-
1
-
-
73649177752
-
Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
-
Goldberger R., et al. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 238 (1963) 628-635
-
(1963)
J. Biol. Chem.
, vol.238
, pp. 628-635
-
-
Goldberger, R.1
-
2
-
-
0026091179
-
Identification of a protein required for disulfide bond formation in vivo
-
Bardwell J., et al. 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.1
-
3
-
-
30344444015
-
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
-
Tian G., et al. 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
-
4
-
-
33645881071
-
Pathways of disulfide bond formation in Escherichia coli
-
Messens J., et al. Pathways of disulfide bond formation in Escherichia coli. Int. J. Biochem. Cell Biol. 38 (2006) 1050-1062
-
(2006)
Int. J. Biochem. Cell Biol.
, vol.38
, pp. 1050-1062
-
-
Messens, J.1
-
5
-
-
0042768090
-
Protein disulfide bond formation in prokaryotes
-
Kadokura H., et al. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72 (2003) 111-135
-
(2003)
Annu. Rev. Biochem.
, vol.72
, pp. 111-135
-
-
Kadokura, H.1
-
6
-
-
0034115404
-
Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
-
Fabianek R., et al. Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli. FEMS Microbiol. Rev. 24 (2000) 303-316
-
(2000)
FEMS Microbiol. Rev.
, vol.24
, pp. 303-316
-
-
Fabianek, R.1
-
7
-
-
0042815104
-
Mechanism of the electron transfer catalyst DsbB from Escherichia coli
-
Grauschopf U., et al. 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
-
8
-
-
0029822654
-
An in vivo pathway for disulfide bond isomerization in Escherichia coli
-
Rietsch A., et al. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 13048-13053
-
(1996)
Proc. Natl. Acad. Sci. U. S. A.
, vol.93
, pp. 13048-13053
-
-
Rietsch, A.1
-
9
-
-
0346096508
-
Quality control in the endoplasmic reticulum protein factory
-
Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
-
(2003)
Nature
, vol.426
, pp. 891-894
-
-
Sitia, R.1
Braakman, I.2
-
10
-
-
23744457478
-
Versatility of the endoplasmic reticulum protein folding factory
-
Anken E., et al. Versatility of the endoplasmic reticulum protein folding factory. Crit. Rev. Biochem. Mol. Biol. 40 (2005) 191-228
-
(2005)
Crit. Rev. Biochem. Mol. Biol.
, vol.40
, pp. 191-228
-
-
Anken, E.1
-
11
-
-
0142215475
-
Global analysis of protein expression in yeast
-
Ghaemmaghami S., et al. Global analysis of protein expression in yeast. Nature 425 (2003) 737-741
-
(2003)
Nature
, vol.425
, pp. 737-741
-
-
Ghaemmaghami, S.1
-
12
-
-
0034604675
-
Endoplasmic reticulum oxidoreductin 1-lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
-
Pagani M., et al. Endoplasmic reticulum oxidoreductin 1-lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275 (2000) 23685-23692
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 23685-23692
-
-
Pagani, M.1
-
13
-
-
0034681340
-
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
-
Cabibbo A., et al. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275 (2000) 4827-4833
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 4827-4833
-
-
Cabibbo, A.1
-
14
-
-
0042262430
-
Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins
-
Dixon D., et al. Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins. Antioxid. Redox Signal. 5 (2003) 389-396
-
(2003)
Antioxid. Redox Signal.
, vol.5
, pp. 389-396
-
-
Dixon, D.1
-
15
-
-
2542475140
-
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
-
Gross E., et al. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117 (2004) 601-610
-
(2004)
Cell
, vol.117
, pp. 601-610
-
-
Gross, E.1
-
16
-
-
31044452359
-
Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
-
Gross E., et al. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 299-304
-
(2006)
Proc. Natl. Acad. Sci. U. S. A.
, vol.103
, pp. 299-304
-
-
Gross, E.1
-
17
-
-
33745761475
-
Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1
-
Sevier C., et al. Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1. Mol. Biol. Cell 17 (2006) 2256-2266
-
(2006)
Mol. Biol. Cell
, vol.17
, pp. 2256-2266
-
-
Sevier, C.1
-
18
-
-
28444436253
-
Structural determinants of substrate access to the disulfide oxidase Erv2p
-
Vala A., et al. Structural determinants of substrate access to the disulfide oxidase Erv2p. J. Mol. Biol. 354 (2005) 952-966
-
(2005)
J. Mol. Biol.
, vol.354
, pp. 952-966
-
-
Vala, A.1
-
19
-
-
0034790475
-
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
-
Sevier C., et al. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat. Cell Biol. 3 (2001) 874-882
-
(2001)
Nat. Cell Biol.
, vol.3
, pp. 874-882
-
-
Sevier, C.1
-
20
-
-
0036142325
-
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
-
Gross E., et al. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9 (2002) 61-67
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 61-67
-
-
Gross, E.1
-
21
-
-
0029165589
-
Thioredoxin - a fold for all reasons
-
Martin J.L. Thioredoxin - a fold for all reasons. Structure 3 (1995) 245-250
-
(1995)
Structure
, vol.3
, pp. 245-250
-
-
Martin, J.L.1
-
22
-
-
14044271131
-
The human protein disulphide isomerase family: substrate interactions and functional properties
-
Ellgaard L., et al. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6 (2005) 28-32
-
(2005)
EMBO Rep.
, vol.6
, pp. 28-32
-
-
Ellgaard, L.1
-
23
-
-
17644395645
-
Thioredoxin and its related molecules: update 2005
-
Nakamura H. Thioredoxin and its related molecules: update 2005. Antioxid. Redox Signal. 7 (2005) 823-828
-
(2005)
Antioxid. Redox Signal.
, vol.7
, pp. 823-828
-
-
Nakamura, H.1
-
24
-
-
2542435948
-
Protein disulfide isomerase
-
Wilkinson B., et al. Protein disulfide isomerase. Biochim. Biophys. Acta 1699 (2004) 35-44
-
(2004)
Biochim. Biophys. Acta
, vol.1699
, pp. 35-44
-
-
Wilkinson, B.1
-
25
-
-
2442761708
-
The protein disulphide-isomerase family: unravelling a string of folds
-
Ferrari D., et al. The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 339 (1999) 1-10
-
(1999)
Biochem. J.
, vol.339
, pp. 1-10
-
-
Ferrari, D.1
-
26
-
-
0842266604
-
Oxidative protein folding in eukaryotes: mechanisms and consequences
-
Tu B., et al. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164 (2004) 341-346
-
(2004)
J. Cell Biol.
, vol.164
, pp. 341-346
-
-
Tu, B.1
-
27
-
-
0036842559
-
Formation and transfer of disulphide bonds in living cells
-
Sevier C., et al. 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.1
-
28
-
-
0029294558
-
A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family
-
McKay R., et al. A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family. Insect Biochem. Mol. Biol. 25 (1995) 647-654
-
(1995)
Insect Biochem. Mol. Biol.
, vol.25
, pp. 647-654
-
-
McKay, R.1
-
29
-
-
19044379862
-
Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins
-
Houston N., et al. Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol. 137 (2005) 762-778
-
(2005)
Plant Physiol.
, vol.137
, pp. 762-778
-
-
Houston, N.1
-
30
-
-
0031826990
-
Molecular evolution of the domain structures of protein disulfide isomerases
-
Kanai S., et al. Molecular evolution of the domain structures of protein disulfide isomerases. J. Mol. Evol. 47 (1998) 200-210
-
(1998)
J. Mol. Evol.
, vol.47
, pp. 200-210
-
-
Kanai, S.1
-
31
-
-
0035868331
-
The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands
-
Klappa P., et al. The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands. Biochem. J. 354 (2001) 553-559
-
(2001)
Biochem. J.
, vol.354
, pp. 553-559
-
-
Klappa, P.1
-
32
-
-
17844410082
-
Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum
-
Levitan A., et al. Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6225-6230
-
(2005)
Proc. Natl. Acad. Sci. U. S. A.
, vol.102
, pp. 6225-6230
-
-
Levitan, A.1
-
33
-
-
0027373949
-
Crystal structure of the DsbA protein required for disulphide bond formation in vivo
-
Martin J., et al. 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.1
-
34
-
-
0029973729
-
15N NMR spectroscopy
-
15N NMR spectroscopy. Biochemistry 35 (1996) 7684-7691
-
(1996)
Biochemistry
, vol.35
, pp. 7684-7691
-
-
Kemmink, J.1
-
35
-
-
0032897837
-
The structure in solution of the b domain of protein disulfide isomerase
-
Kemmink J., et al. The structure in solution of the b domain of protein disulfide isomerase. J. Biomol. NMR 13 (1999) 357-368
-
(1999)
J. Biomol. NMR
, vol.13
, pp. 357-368
-
-
Kemmink, J.1
-
36
-
-
0033144472
-
15N resonances of the a′ domain of protein disulfide isomerase
-
15N resonances of the a′ domain of protein disulfide isomerase. J. Biomol. NMR 14 (1999) 195-196
-
(1999)
J. Biomol. NMR
, vol.14
, pp. 195-196
-
-
Dijkstra, K.1
-
37
-
-
2942669907
-
Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
-
Heras B., et al. 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
-
38
-
-
1042266634
-
Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding
-
Horibe T., et al. Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding. J. Biol. Chem. 279 (2004) 4604-4611
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 4604-4611
-
-
Horibe, T.1
-
39
-
-
0032485920
-
Structure of reduced DsbA from Escherichia coli in solution
-
Schirra H., et al. Structure of reduced DsbA from Escherichia coli in solution. Biochemistry 37 (1998) 6263-6276
-
(1998)
Biochemistry
, vol.37
, pp. 6263-6276
-
-
Schirra, H.1
-
40
-
-
0034048647
-
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
-
McCarthy A., et al. 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.1
-
41
-
-
0036069067
-
Structure of CcmG/DsbE at 1.14 Å resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment
-
Edeling M., et al. Structure of CcmG/DsbE at 1.14 Å resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment. Structure 10 (2002) 973-979
-
(2002)
Structure
, vol.10
, pp. 973-979
-
-
Edeling, M.1
-
42
-
-
0037018912
-
Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD
-
Goulding C., et al. 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.1
-
43
-
-
0037716929
-
Crystal structure of DsbDγ reveals the mechanism of redox potential shift and substrate specificity
-
Kim J., et al. Crystal structure of DsbDγ reveals the mechanism of redox potential shift and substrate specificity. FEBS Lett. 543 (2003) 164-169
-
(2003)
FEBS Lett.
, vol.543
, pp. 164-169
-
-
Kim, J.1
-
44
-
-
2442607486
-
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD
-
Rozhkova A., 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
-
45
-
-
0942287201
-
Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis
-
Goulding C., et al. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. J. Biol. Chem. 279 (2004) 3516-3524
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 3516-3524
-
-
Goulding, C.1
-
46
-
-
0037119945
-
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDα complex
-
Haebel P., et al. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDα complex. EMBO J. 21 (2002) 4774-4784
-
(2002)
EMBO J.
, vol.21
, pp. 4774-4784
-
-
Haebel, P.1
-
47
-
-
0027959156
-
Protein disulphide isomerase: building bridges in protein folding
-
Freedman R., et al. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19 (1994) 331-336
-
(1994)
Trends Biochem. Sci.
, vol.19
, pp. 331-336
-
-
Freedman, R.1
-
48
-
-
0037470064
-
Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase
-
Schwaller M., et al. Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. J. Biol. Chem. 278 (2003) 7154-7159
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 7154-7159
-
-
Schwaller, M.1
-
49
-
-
0029093531
-
Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
-
Darby N., et al. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34 (1995) 11725-11735
-
(1995)
Biochemistry
, vol.34
, pp. 11725-11735
-
-
Darby, N.1
-
50
-
-
0029590754
-
Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase
-
Darby N., et al. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34 (1995) 16770-16780
-
(1995)
Biochemistry
, vol.34
, pp. 16770-16780
-
-
Darby, N.1
-
51
-
-
33644868738
-
Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation
-
Kulp M., et al. Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J. Biol. Chem. 281 (2006) 876-884
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 876-884
-
-
Kulp, M.1
-
52
-
-
15744380512
-
A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain
-
Wilkinson B., et al. A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain. J. Biol. Chem. 280 (2005) 11483-11487
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 11483-11487
-
-
Wilkinson, B.1
-
53
-
-
10344236050
-
The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase
-
Tian R., et al. The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase. J. Biol. Chem. 279 (2004) 48830-48835
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 48830-48835
-
-
Tian, R.1
-
54
-
-
0034739255
-
Contributions of protein disulfide isomerase domains to its chaperone activity
-
Sun X., et al. Contributions of protein disulfide isomerase domains to its chaperone activity. Biochim. Biophys. Acta 1481 (2000) 45-54
-
(2000)
Biochim. Biophys. Acta
, vol.1481
, pp. 45-54
-
-
Sun, X.1
-
55
-
-
0033521682
-
The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
-
Koivunen P., et al. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide. EMBO J. 18 (1999) 65-74
-
(1999)
EMBO J.
, vol.18
, pp. 65-74
-
-
Koivunen, P.1
-
56
-
-
14044256548
-
Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly
-
Koivunen P., et al. Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly. J. Biol. Chem. 280 (2005) 5227-5235
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 5227-5235
-
-
Koivunen, P.1
-
57
-
-
0027220866
-
Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
-
Noiva R., et al. Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J. Biol. Chem. 268 (1993) 19210-19217
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 19210-19217
-
-
Noiva, R.1
-
58
-
-
0032481380
-
The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
-
Klappa P., et al. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 17 (1998) 927-935
-
(1998)
EMBO J.
, vol.17
, pp. 927-935
-
-
Klappa, P.1
-
59
-
-
0036198797
-
Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
-
Freedman R., et al. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep. 3 (2002) 136-140
-
(2002)
EMBO Rep.
, vol.3
, pp. 136-140
-
-
Freedman, R.1
-
60
-
-
12144288546
-
Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase
-
Pirneskoski A., et al. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J. Biol. Chem. 279 (2004) 10374-10381
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 10374-10381
-
-
Pirneskoski, A.1
-
61
-
-
0344255647
-
A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases
-
Lappi A., et al. A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases. J. Mol. Biol. 335 (2004) 283-295
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 283-295
-
-
Lappi, A.1
-
62
-
-
0242497806
-
Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein
-
Ma Q., et al. Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein. J. Biol. Chem. 278 (2003) 44600-44607
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 44600-44607
-
-
Ma, Q.1
-
63
-
-
0043264811
-
Defining the domain boundaries of the human protein disulfide isomerases
-
Alanen H., et al. Defining the domain boundaries of the human protein disulfide isomerases. Antioxid. Redox Signal. 5 (2003) 367-374
-
(2003)
Antioxid. Redox Signal.
, vol.5
, pp. 367-374
-
-
Alanen, H.1
-
64
-
-
0026244229
-
Molscript: a program to produce both detailed and schematic plots of protein structures
-
Kraulis P.J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
-
(1991)
J. Appl. Crystallogr.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
65
-
-
0026319199
-
Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
-
Nicholls A., et al. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
-
(1991)
Proteins
, vol.11
, pp. 281-296
-
-
Nicholls, A.1
|