-
1
-
-
0037830694
-
Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: Photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function
-
Alphey, M.S., Gabrielsen, M., Micossi, E., Leonard, G.A., McSweeney, S.M., Ravelli, R.B., Tetaud, E., Fairlamb, A.H., Bond, C.S., and Hunter, W.N. 2003. Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: Photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function. J. Biol. Chem. 278: 25919-25925.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 25919-25925
-
-
Alphey, M.S.1
Gabrielsen, M.2
Micossi, E.3
Leonard, G.A.4
McSweeney, S.M.5
Ravelli, R.B.6
Tetaud, E.7
Fairlamb, A.H.8
Bond, C.S.9
Hunter, W.N.10
-
2
-
-
0013506276
-
The sulfhydryl groups of crystalline proteins. I. Some albumins, enzymes, and hemoglobins
-
Benesch, R.E., Lardy, H.A., and Benesch, R. 1955. The sulfhydryl groups of crystalline proteins. I. Some albumins, enzymes, and hemoglobins. J. Biol. Chem. 216: 663-676.
-
(1955)
J. Biol. Chem.
, vol.216
, pp. 663-676
-
-
Benesch, R.E.1
Lardy, H.A.2
Benesch, R.3
-
3
-
-
3543012707
-
Crystallography and NMR system: A new software suite for macromolecular structure determination
-
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. 1998. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (Pt. 5): 905-921.
-
(1998)
Acta Crystallogr. D Biol. Crystallogr.
, vol.54
, Issue.5 PART
, pp. 905-921
-
-
Brunger, A.T.1
Adams, P.D.2
Clore, G.M.3
DeLano, W.L.4
Gros, P.5
Grosse-Kunstleve, R.W.6
Jiang, J.S.7
Kuszewski, J.8
Nilges, M.9
Pannu, N.S.10
-
4
-
-
0032060482
-
Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates
-
Chen, L., Xie, Q.W., and Nathan, C. 1998. Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol. Cell 1: 795-805.
-
(1998)
Mol. Cell
, vol.1
, pp. 795-805
-
-
Chen, L.1
Xie, Q.W.2
Nathan, C.3
-
5
-
-
0030934272
-
The CXXC motif: A rheostat in the active site
-
Chivers, P.T., Prehoda, K.E., and Raines, R.T. 1997. The CXXC motif: A rheostat in the active site. Biochemistry 36: 4061-4066.
-
(1997)
Biochemistry
, vol.36
, pp. 4061-4066
-
-
Chivers, P.T.1
Prehoda, K.E.2
Raines, R.T.3
-
6
-
-
0031024788
-
Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57
-
Dyson, H.J., Jeng, M.F., Tennant, L.L., Slaby, I., Lindell, M., Cui, D.S., Kuprin, S., and Holmgren, A. 1997. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 36: 2622-2636.
-
(1997)
Biochemistry
, vol.36
, pp. 2622-2636
-
-
Dyson, H.J.1
Jeng, M.F.2
Tennant, L.L.3
Slaby, I.4
Lindell, M.5
Cui, D.S.6
Kuprin, S.7
Holmgren, A.8
-
7
-
-
1242328666
-
The glutaredoxin -C-P-Y-C- motif: Influence of peripheral residues
-
Foloppe, N. and Nilsson, L. 2004. The glutaredoxin -C-P-Y-C- motif: Influence of peripheral residues. Structure (Camb) 12: 289-300.
-
(2004)
Structure (Camb)
, vol.12
, pp. 289-300
-
-
Foloppe, N.1
Nilsson, L.2
-
8
-
-
0035816224
-
Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: Comparison with functionally related proteins
-
Foloppe, N., Sagemark, J., Nordstrand, K., Berndt, K.D., and Nilsson, L. 2001. Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: Comparison with functionally related proteins. J. Mol. Biol. 310: 449-470.
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 449-470
-
-
Foloppe, N.1
Sagemark, J.2
Nordstrand, K.3
Berndt, K.D.4
Nilsson, L.5
-
9
-
-
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. 1995. A molecular model for the redox potential difference between thioredoxin and DsbA, based on electrostatics calculations. J. Mol. Biol. 249: 376-387.
-
(1995)
J. Mol. Biol.
, vol.249
, pp. 376-387
-
-
Gane, P.J.1
Freedman, R.B.2
Warwicker, J.3
-
10
-
-
0024588467
-
Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase
-
Graminski, G.F., Kubo, Y., and Armstrong, R.N. 1989. Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase. Biochemistry 28: 3562-3568.
-
(1989)
Biochemistry
, vol.28
, pp. 3562-3568
-
-
Graminski, G.F.1
Kubo, Y.2
Armstrong, R.N.3
-
11
-
-
0029559184
-
Why is DsbA such an oxidizing disulfide catalyst?
-
Grauschopf, U., Winther, J.R., Korber, P., Zander, T.P., Dallinger, P., and Bardwell, J.C.A. 1995. Why is DsbA such an oxidizing disulfide catalyst? Cell 83: 947-955.
-
(1995)
Cell
, vol.83
, pp. 947-955
-
-
Grauschopf, U.1
Winther, J.R.2
Korber, P.3
Zander, T.P.4
Dallinger, P.5
Bardwell, J.C.A.6
-
12
-
-
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. 1997. Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6: 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
-
13
-
-
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. 1998. Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization. Structure 6: 757-767.
-
(1998)
Structure
, vol.6
, pp. 757-767
-
-
Guddat, L.W.1
Bardwell, J.C.2
Martin, J.L.3
-
14
-
-
0031776171
-
A single dipeptide sequence modulates the redox properties of a whole enzyme family
-
Huber-Wunderlich, M. and Glockshuber, R. 1998. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold. Des. 3: 161-171.
-
(1998)
Fold. Des.
, vol.3
, pp. 161-171
-
-
Huber-Wunderlich, M.1
Glockshuber, R.2
-
15
-
-
0024599904
-
An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage: Purification and properties
-
Jacobson, F.S., Morgan, R.W., Christman, M.F., and Ames, B.N. 1989. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage: Purification and properties. J. Biol. Chem. 264: 1488-1496.
-
(1989)
J. Biol. Chem.
, vol.264
, pp. 1488-1496
-
-
Jacobson, F.S.1
Morgan, R.W.2
Christman, M.F.3
Ames, B.N.4
-
16
-
-
0029057023
-
Proton sharing between cysteine thiols in Escherichia coli thioredoxin: Implications for the mechanism of protein disulfide reduction
-
Jeng, M.F., Holmgren, A., and Dyson, H.J. 1995. Proton sharing between cysteine thiols in Escherichia coli thioredoxin: Implications for the mechanism of protein disulfide reduction. Biochemistry 34: 10101-10105.
-
(1995)
Biochemistry
, vol.34
, pp. 10101-10105
-
-
Jeng, M.F.1
Holmgren, A.2
Dyson, H.J.3
-
17
-
-
84889120137
-
Improved methods for building protein models in electron density maps and the location of errors in these models
-
Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (Pt. 2): 110-119.
-
(1991)
Acta Crystallogr. A
, vol.47
, Issue.2 PART
, pp. 110-119
-
-
Jones, T.A.1
Zou, J.Y.2
Cowan, S.W.3
Kjeldgaard, M.4
-
18
-
-
24344478927
-
Intramolecular electron transfer pathway in mutants of AhpF, a flavoprotein disulfide reductase
-
eds. S. Chapman et al., Agency for Scientific Publications, Berlin
-
Jönsson, T. and Poole, L.B. 2002. Intramolecular electron transfer pathway in mutants of AhpF, a flavoprotein disulfide reductase. In Flavins and flavoproteins 2002 (eds. S. Chapman et al.), pp. 691-696. Agency for Scientific Publications, Berlin.
-
(2002)
Flavins and Flavoproteins 2002
, pp. 691-696
-
-
Jönsson, T.1
Poole, L.B.2
-
19
-
-
0019163962
-
Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
-
Kallis, G.B. and Holmgren, A. 1980. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 255: 10261-10265.
-
(1980)
J. Biol. Chem.
, vol.255
, pp. 10261-10265
-
-
Kallis, G.B.1
Holmgren, A.2
-
20
-
-
0030446158
-
Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase
-
Kortemme, T., Darby, N.J., and Creighton, T.E. 1996. Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Biochemistry 35: 14503-14511.
-
(1996)
Biochemistry
, vol.35
, pp. 14503-14511
-
-
Kortemme, T.1
Darby, N.J.2
Creighton, T.E.3
-
21
-
-
0025914427
-
Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
-
Krause, G., Lundstrom, J., Barea, J.L., Pueyo de la Cuesta, C., and Holmgren, A. 1991. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J. Biol. Chem. 266: 9494-9500.
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 9494-9500
-
-
Krause, G.1
Lundstrom, J.2
Barea, J.L.3
Pueyo De La Cuesta, C.4
Holmgren, A.5
-
22
-
-
0030736766
-
Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase
-
Li Calzi, M. and Poole, L.B. 1997. Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase. Biochemistry 36: 13357-13364.
-
(1997)
Biochemistry
, vol.36
, pp. 13357-13364
-
-
Li Calzi, M.1
Poole, L.B.2
-
23
-
-
0039714219
-
Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol-disulfide oxidoreductases
-
Mössner, E., Huber-Wunderlich, M., and Glockshuber, R. 1998. Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol-disulfide oxidoreductases. Protein Sci. 7: 1233-1244.
-
(1998)
Protein Sci.
, vol.7
, pp. 1233-1244
-
-
Mössner, E.1
Huber-Wunderlich, M.2
Glockshuber, R.3
-
24
-
-
4243518910
-
Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases
-
Mössner, E., Iwai, H., and Glockshuber, R. 2000. Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases. FEBS Lett. 477: 21-26.
-
(2000)
FEBS Lett.
, vol.477
, pp. 21-26
-
-
Mössner, E.1
Iwai, H.2
Glockshuber, R.3
-
25
-
-
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. 1994. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33: 5974-5983.
-
(1994)
Biochemistry
, vol.33
, pp. 5974-5983
-
-
Nelson, J.W.1
Creighton, T.E.2
-
26
-
-
0028880854
-
Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein component
-
Niimura, Y., Poole, L.B., and Massey, V. 1995. Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein component. J. Biol. Chem. 270: 25645-25650.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 25645-25650
-
-
Niimura, Y.1
Poole, L.B.2
Massey, V.3
-
27
-
-
0032959801
-
Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond
-
Nordstrand, K., Aslund, F., Meunier, S., Holmgren, A., Otting, G., and Berndt, K.D. 1999. Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond. FEBS Lett. 449: 196-200.
-
(1999)
FEBS Lett.
, vol.449
, pp. 196-200
-
-
Nordstrand, K.1
Aslund, F.2
Meunier, S.3
Holmgren, A.4
Otting, G.5
Berndt, K.D.6
-
28
-
-
0031059866
-
Processing of X-ray diffraction data collected in oscillation mode
-
Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
-
(1997)
Methods Enzymol.
, vol.276
, pp. 307-326
-
-
Otwinowski, Z.1
Minor, W.2
-
29
-
-
0016115206
-
Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis
-
Polgar, L. 1974. Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis. FEBS Lett. 47: 15-18.
-
(1974)
FEBS Lett.
, vol.47
, pp. 15-18
-
-
Polgar, L.1
-
30
-
-
0030066091
-
Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction
-
Poole, L.B. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction. Biochemistry 35: 65-75.
-
(1996)
Biochemistry
, vol.35
, pp. 65-75
-
-
Poole, L.B.1
-
31
-
-
0012326355
-
Flavin-linked redox components required for AhpC reduction in alkyl hydroperoxide reductase systems
-
eds. S. Ghisla et al., Agency for Scientific Publications, Berlin
-
_. 1999. Flavin-linked redox components required for AhpC reduction in alkyl hydroperoxide reductase systems. In Flavins and flavoproteins (eds. S. Ghisla et al.), pp. 691-694. Agency for Scientific Publications, Berlin.
-
(1999)
Flavins and Flavoproteins
, pp. 691-694
-
-
-
32
-
-
9744232974
-
Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
-
_. 2005. Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch. Biochem. Biophys. 433: 240-254.
-
(2005)
Arch. Biochem. Biophys.
, vol.433
, pp. 240-254
-
-
-
33
-
-
0030032612
-
Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins
-
Poole, L.B. and Ellis, H.R. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35: 56-64.
-
(1996)
Biochemistry
, vol.35
, pp. 56-64
-
-
Poole, L.B.1
Ellis, H.R.2
-
34
-
-
0034612366
-
AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC
-
Poole, L.B., Godzik, A., Nayeem, A., and Schmitt, J.D. 2000a. AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC. Biochemistry 39: 6602-6615.
-
(2000)
Biochemistry
, vol.39
, pp. 6602-6615
-
-
Poole, L.B.1
Godzik, A.2
Nayeem, A.3
Schmitt, J.D.4
-
35
-
-
0033771859
-
AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase
-
Poole, L.B., Reynolds, C.M., Wood, Z.A., Karplus, P.A., Ellis, H.R., and Li Calzi, M. 2000b. AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur. J. Biochem. 267: 6126-6133.
-
(2000)
Eur. J. Biochem.
, vol.267
, pp. 6126-6133
-
-
Poole, L.B.1
Reynolds, C.M.2
Wood, Z.A.3
Karplus, P.A.4
Ellis, H.R.5
Li Calzi, M.6
-
36
-
-
84944812409
-
Improbed Fourier coefficients for maps using phases from partial structures with errors
-
Read, R.J. 1986. Improbed Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42: 140-149.
-
(1986)
Acta Crystallogr. A
, vol.42
, pp. 140-149
-
-
Read, R.J.1
-
37
-
-
0037124054
-
Catalytic properties, thiol pK value, and redox potential of Trypanosoma brucei tryparedoxin
-
Reckenfelderbaumer, N. and Krauth-Siegel, R.L. 2002. Catalytic properties, thiol pK value, and redox potential of Trypanosoma brucei tryparedoxin. J. Biol. Chem. 277: 17548-17555.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 17548-17555
-
-
Reckenfelderbaumer, N.1
Krauth-Siegel, R.L.2
-
38
-
-
0034254337
-
Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity
-
Reynolds, C.M. and Poole, L.B. 2000. Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity. Biochemistry 39: 8859-8869.
-
(2000)
Biochemistry
, vol.39
, pp. 8859-8869
-
-
Reynolds, C.M.1
Poole, L.B.2
-
39
-
-
0018416496
-
Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid): A reexamination
-
Riddles, P.W., Blakeley, R.L., and Zerner, B. 1979. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid): A reexamination. Anal. Biochem. 94: 75-81.
-
(1979)
Anal. Biochem.
, vol.94
, pp. 75-81
-
-
Riddles, P.W.1
Blakeley, R.L.2
Zerner, B.3
-
40
-
-
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. 1996. 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 (Pt. 3): 1001-1005.
-
(1996)
Biochem. J.
, vol.315
, Issue.3 PART
, pp. 1001-1005
-
-
Ruddock, L.W.1
Hirst, T.R.2
Freedman, R.B.3
-
41
-
-
33847087446
-
Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
-
Szajewski, R.P. and Whitesides, G.M. 1980. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J. Am. Chem. Soc. 102: 2011-2026.
-
(1980)
J. Am. Chem. Soc.
, vol.102
, pp. 2011-2026
-
-
Szajewski, R.P.1
Whitesides, G.M.2
-
42
-
-
0030585429
-
Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
-
Weichsel, A., Gasdaska, J.R., Powis, G., and Montfort, W.R. 1996. Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer. Structure 4: 735-751.
-
(1996)
Structure
, vol.4
, pp. 735-751
-
-
Weichsel, A.1
Gasdaska, J.R.2
Powis, G.3
Montfort, W.R.4
-
43
-
-
12944269052
-
Specific chemical and structural damage to proteins produced by synchrotron radiation
-
Weik, M., Ravelli, R.B., Kryger, G., McSweeney, S., Raves, M.L., Harel, M., Gros, P., Silman, I., Kroon, J., and Sussman, J.L. 2000. Specific chemical and structural damage to proteins produced by synchrotron radiation. Proc. Natl. Acad. Sci. 97: 623-628.
-
(2000)
Proc. Natl. Acad. Sci.
, vol.97
, pp. 623-628
-
-
Weik, M.1
Ravelli, R.B.2
Kryger, G.3
McSweeney, S.4
Raves, M.L.5
Harel, M.6
Gros, P.7
Silman, I.8
Kroon, J.9
Sussman, J.L.10
-
44
-
-
0035799315
-
Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis
-
Wood, Z.A., Poole, L.B., and Karplus, P.A. 2001. Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis. Biochemistry 40: 3900-3911.
-
(2001)
Biochemistry
, vol.40
, pp. 3900-3911
-
-
Wood, Z.A.1
Poole, L.B.2
Karplus, P.A.3
-
45
-
-
0037197672
-
Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
-
Wood, Z.A., Poole, L.B., Hantgan, R.R., and Karplus, P.A. 2002. Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 41: 5493-5504.
-
(2002)
Biochemistry
, vol.41
, pp. 5493-5504
-
-
Wood, Z.A.1
Poole, L.B.2
Hantgan, R.R.3
Karplus, P.A.4
-
46
-
-
0242668686
-
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
-
Wood, Z.A., Poole, L.B., and Karplus, P.A. 2003. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653.
-
(2003)
Science
, vol.300
, pp. 650-653
-
-
Wood, Z.A.1
Poole, L.B.2
Karplus, P.A.3
|