-
2
-
-
84862548210
-
Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals
-
Y. Sato, and K. Inaba Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals FEBS J. 279 2012 2262 2271
-
(2012)
FEBS J.
, vol.279
, pp. 2262-2271
-
-
Sato, Y.1
Inaba, K.2
-
4
-
-
71549132149
-
Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
-
F. Hatahet, and L.W. Ruddock Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation Antioxid. Redox Signal. 11 2009 2807 2850
-
(2009)
Antioxid. Redox Signal.
, vol.11
, pp. 2807-2850
-
-
Hatahet, F.1
Ruddock, L.W.2
-
5
-
-
41549159471
-
The human PDI family: Versatility packed into a single fold
-
C. Appenzeller-Herzog, and L. Ellgaard The human PDI family: versatility packed into a single fold Biochim. Biophys. Acta 1783 2008 535 548
-
(2008)
Biochim. Biophys. Acta
, vol.1783
, pp. 535-548
-
-
Appenzeller-Herzog, C.1
Ellgaard, L.2
-
6
-
-
78651157389
-
Purification and properties of a microsomal enzyme system catalyzing the reactivation of reduced ribonuclease and lysozyme
-
R.F. Goldberger, C.J. Epstein, and C.B. Anfinsen Purification and properties of a microsomal enzyme system catalyzing the reactivation of reduced ribonuclease and lysozyme J. Biol. Chem. 239 1964 1406 1410
-
(1964)
J. Biol. Chem.
, vol.239
, pp. 1406-1410
-
-
Goldberger, R.F.1
Epstein, C.J.2
Anfinsen, C.B.3
-
7
-
-
0022387362
-
Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
-
J.C. Edman, L. Ellis, R.W. Blacher, R.A. Roth, and W.J. Rutter Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin Nature 317 1985 267 270
-
(1985)
Nature
, vol.317
, pp. 267-270
-
-
Edman, J.C.1
Ellis, L.2
Blacher, R.W.3
Roth, R.A.4
Rutter, W.J.5
-
8
-
-
30344444015
-
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
-
G. Tian, S. Xiang, R. Noiva, W.J. Lennarz, and H. Schindelin 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
Xiang, S.2
Noiva, R.3
Lennarz, W.J.4
Schindelin, H.5
-
9
-
-
84878866786
-
Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
-
C. Wang, W. Li, J. Ren, J. Fang, H. Ke, W. Gong, W. Feng, and C.C. Wang Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase Antioxid. Redox Signal. 19 2013 36 45
-
(2013)
Antioxid. Redox Signal.
, vol.19
, pp. 36-45
-
-
Wang, C.1
Li, W.2
Ren, J.3
Fang, J.4
Ke, H.5
Gong, W.6
Feng, W.7
Wang, C.C.8
-
10
-
-
0032481380
-
The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
-
P. Klappa, L.W. Ruddock, N.J. Darby, and R.B. Freedman 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
Ruddock, L.W.2
Darby, N.J.3
Freedman, R.B.4
-
11
-
-
0027270735
-
Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
-
J.S. Weissman, and P.S. Kim Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase Nature 365 1993 185 188
-
(1993)
Nature
, vol.365
, pp. 185-188
-
-
Weissman, J.S.1
Kim, P.S.2
-
12
-
-
84896717675
-
Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family
-
R. Kojima, M. Okumura, S. Masui, S. Kanemura, M. Inoue, M. Saiki, H. Yamaguchi, T. Hikima, M. Suzuki, S. Akiyama, and K. Inaba Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family Structure 22 2014 431 443
-
(2014)
Structure
, vol.22
, pp. 431-443
-
-
Kojima, R.1
Okumura, M.2
Masui, S.3
Kanemura, S.4
Inoue, M.5
Saiki, M.6
Yamaguchi, H.7
Hikima, T.8
Suzuki, M.9
Akiyama, S.10
Inaba, K.11
-
13
-
-
84907587023
-
Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1alpha (Ero1alpha) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A
-
M. Okumura, H. Kadokura, S. Hashimoto, K. Yutani, S. Kanemura, T. Hikima, Y. Hidaka, L. Ito, K. Shiba, S. Masui, D. Imai, S. Imaoka, H. Yamaguchi, and K. Inaba Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1alpha (Ero1alpha) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A J. Biol. Chem. 289 2014 27004 27018
-
(2014)
J. Biol. Chem.
, vol.289
, pp. 27004-27018
-
-
Okumura, M.1
Kadokura, H.2
Hashimoto, S.3
Yutani, K.4
Kanemura, S.5
Hikima, T.6
Hidaka, Y.7
Ito, L.8
Shiba, K.9
Masui, S.10
Imai, D.11
Imaoka, S.12
Yamaguchi, H.13
Inaba, K.14
-
14
-
-
0033199237
-
The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
-
B. van den Berg, E.W. Chung, C.V. Robinson, P.L. Mateo, and C.M. Dobson The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase EMBO J. 18 1999 4794 4803
-
(1999)
EMBO J.
, vol.18
, pp. 4794-4803
-
-
Van Den Berg, B.1
Chung, E.W.2
Robinson, C.V.3
Mateo, P.L.4
Dobson, C.M.5
-
15
-
-
84921721414
-
Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway
-
A.G. Irvine, A.K. Wallis, N. Sanghera, M.L. Rowe, L.W. Ruddock, M.J. Howard, R.A. Williamson, C.A. Blindauer, and R.B. Freedman Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway PLoS One 9 2014 e82511
-
(2014)
PLoS One
, vol.9
, pp. e82511
-
-
Irvine, A.G.1
Wallis, A.K.2
Sanghera, N.3
Rowe, M.L.4
Ruddock, L.W.5
Howard, M.J.6
Williamson, R.A.7
Blindauer, C.A.8
Freedman, R.B.9
-
16
-
-
77449149046
-
Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface
-
O. Serve, Y. Kamiya, A. Maeno, M. Nakano, C. Murakami, H. Sasakawa, Y. Yamaguchi, T. Harada, E. Kurimoto, M. Yagi-Utsumi, T. Iguchi, K. Inaba, J. Kikuchi, O. Asami, T. Kajino, T. Oka, M. Nakasako, and K. Kato Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface J. Mol. Biol. 396 2010 361 374
-
(2010)
J. Mol. Biol.
, vol.396
, pp. 361-374
-
-
Serve, O.1
Kamiya, Y.2
Maeno, A.3
Nakano, M.4
Murakami, C.5
Sasakawa, H.6
Yamaguchi, Y.7
Harada, T.8
Kurimoto, E.9
Yagi-Utsumi, M.10
Iguchi, T.11
Inaba, K.12
Kikuchi, J.13
Asami, O.14
Kajino, T.15
Oka, T.16
Nakasako, M.17
Kato, K.18
-
17
-
-
58149215628
-
Insights into MHC class i peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
-
G. Dong, P.A. Wearsch, D.R. Peaper, P. Cresswell, and K.M. Reinisch Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer Immunity 30 2009 21 32
-
(2009)
Immunity
, vol.30
, pp. 21-32
-
-
Dong, G.1
Wearsch, P.A.2
Peaper, D.R.3
Cresswell, P.4
Reinisch, K.M.5
-
18
-
-
2442761708
-
The protein disulphide-isomerase family: Unravelling a string of folds
-
D.M. Ferrari, and H.D. Soling The protein disulphide-isomerase family: unravelling a string of folds Biochem. J. 339 Pt 1 1999 1 10
-
(1999)
Biochem. J.
, vol.339
, Issue.PART 1
, pp. 1-10
-
-
Ferrari, D.M.1
Soling, H.D.2
-
19
-
-
77957773053
-
Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI
-
K. Inaba, S. Masui, H. Iida, S. Vavassori, R. Sitia, and M. Suzuki Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI EMBO J. 29 2010 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
-
20
-
-
0242649039
-
Tissue distribution of three members of the murine protein disulfide isomerase (PDI) family
-
N. Marcus, D. Shaffer, P. Farrar, and M. Green Tissue distribution of three members of the murine protein disulfide isomerase (PDI) family Biochim. Biophys. Acta 1309 1996 253 260
-
(1996)
Biochim. Biophys. Acta
, vol.1309
, pp. 253-260
-
-
Marcus, N.1
Shaffer, D.2
Farrar, P.3
Green, M.4
-
22
-
-
33846192436
-
ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
-
C.E. Jessop, S. Chakravarthi, N. Garbi, G.J. Hammerling, S. Lovell, and N.J. Bulleid ERp57 is essential for efficient folding of glycoproteins sharing common structural domains EMBO J. 26 2007 28 40
-
(2007)
EMBO J.
, vol.26
, pp. 28-40
-
-
Jessop, C.E.1
Chakravarthi, S.2
Garbi, N.3
Hammerling, G.J.4
Lovell, S.5
Bulleid, N.J.6
-
23
-
-
34547121970
-
Selective loading of high-affinity peptides onto major histocompatibility complex class i molecules by the tapasin-ERp57 heterodimer
-
P.A. Wearsch, and P. Cresswell Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer Nat. Immunol. 8 2007 873 881
-
(2007)
Nat. Immunol.
, vol.8
, pp. 873-881
-
-
Wearsch, P.A.1
Cresswell, P.2
-
24
-
-
35548992416
-
Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells
-
M. Schelhaas, J. Malmstrom, L. Pelkmans, J. Haugstetter, L. Ellgaard, K. Grunewald, and A. Helenius Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells Cell 131 2007 516 529
-
(2007)
Cell
, vol.131
, pp. 516-529
-
-
Schelhaas, M.1
Malmstrom, J.2
Pelkmans, L.3
Haugstetter, J.4
Ellgaard, L.5
Grunewald, K.6
Helenius, A.7
-
25
-
-
0344443678
-
EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor
-
D.C. Sullivan, L. Huminiecki, J.W. Moore, J.J. Boyle, R. Poulsom, D. Creamer, J. Barker, and R. Bicknell EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor J. Biol. Chem. 278 2003 47079 47088
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 47079-47088
-
-
Sullivan, D.C.1
Huminiecki, L.2
Moore, J.W.3
Boyle, J.J.4
Poulsom, R.5
Creamer, D.6
Barker, J.7
Bicknell, R.8
-
26
-
-
2442487968
-
ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins
-
B. Knoblach, B.O. Keller, J. Groenendyk, S. Aldred, J. Zheng, B.D. Lemire, L. Li, and M. Michalak ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins Mol. Cell. Proteomics 2 2003 1104 1119
-
(2003)
Mol. Cell. Proteomics
, vol.2
, pp. 1104-1119
-
-
Knoblach, B.1
Keller, B.O.2
Groenendyk, J.3
Aldred, S.4
Zheng, J.5
Lemire, B.D.6
Li, L.7
Michalak, M.8
-
27
-
-
84866888146
-
Role of ERp46 in beta-cell lipoapoptosis through endoplasmic reticulum stress pathway as well as the protective effect of exendin-4
-
D.L. Chen, J.N. Xiang, and L.Y. Yang Role of ERp46 in beta-cell lipoapoptosis through endoplasmic reticulum stress pathway as well as the protective effect of exendin-4 Biochem. Biophys. Res. Commun. 426 2012 324 329
-
(2012)
Biochem. Biophys. Res. Commun.
, vol.426
, pp. 324-329
-
-
Chen, D.L.1
Xiang, J.N.2
Yang, L.Y.3
-
28
-
-
75749115950
-
ERp46 binds to AdipoR1, but not AdipoR2, and modulates adiponectin signalling
-
H.K. Charlton, J. Webster, S. Kruger, F. Simpson, A.A. Richards, and J.P. Whitehead ERp46 binds to AdipoR1, but not AdipoR2, and modulates adiponectin signalling Biochem. Biophys. Res. Commun. 392 2010 234 239
-
(2010)
Biochem. Biophys. Res. Commun.
, vol.392
, pp. 234-239
-
-
Charlton, H.K.1
Webster, J.2
Kruger, S.3
Simpson, F.4
Richards, A.A.5
Whitehead, J.P.6
-
29
-
-
84902338966
-
Inactivation of mammalian Ero1alpha is catalysed by specific protein disulfide-isomerases
-
C. Shepherd, O.B. Oka, and N.J. Bulleid Inactivation of mammalian Ero1alpha is catalysed by specific protein disulfide-isomerases Biochem. J. 461 2014 107 113
-
(2014)
Biochem. J.
, vol.461
, pp. 107-113
-
-
Shepherd, C.1
Oka, O.B.2
Bulleid, N.J.3
-
30
-
-
84857570189
-
Structure, mechanism, and evolution of Ero1 family enzymes
-
K. Araki, and K. Inaba Structure, mechanism, and evolution of Ero1 family enzymes Antioxid. Redox Signal. 16 2012 790 799
-
(2012)
Antioxid. Redox Signal.
, vol.16
, pp. 790-799
-
-
Araki, K.1
Inaba, K.2
-
31
-
-
77956334107
-
Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum
-
T.J. Tavender, and N.J. Bulleid Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum Antioxid. Redox Signal. 13 2010 1177 1187
-
(2010)
Antioxid. Redox Signal.
, vol.13
, pp. 1177-1187
-
-
Tavender, T.J.1
Bulleid, N.J.2
-
32
-
-
79955527426
-
Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI)
-
S. Masui, S. Vavassori, C. Fagioli, R. Sitia, and K. Inaba Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI) J. Biol. Chem. 286 2011 16261 16271
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 16261-16271
-
-
Masui, S.1
Vavassori, S.2
Fagioli, C.3
Sitia, R.4
Inaba, K.5
-
33
-
-
78650270477
-
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
-
T.J. Tavender, J.J. Springate, and N.J. Bulleid Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum EMBO J. 29 2010 4185 4197
-
(2010)
EMBO J.
, vol.29
, pp. 4185-4197
-
-
Tavender, T.J.1
Springate, J.J.2
Bulleid, N.J.3
-
34
-
-
78649918283
-
Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
-
E. Zito, E.P. Melo, Y. Yang, A. Wahlander, T.A. Neubert, and D. Ron Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin Mol. Cell 40 2010 787 797
-
(2010)
Mol. Cell
, vol.40
, pp. 787-797
-
-
Zito, E.1
Melo, E.P.2
Yang, Y.3
Wahlander, A.4
Neubert, T.A.5
Ron, D.6
-
35
-
-
79551689187
-
Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation
-
V.D. Nguyen, M.J. Saaranen, A.R. Karala, A.K. Lappi, L. Wang, I.B. Raykhel, H.I. Alanen, K.E. Salo, C.C. Wang, and L.W. Ruddock Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation J. Mol. Biol. 406 2011 503 515
-
(2011)
J. Mol. Biol.
, vol.406
, pp. 503-515
-
-
Nguyen, V.D.1
Saaranen, M.J.2
Karala, A.R.3
Lappi, A.K.4
Wang, L.5
Raykhel, I.B.6
Alanen, H.I.7
Salo, K.E.8
Wang, C.C.9
Ruddock, L.W.10
-
36
-
-
84861662334
-
Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
-
L.A. Rutkevich, and D.B. Williams Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum Mol. Biol. Cell 23 2012 2017 2027
-
(2012)
Mol. Biol. Cell
, vol.23
, pp. 2017-2027
-
-
Rutkevich, L.A.1
Williams, D.B.2
-
37
-
-
84882771697
-
Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding
-
Y. Sato, R. Kojima, M. Okumura, M. Hagiwara, S. Masui, K. Maegawa, M. Saiki, T. Horibe, M. Suzuki, and K. Inaba Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding Sci. Rep 3 2013 2456
-
(2013)
Sci. Rep
, vol.3
, pp. 2456
-
-
Sato, Y.1
Kojima, R.2
Okumura, M.3
Hagiwara, M.4
Masui, S.5
Maegawa, K.6
Saiki, M.7
Horibe, T.8
Suzuki, M.9
Inaba, K.10
-
38
-
-
84055178426
-
Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4
-
X. Wang, L. Wang, X. Wang, F. Sun, and C.C. Wang Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4 Biochem. J. 441 2012 113 118
-
(2012)
Biochem. J.
, vol.441
, pp. 113-118
-
-
Wang, X.1
Wang, L.2
Wang, X.3
Sun, F.4
Wang, C.C.5
-
39
-
-
82755171868
-
Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle
-
Z. Cao, T.J. Tavender, A.W. Roszak, R.J. Cogdell, and N.J. Bulleid Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle J. Biol. Chem. 286 2011 42257 42266
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 42257-42266
-
-
Cao, Z.1
Tavender, T.J.2
Roszak, A.W.3
Cogdell, R.J.4
Bulleid, N.J.5
-
40
-
-
0033853089
-
SAGEmap: A public gene expression resource
-
A.E. Lash, C.M. Tolstoshev, L. Wagner, G.D. Schuler, R.L. Strausberg, G.J. Riggins, and S.F. Altschul SAGEmap: a public gene expression resource Genome Res. 10 2000 1051 1060
-
(2000)
Genome Res.
, vol.10
, pp. 1051-1060
-
-
Lash, A.E.1
Tolstoshev, C.M.2
Wagner, L.3
Schuler, G.D.4
Strausberg, R.L.5
Riggins, G.J.6
Altschul, S.F.7
-
41
-
-
84874024456
-
Studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility
-
N.T. Amin, A.K. Wallis, S.A. Wells, M.L. Rowe, R.A. Williamson, M.J. Howard, R.B. Freedman, and NMR High-resolution studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility Biochem. J. 450 2013 321 332
-
(2013)
Biochem. J.
, vol.450
, pp. 321-332
-
-
Amin, N.T.1
Wallis, A.K.2
Wells, S.A.3
Rowe, M.L.4
Williamson, R.A.5
Howard, M.J.6
Freedman, R.B.7
High-Resolution, N.M.R.8
-
42
-
-
84872744555
-
The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities
-
F.X. Kober, W. Koelmel, J. Kuper, J. Drechsler, C. Mais, H.M. Hermanns, and H. Schindelin The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities J. Biol. Chem. 288 2013 2029 2039
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 2029-2039
-
-
Kober, F.X.1
Koelmel, W.2
Kuper, J.3
Drechsler, J.4
Mais, C.5
Hermanns, H.M.6
Schindelin, H.7
-
43
-
-
33845937716
-
ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57
-
H.I. Alanen, R.A. Williamson, M.J. Howard, F.S. Hatahet, K.E. Salo, A. Kauppila, S. Kellokumpu, and L.W. Ruddock ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57 J. Biol. Chem. 281 2006 33727 33738
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 33727-33738
-
-
Alanen, H.I.1
Williamson, R.A.2
Howard, M.J.3
Hatahet, F.S.4
Salo, K.E.5
Kauppila, A.6
Kellokumpu, S.7
Ruddock, L.W.8
-
44
-
-
0037428470
-
ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress
-
P.M. Cunnea, A. Miranda-Vizuete, G. Bertoli, T. Simmen, A.E. Damdimopoulos, S. Hermann, S. Leinonen, M.P. Huikko, J.A. Gustafsson, R. Sitia, and G. Spyrou ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress J. Biol. Chem. 278 2003 1059 1066
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 1059-1066
-
-
Cunnea, P.M.1
Miranda-Vizuete, A.2
Bertoli, G.3
Simmen, T.4
Damdimopoulos, A.E.5
Hermann, S.6
Leinonen, S.7
Huikko, M.P.8
Gustafsson, J.A.9
Sitia, R.10
Spyrou, G.11
-
45
-
-
0037462652
-
JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs
-
A. Hosoda, Y. Kimata, A. Tsuru, and K. Kohno JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs J. Biol. Chem. 278 2003 2669 2676
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 2669-2676
-
-
Hosoda, A.1
Kimata, Y.2
Tsuru, A.3
Kohno, K.4
-
46
-
-
48249117110
-
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
-
R. Ushioda, J. Hoseki, K. Araki, G. Jansen, D.Y. Thomas, and K. Nagata ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER Science 321 2008 569 572
-
(2008)
Science
, vol.321
, pp. 569-572
-
-
Ushioda, R.1
Hoseki, J.2
Araki, K.3
Jansen, G.4
Thomas, D.Y.5
Nagata, K.6
-
47
-
-
79951491416
-
Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5
-
M. Hagiwara, K. Maegawa, M. Suzuki, R. Ushioda, K. Araki, Y. Matsumoto, J. Hoseki, K. Nagata, and K. Inaba Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5 Mol. Cell 41 2011 432 444
-
(2011)
Mol. Cell
, vol.41
, pp. 432-444
-
-
Hagiwara, M.1
Maegawa, K.2
Suzuki, M.3
Ushioda, R.4
Araki, K.5
Matsumoto, Y.6
Hoseki, J.7
Nagata, K.8
Inaba, K.9
-
48
-
-
84885647401
-
Glycosylation-independent ERAD pathway serves as a backup system under ER stress
-
R. Ushioda, J. Hoseki, and K. Nagata Glycosylation-independent ERAD pathway serves as a backup system under ER stress Mol. Biol. Cell 24 2013 3155 3163
-
(2013)
Mol. Biol. Cell
, vol.24
, pp. 3155-3163
-
-
Ushioda, R.1
Hoseki, J.2
Nagata, K.3
-
49
-
-
84880819436
-
ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor
-
O.B. Oka, M.A. Pringle, I.M. Schopp, I. Braakman, and N.J. Bulleid ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor Mol. Cell 50 2013 793 804
-
(2013)
Mol. Cell
, vol.50
, pp. 793-804
-
-
Oka, O.B.1
Pringle, M.A.2
Schopp, I.M.3
Braakman, I.4
Bulleid, N.J.5
-
50
-
-
84890233980
-
Two phases of disulfide bond formation have differing requirements for oxygen
-
M. Koritzinsky, F. Levitin, T. van den Beucken, R.A. Rumantir, N.J. Harding, K.C. Chu, P.C. Boutros, I. Braakman, and B.G. Wouters Two phases of disulfide bond formation have differing requirements for oxygen J. Cell Biol. 203 2013 615 627
-
(2013)
J. Cell Biol.
, vol.203
, pp. 615-627
-
-
Koritzinsky, M.1
Levitin, F.2
Van Den Beucken, T.3
Rumantir, R.A.4
Harding, N.J.5
Chu, K.C.6
Boutros, P.C.7
Braakman, I.8
Wouters, B.G.9
-
51
-
-
0141753993
-
Thiol-mediated protein retention in the endoplasmic reticulum: The role of ERp44
-
T. Anelli, M. Alessio, A. Bachi, L. Bergamelli, G. Bertoli, S. Camerini, A. Mezghrani, E. Ruffato, T. Simmen, and R. Sitia Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44 EMBO J. 22 2003 5015 5022
-
(2003)
EMBO J.
, vol.22
, pp. 5015-5022
-
-
Anelli, T.1
Alessio, M.2
Bachi, A.3
Bergamelli, L.4
Bertoli, G.5
Camerini, S.6
Mezghrani, A.7
Ruffato, E.8
Simmen, T.9
Sitia, R.10
-
52
-
-
0037083869
-
ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
-
T. Anelli, M. Alessio, A. Mezghrani, T. Simmen, F. Talamo, A. Bachi, and R. Sitia ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family EMBO J. 21 2002 835 844
-
(2002)
EMBO J.
, vol.21
, pp. 835-844
-
-
Anelli, T.1
Alessio, M.2
Mezghrani, A.3
Simmen, T.4
Talamo, F.5
Bachi, A.6
Sitia, R.7
-
53
-
-
11844269232
-
Lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
-
T. Higo, M. Hattori, T. Nakamura, T. Natsume, T. Michikawa, K. Mikoshiba, and ER Subtype-specific lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44 Cell 120 2005 85 98
-
(2005)
Cell
, vol.120
, pp. 85-98
-
-
Higo, T.1
Hattori, M.2
Nakamura, T.3
Natsume, T.4
Michikawa, T.5
Mikoshiba, K.6
Subtype-Specific, E.R.7
-
54
-
-
34248197560
-
Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention
-
Z.V. Wang, T.D. Schraw, J.Y. Kim, T. Khan, M.W. Rajala, A. Follenzi, and P.E. Scherer Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention Mol. Cell. Biol. 27 2007 3716 3731
-
(2007)
Mol. Cell. Biol.
, vol.27
, pp. 3716-3731
-
-
Wang, Z.V.1
Schraw, T.D.2
Kim, J.Y.3
Khan, T.4
Rajala, M.W.5
Follenzi, A.6
Scherer, P.E.7
-
55
-
-
34948899397
-
Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis
-
T. Anelli, S. Ceppi, L. Bergamelli, M. Cortini, S. Masciarelli, C. Valetti, and R. Sitia Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis EMBO J. 26 2007 4177 4188
-
(2007)
EMBO J.
, vol.26
, pp. 4177-4188
-
-
Anelli, T.1
Ceppi, S.2
Bergamelli, L.3
Cortini, M.4
Masciarelli, S.5
Valetti, C.6
Sitia, R.7
-
56
-
-
84885668419
-
Dynamic regulation of Ero1alpha and peroxiredoxin 4 localization in the secretory pathway
-
T. Kakihana, K. Araki, S. Vavassori, S. Iemura, M. Cortini, C. Fagioli, T. Natsume, R. Sitia, and K. Nagata Dynamic regulation of Ero1alpha and peroxiredoxin 4 localization in the secretory pathway J. Biol. Chem. 288 2013 29586 29594
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 29586-29594
-
-
Kakihana, T.1
Araki, K.2
Vavassori, S.3
Iemura, S.4
Cortini, M.5
Fagioli, C.6
Natsume, T.7
Sitia, R.8
Nagata, K.9
-
57
-
-
49649122527
-
Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44
-
A. Fraldi, E. Zito, F. Annunziata, A. Lombardi, M. Cozzolino, M. Monti, C. Spampanato, A. Ballabio, P. Pucci, R. Sitia, and M.P. Cosma Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44 Hum. Mol. Genet 17 2008 2610 2621
-
(2008)
Hum. Mol. Genet
, vol.17
, pp. 2610-2621
-
-
Fraldi, A.1
Zito, E.2
Annunziata, F.3
Lombardi, A.4
Cozzolino, M.5
Monti, M.6
Spampanato, C.7
Ballabio, A.8
Pucci, P.9
Sitia, R.10
Cosma, M.P.11
-
58
-
-
33646699342
-
Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44
-
M. Otsu, G. Bertoli, C. Fagioli, E. Guerini-Rocco, S. Nerini-Molteni, E. Ruffato, and R. Sitia Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44 Antioxid. Redox Signal. 8 2006 274 282
-
(2006)
Antioxid. Redox Signal.
, vol.8
, pp. 274-282
-
-
Otsu, M.1
Bertoli, G.2
Fagioli, C.3
Guerini-Rocco, E.4
Nerini-Molteni, S.5
Ruffato, E.6
Sitia, R.7
-
59
-
-
46449120166
-
Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail
-
L. Wang, L. Wang, S. Vavassori, S. Li, H. Ke, T. Anelli, M. Degano, R. Ronzoni, R. Sitia, F. Sun, and C.C. Wang Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail EMBO Rep. 9 2008 642 647
-
(2008)
EMBO Rep.
, vol.9
, pp. 642-647
-
-
Wang, L.1
Wang, L.2
Vavassori, S.3
Li, S.4
Ke, H.5
Anelli, T.6
Degano, M.7
Ronzoni, R.8
Sitia, R.9
Sun, F.10
Wang, C.C.11
-
60
-
-
84880809859
-
A pH-regulated quality control cycle for surveillance of secretory protein assembly
-
S. Vavassori, M. Cortini, S. Masui, S. Sannino, T. Anelli, I.R. Caserta, C. Fagioli, M.F. Mossuto, A. Fornili, E. van Anken, M. Degano, K. Inaba, and R. Sitia A pH-regulated quality control cycle for surveillance of secretory protein assembly Mol. Cell 50 2013 783 792
-
(2013)
Mol. Cell
, vol.50
, pp. 783-792
-
-
Vavassori, S.1
Cortini, M.2
Masui, S.3
Sannino, S.4
Anelli, T.5
Caserta, I.R.6
Fagioli, C.7
Mossuto, M.F.8
Fornili, A.9
Van Anken, E.10
Degano, M.11
Inaba, K.12
Sitia, R.13
-
61
-
-
84913606032
-
Progressive quality control of secretory proteins in the early secretory compartment by ERp44
-
S. Sannino, T. Anelli, M. Cortini, S. Masui, M. Degano, C. Fagioli, K. Inaba, and R. Sitia Progressive quality control of secretory proteins in the early secretory compartment by ERp44 J. Cell Sci. 127 2014 4260 4269
-
(2014)
J. Cell Sci.
, vol.127
, pp. 4260-4269
-
-
Sannino, S.1
Anelli, T.2
Cortini, M.3
Masui, S.4
Degano, M.5
Fagioli, C.6
Inaba, K.7
Sitia, R.8
-
62
-
-
77949716997
-
ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
-
E. Zito, K.T. Chin, J. Blais, H.P. Harding, and D. Ron ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis J. Cell Biol. 188 2010 821 832
-
(2010)
J. Cell Biol.
, vol.188
, pp. 821-832
-
-
Zito, E.1
Chin, K.T.2
Blais, J.3
Harding, H.P.4
Ron, D.5
-
63
-
-
34047258016
-
Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction
-
N. Wajih, S.M. Hutson, and R. Wallin Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction J. Biol. Chem. 282 2007 2626 2635
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 2626-2635
-
-
Wajih, N.1
Hutson, S.M.2
Wallin, R.3
-
64
-
-
77957007036
-
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners
-
S. Schulman, B. Wang, W. Li, and T.A. Rapoport Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners Proc. Natl. Acad. Sci. USA 107 2010 15027 15032
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 15027-15032
-
-
Schulman, S.1
Wang, B.2
Li, W.3
Rapoport, T.A.4
-
65
-
-
84887465759
-
Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1alpha to promote oxidative protein folding
-
L. Wang, L. Zhang, Y. Niu, R. Sitia, and C.C. Wang Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1alpha to promote oxidative protein folding Antioxid. Redox Signal. 20 2014 545 556
-
(2014)
Antioxid. Redox Signal.
, vol.20
, pp. 545-556
-
-
Wang, L.1
Zhang, L.2
Niu, Y.3
Sitia, R.4
Wang, C.C.5
-
67
-
-
34250899722
-
Signal integration in the endoplasmic reticulum unfolded protein response
-
D. Ron, and P. Walter Signal integration in the endoplasmic reticulum unfolded protein response Nat. Rev. Mol. Cell. Biol. 8 2007 519 529
-
(2007)
Nat. Rev. Mol. Cell. Biol.
, vol.8
, pp. 519-529
-
-
Ron, D.1
Walter, P.2
-
68
-
-
0037147191
-
Coordinated nonvectorial folding in a newly synthesized multidomain protein
-
A. Jansens, E. van Duijn, and I. Braakman Coordinated nonvectorial folding in a newly synthesized multidomain protein Science 298 2002 2401 2403
-
(2002)
Science
, vol.298
, pp. 2401-2403
-
-
Jansens, A.1
Van Duijn, E.2
Braakman, I.3
-
69
-
-
84939965084
-
-
7th ed. Freeman and Co New York chap. 28
-
J.M. Berg, J.L. Tymoczko, L. Stryer, J. Gregory, and Gatto Jr. Metabolism: basic concepts and design in biochemistry, international 7th ed. 2012 Freeman and Co New York chap. 28
-
(2012)
Metabolism: Basic Concepts and Design in Biochemistry, International
-
-
Berg, J.M.1
Tymoczko, J.L.2
Stryer, L.3
Gregory, J.4
Gatto, J.R.5
-
70
-
-
85047688796
-
Ero1-alpha and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases
-
K. Araki, S. Iemura, Y. Kamiya, D. Ron, K. Kato, T. Natsume, and K. Nagata Ero1-alpha and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases J. Cell Biol. 202 2013 861 874
-
(2013)
J. Cell Biol.
, vol.202
, pp. 861-874
-
-
Araki, K.1
Iemura, S.2
Kamiya, Y.3
Ron, D.4
Kato, K.5
Natsume, T.6
Nagata, K.7
-
71
-
-
84857591674
-
Erv2 and quiescin sulfhydryl oxidases: Erv-domain enzymes associated with the secretory pathway
-
C.S. Sevier Erv2 and quiescin sulfhydryl oxidases: Erv-domain enzymes associated with the secretory pathway Antioxid. Redox Signal. 16 2012 800 808
-
(2012)
Antioxid. Redox Signal.
, vol.16
, pp. 800-808
-
-
Sevier, C.S.1
-
73
-
-
84879795833
-
A secreted disulfide catalyst controls extracellular matrix composition and function
-
T. Ilani, A. Alon, I. Grossman, B. Horowitz, E. Kartvelishvily, S.R. Cohen, and D. Fass A secreted disulfide catalyst controls extracellular matrix composition and function Science 341 2013 74 76
-
(2013)
Science
, vol.341
, pp. 74-76
-
-
Ilani, T.1
Alon, A.2
Grossman, I.3
Horowitz, B.4
Kartvelishvily, E.5
Cohen, S.R.6
Fass, D.7
-
74
-
-
77956318615
-
Mechanisms of oxidative protein folding in the bacterial cell envelope
-
H. Kadokura, and J. Beckwith Mechanisms of oxidative protein folding in the bacterial cell envelope Antioxid. Redox Signal. 13 2010 1231 1246
-
(2010)
Antioxid. Redox Signal.
, vol.13
, pp. 1231-1246
-
-
Kadokura, H.1
Beckwith, J.2
-
75
-
-
0033163758
-
Competition between glutathione and protein thiols for disulphide-bond formation
-
J.W. Cuozzo, and C.A. Kaiser Competition between glutathione and protein thiols for disulphide-bond formation Nat. Cell Biol. 1 1999 130 135
-
(1999)
Nat. Cell Biol.
, vol.1
, pp. 130-135
-
-
Cuozzo, J.W.1
Kaiser, C.A.2
-
77
-
-
4544249202
-
Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway
-
S. Chakravarthi, and N.J. Bulleid Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway J. Biol. Chem. 279 2004 39872 39879
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 39872-39879
-
-
Chakravarthi, S.1
Bulleid, N.J.2
-
78
-
-
84902253458
-
Balancing oxidative protein folding: The influences of reducing pathways on disulfide bond formation
-
K. Kojer, and J. Riemer Balancing oxidative protein folding: the influences of reducing pathways on disulfide bond formation Biochim. Biophys. Acta 1844 2014 1383 1390
-
(2014)
Biochim. Biophys. Acta
, vol.1844
, pp. 1383-1390
-
-
Kojer, K.1
Riemer, J.2
-
79
-
-
84905170031
-
Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants
-
S. Tsunoda, E. Avezov, A. Zyryanova, T. Konno, L. Mendes-Silva, E. Pinho Melo, H.P. Harding, and D. Ron Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants Elife 3 2014 e03421
-
(2014)
Elife
, vol.3
, pp. e03421
-
-
Tsunoda, S.1
Avezov, E.2
Zyryanova, A.3
Konno, T.4
Mendes-Silva, L.5
Pinho Melo, E.6
Harding, H.P.7
Ron, D.8
-
80
-
-
84885846700
-
Identification of the redox partners of ERdj5/JPDI, a PDI family member, from an animal tissue
-
H. Kadokura, M. Saito, A. Tsuru, A. Hosoda, T. Iwawaki, K. Inaba, and K. Kohno Identification of the redox partners of ERdj5/JPDI, a PDI family member, from an animal tissue Biochem. Biophys. Res. Commun. 440 2013 245 250
-
(2013)
Biochem. Biophys. Res. Commun.
, vol.440
, pp. 245-250
-
-
Kadokura, H.1
Saito, M.2
Tsuru, A.3
Hosoda, A.4
Iwawaki, T.5
Inaba, K.6
Kohno, K.7
-
81
-
-
84899139079
-
Endoplasmic reticulum stress-activated transcription factor ATF6alpha requires the disulfide isomerase PDIA5 to modulate chemoresistance
-
A. Higa, S. Taouji, S. Lhomond, D. Jensen, M.E. Fernandez-Zapico, J.C. Simpson, J.M. Pasquet, R. Schekman, and E. Chevet Endoplasmic reticulum stress-activated transcription factor ATF6alpha requires the disulfide isomerase PDIA5 to modulate chemoresistance Mol. Cell. Biol. 34 2014 1839 1849
-
(2014)
Mol. Cell. Biol.
, vol.34
, pp. 1839-1849
-
-
Higa, A.1
Taouji, S.2
Lhomond, S.3
Jensen, D.4
Fernandez-Zapico, M.E.5
Simpson, J.C.6
Pasquet, J.M.7
Schekman, R.8
Chevet, E.9
-
82
-
-
0036069980
-
ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
-
J. Shen, X. Chen, L. Hendershot, and R. Prywes ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals Dev. Cell 3 2002 99 111
-
(2002)
Dev. Cell
, vol.3
, pp. 99-111
-
-
Shen, J.1
Chen, X.2
Hendershot, L.3
Prywes, R.4
-
83
-
-
33846223428
-
Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
-
S. Nadanaka, T. Okada, H. Yoshida, and K. Mori Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress Mol. Cell. Biol. 27 2007 1027 1043
-
(2007)
Mol. Cell. Biol.
, vol.27
, pp. 1027-1043
-
-
Nadanaka, S.1
Okada, T.2
Yoshida, H.3
Mori, K.4
-
84
-
-
84894236302
-
Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling via disulfide-dependent association
-
D. Eletto, D. Eletto, D. Dersh, T. Gidalevitz, and Y. Argon Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling via disulfide-dependent association Mol. Cell 53 2014 562 576
-
(2014)
Mol. Cell
, vol.53
, pp. 562-576
-
-
Eletto, D.1
Eletto, D.2
Dersh, D.3
Gidalevitz, T.4
Argon, Y.5
-
85
-
-
84902676536
-
Interplay between the oxidoreductase PDIA6 and microRNA-322 controls the response to disrupted endoplasmic reticulum calcium homeostasis
-
Groenendyk, J.; Peng, Z.; Dudek, E.; Fan, X.; Mizianty, M.J.; Dufey, E.; Urra, H.; Sepulveda, D.; Rojas-Rivera, D.; Lim, Y.; Kim do, H.; Baretta, K.; Srikanth, S.; Gwack, Y.; Ahnn, J.; Kaufman, R.J.; Lee, S.K.; Hetz, C.; Kurgan, L.; Michalak M.Interplay between the oxidoreductase PDIA6 and microRNA-322 controls the response to disrupted endoplasmic reticulum calcium homeostasis. Sci. Signal.7:ra54; 2014.
-
(2014)
Sci. Signal.7:ra54
-
-
Groenendyk, J.1
Peng, Z.2
Dudek, E.3
Fan, X.4
Mizianty M. ., J.5
Dufey, E.6
Urra, H.7
Sepulveda, D.8
Rojas-Rivera, D.9
Lim, Y.10
Kim Do, H.11
Baretta, K.12
Srikanth, S.13
Gwack, Y.14
Ahnn, J.15
Kaufman R. ., J.16
Lee S. ., K.17
Hetz, C.18
Kurgan, L.19
Michalak, M.20
more..
-
86
-
-
84939934550
-
Protein disulfide isomerase superfamily in disease and the regulation of apoptosis
-
C. Grek, and D.M. Townsend Protein disulfide isomerase superfamily in disease and the regulation of apoptosis Endoplasmic Reticulum Stress Dis 1 2014 4 17
-
(2014)
Endoplasmic Reticulum Stress Dis
, vol.1
, pp. 4-17
-
-
Grek, C.1
Townsend, D.M.2
|