-
Tan, J.1
Lu, Y.2
Bardwell, J.C.3
-
68
-
-
0036671471
-
Cytochrome c maturation: A complex pathway for a simple task?
-
Thony-Meyer L. Cytochrome c maturation: A complex pathway for a simple task?. Biochem. Soc. Trans. 30 (2002) 633-638
-
(2002)
Biochem. Soc. Trans.
, vol.30
, pp. 633-638
-
-
Thony-Meyer, L.1
-
69
-
-
0032577637
-
The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli
-
van Straaten M., Missiakas D., Raina S., and Darby N.J. The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli. FEBS Lett. 428 (1998) 255-258
-
(1998)
FEBS Lett.
, vol.428
, pp. 255-258
-
-
van Straaten, M.1
Missiakas, D.2
Raina, S.3
Darby, N.J.4
-
70
-
-
0036084052
-
Description of the topographical changes associated to the different stages of the DsbA catalytic cycle
-
Vinci F., Couprie J., Pucci P., Quemeneur E., and Moutiez M. Description of the topographical changes associated to the different stages of the DsbA catalytic cycle. Protein Sci. 11 (2002) 1600-1612
-
(2002)
Protein Sci.
, vol.11
, pp. 1600-1612
-
-
Vinci, F.1
Couprie, J.2
Pucci, P.3
Quemeneur, E.4
Moutiez, M.5
-
71
-
-
0037127202
-
Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B
-
Xie T., Yu L., Bader M.W., Bardwell J.C., and Yu C.A. Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. J. Biol. Chem. 277 (2002) 1649-1652
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 1649-1652
-
-
Xie, T.1
Yu, L.2
Bader, M.W.3
Bardwell, J.C.4
Yu, C.A.5
-
72
-
-
0027254133
-
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
-
Zapun A., Bardwell J.C., and Creighton T.E. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32 (1993) 5083-5092
-
(1993)
Biochemistry
, vol.32
, pp. 5083-5092
-
-
Zapun, A.1
Bardwell, J.C.2
Creighton, T.E.3
-
73
-
-
0028949156
-
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
-
Zapun A., Missiakas D., Raina S., and Creighton T.E. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34 (1995) 5075-5089
-
(1995)
Biochemistry
, vol.34
, pp. 5075-5089
-
-
Zapun, A.1
Missiakas, D.2
Raina, S.3
Creighton, T.E.4
-
74
-
-
0242353305
-
Dimerization by domain hybridization bestows chaperone and isomerase activities
-
Zhao Z., Peng Y., Hao S.F., Zeng Z.H., and Wang C.C. Dimerization by domain hybridization bestows chaperone and isomerase activities. J. Biol. Chem. 278 (2003) 43292-43298
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 43292-43298
-
-
Zhao, Z.1
Peng, Y.2
Hao, S.F.3
Zeng, Z.H.4
Wang, C.C.5
|