-
1
-
-
0037083869
-
ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
-
Anelli, T., M. Alessio, A. Mezghrani, T. Simmen, F. Talamo, A. Bachi, and R. Sitia. 2002. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBOJ. 21:835-844.
-
(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
-
2
-
-
0034681340
-
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
-
Cabibbo, A., M. Pagani, M. Fabbri, M. Rocchi, M.R. Farmery, N.J. Bulleid, and R. Sitia. 2000. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275:4827-4833.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 4827-4833
-
-
Cabibbo, A.1
Pagani, M.2
Fabbri, M.3
Rocchi, M.4
Farmery, M.R.5
Bulleid, N.J.6
Sitia, R.7
-
3
-
-
0031609760
-
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
-
Frand, A.R., and C.A. Kaiser. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell. 1: 161-170.
-
(1998)
Mol. Cell
, vol.1
, pp. 161-170
-
-
Frand, A.R.1
Kaiser, C.A.2
-
4
-
-
0033213605
-
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
-
Frand, A.R., and C.A. Kaiser. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell. 4:469-477.
-
(1999)
Mol. Cell
, vol.4
, pp. 469-477
-
-
Frand, A.R.1
Kaiser, C.A.2
-
5
-
-
0033611127
-
Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase
-
Gillece, P., J.M. Luz, W.J. Lennarz, F.J. de La Cruz, and K. Romisch. 1999. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J. Cell Biol. 147:1443-1456.
-
(1999)
J. Cell Biol.
, vol.147
, pp. 1443-1456
-
-
Gillece, P.1
Luz, J.M.2
Lennarz, W.J.3
De La Cruz, F.J.4
Romisch, K.5
-
6
-
-
0027424601
-
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
-
Gorlich, D., and T.A. Rapoport. 1993. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell. 75:615-630.
-
(1993)
Cell
, vol.75
, pp. 615-630
-
-
Gorlich, D.1
Rapoport, T.A.2
-
7
-
-
0030807389
-
Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum
-
Holst, B., C. Tachibana, and J.R. Winther. 1997. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J. Cell Biol. 138:1229-1238.
-
(1997)
J. Cell Biol.
, vol.138
, pp. 1229-1238
-
-
Holst, B.1
Tachibana, C.2
Winther, J.R.3
-
8
-
-
0033055636
-
Membrane traffic and the cellular uptake of cholera toxin
-
Lencer, W.I., T.R. Hirst, and R.K. Holmes. 1999. Membrane traffic and the cellular uptake of cholera toxin. Biochim. Biophys. Acta. 1450:177-190.
-
(1999)
Biochim. Biophys. Acta
, vol.1450
, pp. 177-190
-
-
Lencer, W.I.1
Hirst, T.R.2
Holmes, R.K.3
-
9
-
-
0032488845
-
Protein translocation: Tunnel vision
-
Matlack, K.E., W. Mothes, and T.A. Rapoport. 1998. Protein translocation: Tunnel vision. Cell. 92:381-390.
-
(1998)
Cell
, vol.92
, pp. 381-390
-
-
Matlack, K.E.1
Mothes, W.2
Rapoport, T.A.3
-
10
-
-
0034604675
-
Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
-
Pagani, M., M. Fabbri, C. Benedetti, A. Fassio, S. Pilati, N.J. Bulleid, A. Cabibbo, and R. Sitia. 2000. Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275:23685-23692.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 23685-23692
-
-
Pagani, M.1
Fabbri, M.2
Benedetti, C.3
Fassio, A.4
Pilati, S.5
Bulleid, N.J.6
Cabibbo, A.7
Sitia, R.8
-
11
-
-
0031610364
-
Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
-
Pollard, M.G., K.J. Travers, and J.S. Weissman. 1998. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 1:171-182.
-
(1998)
Mol. Cell
, vol.1
, pp. 171-182
-
-
Pollard, M.G.1
Travers, K.J.2
Weissman, J.S.3
-
12
-
-
0034689054
-
Cholera toxin is exported from microsomes by the Sec61p complex
-
Schmitz, A., H. Herrgen, A. Winkeler, and V. Herzog. 2000. Cholera toxin is exported from microsomes by the Sec61p complex. J. Cell Biol. 148:1203-1212.
-
(2000)
J. Cell Biol.
, vol.148
, pp. 1203-1212
-
-
Schmitz, A.1
Herrgen, H.2
Winkeler, A.3
Herzog, V.4
-
13
-
-
0029942531
-
Enteric bacterial toxins: Mechanisms of action and linkage to intestinal secretion
-
Sears, C.L., and J.B. Kaper. 1996. Enteric bacterial toxins: Mechanisms of action and linkage to intestinal secretion. Microbiol. Rev. 60:167-215.
-
(1996)
Microbiol. Rev.
, vol.60
, pp. 167-215
-
-
Sears, C.L.1
Kaper, J.B.2
-
14
-
-
0035937408
-
Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
-
Tsai, B., C. Rodighiero, W.I. Lencer, and T.A. Rapoport. 2001. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell. 104:937-948.
-
(2001)
Cell
, vol.104
, pp. 937-948
-
-
Tsai, B.1
Rodighiero, C.2
Lencer, W.I.3
Rapoport, T.A.4
-
15
-
-
0036270698
-
Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
-
Tsai, B., Y. Ye, and T.A. Rapoport. 2002. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3:246-255.
-
(2002)
Nat. Rev. Mol. Cell Biol.
, vol.3
, pp. 246-255
-
-
Tsai, B.1
Ye, Y.2
Rapoport, T.A.3
-
16
-
-
0034711439
-
Biochemical basis of oxidative protein folding in the endoplasmic reticulum
-
Tu, B.P., S.C. Ho-Schleyer, K.J. Travers, and J.S. Weissman. 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
-
17
-
-
0033230434
-
Eps1, a novel PDI-related protein involved in ER quality control in yeast
-
Wang, Q., and A. Chang. 1999. Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18:5972-5982.
-
(1999)
EMBO J.
, vol.18
, pp. 5972-5982
-
-
Wang, Q.1
Chang, A.2
-
18
-
-
0033525472
-
Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo
-
Westphal, V., N.J. Darby, and J.R. Winther. 1999. Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo. J. Mol. Biol. 286:1229-1239.
-
(1999)
J. Mol. Biol.
, vol.286
, pp. 1229-1239
-
-
Westphal, V.1
Darby, N.J.2
Winther, J.R.3
|