-
1
-
-
14244272868
-
PHENIX: Building new software for automated crystallographic structure determination
-
DOI 10.1107/S0907444902016657
-
Adams PD, Grosse-Kunstleve RW, Hung LW, Ioerger TR, McCoy AJ, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK, and Terwilliger TC. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58: 1948-1954, 2002. (Pubitemid 35337293)
-
(2002)
Acta Crystallographica Section D: Biological Crystallography
, vol.58
, Issue.11
, pp. 1948-1954
-
-
Adams, P.D.1
Grosse-Kunstleve, R.W.2
Hung, L.-W.3
Ioerger, T.R.4
McCoy, A.J.5
Moriarty, N.W.6
Read, R.J.7
Sacchettini, J.C.8
Sauter, N.K.9
Terwilliger, T.C.10
-
2
-
-
0043264811
-
Defining the domain boundaries of the human protein disulfide isomerases
-
Alanen HI, Salo KE, Pekkala M, Siekkinen HM, Pirneskoski A, and Ruddock LW. Defining the domain boundaries of the human protein disulfide isomerases. Antioxid Redox Signal 5: 367-374, 2003. (Pubitemid 37087395)
-
(2003)
Antioxidants and Redox Signaling
, vol.5
, Issue.4
, pp. 367-374
-
-
Alanen, H.I.1
Salo, K.E.H.2
Pekkala, M.3
Siekkinen, H.M.4
Pirneskoski, A.5
Ruddock, L.W.6
-
3
-
-
77957806157
-
Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated
-
Appenzeller-Herzog C, Riemer J, Zito E, Chin KT, Ron D, Spiess M, and Ellgaard L. Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated. EMBO J 29: 3318-3329, 2010.
-
(2010)
EMBO J
, vol.29
, pp. 3318-3329
-
-
Appenzeller-Herzog, C.1
Riemer, J.2
Zito, E.3
Chin, K.T.4
Ron, D.5
Spiess, M.6
Ellgaard, L.7
-
4
-
-
84857530189
-
The protein disulfide isomerase family: Key players in health and disease
-
Benham AM. The protein disulfide isomerase family: key players in health and disease. Antioxid Redox Signal 16: 781-789, 2012.
-
(2012)
Antioxid Redox Signal
, vol.16
, pp. 781-789
-
-
Benham, A.M.1
-
5
-
-
0028131648
-
Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
-
Cai H, Wang CC, and Tsou CL. Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J Biol Chem 269: 24550-24552, 1994. (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
-
6
-
-
0029093531
-
Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
-
Darby NJ and Creighton TE. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34: 11725-11735, 1995.
-
(1995)
Biochemistry
, vol.34
, pp. 11725-11735
-
-
Darby, N.J.1
Creighton, T.E.2
-
7
-
-
34547592557
-
MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
-
Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB, Snoeyink J, Richardson JS, and Richardson DC. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-W383, 2007.
-
(2007)
Nucleic Acids Res
, vol.35
-
-
Davis, I.W.1
Leaver-Fay, A.2
Chen, V.B.3
Block, J.N.4
Kapral, G.J.5
Wang, X.6
Murray, L.W.7
Arendall, W.B.8
Snoeyink, J.9
Richardson, J.S.10
Richardson, D.C.11
-
8
-
-
60349123960
-
Solution structure of the bb¢ domains of human protein disulfide isomerase
-
Denisov AY, Maattanen P, Dabrowski C, Kozlov G, and Thomas DY, Gehring K. Solution structure of the bb¢ domains of human protein disulfide isomerase. FEBS J 276: 1440-1449, 2009.
-
(2009)
FEBS J
, vol.276
, pp. 1440-1449
-
-
Denisov, A.Y.1
Maattanen, P.2
Dabrowski, C.3
Kozlov, G.4
Thomas, D.Y.5
Gehring, K.6
-
10
-
-
0021691817
-
Analysis of membrane and surface protein sequences with the hydrophobic moment plot
-
DOI 10.1016/0022-2836(84)90309-7
-
Eisenberg D, Schwarz E, Komaromy M, and Wall R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179: 125-142, 1984. (Pubitemid 16223392)
-
(1984)
Journal of Molecular Biology
, vol.179
, Issue.1
, pp. 125-142
-
-
Eisenberg, D.1
Schwarz, E.2
Komaromy, M.3
Wall, R.4
-
12
-
-
0031954077
-
Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase
-
Freedman RB, Gane PJ, Hawkins HC, Hlodan R, McLaughlin SH, and Parry JW. Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase. Biol Chem 379: 321-328, 1998. (Pubitemid 28152096)
-
(1998)
Biological Chemistry
, vol.379
, Issue.3
, pp. 321-328
-
-
Freedman, R.B.1
Gane, P.J.2
Hawkins, H.C.3
Hlodan, R.4
McLaughlin, S.H.5
Parry, J.W.L.6
-
13
-
-
0036198797
-
Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
-
DOI 10.1093/embo-reports/kvf035
-
Freedman RB, Klappa P, and Ruddock LW. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 3: 136-140, 2002. (Pubitemid 34213490)
-
(2002)
EMBO Reports
, vol.3
, Issue.2
, pp. 136-140
-
-
Freedman, R.B.1
Klappa, P.2
Ruddock, L.W.3
-
14
-
-
73649177752
-
Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
-
Goldberger RF, Epstein CJ, and Anfinsen CB. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J Biol Chem238: 628-635, 1963.
-
(1963)
J Biol Chem
, vol.238
, pp. 628-635
-
-
Goldberger, R.F.1
Epstein, C.J.2
Anfinsen, C.B.3
-
15
-
-
71549132149
-
Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
-
Hatahet F and Ruddock LW. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 11: 2807-2850, 2009.
-
(2009)
Antioxid Redox Signal
, vol.11
, pp. 2807-2850
-
-
Hatahet, F.1
Ruddock, L.W.2
-
16
-
-
2942669907
-
Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
-
DOI 10.1073/pnas.0402769101
-
Heras B, Edeling MA, Schirra HJ, Raina S, and Martin JL. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. Proc Natl Acad Sci USA 101: 8876-8881, 2004. (Pubitemid 38781579)
-
(2004)
Proceedings of the National Academy of Sciences of the United States of America
, vol.101
, Issue.24
, pp. 8876-8881
-
-
Heras, B.1
Edeling, M.A.2
Schirra, H.J.3
Raina, S.4
Martin, J.L.5
-
17
-
-
0035832893
-
Studies on the function of yeast protein disulfide isomerase in renaturation of proteins
-
DOI 10.1016/S0167-4838(01)00214-X, PII S016748380100214X
-
Katiyar S, Till EA, and Lennarz WJ. Studies on the function of yeast protein disulfide isomerase in renaturation of proteins. Biochim Biophys Acta 1548: 47-56, 2001. (Pubitemid 32622819)
-
(2001)
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
, vol.1548
, Issue.1
, pp. 47-56
-
-
Katiyar, S.1
Till, E.A.2
Lennarz, W.J.3
-
18
-
-
0029973729
-
Structure determination of the N-terminal thioredoxinlike domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy
-
Kemmink J, Darby NJ, Dijkstra K, Nilges M, and Creighton TE. Structure determination of the N-terminal thioredoxinlike domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 35: 7684-7691, 1996.
-
(1996)
Biochemistry
, vol.35
, pp. 7684-7691
-
-
Kemmink, J.1
Darby, N.J.2
Dijkstra, K.3
Nilges, M.4
Creighton, T.E.5
-
19
-
-
0032897837
-
The structure in solution of the b domain of protein disulfide isomerase
-
DOI 10.1023/A:1008341820489
-
Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, and Darby NJ. The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR 13: 357-368, 1999. (Pubitemid 29210328)
-
(1999)
Journal of Biomolecular NMR
, vol.13
, Issue.4
, pp. 357-368
-
-
Kemmink, J.1
Dijkstra, K.2
Mariani, M.3
Scheek, R.M.4
Penka, E.5
Nilges, M.6
Darby, N.J.7
-
20
-
-
84860273170
-
Balanced Ero1 activation and inactivation establishes ER redox homeostasis
-
Kim S, Sideris DP, Sevier CS, and Kaiser CA. Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196: 713-725, 2012.
-
(2012)
J Cell Biol
, vol.196
, pp. 713-725
-
-
Kim, S.1
Sideris, D.P.2
Sevier, C.S.3
Kaiser, C.A.4
-
21
-
-
2942718758
-
Functional differences between human and yeast protein disulfide isomerase family proteins
-
DOI 10.1016/j.bbrc.2004.05.178, PII S0006291X0401188X
-
Kimura T, Hosoda Y, Kitamura Y, Nakamura H, Horibe T, and Kikuchi M. Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320: 359-365, 2004. (Pubitemid 38798874)
-
(2004)
Biochemical and Biophysical Research Communications
, vol.320
, Issue.2
, pp. 359-365
-
-
Kimura, T.1
Hosoda, Y.2
Kitamura, Y.3
Nakamura, H.4
Horibe, T.5
Kikuchi, M.6
-
22
-
-
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, and Freedman RB. 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, 1998. (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
-
23
-
-
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
-
DOI 10.1093/emboj/18.1.65
-
Koivunen P, Pirneskoski A, Karvonen P, Ljung J, Helaakoski T, NotbohmH, andKivirikkoKI. The acidicC-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: 65-74, 1999. (Pubitemid 29005024)
-
(1999)
EMBO Journal
, vol.18
, Issue.1
, pp. 65-74
-
-
Koivunen, P.1
Pirneskoski, A.2
Karvonen, P.3
Ljung, J.4
Helaakoski, T.5
Notbohm, H.6
Kivirikko, K.I.7
-
24
-
-
33646546083
-
Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: A small angle x-ray scattering study in solution
-
DOI 10.1074/jbc.M508422200
-
Li SJ, Hong XG, Shi YY, Li H, and Wang CC. Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution. J Biol Chem 281: 6581-6588, 2006. (Pubitemid 43847592)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.10
, pp. 6581-6588
-
-
Li, S.-J.1
Hong, X.-G.2
Shi, Y.-Y.3
Li, H.4
Wang, C.-C.5
-
25
-
-
33947356717
-
ERp57 and PDI: Multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations
-
DOI 10.1139/O06-186
-
Maattanen P, Kozlov G, Gehring K, and Thomas DY. ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations. Biochem Cell Biol 84: 881-889, 2006. (Pubitemid 46450688)
-
(2006)
Biochemistry and Cell Biology
, vol.84
, Issue.6
, pp. 881-889
-
-
Maattanen, P.1
Kozlov, G.2
Gehring, K.3
Thomas, D.Y.4
-
27
-
-
53549090995
-
Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b¢ domain
-
Nguyen VD, Wallis K, Howard MJ, Haapalainen AM, Salo KE, Saaranen MJ, Sidhu A, Wierenga RK, Freedman RB, Ruddock LW, and Williamson RA. Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b¢ domain. J Mol Biol 383: 1144-1155, 2008.
-
(2008)
J Mol Biol
, vol.383
, pp. 1144-1155
-
-
Nguyen, V.D.1
Wallis, K.2
Howard, M.J.3
Haapalainen, A.M.4
Salo, K.E.5
Saaranen, M.J.6
Sidhu, A.7
Wierenga, R.K.8
Freedman, R.B.9
Ruddock, L.W.10
Williamson, R.A.11
-
28
-
-
0031059866
-
Processing of X-ray diffraction data collected in oscillation mode
-
DOI 10.1016/S0076-6879(97)76066-X
-
Otwinowski Z and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326, 1997. (Pubitemid 27085611)
-
(1997)
Methods in Enzymology
, vol.276
, pp. 307-326
-
-
Otwinowski, Z.1
Minor, W.2
-
29
-
-
12144288546
-
Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase
-
DOI 10.1074/jbc.M312193200
-
Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, and Ruddock LW. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J Biol Chem 279: 10374-10381, 2004. (Pubitemid 38372645)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.11
, pp. 10374-10381
-
-
Pirneskoski, A.1
Klappa, P.2
Lobell, M.3
Williamson, R.A.4
Byrne, L.5
Alanen, H.I.6
Salo, K.E.H.7
Kivirikko, K.I.8
Freedman, R.B.9
Ruddock, L.W.10
-
30
-
-
41449116766
-
Ero1 and redox homeostasis in the endoplasmic reticulum
-
Sevier CS and Kaiser CA. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim BiophysActa 1783: 549-556, 2008.
-
(2008)
Biochim BiophysActa
, vol.1783
, pp. 549-556
-
-
Sevier, C.S.1
Kaiser, C.A.2
-
31
-
-
57749102824
-
The catalytic activity of protein disulfide isomerase requires a conformationally flexible molecule
-
Tian G, Kober FX, Lewandrowski U, Sickmann A, Lennarz WJ, and Schindelin H. The catalytic activity of protein disulfide isomerase requires a conformationally flexible molecule. J Biol Chem 238: 33630-33640, 2008.
-
(2008)
J Biol Chem
, vol.238
, pp. 33630-33640
-
-
Tian, G.1
Kober, F.X.2
Lewandrowski, U.3
Sickmann, A.4
Lennarz, W.J.5
Schindelin, H.6
-
32
-
-
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, and Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124: 61-73, 2006. (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
-
33
-
-
84874506387
-
Assisting oxidative protein folding: How do protein disulphide-isomerases couple conformational and chemical processes in protein folding?
-
Epub ahead of print DOI: 10.1007/128-2011-171
-
Wallis AK and Freedman RB. Assisting oxidative protein folding: how do protein disulphide-isomerases couple conformational and chemical processes in protein folding? Top Curr Chem 2012 [Epub ahead of print]; DOI: 10.1007/128-2011-171.
-
(2012)
Top Curr Chem
-
-
Wallis, A.K.1
Freedman, R.B.2
-
34
-
-
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, and Wang CC. 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.
-
(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
-
35
-
-
84862907646
-
Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a¢
-
Wang C, Yu J, Huo L, Wang L, Feng W, and Wang CC. Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a¢. J Biol Chem 287: 1139-1149, 2012.
-
(2012)
J Biol Chem
, vol.287
, pp. 1139-1149
-
-
Wang, C.1
Yu, J.2
Huo, L.3
Wang, L.4
Feng, W.5
Wang, C.C.6
-
36
-
-
58649096169
-
Reconstitution of human Ero1-Lalpha/proteindisulfide 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, and Wang CC. Reconstitution of human Ero1-Lalpha/proteindisulfide 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.
-
(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
-
37
-
-
0031034725
-
2
-
DOI 10.1093/emboj/16.3.651
-
Yao Y, Zhou Y, and Wang C. 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, 1997. (Pubitemid 27067793)
-
(1997)
EMBO Journal
, vol.16
, Issue.3
, pp. 651-658
-
-
Yao, Y.1
Zhou, Y.-C.2
Wang, C.-C.3
|