-
1
-
-
34547595514
-
Meningitis epidemics in Africa: a brief overview
-
Teyssou R., and Muros-Le Rouzic E. Meningitis epidemics in Africa: a brief overview. Vaccine 25 (2007) A3-A7
-
(2007)
Vaccine
, vol.25
-
-
Teyssou, R.1
Muros-Le Rouzic, E.2
-
2
-
-
0034051214
-
Epidemiology and pathogenesis of Neisseria meningitidis
-
Tzeng Y.L., and Stephens D.S. Epidemiology and pathogenesis of Neisseria meningitidis. Microbes Infect. 2 (2000) 687-700
-
(2000)
Microbes Infect.
, vol.2
, pp. 687-700
-
-
Tzeng, Y.L.1
Stephens, D.S.2
-
3
-
-
60749109471
-
DSB proteins and bacterial pathogenicity
-
Heras B., Shouldice S.R., Totsika M., Scanlon M.J., Schembri M.A., and Martin J.L. DSB proteins and bacterial pathogenicity. Nat. Rev. Microbiol. 7 (2009) 215-225
-
(2009)
Nat. Rev. Microbiol.
, vol.7
, pp. 215-225
-
-
Heras, B.1
Shouldice, S.R.2
Totsika, M.3
Scanlon, M.J.4
Schembri, M.A.5
Martin, J.L.6
-
4
-
-
49549119981
-
The disulfide bond formation (Dsb) system
-
Ito K., and Inaba K. The disulfide bond formation (Dsb) system. Curr. Opin. Struct. Biol. 18 (2008) 450-458
-
(2008)
Curr. Opin. Struct. Biol.
, vol.18
, pp. 450-458
-
-
Ito, K.1
Inaba, K.2
-
5
-
-
0034629478
-
Complete genome sequence of Neisseria meningitidis serogroup B strain MC58
-
Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., Eisen J.A., et al. Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. Science 287 (2000) 1809-1815
-
(2000)
Science
, vol.287
, pp. 1809-1815
-
-
Tettelin, H.1
Saunders, N.J.2
Heidelberg, J.3
Jeffries, A.C.4
Nelson, K.E.5
Eisen, J.A.6
-
6
-
-
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
-
7
-
-
0028953741
-
Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
-
Darby N.J., and Creighton T.E. Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry 34 (1995) 3576-3587
-
(1995)
Biochemistry
, vol.34
, pp. 3576-3587
-
-
Darby, N.J.1
Creighton, T.E.2
-
8
-
-
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
-
9
-
-
0032871341
-
DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia pestis
-
Jackson M.W., and Plano G.V. DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia pestis. J. Bacteriol. 181 (1999) 5126-5130
-
(1999)
J. Bacteriol.
, vol.181
, pp. 5126-5130
-
-
Jackson, M.W.1
Plano, G.V.2
-
10
-
-
0029025060
-
Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells
-
Watarai M., Tobe T., Yoshikawa M., and Sasakawa C. Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells. Proc. Natl Acad. Sci. USA 92 (1995) 4927-4931
-
(1995)
Proc. Natl Acad. Sci. USA
, vol.92
, pp. 4927-4931
-
-
Watarai, M.1
Tobe, T.2
Yoshikawa, M.3
Sasakawa, C.4
-
11
-
-
0026668342
-
Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae
-
Peek J.A., and Taylor R.K. Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc. Natl Acad. Sci. USA 89 (1992) 6210-6214
-
(1992)
Proc. Natl Acad. Sci. USA
, vol.89
, pp. 6210-6214
-
-
Peek, J.A.1
Taylor, R.K.2
-
12
-
-
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. USA 90 (1993) 1043-1047
-
(1993)
Proc. Natl Acad. Sci. USA
, vol.90
, pp. 1043-1047
-
-
Dailey, F.E.1
Berg, H.C.2
-
13
-
-
3042695340
-
Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili
-
Tinsley C.R., Voulhoux R., Beretti J.L., Tommassen J., and Nassif X. Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili. J. Biol. Chem. 279 (2004) 27078-27087
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 27078-27087
-
-
Tinsley, C.R.1
Voulhoux, R.2
Beretti, J.L.3
Tommassen, J.4
Nassif, X.5
-
14
-
-
0034062859
-
Molecular and biological analysis of eight genetic islands that distinguish Neisseria meningitidis from the closely related pathogen Neisseria gonorrhoeae
-
Klee S.R., Nassif X., Kusecek B., Merker P., Beretti J.L., Achtman M., and Tinsley C.R. Molecular and biological analysis of eight genetic islands that distinguish Neisseria meningitidis from the closely related pathogen Neisseria gonorrhoeae. Infect. Immun. 68 (2000) 2082-2095
-
(2000)
Infect. Immun.
, vol.68
, pp. 2082-2095
-
-
Klee, S.R.1
Nassif, X.2
Kusecek, B.3
Merker, P.4
Beretti, J.L.5
Achtman, M.6
Tinsley, C.R.7
-
15
-
-
4844227315
-
Functional diversity of three different DsbA proteins from Neisseria meningitidis
-
Sinha S., Langford P.R., and Kroll J.S. Functional diversity of three different DsbA proteins from Neisseria meningitidis. Microbiology 150 (2004) 2993-3000
-
(2004)
Microbiology
, vol.150
, pp. 2993-3000
-
-
Sinha, S.1
Langford, P.R.2
Kroll, J.S.3
-
16
-
-
0037309117
-
Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae
-
Bouwman C.W., Kohli M., Killoran A., Touchie G.A., Kadner R.J., and Martin N.L. Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae. J. Bacteriol. 185 (2003) 991-1000
-
(2003)
J. Bacteriol.
, vol.185
, pp. 991-1000
-
-
Bouwman, C.W.1
Kohli, M.2
Killoran, A.3
Touchie, G.A.4
Kadner, R.J.5
Martin, N.L.6
-
17
-
-
38849185996
-
Reduced DNA binding and uptake in the absence of DsbA1 and DsbA2 of Neisseria meningitidis due to inefficient folding of the outer-membrane secretin PilQ
-
Sinha S., Ambur O.H., Langford P.R., Tonjum T., and Kroll J.S. Reduced DNA binding and uptake in the absence of DsbA1 and DsbA2 of Neisseria meningitidis due to inefficient folding of the outer-membrane secretin PilQ. Microbiology 154 (2008) 217-225
-
(2008)
Microbiology
, vol.154
, pp. 217-225
-
-
Sinha, S.1
Ambur, O.H.2
Langford, P.R.3
Tonjum, T.4
Kroll, J.S.5
-
18
-
-
57749094216
-
Structural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidis
-
Vivian J.P., Scoullar J., Robertson A.L., Bottomley S.P., Horne J., Chin Y., et al. Structural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidis. J. Biol. Chem. 283 (2008) 32452-32461
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 32452-32461
-
-
Vivian, J.P.1
Scoullar, J.2
Robertson, A.L.3
Bottomley, S.P.4
Horne, J.5
Chin, Y.6
-
19
-
-
67650566330
-
The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes
-
Paxman J.J., Borg N.A., Horne J., Thompson P.E., Chin Y., Sharma P., et al. The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes. J. Biol. Chem. 284 (2009) 17835-17845
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 17835-17845
-
-
Paxman, J.J.1
Borg, N.A.2
Horne, J.3
Thompson, P.E.4
Chin, Y.5
Sharma, P.6
-
20
-
-
65249146593
-
Structural and biochemical characterization of Xylella fastidiosa DsbA family members: new insights into the enzyme-substrate interaction
-
Rinaldi F.C., Meza A.N., and Guimaraes B.G. Structural and biochemical characterization of Xylella fastidiosa DsbA family members: new insights into the enzyme-substrate interaction. Biochemistry 48 (2009) 3508-3518
-
(2009)
Biochemistry
, vol.48
, pp. 3508-3518
-
-
Rinaldi, F.C.1
Meza, A.N.2
Guimaraes, B.G.3
-
21
-
-
0030880594
-
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability
-
Guddat L.W., Bardwell J.C., Glockshuber R., Huber-Wunderlich M., Zander T., and Martin J.L. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6 (1997) 1893-1900
-
(1997)
Protein Sci.
, vol.6
, pp. 1893-1900
-
-
Guddat, L.W.1
Bardwell, J.C.2
Glockshuber, R.3
Huber-Wunderlich, M.4
Zander, T.5
Martin, J.L.6
-
22
-
-
0031585999
-
Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae
-
Hu S.H., Peek J.A., Rattigan E., Taylor R.K., and Martin J.L. Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. J. Mol. Biol. 268 (1997) 137-146
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 137-146
-
-
Hu, S.H.1
Peek, J.A.2
Rattigan, E.3
Taylor, R.K.4
Martin, J.L.5
-
23
-
-
66749152520
-
Structural and functional characterization of the oxidoreductase α-DsbA1 from Wolbachia pipientis. Antioxid
-
Kurz M., Iturbe-Ormaetxe I., Jarrott R., Shouldice S.R., Wouters M.A., Frei P., et al. Structural and functional characterization of the oxidoreductase α-DsbA1 from Wolbachia pipientis. Antioxid. Redox Signal. 11 (2009) 1485-1500
-
(2009)
Redox Signal.
, vol.11
, pp. 1485-1500
-
-
Kurz, M.1
Iturbe-Ormaetxe, I.2
Jarrott, R.3
Shouldice, S.R.4
Wouters, M.A.5
Frei, P.6
-
24
-
-
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
-
26
-
-
0029062201
-
A molecular model for the redox potential difference between thioredoxin and DsbA, based on electrostatics calculations
-
Gane P.J., Freedman R.B., and Warwicker J. A molecular model for the redox potential difference between thioredoxin and DsbA, based on electrostatics calculations. J. Mol. Biol. 249 (1995) 376-387
-
(1995)
J. Mol. Biol.
, vol.249
, pp. 376-387
-
-
Gane, P.J.1
Freedman, R.B.2
Warwicker, J.3
-
27
-
-
0027136282
-
Comparative protein modelling by satisfaction of spatial restraints
-
Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
-
(1993)
J. Mol. Biol.
, vol.234
, pp. 779-815
-
-
Sali, A.1
Blundell, T.L.2
-
28
-
-
0035964342
-
Electrostatics of nanosystems: application to microtubules and the ribosome
-
Baker N.A., Sept D., Joseph S., Holst M.J., and McCammon J.A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98 (2001) 10037-10041
-
(2001)
Proc. Natl Acad. Sci. USA
, vol.98
, pp. 10037-10041
-
-
Baker, N.A.1
Sept, D.2
Joseph, S.3
Holst, M.J.4
McCammon, J.A.5
-
29
-
-
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
-
30
-
-
65649140478
-
Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue
-
Ren G., Stephan D., Xu Z., Zheng Y., Tang D., Harrison R.S., et al. Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J. Biol. Chem. 284 (2009) 10150-10159
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 10150-10159
-
-
Ren, G.1
Stephan, D.2
Xu, Z.3
Zheng, Y.4
Tang, D.5
Harrison, R.S.6
-
31
-
-
45549122242
-
DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli
-
Grimshaw J.P., Stirnimann C.U., Brozzo M.S., Malojcic G., Grutter M.G., Capitani G., and Glockshuber R. DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli. J. Mol. Biol. 380 (2008) 667-680
-
(2008)
J. Mol. Biol.
, vol.380
, pp. 667-680
-
-
Grimshaw, J.P.1
Stirnimann, C.U.2
Brozzo, M.S.3
Malojcic, G.4
Grutter, M.G.5
Capitani, G.6
Glockshuber, R.7
-
32
-
-
42949135118
-
Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding
-
Heras B., Kurz M., Jarrott R., Shouldice S.R., Frei P., Robin G., et al. Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding. J. Biol. Chem. 283 (2008) 4261-4271
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 4261-4271
-
-
Heras, B.1
Kurz, M.2
Jarrott, R.3
Shouldice, S.R.4
Frei, P.5
Robin, G.6
-
33
-
-
34447120818
-
Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase
-
Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., Schurmann P., and Eklund H. Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Nature 448 (2007) 92-96
-
(2007)
Nature
, vol.448
, pp. 92-96
-
-
Dai, S.1
Friemann, R.2
Glauser, D.A.3
Bourquin, F.4
Manieri, W.5
Schurmann, P.6
Eklund, H.7
-
34
-
-
33750813327
-
Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
-
Inaba K., Murakami S., Suzuki M., Nakagawa A., Yamashita E., Okada K., and Ito K. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127 (2006) 789-801
-
(2006)
Cell
, vol.127
, pp. 789-801
-
-
Inaba, K.1
Murakami, S.2
Suzuki, M.3
Nakagawa, A.4
Yamashita, E.5
Okada, K.6
Ito, K.7
-
35
-
-
33846393586
-
Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
-
Maeda K., Hagglund P., Finnie C., Svensson B., and Henriksen A. Structural basis for target protein recognition by the protein disulfide reductase thioredoxin. Structure 14 (2006) 1701-1710
-
(2006)
Structure
, vol.14
, pp. 1701-1710
-
-
Maeda, K.1
Hagglund, P.2
Finnie, C.3
Svensson, B.4
Henriksen, A.5
-
36
-
-
0032562757
-
Reconstitution of a protein disulfide catalytic system
-
Bader M., Muse W., Zander T., and Bardwell J. Reconstitution of a protein disulfide catalytic system. J. Biol. Chem. 273 (1998) 10302-10307
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 10302-10307
-
-
Bader, M.1
Muse, W.2
Zander, T.3
Bardwell, J.4
-
37
-
-
52049098074
-
NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation
-
Zhou Y., Cierpicki T., Jimenez R.H., Lukasik S.M., Ellena J.F., Cafiso D.S., et al. NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol. Cell 31 (2008) 896-908
-
(2008)
Mol. Cell
, vol.31
, pp. 896-908
-
-
Zhou, Y.1
Cierpicki, T.2
Jimenez, R.H.3
Lukasik, S.M.4
Ellena, J.F.5
Cafiso, D.S.6
-
38
-
-
62649151322
-
Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB
-
Inaba K., Murakami S., Nakagawa A., Iida H., Kinjo M., Ito K., and Suzuki M. Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB. EMBO J. 28 (2009) 779-791
-
(2009)
EMBO J.
, vol.28
, pp. 779-791
-
-
Inaba, K.1
Murakami, S.2
Nakagawa, A.3
Iida, H.4
Kinjo, M.5
Ito, K.6
Suzuki, M.7
-
39
-
-
0037093512
-
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
-
Kadokura H., and Beckwith J. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 21 (2002) 2354-2363
-
(2002)
EMBO J.
, vol.21
, pp. 2354-2363
-
-
Kadokura, H.1
Beckwith, J.2
-
40
-
-
0028103275
-
The CCP4 suite: programs for protein crystallography
-
Collaborative
-
Collaborative. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
-
(1994)
Acta Crystallogr. Sect. D
, vol.50
, pp. 760-763
-
-
-
41
-
-
0000560808
-
MOLREP: an automated program for molecular replacement
-
Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
-
(1997)
J. Appl. Crystallogr.
, vol.30
, pp. 1022-1025
-
-
Vagin, A.1
Teplyakov, A.2
-
42
-
-
43749083257
-
CHAINSAW: a program for mutating pdb files used as templates in molecular replacement
-
Stein N. CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J. Appl. Crystallogr. 41 (2008) 641-643
-
(2008)
J. Appl. Crystallogr.
, vol.41
, pp. 641-643
-
-
Stein, N.1
-
43
-
-
0030924992
-
Refinement of macromolecular structures by the maximum-likelihood method
-
Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
-
(1997)
Acta Crystallogr. Sect. D
, vol.53
, pp. 240-255
-
-
Murshudov, G.N.1
Vagin, A.A.2
Dodson, E.J.3
-
44
-
-
13244281317
-
Coot: model-building tools for molecular graphics
-
Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
-
(2004)
Acta Crystallogr. Sect. D
, vol.60
, pp. 2126-2132
-
-
Emsley, P.1
Cowtan, K.2
-
45
-
-
33646260450
-
Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
-
Painter J., and Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. Sect. D 62 (2006) 439-450
-
(2006)
Acta Crystallogr. Sect. D
, vol.62
, pp. 439-450
-
-
Painter, J.1
Merritt, E.A.2
-
46
-
-
50249136103
-
Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
-
Langer G., Cohen S.X., Lamzin V.S., and Perrakis A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3 (2008) 1171-1179
-
(2008)
Nat. Protoc.
, vol.3
, pp. 1171-1179
-
-
Langer, G.1
Cohen, S.X.2
Lamzin, V.S.3
Perrakis, A.4
-
47
-
-
34547592557
-
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
-
Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., Wang X., et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35 (2007) W375-W383
-
(2007)
Nucleic Acids Res.
, vol.35
-
-
Davis, I.W.1
Leaver-Fay, A.2
Chen, V.B.3
Block, J.N.4
Kapral, G.J.5
Wang, X.6
-
48
-
-
0031776171
-
A single dipeptide sequence modulates the redox properties of a whole enzyme family
-
Huber-Wunderlich M., and Glockshuber R. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold. Des. 3 (1998) 161-171
-
(1998)
Fold. Des.
, vol.3
, pp. 161-171
-
-
Huber-Wunderlich, M.1
Glockshuber, R.2
-
49
-
-
0039700271
-
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli
-
Mossner E., Huber-Wunderlich M., Rietsch A., Beckwith J., Glockshuber R., and Aslund F. Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli. J. Biol. Chem. 274 (1999) 25254-25259
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 25254-25259
-
-
Mossner, E.1
Huber-Wunderlich, M.2
Rietsch, A.3
Beckwith, J.4
Glockshuber, R.5
Aslund, F.6
-
50
-
-
6444240771
-
De novo designed peptidic redox potential probe: linking sensitized emission to disulfide bond formation
-
Lee K., Dzubeck V., Latshaw L., and Schneider J.P. De novo designed peptidic redox potential probe: linking sensitized emission to disulfide bond formation. J. Am. Chem. Soc. 126 (2004) 13616-13617
-
(2004)
J. Am. Chem. Soc.
, vol.126
, pp. 13616-13617
-
-
Lee, K.1
Dzubeck, V.2
Latshaw, L.3
Schneider, J.P.4
-
51
-
-
0029918154
-
pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate
-
Ruddock L.W., Hirst T.R., and Freedman R.B. pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate. Biochem. J. 315 (1996) 1001-1005
-
(1996)
Biochem. J.
, vol.315
, pp. 1001-1005
-
-
Ruddock, L.W.1
Hirst, T.R.2
Freedman, R.B.3
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