-
1
-
-
84874024997
-
1, 3, 5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification
-
Banerjee, R., Pace, N. J., Brown, D. R., and Weerapana, E. (2013). 1, 3, 5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification. J. Am. Chem. Soc. 135, 2497-2500. doi: 10.1021/ja400427e
-
(2013)
J. Am. Chem. Soc
, vol.135
, pp. 2497-2500
-
-
Banerjee, R.1
Pace, N.J.2
Brown, D.R.3
Weerapana, E.4
-
2
-
-
0028131648
-
Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
-
Cai, H., Wang, C. C., and Tsou, C. L. (1994). Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem. 269, 24550-24552.
-
(1994)
J. Biol. Chem
, vol.269
, pp. 24550-24552
-
-
Cai, H.1
Wang, C.C.2
Tsou, C.L.3
-
3
-
-
4444378921
-
Fluorometricpolyethyleneglycol-peptide hybrid substrates for quantitative assay of protein disulfide isomerase
-
Christiansen, C., St Hilaire, P. M., and Winther, J. R. (2004). Fluorometricpolyethyleneglycol-peptide hybrid substrates for quantitative assay of protein disulfide isomerase. Anal. Biochem. 333, 148-155. doi: 10.1016/j.ab.2004.06.027
-
(2004)
Anal. Biochem
, vol.333
, pp. 148-155
-
-
Christiansen, C.1
St Hilaire, P.M.2
Winther, J.R.3
-
4
-
-
84900396980
-
The branched-chain aminotransferase proteins: novel redox chaperones for protein disulfide isomerase-implications in Alzheimer's disease
-
El Hindy, M., Hezwani, M., Corry, D., Hull, J., El Amraoui, F., Harris, M., et al. (2014). The branched-chain aminotransferase proteins: novel redox chaperones for protein disulfide isomerase-implications in Alzheimer's disease. Antioxid. Redox Signal 20, 2497-2513. doi: 10.1089/ars.2012.4869
-
(2014)
Antioxid. Redox Signal
, vol.20
, pp. 2497-2513
-
-
El Hindy, M.1
Hezwani, M.2
Corry, D.3
Hull, J.4
El Amraoui, F.5
Harris, M.6
-
5
-
-
0345772126
-
Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry
-
Gallina, A., Hanley, T. M., Mandel, R., Trahey, M., Broder, C. C., Viglianti, G. A., et al. (2002). Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry. J. Biol. Chem. 277, 50579-50588. doi: 10.1074/jbc.M204547200
-
(2002)
J. Biol. Chem
, vol.277
, pp. 50579-50588
-
-
Gallina, A.1
Hanley, T.M.2
Mandel, R.3
Trahey, M.4
Broder, C.C.5
Viglianti, G.A.6
-
6
-
-
78651157389
-
Purification and properties of a microsomal enzyme system catalyzing the reactivation of reduced ribonuclease and lysozyme
-
Goldberger, R. F., Epstein, C. J., and Anfinsen, C. B. (1964). Purification and properties of a microsomal enzyme system catalyzing the reactivation of reduced ribonuclease and lysozyme. J. Biol. Chem. 239, 1406-1410.
-
(1964)
J. Biol. Chem
, vol.239
, pp. 1406-1410
-
-
Goldberger, R.F.1
Epstein, C.J.2
Anfinsen, C.B.3
-
7
-
-
71549132149
-
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation
-
Hatahet, F., and Ruddock, L. W. (2009). Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid. Redox Signal 11, 2807-2850. doi: 10.1089/ars.2009.2466
-
(2009)
Antioxid. Redox Signal
, vol.11
, pp. 2807-2850
-
-
Hatahet, F.1
Ruddock, L.W.2
-
8
-
-
0021152329
-
Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase
-
Hillson, D. A., Lambert, N., and Freedman, R. B. (1984). Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol. 107, 281-294. doi: 10.1016/0076-6879(84)07018-X
-
(1984)
Methods Enzymol
, vol.107
, pp. 281-294
-
-
Hillson, D.A.1
Lambert, N.2
Freedman, R.B.3
-
9
-
-
78649246847
-
Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins
-
Hoffstrom, B. G., Kaplan, A., Letso, R., Schmid, R. S., Turmel, G. J., Lo, D. C., et al. (2010). Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins. Nat. Chem. Biol. 6, 900-906. doi: 10.1038/nchembio.467
-
(2010)
Nat. Chem. Biol
, vol.6
, pp. 900-906
-
-
Hoffstrom, B.G.1
Kaplan, A.2
Letso, R.3
Schmid, R.S.4
Turmel, G.J.5
Lo, D.C.6
-
10
-
-
0018723651
-
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
-
Holmgren, A. (1979). Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632.
-
(1979)
J. Biol. Chem
, vol.254
, pp. 9627-9632
-
-
Holmgren, A.1
-
11
-
-
84921721414
-
Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway
-
Irvine, A. G., Wallis, A. K., Sanghera, N., Rowe, M. L., Ruddock, L. W., Howard, M. J., et al. (2014). Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway. PLoS ONE 9:e82511. doi: 10.1371/journal.pone.0082511
-
(2014)
PLoS ONE
, vol.9
-
-
Irvine, A.G.1
Wallis, A.K.2
Sanghera, N.3
Rowe, M.L.4
Ruddock, L.W.5
Howard, M.J.6
-
12
-
-
28844477782
-
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells
-
Janiszewski, M., Lopes, L. R., Carmo, A. O., Pedro, M. A., Brandes, R. P., Santos, C. X., et al. (2005). Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J. Biol. Chem. 280, 40813-40819. doi: 10.1074/jbc.M509255200
-
(2005)
J. Biol. Chem
, vol.280
, pp. 40813-40819
-
-
Janiszewski, M.1
Lopes, L.R.2
Carmo, A.O.3
Pedro, M.A.4
Brandes, R.P.5
Santos, C.X.6
-
13
-
-
84861808529
-
Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents
-
Jasuja, R., Passam, F. H., Kennedy, D. R., Kim, S. H., van Hessem, L., Lin, L., et al. (2012). Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents. J. Clin. Invest. 122, 2104-2113. doi: 10.1172/JCI61228
-
(2012)
J. Clin. Invest
, vol.122
, pp. 2104-2113
-
-
Jasuja, R.1
Passam, F.H.2
Kennedy, D.R.3
Kim, S.H.4
van Hessem, L.5
Lin, L.6
-
14
-
-
33846192436
-
ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
-
Jessop, C. E., Chakravarthi, S., Garbi, N., Hämmerling, G. J., Lovell, S., and Bulleid, N. J. (2007). ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J. 26, 28-40. doi: 10.1038/sj.emboj.7601505
-
(2007)
EMBO J
, vol.26
, pp. 28-40
-
-
Jessop, C.E.1
Chakravarthi, S.2
Garbi, N.3
Hämmerling, G.J.4
Lovell, S.5
Bulleid, N.J.6
-
15
-
-
77952680368
-
Bacitracin is not a specific inhibitor of protein disulfide isomerase
-
Karala, A. R., and Ruddock, L. W. (2010). Bacitracin is not a specific inhibitor of protein disulfide isomerase. FEBS J. 277, 2454-2462. doi: 10.1111/j.1742-4658.2010.07660.x
-
(2010)
FEBS J
, vol.277
, pp. 2454-2462
-
-
Karala, A.R.1
Ruddock, L.W.2
-
16
-
-
24644501647
-
Catalysis of protein disulfide bond isomerization in a homogeneous substrate
-
Kersteen, E. A., Barrows, S. R., and Raines, R. T. (2005). Catalysis of protein disulfide bond isomerization in a homogeneous substrate. Biochemistry 44, 12168-12178. doi: 10.1021/bi0507985
-
(2005)
Biochemistry
, vol.44
, pp. 12168-12178
-
-
Kersteen, E.A.1
Barrows, S.R.2
Raines, R.T.3
-
17
-
-
79955574624
-
Discovery of a small molecule PDI inhibitor that inhibits reduction of HIV-1 envelope glycoprotein gp120
-
Khan, M. M. G., Simizu, S., Lai, N. S., Kawatani, M., Shimizu, T., and Osada, H. (2011). Discovery of a small molecule PDI inhibitor that inhibits reduction of HIV-1 envelope glycoprotein gp120. ACS Chem. Biol. 6, 245-251. doi: 10.1021/cb100387r
-
(2011)
ACS Chem. Biol
, vol.6
, pp. 245-251
-
-
Khan, M.M.G.1
Simizu, S.2
Lai, N.S.3
Kawatani, M.4
Shimizu, T.5
Osada, H.6
-
18
-
-
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., Ruddock, L. W., Darby, N. J., and Freedman, R. B. (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. doi: 10.1093/emboj/17.4.927
-
(1998)
EMBO J
, vol.17
, pp. 927-935
-
-
Klappa, P.1
Ruddock, L.W.2
Darby, N.J.3
Freedman, R.B.4
-
19
-
-
84877930702
-
Rapid activation of monocyte tissue factor by antithymocyte globulin is dependent on complement and protein disulfide isomerase
-
Langer, F., Spath, B., Fischer, C., Stolz, M., Ayuk, F. A., Kröger, N., et al. (2013). Rapid activation of monocyte tissue factor by antithymocyte globulin is dependent on complement and protein disulfide isomerase. Blood 121, 2324-2335. doi: 10.1182/blood-2012-10-460493
-
(2013)
Blood
, vol.121
, pp. 2324-2335
-
-
Langer, F.1
Spath, B.2
Fischer, C.3
Stolz, M.4
Ayuk, F.A.5
Kröger, N.6
-
20
-
-
84859480323
-
Protein disulfide isomerase in redox cell signaling and homeostasis
-
Laurindo, F. R., Pescatore, L. A., and Fernandes, D. C. (2012). Protein disulfide isomerase in redox cell signaling and homeostasis. Free Radic. Biol. Med. 52, 1954-1969. doi: 10.1016/j.freeradbiomed.2012.02.037
-
(2012)
Free Radic. Biol. Med
, vol.52
, pp. 1954-1969
-
-
Laurindo, F.R.1
Pescatore, L.A.2
Fernandes, D.C.3
-
21
-
-
84901825185
-
Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress
-
Lee, S., Min Kim, S., Dotimas, J., Li, L., Feener, E. P., Baldus, S., et al. (2014). Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress. EMBO Mol. Med. 6, 732-743. doi: 10.15252/emmm.201302561
-
(2014)
EMBO Mol. Med
, vol.6
, pp. 732-743
-
-
Lee, S.1
Min Kim, S.2
Dotimas, J.3
Li, L.4
Feener, E.P.5
Baldus, S.6
-
22
-
-
84903784187
-
The thioredoxin superfamily in oxidative protein folding
-
Lu, J., and Holmgren, A. (2014). The thioredoxin superfamily in oxidative protein folding. Antioxid. Redox Signal 21, 457-470. doi: 10.1089/ars.2014.5849
-
(2014)
Antioxid. Redox Signal
, vol.21
, pp. 457-470
-
-
Lu, J.1
Holmgren, A.2
-
23
-
-
0026062381
-
Catalysis of the oxidative folding of ribonuclease a by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer
-
Lyles, M. M., and Gilbert, H. F. (1991). Catalysis of the oxidative folding of ribonuclease a by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-619. doi: 10.1021/bi00217a004
-
(1991)
Biochemistry
, vol.30
, pp. 613-619
-
-
Lyles, M.M.1
Gilbert, H.F.2
-
24
-
-
79960800956
-
Acid-denatured green fluorescent protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase
-
Mares, R. E., Meléndez-López, S. G., and Ramos, M. A. (2011). Acid-denatured green fluorescent protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase. Int. J. Mol. Sci. 12, 4625-4636. doi: 10.3390/ijms12074625
-
(2011)
Int. J. Mol. Sci
, vol.12
, pp. 4625-4636
-
-
Mares, R.E.1
Meléndez-López, S.G.2
Ramos, M.A.3
-
25
-
-
84892924777
-
Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples
-
Montano, S. J., Lu, J., Gustafsson, T. N., and Holmgren, A. (2014). Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples. Anal. Biochem. 449, 139-146. doi: 10.1016/j.ab.2013.12.025
-
(2014)
Anal. Biochem
, vol.449
, pp. 139-146
-
-
Montano, S.J.1
Lu, J.2
Gustafsson, T.N.3
Holmgren, A.4
-
26
-
-
0025861453
-
Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase
-
Morjana, N. A., and Gilbert, H. F. (1991). Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase. Biochemistry 30, 4985-4990.
-
(1991)
Biochemistry
, vol.30
, pp. 4985-4990
-
-
Morjana, N.A.1
Gilbert, H.F.2
-
27
-
-
84872978155
-
Protein disulfide isomerase modification and inhibition contribute to ER stress and apoptosis induced by oxidized low density lipoproteins
-
Muller, C., Bandemer, J., Vindis, C., Camaré, C., Mucher, E., Guéraud, F., et al. (2013). Protein disulfide isomerase modification and inhibition contribute to ER stress and apoptosis induced by oxidized low density lipoproteins. Antioxid. Redox Signal 18, 731-742. doi: 10.1089/ars.2012.4577
-
(2013)
Antioxid. Redox Signal
, vol.18
, pp. 731-742
-
-
Muller, C.1
Bandemer, J.2
Vindis, C.3
Camaré, C.4
Mucher, E.5
Guéraud, F.6
-
28
-
-
80053413462
-
Protein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation
-
Paes, A. M., Veríssimo-Filho, S., Guimarães, L. L., Silva, A. C., Takiuti, J. T., Santos, C. X., et al. (2011). Protein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation. J. Leukoc. Biol. 90, 799-810. doi: 10.1189/jlb.0610324
-
(2011)
J. Leukoc. Biol
, vol.90
, pp. 799-810
-
-
Paes, A.M.1
Veríssimo-Filho, S.2
Guimarães, L.L.3
Silva, A.C.4
Takiuti, J.T.5
Santos, C.X.6
-
29
-
-
84887082945
-
Endothelin-1 receptor antagonists regulate cell surface-associated protein disulfide isomerase in sickle cell disease
-
Prado, G. N., Romero, J. R., and Rivera, A. (2013). Endothelin-1 receptor antagonists regulate cell surface-associated protein disulfide isomerase in sickle cell disease. FASEB J. 27, 4619-4629. doi: 10.1096/fj.13-228577
-
(2013)
FASEB J
, vol.27
, pp. 4619-4629
-
-
Prado, G.N.1
Romero, J.R.2
Rivera, A.3
-
30
-
-
56249094492
-
Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase
-
Rancy, P. C., and Thorpe, C. (2008). Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase. Biochemistry 47, 12047-12056. doi: 10.1021/bi801604x
-
(2008)
Biochemistry
, vol.47
, pp. 12047-12056
-
-
Rancy, P.C.1
Thorpe, C.2
-
31
-
-
34249903638
-
Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay
-
Raturi, A., and Mutus, B. (2007). Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay. Free Radic. Biol. Med. 43, 62-70. doi: 10.1016/j.freeradbiomed.2007.03.025
-
(2007)
Free Radic. Biol. Med
, vol.43
, pp. 62-70
-
-
Raturi, A.1
Mutus, B.2
-
32
-
-
40549121595
-
Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation
-
Reinhardt, C., von Brüh, M. L., Manukyan, D., Grahl, L., Lorenz, M., Altmann, B., et al. (2008). Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. J. Clin. Invest. 118, 1110-1122. doi: 10.1172/JCI32376
-
(2008)
J. Clin. Invest
, vol.118
, pp. 1110-1122
-
-
Reinhardt, C.1
von Brüh, M.L.2
Manukyan, D.3
Grahl, L.4
Lorenz, M.5
Altmann, B.6
-
33
-
-
0029155302
-
Refolding by disulfide isomerization: the mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate
-
Ruoppolo, M., and Freedman, R. B. (1995). Refolding by disulfide isomerization: the mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate. Biochemistry 34, 9380-9388. doi: 10.1021/bi00029a014
-
(1995)
Biochemistry
, vol.34
, pp. 9380-9388
-
-
Ruoppolo, M.1
Freedman, R.B.2
-
34
-
-
0029861578
-
Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase
-
Ruoppolo, M., Freedman, R. B., Pucci, P., and Marino, G. (1996). Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase. Biochemistry 35, 13636-13646. doi: 10.1021/bi960755b
-
(1996)
Biochemistry
, vol.35
, pp. 13636-13646
-
-
Ruoppolo, M.1
Freedman, R.B.2
Pucci, P.3
Marino, G.4
-
35
-
-
17044417590
-
A high-throughput turbidometric assay for screening inhibitors of protein disulfide isomerase activity
-
Smith, A. M., Chan, J., Oksenberg, D., Urfer, R., Wexler, D. S., Ow, A., et al. (2004). A high-throughput turbidometric assay for screening inhibitors of protein disulfide isomerase activity. J. Biomol. Screen. 9, 614-620. doi: 10.1177/1087057104265292
-
(2004)
J. Biomol. Screen
, vol.9
, pp. 614-620
-
-
Smith, A.M.1
Chan, J.2
Oksenberg, D.3
Urfer, R.4
Wexler, D.S.5
Ow, A.6
-
36
-
-
70350218853
-
Nitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response
-
Townsend, D. M., Manevich, Y., He, L., Xiong, Y., Bowers, R. R. Jr., Hutchens, S., et al. (2009). Nitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response. Cancer Res. 69, 7626-7634. doi: 10.1158/0008-5472.CAN-09-0493
-
(2009)
Cancer Res
, vol.69
, pp. 7626-7634
-
-
Townsend, D.M.1
Manevich, Y.2
He, L.3
Xiong, Y.4
Bowers, R.R.5
Hutchens, S.6
-
37
-
-
0033199237
-
The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
-
van den Berg, B., Chung, E. W., Robinson, C. V., Mateo, P. L., and Dobson, C. M. (1999). The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase. EMBO J. 18, 4794-4803. doi: 10.1093/emboj/18.17.4794
-
(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
-
38
-
-
84878866786
-
Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
-
Wang, C., Li, W., Ren, J., Fang, J., Ke, H., Gong, W., et al. (2013). Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase. Antioxid. Redox Signal 19, 36-45. doi: 10.1089/ars.2012.4630
-
(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
-
39
-
-
84863139700
-
The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis
-
Wu, Y., Ahmad, S. S., Zhou, J., Wang, L., Cully, M. P., and Essex, D. W. (2012). The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis. Blood 119, 1737-1746. doi: 10.1182/blood-2011-06-360685
-
(2012)
Blood
, vol.119
, pp. 1737-1746
-
-
Wu, Y.1
Ahmad, S.S.2
Zhou, J.3
Wang, L.4
Cully, M.P.5
Essex, D.W.6
-
40
-
-
84867095394
-
Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment
-
Xu, S., Butkevich, A. N., Yamada, R., Zhou, Y., Debnath, B., Duncan, R., et al. (2012). Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment. Proc. Natl. Acad. Sci. U.S.A. 109, 16348-16353. doi: 10.1073/pnas.1205226109
-
(2012)
Proc. Natl. Acad. Sci. U.S.A
, vol.109
, pp. 16348-16353
-
-
Xu, S.1
Butkevich, A.N.2
Yamada, R.3
Zhou, Y.4
Debnath, B.5
Duncan, R.6
-
41
-
-
84896394053
-
Protein disulfide isomerase: a promising target for cancer therapy
-
Xu, S., Sankar, S., and Neamati, N. (2014). Protein disulfide isomerase: a promising target for cancer therapy. Drug Discov. Today 19, 222-240. doi: 10.1016/j.drudis.2013.10.017
-
(2014)
Drug Discov. Today
, vol.19
, pp. 222-240
-
-
Xu, S.1
Sankar, S.2
Neamati, N.3
-
42
-
-
84876034428
-
Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling
-
Zhou, H. Z. (2013). Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling. FEBS Lett. 587, 1053-1061. doi: 10.1016/j.febslet.2013.01.064
-
(2013)
FEBS Lett
, vol.587
, pp. 1053-1061
-
-
Zhou, H.Z.1
-
43
-
-
78649918283
-
Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
-
Zito, E., Melo, E. P., Yang, Y., Wahlander, A., Neubert, T. A., and Ron, D. (2010). Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol. Cell 40, 787-797. doi: 10.1016/j.molcel.2010.11.010
-
(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
|