-
1
-
-
0014197652
-
Studies on the mechanism of the enzymic catalysis of disulfide interchange in proteins
-
Fuchs S, De Lorenzo F, Anfinsen CB (1967) Studies on the mechanism of the enzymic catalysis of disulfide interchange in proteins. J Biol Chem 242:398-402.
-
(1967)
J Biol Chem
, vol.242
, pp. 398-402
-
-
Fuchs, S.1
De Lorenzo, F.2
Anfinsen, C.B.3
-
2
-
-
0031609760
-
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
-
Frand AR, Kaiser CA (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1:161-170. (Pubitemid 128378657)
-
(1998)
Molecular Cell
, vol.1
, Issue.2
, pp. 161-170
-
-
Frand, A.R.1
Kaiser, C.A.2
-
3
-
-
0028334043
-
Influence of protein disulfide isomerase (PDI) on antibody folding in vitro
-
Lilie H, McLaughlin S, Freedman R, Buchner J (1994) Influence of protein disulfide isomerase (PDI) on antibody folding in vitro. J Biol Chem 269:14290-14296. (Pubitemid 24191192)
-
(1994)
Journal of Biological Chemistry
, vol.269
, Issue.19
, pp. 14290-14296
-
-
Lilie, H.1
McLaughlin, S.2
Freedman, R.3
Buchnert, J.4
-
4
-
-
0037016671
-
Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
-
DOI 10.1074/jbc.M107832200
-
Winter J, Klappa P, Freedman RB, Lilie H, Rudolph R (2002) Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. J Biol Chem 277:310-317. (Pubitemid 34952060)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.1
, pp. 310-317
-
-
Winter, J.1
Klappa, P.2
Freedman, R.B.3
Lilie, H.4
Rudolph, R.5
-
5
-
-
0032540353
-
Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen
-
DOI 10.1074/jbc.273.16.9637
-
Wilson R, Lees JF, Bulleid NJ (1998) Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen. J Biol Chem 273:9637-9643. (Pubitemid 28183052)
-
(1998)
Journal of Biological Chemistry
, vol.273
, Issue.16
, pp. 9637-9643
-
-
Wilson, R.1
Lees, J.F.2
Bulleid, N.J.3
-
6
-
-
0031034725
-
2
-
DOI 10.1093/emboj/16.3.651
-
Yao Y, Zhou Y, Wang C (1997) Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. EMBO J 16:651-658. (Pubitemid 27067793)
-
(1997)
EMBO Journal
, vol.16
, Issue.3
, pp. 651-658
-
-
Yao, Y.1
Zhou, Y.-C.2
Wang, C.-C.3
-
7
-
-
0028131648
-
Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
-
Cai H, Wang CC, Tsou CL (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J Biol Chem 269:24550-24552. (Pubitemid 24311703)
-
(1994)
Journal of Biological Chemistry
, vol.269
, Issue.40
, pp. 24550-24552
-
-
Cai, H.1
Wang, C.-C.2
Tsou, C.-L.3
-
8
-
-
0034711439
-
Biochemical basis of oxidative protein folding in the endoplasmic reticulum
-
Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290:1571-1574.
-
(2000)
Science
, vol.290
, pp. 1571-1574
-
-
Tu, B.P.1
Ho-Schleyer, S.C.2
Travers, K.J.3
Weissman, J.S.4
-
9
-
-
0033523910
-
Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
-
Molinari M, Helenius A (1999) Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402:90-93.
-
(1999)
Nature
, vol.402
, pp. 90-93
-
-
Molinari, M.1
Helenius, A.2
-
10
-
-
77952584245
-
A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules
-
Kang K, Park B, Oh C, Cho K, Ahn K (2009) A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules. Antioxid Redox Signal 11:2553-2561.
-
(2009)
Antioxid Redox Signal
, vol.11
, pp. 2553-2561
-
-
Kang, K.1
Park, B.2
Oh, C.3
Cho, K.4
Ahn, K.5
-
11
-
-
0027270735
-
Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
-
DOI 10.1038/365185a0
-
Weissman JS, Kim PS (1993) Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365:185-188. (Pubitemid 23282068)
-
(1993)
Nature
, vol.365
, Issue.6442
, pp. 185-188
-
-
Weissman, J.S.1
Kim, P.S.2
-
12
-
-
71549132149
-
Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
-
Hatahet F, Ruddock LW (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 11:2807-2850.
-
(2009)
Antioxid Redox Signal
, vol.11
, pp. 2807-2850
-
-
Hatahet, F.1
Ruddock, L.W.2
-
13
-
-
0036198797
-
Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
-
DOI 10.1093/embo-reports/kvf035
-
Freedman RB, Klappa P, Ruddock LW (2002) Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 3:136-140. (Pubitemid 34213490)
-
(2002)
EMBO Reports
, vol.3
, Issue.2
, pp. 136-140
-
-
Freedman, R.B.1
Klappa, P.2
Ruddock, L.W.3
-
14
-
-
30344444015
-
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
-
DOI 10.1016/j.cell.2005.10.044, PII S0092867405014121
-
Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124:61-73. (Pubitemid 43069310)
-
(2006)
Cell
, vol.124
, Issue.1
, pp. 61-73
-
-
Tian, G.1
Xiang, S.2
Noiva, R.3
Lennarz, W.J.4
Schindelin, H.5
-
15
-
-
0032481380
-
The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
-
DOI 10.1093/emboj/17.4.927
-
Klappa P, Ruddock LW, Darby NJ, Freedman RB (1998) The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 17:927-935. (Pubitemid 28077647)
-
(1998)
EMBO Journal
, vol.17
, Issue.4
, pp. 927-935
-
-
Klappa, P.1
Ruddock, L.W.2
Darby, N.J.3
Freedman, R.B.4
-
16
-
-
70350124054
-
Mapping of the ligand-binding site on the b′ domain of human PDI: Interaction with peptide ligands and the x-linker region
-
Byrne LJ, Sidhu A, Wallis AK, Ruddock LW, Freedman RB, Howard MJ, Williamson RA (2009) Mapping of the ligand-binding site on the b′ domain of human PDI: interaction with peptide ligands and the x-linker region. Biochem J 423:209-217.
-
(2009)
Biochem J
, vol.423
, pp. 209-217
-
-
Byrne, L.J.1
Sidhu, A.2
Wallis, A.K.3
Ruddock, L.W.4
Freedman, R.B.5
Howard, M.J.6
Williamson, R.A.7
-
17
-
-
77956234972
-
Plasticity of human protein disulfide isomerase: Evidence for mobility around the X-linker region and its functional significance
-
Wang C, Chen S, Wang X, Wang L, Wallis AK, Freedman RB, Wang CC (2010) Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance. J Biol Chem 285:26788-26797.
-
(2010)
J Biol Chem
, vol.285
, pp. 26788-26797
-
-
Wang, C.1
Chen, S.2
Wang, X.3
Wang, L.4
Wallis, A.K.5
Freedman, R.B.6
Wang, C.C.7
-
18
-
-
77957773053
-
Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI
-
Inaba K, Masui S, Iida H, Vavassori S, Sitia R, Suzuki M (2010) Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J 29:3330-3343.
-
(2010)
EMBO J
, vol.29
, pp. 3330-3343
-
-
Inaba, K.1
Masui, S.2
Iida, H.3
Vavassori, S.4
Sitia, R.5
Suzuki, M.6
-
19
-
-
2542475140
-
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
-
DOI 10.1016/S0092-8674(04)00418-0, PII S0092867404004180
-
Gross E, Kastner DB, Kaiser CA, Fass D (2004) Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117:601-610. (Pubitemid 38692526)
-
(2004)
Cell
, vol.117
, Issue.5
, pp. 601-610
-
-
Gross, E.1
Kastner, D.B.2
Kaiser, C.A.3
Fass, D.4
-
20
-
-
0025831094
-
Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae
-
Farquhar R, Honey N, Murant SJ, Bossier P, Schultz L, Montgomery D, Ellis RW, Freedman RB, Tuite MF (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108:81-89.
-
(1991)
Gene
, vol.108
, pp. 81-89
-
-
Farquhar, R.1
Honey, N.2
Murant, S.J.3
Bossier, P.4
Schultz, L.5
Montgomery, D.6
Ellis, R.W.7
Freedman, R.B.8
Tuite, M.F.9
-
21
-
-
0032512878
-
The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
-
DOI 10.1006/jmbi.1997.1504
-
Darby NJ, Penka E, Vincentelli R (1998) The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J Mol Biol 276:239-247. (Pubitemid 28085421)
-
(1998)
Journal of Molecular Biology
, vol.276
, Issue.1
, pp. 239-247
-
-
Darby, N.J.1
Penka, E.2
Vincentelli, R.3
-
22
-
-
58649096169
-
Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase
-
Wang L, Li SJ, Sidhu A, Zhu L, Liang Y, Freedman RB, Wang CC (2009) Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase. J Biol Chem 284:199-206.
-
(2009)
J Biol Chem
, vol.284
, pp. 199-206
-
-
Wang, L.1
Li, S.J.2
Sidhu, A.3
Zhu, L.4
Liang, Y.5
Freedman, R.B.6
Wang, C.C.7
-
23
-
-
0035815678
-
Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase: The N-terminal domains a and b enhance this function and can be substituted in part by those of ERp57
-
DOI 10.1074/jbc.M010656200
-
Pirneskoski A, Ruddock LW, Klappa P, Freedman RB, Kivirikko KI, Koivunen P (2001) Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57. J Biol Chem 276:11287-11293. (Pubitemid 38089317)
-
(2001)
Journal of Biological Chemistry
, vol.276
, Issue.14
, pp. 11287-11293
-
-
Pirneskoski, A.1
Ruddock, L.W.2
Klappa, P.3
Freedman, R.B.4
Kivirikko, K.I.5
Koivunen, P.6
-
24
-
-
67649746317
-
Generating an unfoldase from thioredoxin-like domains
-
Forster ML, Mahn JJ, Tsai B (2009) Generating an unfoldase from thioredoxin-like domains. J Biol Chem 284:13045-13056.
-
(2009)
J Biol Chem
, vol.284
, pp. 13045-13056
-
-
Forster, M.L.1
Mahn, J.J.2
Tsai, B.3
-
25
-
-
0030586703
-
Characteristic, activity and conformational studies of [A6-Ser, A11-Ser]-insulin
-
DOI 10.1016/0167-4838(96)00054-4
-
Dai Y, Tang JG (1996) Characteristic, activity and conformational studies of [A6-Ser, A11-Ser]-insulin. Biochim Biophys Acta 1296:63-68. (Pubitemid 26259809)
-
(1996)
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
, vol.1296
, Issue.1
, pp. 63-68
-
-
Dai, Y.1
Tang, J.-G.2
-
26
-
-
0038043253
-
In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process
-
Qiao ZS, Min CY, Hua QX, Weiss MA, Feng YM (2003) In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process. J Biol Chem 278:17800-17809.
-
(2003)
J Biol Chem
, vol.278
, pp. 17800-17809
-
-
Qiao, Z.S.1
Min, C.Y.2
Hua, Q.X.3
Weiss, M.A.4
Feng, Y.M.5
-
27
-
-
0035814878
-
Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro
-
Qiao ZS, Guo ZY, Feng YM (2001) Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro. Biochemistry 40:2662-2668.
-
(2001)
Biochemistry
, vol.40
, pp. 2662-2668
-
-
Qiao, Z.S.1
Guo, Z.Y.2
Feng, Y.M.3
-
28
-
-
0026530383
-
Quantitative analysis of protein far UV circular dichroism spectra by neural networks
-
Bohm G, Muhr R, Jaenicke R (1992) Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng 5:191-195.
-
(1992)
Protein Eng
, vol.5
, pp. 191-195
-
-
Bohm, G.1
Muhr, R.2
Jaenicke, R.3
-
29
-
-
0029146852
-
Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
-
Quan H, Fan G, Wang CC (1995) Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J Biol Chem 270:17078-17080.
-
(1995)
J Biol Chem
, vol.270
, pp. 17078-17080
-
-
Quan, H.1
Fan, G.2
Wang, C.C.3
-
30
-
-
77956514975
-
The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α
-
Chambers JE, Tavender TJ, Oka OB, Warwood S, Knight D, Bulleid NJ (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α. J Biol Chem 285:29200-29207.
-
(2010)
J Biol Chem
, vol.285
, pp. 29200-29207
-
-
Chambers, J.E.1
Tavender, T.J.2
Oka, O.B.3
Warwood, S.4
Knight, D.5
Bulleid, N.J.6
-
31
-
-
0027293791
-
Determination of the reduction-oxidation potential of the thioredoxin- Like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
-
Lundstrom J, Holmgren A (1993) Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32:6649-6655. (Pubitemid 23217134)
-
(1993)
Biochemistry
, vol.32
, Issue.26
, pp. 6649-6655
-
-
Lundstrom, J.1
Holmgren, A.2
-
32
-
-
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 RS, Kurz M, Jarrott R, Shouldice SR, Hiniker A, Martin JL, Heras B, Bardwell JC (2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem 284:10150-10159.
-
(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
Kurz, M.7
Jarrott, R.8
Shouldice, S.R.9
Hiniker, A.10
Martin, J.L.11
Heras, B.12
Bardwell, J.C.13
-
33
-
-
0037112617
-
Renaturation of human proinsulin - A study on refolding and conversion to insulin
-
DOI 10.1016/S0003-2697(02)00287-7, PII S0003269702002877
-
Winter J, Lilie H, Rudolph R (2002) Renaturation of human proinsulin - a study on refolding and conversion to insulin. Anal Biochem 310:148-155. (Pubitemid 35388255)
-
(2002)
Analytical Biochemistry
, vol.310
, Issue.2
, pp. 148-155
-
-
Winter, J.1
Lilie, H.2
Rudolph, R.3
-
34
-
-
0031570750
-
Putative folding pathway of insulin-like growth factor-1
-
DOI 10.1006/abbi.1997.9996
-
Rosenfeld RD, Miller JA, Narhi LO, Hawkins N, Katta V, Lauren S, Weiss MA, Arakawa T (1997) Putative folding pathway of insulin-like growth factor-I. Arch Biochem Biophys 342:298-305. (Pubitemid 27251251)
-
(1997)
Archives of Biochemistry and Biophysics
, vol.342
, Issue.2
, pp. 298-305
-
-
Rosenfeld, R.D.1
Miller, J.A.2
Narhi, L.O.3
Hawkins, N.4
Katta, V.5
Lauren, S.6
Weiss, M.A.7
Arakawa, T.8
-
35
-
-
0037126725
-
A protein caught in a kinetic trap: Structures and stabilities of insulin disulfide isomers
-
DOI 10.1021/bi0202981
-
Hua QX, Jia W, Frank BH, Phillips NF, Weiss MA (2002) A protein caught in a kinetic trap: structures and stabilities of insulin disulfide isomers. Biochemistry 41:14700-14715. (Pubitemid 35470650)
-
(2002)
Biochemistry
, vol.41
, Issue.50
, pp. 14700-14715
-
-
Hua, Q.-X.1
Jia, W.2
Frank, B.H.3
Phillips, N.F.B.4
Weiss, M.A.5
-
36
-
-
0027481123
-
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
-
Wunderlich M, Glockshuber R (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci 2:717-726. (Pubitemid 23121086)
-
(1993)
Protein Science
, vol.2
, Issue.5
, pp. 717-726
-
-
Wunderlich, M.1
Glockshuber, R.2
|