-
1
-
-
13444269483
-
SPD-a web-based secreted protein database
-
Chen Y., Zhang Y., Yin Y., Gao G., Li S., Jiang Y., Gu X., Luo J. SPD-a web-based secreted protein database. Nucleic Acids Res. 2005, 33:D169-D173.
-
(2005)
Nucleic Acids Res.
, vol.33
-
-
Chen, Y.1
Zhang, Y.2
Yin, Y.3
Gao, G.4
Li, S.5
Jiang, Y.6
Gu, X.7
Luo, J.8
-
2
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfinsen C.B. Principles that govern the folding of protein chains. Science 1973, 181:223-230.
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
3
-
-
67349189383
-
The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
-
Anfinsen C.B., Haber E., Sela M., White F.H.J. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc. Natl. Acad. Sci. U. S. A. 1961, 47:1309-1314.
-
(1961)
Proc. Natl. Acad. Sci. U. S. A.
, vol.47
, pp. 1309-1314
-
-
Anfinsen, C.B.1
Haber, E.2
Sela, M.3
White, F.H.J.4
-
4
-
-
0002006297
-
Are there pathways for protein folding?
-
Levinthal C. Are there pathways for protein folding?. J. Chim. Phys. 1968, 65:44-45.
-
(1968)
J. Chim. Phys.
, vol.65
, pp. 44-45
-
-
Levinthal, C.1
-
5
-
-
0030626588
-
The Levinthal paradox: yesterday and today
-
Karplus M. The Levinthal paradox: yesterday and today. Fold. Des. 1997, 2:S69-S75.
-
(1997)
Fold. Des.
, vol.2
-
-
Karplus, M.1
-
6
-
-
33846901901
-
Intermediates: ubiquitous species on folding energy landscapes?
-
Brockwell D.J., Radford S.E. Intermediates: ubiquitous species on folding energy landscapes?. Curr. Opin. Struct. Biol. 2007, 17:30-37.
-
(2007)
Curr. Opin. Struct. Biol.
, vol.17
, pp. 30-37
-
-
Brockwell, D.J.1
Radford, S.E.2
-
7
-
-
0028037217
-
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
-
Fersht A.R., Itzhaki L.S., El-Masry N.F., Matthews J.M., Otzen D.E. Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:10426-10429.
-
(1994)
Proc. Natl. Acad. Sci. U. S. A.
, vol.91
, pp. 10426-10429
-
-
Fersht, A.R.1
Itzhaki, L.S.2
El-Masry, N.F.3
Matthews, J.M.4
Otzen, D.E.5
-
8
-
-
33847306593
-
A unified mechanism for protein folding: predetermined pathways with optional errors
-
Krishna M.M., Englander S.W. A unified mechanism for protein folding: predetermined pathways with optional errors. Protein Sci. 2007, 16:449-464.
-
(2007)
Protein Sci.
, vol.16
, pp. 449-464
-
-
Krishna, M.M.1
Englander, S.W.2
-
10
-
-
0032924105
-
Chaperone-mediated protein folding
-
Fink A.L. Chaperone-mediated protein folding. Physiol. Rev. 1999, 79:425-449.
-
(1999)
Physiol. Rev.
, vol.79
, pp. 425-449
-
-
Fink, A.L.1
-
11
-
-
0028170231
-
Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
-
Melnick J., Dul J.L., Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 1994, 370:373-375.
-
(1994)
Nature
, vol.370
, pp. 373-375
-
-
Melnick, J.1
Dul, J.L.2
Argon, Y.3
-
12
-
-
0033214526
-
Mapping the major interaction between BiP and immunoglobulin light chains to sites within the variable domain
-
Davis D.P., Khurana R., Meredith S., Stevens F.J., Argon Y. Mapping the major interaction between BiP and immunoglobulin light chains to sites within the variable domain. J. Immunol. 1999, 163:3842-3850.
-
(1999)
J. Immunol.
, vol.163
, pp. 3842-3850
-
-
Davis, D.P.1
Khurana, R.2
Meredith, S.3
Stevens, F.J.4
Argon, Y.5
-
13
-
-
0033715831
-
Inhibition of amyloid fiber assembly by both BiP and its target peptide
-
Davis D.P., Raffen R., Dul J.L., Vogen S.M., Williamson E.K., Stevens F.J., Argon Y. Inhibition of amyloid fiber assembly by both BiP and its target peptide. Immunity 2000, 13:433-442.
-
(2000)
Immunity
, vol.13
, pp. 433-442
-
-
Davis, D.P.1
Raffen, R.2
Dul, J.L.3
Vogen, S.M.4
Williamson, E.K.5
Stevens, F.J.6
Argon, Y.7
-
14
-
-
29144452851
-
The C-type lectin-like domain superfamily
-
Zelensky A.N., Gready J.E. The C-type lectin-like domain superfamily. FEBS J. 2005, 272:6179-6217.
-
(2005)
FEBS J.
, vol.272
, pp. 6179-6217
-
-
Zelensky, A.N.1
Gready, J.E.2
-
15
-
-
0024400060
-
Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
-
Hurtley S.M., Bole D.G., Hoover-Litty H., Helenius A., Copeland C.S. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 1989, 108:2117-2126.
-
(1989)
J. Cell Biol.
, vol.108
, pp. 2117-2126
-
-
Hurtley, S.M.1
Bole, D.G.2
Hoover-Litty, H.3
Helenius, A.4
Copeland, C.S.5
-
16
-
-
0026697158
-
Disulfide bond formation during the folding of influenza virus hemagglutinin
-
Segal M.S., Bye J.M., Sambrook J.F., Gething M.J. Disulfide bond formation during the folding of influenza virus hemagglutinin. J. Cell Biol. 1992, 118:227-244.
-
(1992)
J. Cell Biol.
, vol.118
, pp. 227-244
-
-
Segal, M.S.1
Bye, J.M.2
Sambrook, J.F.3
Gething, M.J.4
-
17
-
-
0033998246
-
Role of ribosome and translocon complex during folding of influenza hemagglutinin in the endoplasmic reticulum of living cells
-
Chen W., Helenius A. Role of ribosome and translocon complex during folding of influenza hemagglutinin in the endoplasmic reticulum of living cells. Mol. Biol. Cell 2000, 11:765-772.
-
(2000)
Mol. Biol. Cell
, vol.11
, pp. 765-772
-
-
Chen, W.1
Helenius, A.2
-
18
-
-
0030037083
-
Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit
-
Ruddon R.W., Sherman S.A., Bedows E. Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit. Protein Sci. 1996, 5:1443-1452.
-
(1996)
Protein Sci.
, vol.5
, pp. 1443-1452
-
-
Ruddon, R.W.1
Sherman, S.A.2
Bedows, E.3
-
19
-
-
0033059157
-
Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
-
Dayel M.J., Hom E.F., Verkman A.S. Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys. J. 1999, 76:2843-2851.
-
(1999)
Biophys. J.
, vol.76
, pp. 2843-2851
-
-
Dayel, M.J.1
Hom, E.F.2
Verkman, A.S.3
-
20
-
-
0026698060
-
Oxidized redox state of glutathione in the endoplasmic reticulum
-
Hwang C., Sinskey A.J., Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257:1496-1502.
-
(1992)
Science
, vol.257
, pp. 1496-1502
-
-
Hwang, C.1
Sinskey, A.J.2
Lodish, H.F.3
-
21
-
-
0028832662
-
+ concentration in the endoplasmic reticulum of intact cells
-
+ concentration in the endoplasmic reticulum of intact cells. EMBO J. 1995, 14:5467-5475.
-
(1995)
EMBO J.
, vol.14
, pp. 5467-5475
-
-
Montero, M.1
Brini, M.2
Marsault, R.3
Alvarez, J.4
Sitia, R.5
Pozzan, T.6
Rizzuto, R.7
-
22
-
-
0037185013
-
Surface-catalyzed amyloid fibril formation
-
Zhu M., Souillac P.O., Ionescu-Zanetti C., Carter S.A., Fink A.L. Surface-catalyzed amyloid fibril formation. J. Biol. Chem. 2002, 277:50914-50922.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 50914-50922
-
-
Zhu, M.1
Souillac, P.O.2
Ionescu-Zanetti, C.3
Carter, S.A.4
Fink, A.L.5
-
23
-
-
34447291808
-
Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association
-
Gorbenko G.P., Ioffe V.M., Kinnunen P.K. Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association. Biophys. J. 2007, 93:140-153.
-
(2007)
Biophys. J.
, vol.93
, pp. 140-153
-
-
Gorbenko, G.P.1
Ioffe, V.M.2
Kinnunen, P.K.3
-
24
-
-
14344250143
-
Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers
-
Zhao H., Jutila A., Nurminen T., Wickstrom S.A., Keski-Oja J., Kinnunen P.K. Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry 2005, 44:2857-2863.
-
(2005)
Biochemistry
, vol.44
, pp. 2857-2863
-
-
Zhao, H.1
Jutila, A.2
Nurminen, T.3
Wickstrom, S.A.4
Keski-Oja, J.5
Kinnunen, P.K.6
-
25
-
-
4043100348
-
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
-
Zhao H., Tuominen E.K., Kinnunen P.K. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 2004, 43:10302-10307.
-
(2004)
Biochemistry
, vol.43
, pp. 10302-10307
-
-
Zhao, H.1
Tuominen, E.K.2
Kinnunen, P.K.3
-
26
-
-
0032549767
-
BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
-
Hamman B.D., Hendershot L.M., Johnson A.E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 1998, 92:747-758.
-
(1998)
Cell
, vol.92
, pp. 747-758
-
-
Hamman, B.D.1
Hendershot, L.M.2
Johnson, A.E.3
-
27
-
-
0029991763
-
Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase
-
Silberstein S., Gilmore R. Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB J. 1996, 10:849-858.
-
(1996)
FASEB J.
, vol.10
, pp. 849-858
-
-
Silberstein, S.1
Gilmore, R.2
-
28
-
-
0033572725
-
Effects of macromolecular crowding on protein folding and aggregation
-
van den Berg B., Ellis R.J., Dobson C.M. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 1999, 18:6927-6933.
-
(1999)
EMBO J.
, vol.18
, pp. 6927-6933
-
-
van den Berg, B.1
Ellis, R.J.2
Dobson, C.M.3
-
29
-
-
39049105287
-
Effects of macromolecular crowding on glycoprotein processing enzymes
-
Totani K., Ihara Y., Matsuo I., Ito Y. Effects of macromolecular crowding on glycoprotein processing enzymes. J. Am. Chem. Soc. 2008, 130:2101-2107.
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 2101-2107
-
-
Totani, K.1
Ihara, Y.2
Matsuo, I.3
Ito, Y.4
-
30
-
-
0030297071
-
Functions for MHC class I carbohydrates inside and outside the cell
-
Parham P. Functions for MHC class I carbohydrates inside and outside the cell. Trends Biochem. Sci. 1996, 21:427-433.
-
(1996)
Trends Biochem. Sci.
, vol.21
, pp. 427-433
-
-
Parham, P.1
-
31
-
-
0023879525
-
Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding
-
Machamer C.E., Rose J.K. Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. J. Biol. Chem. 1988, 263:5955-5960.
-
(1988)
J. Biol. Chem.
, vol.263
, pp. 5955-5960
-
-
Machamer, C.E.1
Rose, J.K.2
-
32
-
-
0030667061
-
The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
-
Hebert D.N., Zhang J.X., Chen W., Foellmer B., Helenius A. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol. 1997, 139:613-623.
-
(1997)
J. Cell Biol.
, vol.139
, pp. 613-623
-
-
Hebert, D.N.1
Zhang, J.X.2
Chen, W.3
Foellmer, B.4
Helenius, A.5
-
33
-
-
0022236656
-
A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface
-
Machamer C.E., Florkiewicz R.Z., Rose J.K. A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface. Mol. Cell. Biol. 1985, 5:3074-3083.
-
(1985)
Mol. Cell. Biol.
, vol.5
, pp. 3074-3083
-
-
Machamer, C.E.1
Florkiewicz, R.Z.2
Rose, J.K.3
-
34
-
-
0026489261
-
Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus
-
Gallagher P.J., Henneberry J.M., Sambrook J.F., Gething M.J. Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus. J. Virol. 1992, 66:7136-7145.
-
(1992)
J. Virol.
, vol.66
, pp. 7136-7145
-
-
Gallagher, P.J.1
Henneberry, J.M.2
Sambrook, J.F.3
Gething, M.J.4
-
35
-
-
47749126995
-
N-linked glycosylation selectively regulates the generic folding of HLA-Cw1
-
Martayan A., Sibilio L., Setini A., Lo Monaco E., Tremante E., Fruci D., Colonna M., Giacomini P. N-linked glycosylation selectively regulates the generic folding of HLA-Cw1. J. Biol. Chem. 2008, 283:16469-16476.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 16469-16476
-
-
Martayan, A.1
Sibilio, L.2
Setini, A.3
Lo Monaco, E.4
Tremante, E.5
Fruci, D.6
Colonna, M.7
Giacomini, P.8
-
36
-
-
0031963654
-
Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation
-
Zhang Q., Salter R.D. Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation. J. Immunol. 1998, 160:831-837.
-
(1998)
J. Immunol.
, vol.160
, pp. 831-837
-
-
Zhang, Q.1
Salter, R.D.2
-
37
-
-
0027970870
-
Mammalian expression and secretion of functional single-chain Fv molecules
-
Jost C.R., Kurucz I., Jacobus C.M., Titus J.A., George A.J., Segal D.M. Mammalian expression and secretion of functional single-chain Fv molecules. J. Biol. Chem. 1994, 269:26267-26273.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 26267-26273
-
-
Jost, C.R.1
Kurucz, I.2
Jacobus, C.M.3
Titus, J.A.4
George, A.J.5
Segal, D.M.6
-
38
-
-
1342327544
-
Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding
-
Petrescu A.J., Milac A.L., Petrescu S.M., Dwek R.A., Wormald M.R. Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. Glycobiology 2004, 14:103-114.
-
(2004)
Glycobiology
, vol.14
, pp. 103-114
-
-
Petrescu, A.J.1
Milac, A.L.2
Petrescu, S.M.3
Dwek, R.A.4
Wormald, M.R.5
-
39
-
-
79551626904
-
Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns
-
Culyba E.K., Price J.L., Hanson S.R., Dhar A., Wong C.H., Gruebele M., Powers E.T., Kelly J.W. Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns. Science 2011, 331:571-575.
-
(2011)
Science
, vol.331
, pp. 571-575
-
-
Culyba, E.K.1
Price, J.L.2
Hanson, S.R.3
Dhar, A.4
Wong, C.H.5
Gruebele, M.6
Powers, E.T.7
Kelly, J.W.8
-
40
-
-
0026091179
-
Identification of a protein required for disulfide bond formation in vivo
-
Bardwell J.C., McGovern K., Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 1991, 67:581-589.
-
(1991)
Cell
, vol.67
, pp. 581-589
-
-
Bardwell, J.C.1
McGovern, K.2
Beckwith, J.3
-
41
-
-
0842266604
-
Oxidative protein folding in eukaryotes: mechanisms and consequences
-
Tu B.P., Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 2004, 164:341-346.
-
(2004)
J. Cell Biol.
, vol.164
, pp. 341-346
-
-
Tu, B.P.1
Weissman, J.S.2
-
42
-
-
41449116766
-
Ero1 and redox homeostasis in the endoplasmic reticulum
-
Sevier C.S., Kaiser C.A. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim. Biophys. Acta 2008, 1783:549-556.
-
(2008)
Biochim. Biophys. Acta
, vol.1783
, pp. 549-556
-
-
Sevier, C.S.1
Kaiser, C.A.2
-
43
-
-
41649110016
-
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells
-
Tavender T.J., Sheppard A.M., Bulleid N.J. Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. Biochem. J. 2008, 411:191-199.
-
(2008)
Biochem. J.
, vol.411
, pp. 191-199
-
-
Tavender, T.J.1
Sheppard, A.M.2
Bulleid, N.J.3
-
44
-
-
78650270477
-
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
-
Tavender T.J., Springate J.J., Bulleid N.J. Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J. 2010, 29:4185-4197.
-
(2010)
EMBO J.
, vol.29
, pp. 4185-4197
-
-
Tavender, T.J.1
Springate, J.J.2
Bulleid, N.J.3
-
46
-
-
78649918283
-
Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
-
Zito E., Melo E.P., Yang Y., Wahlander A., Neubert T.A., Ron D. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol. Cell 2010, 40:787-797.
-
(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
-
47
-
-
0041761700
-
Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxidant status and implications for protein maturation
-
van der Vlies D., Makkinje M., Jansens A., Braakman I., Verkleij A.J., Wirtz K.W., Post J.A. Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxidant status and implications for protein maturation. Antioxid. Redox Signal. 2003, 5:381-387.
-
(2003)
Antioxid. Redox Signal.
, vol.5
, pp. 381-387
-
-
van der Vlies, D.1
Makkinje, M.2
Jansens, A.3
Braakman, I.4
Verkleij, A.J.5
Wirtz, K.W.6
Post, J.A.7
-
48
-
-
0030797806
-
Protein folding coupled to disulphide bond formation
-
Creighton T.E. Protein folding coupled to disulphide bond formation. Biol. Chem. 1997, 378:731-744.
-
(1997)
Biol. Chem.
, vol.378
, pp. 731-744
-
-
Creighton, T.E.1
-
49
-
-
0018647555
-
Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides
-
Bergman L.W., Kuehl W.M. Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides. J. Biol. Chem. 1979, 254:5690-5694.
-
(1979)
J. Biol. Chem.
, vol.254
, pp. 5690-5694
-
-
Bergman, L.W.1
Kuehl, W.M.2
-
50
-
-
0026563680
-
Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
-
Marquardt T., Helenius A. Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 1992, 117:505-513.
-
(1992)
J. Cell Biol.
, vol.117
, pp. 505-513
-
-
Marquardt, T.1
Helenius, A.2
-
51
-
-
17644422480
-
Cysteines in CH1 underlie retention of unassembled Ig heavy chains
-
Elkabetz Y., Argon Y., Bar-Nun S. Cysteines in CH1 underlie retention of unassembled Ig heavy chains. J. Biol. Chem. 2005, 280:14402-14412.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 14402-14412
-
-
Elkabetz, Y.1
Argon, Y.2
Bar-Nun, S.3
-
52
-
-
0026604334
-
Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
-
Braakman I., Helenius J., Helenius A. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. 1992, 11:1717-1722.
-
(1992)
EMBO J.
, vol.11
, pp. 1717-1722
-
-
Braakman, I.1
Helenius, J.2
Helenius, A.3
-
53
-
-
0035890070
-
Manipulation of oxidative protein folding and PDI redox state in mammalian cells
-
Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 2001, 20:6288-6296.
-
(2001)
EMBO J.
, vol.20
, pp. 6288-6296
-
-
Mezghrani, A.1
Fassio, A.2
Benham, A.3
Simmen, T.4
Braakman, I.5
Sitia, R.6
-
54
-
-
0026701319
-
Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast
-
Taniyama Y., Ogasahara K., Yutani K., Kikuchi M. Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast. J. Biol. Chem. 1992, 267:4619-4624.
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 4619-4624
-
-
Taniyama, Y.1
Ogasahara, K.2
Yutani, K.3
Kikuchi, M.4
-
55
-
-
0032524034
-
An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly
-
Worn A., Pluckthun A. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett. 1998, 427:357-361.
-
(1998)
FEBS Lett.
, vol.427
, pp. 357-361
-
-
Worn, A.1
Pluckthun, A.2
-
56
-
-
84855289267
-
Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic beta-cells
-
Rajpal G., Schuiki I., Liu M., Volchuk A., Arvan P. Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic beta-cells. J. Biol. Chem. 2012, 287:43-47.
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 43-47
-
-
Rajpal, G.1
Schuiki, I.2
Liu, M.3
Volchuk, A.4
Arvan, P.5
-
57
-
-
0023749218
-
Identification of a set of calcium-binding protein in reticuloplasm, the luminal content of the endoplasmic reticulum
-
Macer D.P.J., Koch G.L.E. Identification of a set of calcium-binding protein in reticuloplasm, the luminal content of the endoplasmic reticulum. J. Cell Sci. 1988, 91:61-70.
-
(1988)
J. Cell Sci.
, vol.91
, pp. 61-70
-
-
Macer, D.P.J.1
Koch, G.L.E.2
-
58
-
-
0026468393
-
Establishment of a Chinese hamster ovary cell line that expresses grp78 antisense transcripts and suppresses A23187 induction of both GRP78 and GRP94
-
Li L.J., Li X., Ferrario A., Rucker N., Liu E.S., Wong S., Gomer C.J., Lee A.S. Establishment of a Chinese hamster ovary cell line that expresses grp78 antisense transcripts and suppresses A23187 induction of both GRP78 and GRP94. J. Cell. Physiol. 1992, 153:575-582.
-
(1992)
J. Cell. Physiol.
, vol.153
, pp. 575-582
-
-
Li, L.J.1
Li, X.2
Ferrario, A.3
Rucker, N.4
Liu, E.S.5
Wong, S.6
Gomer, C.J.7
Lee, A.S.8
-
59
-
-
0033525232
-
+ regulation of interactions between endoplasmic reticulum chaperones
-
+ regulation of interactions between endoplasmic reticulum chaperones. J. Biol. Chem. 1999, 274:6203-6211.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 6203-6211
-
-
Corbett, E.F.1
Oikawa, K.2
Francois, P.3
Tessier, D.C.4
Kay, C.5
Bergeron, J.J.6
Thomas, D.Y.7
Krause, K.H.8
Michalak, M.9
-
61
-
-
0028070754
-
Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase
-
Rupp K., Birnbach U., Lundstrom J., Van P.N., Soling H.D. Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase. J. Biol. Chem. 1994, 269:2501-2507.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 2501-2507
-
-
Rupp, K.1
Birnbach, U.2
Lundstrom, J.3
Van, P.N.4
Soling, H.D.5
-
62
-
-
34447132178
-
The peptide binding activity of GRP94 is regulated by calcium
-
Biswas C., Ostrovsky O., Makarewich C.A., Wanderling S., Gidalevitz T., Argon Y. The peptide binding activity of GRP94 is regulated by calcium. Biochem. J. 2007, 405:233-241.
-
(2007)
Biochem. J.
, vol.405
, pp. 233-241
-
-
Biswas, C.1
Ostrovsky, O.2
Makarewich, C.A.3
Wanderling, S.4
Gidalevitz, T.5
Argon, Y.6
-
63
-
-
0026654505
-
Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum
-
Lodish H.F., Kong N., Wikstrom L. Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J. Biol. Chem. 1992, 267:12753-12760.
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 12753-12760
-
-
Lodish, H.F.1
Kong, N.2
Wikstrom, L.3
-
64
-
-
0025313861
-
Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
-
Lodish H.F., Kong N. Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J. Biol. Chem. 1990, 265:10893-10899.
-
(1990)
J. Biol. Chem.
, vol.265
, pp. 10893-10899
-
-
Lodish, H.F.1
Kong, N.2
-
65
-
-
0027269902
-
Biosynthesis of the gp330/44-kDa Heymann nephritis antigenic complex: assembly takes place in the ER
-
Biemesderfer D., Dekan G., Aronson P.S., Farquhar M.G. Biosynthesis of the gp330/44-kDa Heymann nephritis antigenic complex: assembly takes place in the ER. Am. J. Physiol. 1993, 264:F1011-F1020.
-
(1993)
Am. J. Physiol.
, vol.264
-
-
Biemesderfer, D.1
Dekan, G.2
Aronson, P.S.3
Farquhar, M.G.4
-
66
-
-
14444280363
-
Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum
-
Kuznetsov G., Chen L.B., Nigam S.K. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J. Biol. Chem. 1997, 272:3057-3063.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 3057-3063
-
-
Kuznetsov, G.1
Chen, L.B.2
Nigam, S.K.3
-
67
-
-
0037338462
-
+ from the endoplasmic reticulum
-
+ from the endoplasmic reticulum. Biochem. J. 2003, 370:449-458.
-
(2003)
Biochem. J.
, vol.370
, pp. 449-458
-
-
Di Jeso, B.1
Ulianich, L.2
Pacifico, F.3
Leonardi, A.4
Vito, P.5
Consiglio, E.6
Formisano, S.7
Arvan, P.8
-
68
-
-
5144220785
-
Comparison of the transition states for folding of two Ig-like proteins from different superfamilies
-
Geierhaas C.D., Paci E., Vendruscolo M., Clarke J. Comparison of the transition states for folding of two Ig-like proteins from different superfamilies. J. Mol. Biol. 2004, 343:1111-1123.
-
(2004)
J. Mol. Biol.
, vol.343
, pp. 1111-1123
-
-
Geierhaas, C.D.1
Paci, E.2
Vendruscolo, M.3
Clarke, J.4
-
69
-
-
0034646442
-
Solution structure of the sixth LDL-A module of the LDL receptor
-
North C.L., Blacklow S.C. Solution structure of the sixth LDL-A module of the LDL receptor. Biochemistry 2000, 39:2564-2571.
-
(2000)
Biochemistry
, vol.39
, pp. 2564-2571
-
-
North, C.L.1
Blacklow, S.C.2
-
70
-
-
0030759357
-
Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
-
Fass D., Blacklow S., Kim P.S., Berger J.M. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature 1997, 388:691-693.
-
(1997)
Nature
, vol.388
, pp. 691-693
-
-
Fass, D.1
Blacklow, S.2
Kim, P.S.3
Berger, J.M.4
-
72
-
-
0033546699
-
Tyrosinase folding and copper loading in vivo: a crucial role for calnexin and alpha-glucosidase II
-
Branza-Nichita N., Petrescu A.J., Dwek R.A., Wormald M.R., Platt F.M., Petrescu S.M. Tyrosinase folding and copper loading in vivo: a crucial role for calnexin and alpha-glucosidase II. Biochem. Biophys. Res. Commun. 1999, 261:720-725.
-
(1999)
Biochem. Biophys. Res. Commun.
, vol.261
, pp. 720-725
-
-
Branza-Nichita, N.1
Petrescu, A.J.2
Dwek, R.A.3
Wormald, M.R.4
Platt, F.M.5
Petrescu, S.M.6
-
73
-
-
0028818785
-
A kinetic explanation for the rearrangement pathway of BPTI folding
-
Weissman J.S., Kim P.S. A kinetic explanation for the rearrangement pathway of BPTI folding. Nat. Struct. Biol. 1995, 2:1123-1130.
-
(1995)
Nat. Struct. Biol.
, vol.2
, pp. 1123-1130
-
-
Weissman, J.S.1
Kim, P.S.2
-
74
-
-
77951643591
-
Protein folding stability and dynamics imaged in a living cell
-
Ebbinghaus S., Dhar A., McDonald J.D., Gruebele M. Protein folding stability and dynamics imaged in a living cell. Nat. Methods 2010, 7:319-323.
-
(2010)
Nat. Methods
, vol.7
, pp. 319-323
-
-
Ebbinghaus, S.1
Dhar, A.2
McDonald, J.D.3
Gruebele, M.4
-
75
-
-
0032539619
-
The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
-
Skowronek M.H., Hendershot L.M., Haas I.G. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:1574-1578.
-
(1998)
Proc. Natl. Acad. Sci. U. S. A.
, vol.95
, pp. 1574-1578
-
-
Skowronek, M.H.1
Hendershot, L.M.2
Haas, I.G.3
-
76
-
-
0034896499
-
Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
-
Vanhove M., Usherwood Y.K., Hendershot L.M. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 2001, 15:105-114.
-
(2001)
Immunity
, vol.15
, pp. 105-114
-
-
Vanhove, M.1
Usherwood, Y.K.2
Hendershot, L.M.3
-
77
-
-
33747641643
-
A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog
-
Hua Q.X., Liu M., Hu S.Q., Jia W., Arvan P., Weiss M.A. A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog. J. Biol. Chem. 2006, 281:24889-24899.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 24889-24899
-
-
Hua, Q.X.1
Liu, M.2
Hu, S.Q.3
Jia, W.4
Arvan, P.5
Weiss, M.A.6
-
78
-
-
78049281798
-
Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth
-
Liu M., Hodish I., Haataja L., Lara-Lemus R., Rajpal G., Wright J., Arvan P. Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth. Trends Endocrinol. Metab. 2010, 21:652-659.
-
(2010)
Trends Endocrinol. Metab.
, vol.21
, pp. 652-659
-
-
Liu, M.1
Hodish, I.2
Haataja, L.3
Lara-Lemus, R.4
Rajpal, G.5
Wright, J.6
Arvan, P.7
-
79
-
-
0023006195
-
Assembly of influenza hemagglutinin trimers and its role in intracellular transport
-
Copeland C.S., Doms R.W., Bolzau E.M., Webster R.G., Helenius A. Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J. Cell Biol. 1986, 103:1179-1191.
-
(1986)
J. Cell Biol.
, vol.103
, pp. 1179-1191
-
-
Copeland, C.S.1
Doms, R.W.2
Bolzau, E.M.3
Webster, R.G.4
Helenius, A.5
-
80
-
-
0023550869
-
Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
-
Doms R.W., Keller D.S., Helenius A., Balch W.E. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J. Cell Biol. 1987, 105:1957-1969.
-
(1987)
J. Cell Biol.
, vol.105
, pp. 1957-1969
-
-
Doms, R.W.1
Keller, D.S.2
Helenius, A.3
Balch, W.E.4
-
81
-
-
0032838622
-
BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
-
Lee Y.K., Brewer J.W., Hellman R., Hendershot L.M. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol. Biol. Cell 1999, 10:2209-2219.
-
(1999)
Mol. Biol. Cell
, vol.10
, pp. 2209-2219
-
-
Lee, Y.K.1
Brewer, J.W.2
Hellman, R.3
Hendershot, L.M.4
-
82
-
-
52949125581
-
Alternative pathways of disulfide bond formation yield secretion-competent, stable and functional immunoglobulins
-
Elkabetz Y., Ofir A., Argon Y., Bar-Nun S. Alternative pathways of disulfide bond formation yield secretion-competent, stable and functional immunoglobulins. Mol. Immunol. 2008.
-
(2008)
Mol. Immunol.
-
-
Elkabetz, Y.1
Ofir, A.2
Argon, Y.3
Bar-Nun, S.4
-
83
-
-
0030817962
-
In vitro translation and assembly of a complete T cell receptor-CD3 complex
-
Huppa J.B., Ploegh H.L. In vitro translation and assembly of a complete T cell receptor-CD3 complex. J. Exp. Med. 1997, 186:393-403.
-
(1997)
J. Exp. Med.
, vol.186
, pp. 393-403
-
-
Huppa, J.B.1
Ploegh, H.L.2
-
84
-
-
35748962628
-
Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly
-
Wanamaker C.P., Green W.N. Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly. J. Biol. Chem. 2007, 282:31113-31123.
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 31113-31123
-
-
Wanamaker, C.P.1
Green, W.N.2
-
85
-
-
66449119429
-
An unfolded CH1 domain controls the assembly and secretion of IgG antibodies
-
Feige M.J., Groscurth S., Marcinowski M., Shimizu Y., Kessler H., Hendershot L.M., Buchner J. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Mol. Cell 2009, 34:569-579.
-
(2009)
Mol. Cell
, vol.34
, pp. 569-579
-
-
Feige, M.J.1
Groscurth, S.2
Marcinowski, M.3
Shimizu, Y.4
Kessler, H.5
Hendershot, L.M.6
Buchner, J.7
-
86
-
-
0033545187
-
The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
-
Hellman R., Vanhove M., Lejeune A., Stevens F.J., Hendershot L.M. The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J. Cell Biol. 1999, 144:21-30.
-
(1999)
J. Cell Biol.
, vol.144
, pp. 21-30
-
-
Hellman, R.1
Vanhove, M.2
Lejeune, A.3
Stevens, F.J.4
Hendershot, L.M.5
-
87
-
-
0025114865
-
Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains
-
Bonifacino J.S., Cosson P., Klausner R.D. Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains. Cell 1990, 63:503-513.
-
(1990)
Cell
, vol.63
, pp. 503-513
-
-
Bonifacino, J.S.1
Cosson, P.2
Klausner, R.D.3
-
88
-
-
0025885341
-
Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum
-
Bonifacino J.S., Cosson P., Shah N., Klausner R.D. Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum. EMBO J. 1991, 10:2783-2793.
-
(1991)
EMBO J.
, vol.10
, pp. 2783-2793
-
-
Bonifacino, J.S.1
Cosson, P.2
Shah, N.3
Klausner, R.D.4
-
89
-
-
0025012782
-
A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum
-
Bonifacino J.S., Suzuki C.K., Klausner R.D. A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. Science 1990, 247:79-82.
-
(1990)
Science
, vol.247
, pp. 79-82
-
-
Bonifacino, J.S.1
Suzuki, C.K.2
Klausner, R.D.3
-
90
-
-
0026782498
-
Transmembrane helical interactions: zeta chain dimerization and functional association with the T cell antigen receptor
-
Rutledge T., Cosson P., Manolios N., Bonifacino J.S., Klausner R.D. Transmembrane helical interactions: zeta chain dimerization and functional association with the T cell antigen receptor. EMBO J. 1992, 11:3245-3254.
-
(1992)
EMBO J.
, vol.11
, pp. 3245-3254
-
-
Rutledge, T.1
Cosson, P.2
Manolios, N.3
Bonifacino, J.S.4
Klausner, R.D.5
-
91
-
-
77951199047
-
Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulum
-
Soetandyo N., Wang Q., Ye Y., Li L. Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulum. J. Cell Sci. 2010, 123:1031-1038.
-
(2010)
J. Cell Sci.
, vol.123
, pp. 1031-1038
-
-
Soetandyo, N.1
Wang, Q.2
Ye, Y.3
Li, L.4
-
92
-
-
2642562962
-
Identification of motifs involved in endoplasmic reticulum retention-forward trafficking of the GLT-1 subtype of glutamate transporter
-
Kalandadze A., Wu Y., Fournier K., Robinson M.B. Identification of motifs involved in endoplasmic reticulum retention-forward trafficking of the GLT-1 subtype of glutamate transporter. J. Neurosci. 2004, 24:5183-5192.
-
(2004)
J. Neurosci.
, vol.24
, pp. 5183-5192
-
-
Kalandadze, A.1
Wu, Y.2
Fournier, K.3
Robinson, M.B.4
-
93
-
-
58849165669
-
Agonist occupancy is essential for forward trafficking of AMPA receptors
-
Coleman S.K., Moykkynen T., Jouppila A., Koskelainen S., Rivera C., Korpi E.R., Keinanen K. Agonist occupancy is essential for forward trafficking of AMPA receptors. J. Neurosci. 2009, 29:303-312.
-
(2009)
J. Neurosci.
, vol.29
, pp. 303-312
-
-
Coleman, S.K.1
Moykkynen, T.2
Jouppila, A.3
Koskelainen, S.4
Rivera, C.5
Korpi, E.R.6
Keinanen, K.7
-
94
-
-
33751082926
-
Isoform-specific early trafficking of AMPA receptor flip and flop variants
-
Coleman S.K., Moykkynen T., Cai C., von Ossowski L., Kuismanen E., Korpi E.R., Keinanen K. Isoform-specific early trafficking of AMPA receptor flip and flop variants. J. Neurosci. 2006, 26:11220-11229.
-
(2006)
J. Neurosci.
, vol.26
, pp. 11220-11229
-
-
Coleman, S.K.1
Moykkynen, T.2
Cai, C.3
von Ossowski, L.4
Kuismanen, E.5
Korpi, E.R.6
Keinanen, K.7
-
96
-
-
33746500168
-
GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development
-
Luo S., Mao C., Lee B., Lee A.S. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol. Cell. Biol. 2006, 26:5688-5697.
-
(2006)
Mol. Cell. Biol.
, vol.26
, pp. 5688-5697
-
-
Luo, S.1
Mao, C.2
Lee, B.3
Lee, A.S.4
-
97
-
-
0026059137
-
Peptide-binding specificity of the molecular chaperone BiP
-
Flynn G.C., Pohl J., Flocco M.T., Rothman J.E. Peptide-binding specificity of the molecular chaperone BiP. Nature 1991, 353:726-730.
-
(1991)
Nature
, vol.353
, pp. 726-730
-
-
Flynn, G.C.1
Pohl, J.2
Flocco, M.T.3
Rothman, J.E.4
-
98
-
-
0027484417
-
Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
-
Blond-Elguindi S., Cwirla S.E., Dower W.J., Lipshutz R.J., Sprang S.R., Sambrook J.F., Gething M.J. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 1993, 75:717-728.
-
(1993)
Cell
, vol.75
, pp. 717-728
-
-
Blond-Elguindi, S.1
Cwirla, S.E.2
Dower, W.J.3
Lipshutz, R.J.4
Sprang, S.R.5
Sambrook, J.F.6
Gething, M.J.7
-
99
-
-
0025210448
-
Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein
-
Machamer C.E., Doms R.W., Bole D.G., Helenius A., Rose J.K. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. J. Biol. Chem. 1990, 265:6879-6883.
-
(1990)
J. Biol. Chem.
, vol.265
, pp. 6879-6883
-
-
Machamer, C.E.1
Doms, R.W.2
Bole, D.G.3
Helenius, A.4
Rose, J.K.5
-
100
-
-
0035911163
-
Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains
-
Dul J.L., Davis D.P., Williamson E.K., Stevens F.J., Argon Y. Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains. J. Cell Biol. 2001, 152:705-716.
-
(2001)
J. Cell Biol.
, vol.152
, pp. 705-716
-
-
Dul, J.L.1
Davis, D.P.2
Williamson, E.K.3
Stevens, F.J.4
Argon, Y.5
-
101
-
-
0029890917
-
Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutant
-
Hendershot L., Wei J., Gaut J., Melnick J., Aviel S., Argon Y. Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutant. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:5269-5274.
-
(1996)
Proc. Natl. Acad. Sci. U. S. A.
, vol.93
, pp. 5269-5274
-
-
Hendershot, L.1
Wei, J.2
Gaut, J.3
Melnick, J.4
Aviel, S.5
Argon, Y.6
-
102
-
-
0026665249
-
Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94
-
Clairmont C.A., De Maio A., Hirschberg C.B. Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94. J. Biol. Chem. 1992, 267:3983-3990.
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 3983-3990
-
-
Clairmont, C.A.1
De Maio, A.2
Hirschberg, C.B.3
-
103
-
-
12644318785
-
A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum
-
Dierks T., Volkmer J., Schlenstedt G., Jung C., Sandholzer U., Zachmann K., Schlotterhose P., Neifer K., Schmidt B., Zimmermann R. A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. EMBO J. 1996, 15:6931-6942.
-
(1996)
EMBO J.
, vol.15
, pp. 6931-6942
-
-
Dierks, T.1
Volkmer, J.2
Schlenstedt, G.3
Jung, C.4
Sandholzer, U.5
Zachmann, K.6
Schlotterhose, P.7
Neifer, K.8
Schmidt, B.9
Zimmermann, R.10
-
104
-
-
0027164203
-
Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
-
Blond-Elguindi S., Fourie A.M., Sambrook J.F., Gething M.J. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J. Biol. Chem. 1993, 268:12730-12735.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 12730-12735
-
-
Blond-Elguindi, S.1
Fourie, A.M.2
Sambrook, J.F.3
Gething, M.J.4
-
105
-
-
77954947810
-
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
-
Kampinga H.H., Craig E.A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 2010, 11:579-592.
-
(2010)
Nat. Rev. Mol. Cell Biol.
, vol.11
, pp. 579-592
-
-
Kampinga, H.H.1
Craig, E.A.2
-
106
-
-
77951229568
-
The endoplasmic reticulum GRP170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110
-
Andreasson C., Rampelt H., Fiaux J., Druffel-Augustin S., Bukau B. The endoplasmic reticulum GRP170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J. Biol. Chem. 2010, 285:12445-12453.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 12445-12453
-
-
Andreasson, C.1
Rampelt, H.2
Fiaux, J.3
Druffel-Augustin, S.4
Bukau, B.5
-
107
-
-
34748918368
-
The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum-a quantitative approach
-
Weitzmann A., Baldes C., Dudek J., Zimmermann R. The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum-a quantitative approach. FEBS J. 2007, 274:5175-5187.
-
(2007)
FEBS J.
, vol.274
, pp. 5175-5187
-
-
Weitzmann, A.1
Baldes, C.2
Dudek, J.3
Zimmermann, R.4
-
108
-
-
79956322553
-
Global quantification of mammalian gene expression control
-
Schwanhausser B., Busse D., Li N., Dittmar G., Schuchhardt J., Wolf J., Chen W., Selbach M. Global quantification of mammalian gene expression control. Nature 2011, 473:337-342.
-
(2011)
Nature
, vol.473
, pp. 337-342
-
-
Schwanhausser, B.1
Busse, D.2
Li, N.3
Dittmar, G.4
Schuchhardt, J.5
Wolf, J.6
Chen, W.7
Selbach, M.8
-
109
-
-
0033543175
-
Identification of novel peptide binding proteins in the endoplasmic reticulum: ERp72, calnexin, and GRP170
-
Spee P., Subjeck J., Neefjes J. Identification of novel peptide binding proteins in the endoplasmic reticulum: ERp72, calnexin, and GRP170. Biochemistry 1999, 38:10559-10566.
-
(1999)
Biochemistry
, vol.38
, pp. 10559-10566
-
-
Spee, P.1
Subjeck, J.2
Neefjes, J.3
-
110
-
-
0346365101
-
The chaperoning properties of mouse GRP170, a member of the third family of hsp70 related proteins
-
Park J., Easton D.P., Chen X., MacDonald I.J., Wang X.Y., Subjeck J.R. The chaperoning properties of mouse GRP170, a member of the third family of hsp70 related proteins. Biochemistry 2003, 42:14893-14902.
-
(2003)
Biochemistry
, vol.42
, pp. 14893-14902
-
-
Park, J.1
Easton, D.P.2
Chen, X.3
MacDonald, I.J.4
Wang, X.Y.5
Subjeck, J.R.6
-
111
-
-
0027136174
-
The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
-
Lin H.Y., Masso-Welch P., Di Y.P., Cai J.W., Shen J.W., Subjeck J.R. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol. Biol. Cell 1993, 4:1109-1119.
-
(1993)
Mol. Biol. Cell
, vol.4
, pp. 1109-1119
-
-
Lin, H.Y.1
Masso-Welch, P.2
Di, Y.P.3
Cai, J.W.4
Shen, J.W.5
Subjeck, J.R.6
-
112
-
-
24044535062
-
Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum
-
Schmidt B.Z., Perlmutter D.H. Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum. Am. J. Physiol. Gastrointest. Liver Physiol. 2005, 289:G444-G455.
-
(2005)
Am. J. Physiol. Gastrointest. Liver Physiol.
, vol.289
-
-
Schmidt, B.Z.1
Perlmutter, D.H.2
-
113
-
-
11144249887
-
ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates
-
Shen Y., Hendershot L.M. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol. Biol. Cell 2005, 16:40-50.
-
(2005)
Mol. Biol. Cell
, vol.16
, pp. 40-50
-
-
Shen, Y.1
Hendershot, L.M.2
-
114
-
-
55549139747
-
Regulated release of ERdj3 from unfolded proteins by BiP
-
Jin Y., Awad W., Petrova K., Hendershot L.M. Regulated release of ERdj3 from unfolded proteins by BiP. EMBO J. 2008, 27:2873-2882.
-
(2008)
EMBO J.
, vol.27
, pp. 2873-2882
-
-
Jin, Y.1
Awad, W.2
Petrova, K.3
Hendershot, L.M.4
-
115
-
-
55549141494
-
Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
-
Petrova K., Oyadomari S., Hendershot L.M., Ron D. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J. 2008, 27:2862-2872.
-
(2008)
EMBO J.
, vol.27
, pp. 2862-2872
-
-
Petrova, K.1
Oyadomari, S.2
Hendershot, L.M.3
Ron, D.4
-
116
-
-
48249117110
-
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
-
Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 2008, 321:569-572.
-
(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
-
117
-
-
77954604855
-
J domain co-chaperone specificity defines the role of BiP during protein translocation
-
Vembar S.S., Jonikas M.C., Hendershot L.M., Weissman J.S., Brodsky J.L. J domain co-chaperone specificity defines the role of BiP during protein translocation. J. Biol. Chem. 2010, 285:22484-22494.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 22484-22494
-
-
Vembar, S.S.1
Jonikas, M.C.2
Hendershot, L.M.3
Weissman, J.S.4
Brodsky, J.L.5
-
118
-
-
27944464985
-
Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence
-
Molinari M., Galli C., Vanoni O., Arnold S.M., Kaufman R.J. Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol. Cell 2005, 20:503-512.
-
(2005)
Mol. Cell
, vol.20
, pp. 503-512
-
-
Molinari, M.1
Galli, C.2
Vanoni, O.3
Arnold, S.M.4
Kaufman, R.J.5
-
119
-
-
0034703863
-
Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila
-
Chan H.Y., Warrick J.M., Gray-Board G.L., Paulson H.L., Bonini N.M. Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum. Mol. Genet. 2000, 9:2811-2820.
-
(2000)
Hum. Mol. Genet.
, vol.9
, pp. 2811-2820
-
-
Chan, H.Y.1
Warrick, J.M.2
Gray-Board, G.L.3
Paulson, H.L.4
Bonini, N.M.5
-
120
-
-
0033215279
-
Pathogenic light chains and the B-cell repertoire
-
Stevens F.J., Argon Y. Pathogenic light chains and the B-cell repertoire. Immunol. Today 1999, 20:451-457.
-
(1999)
Immunol. Today
, vol.20
, pp. 451-457
-
-
Stevens, F.J.1
Argon, Y.2
-
121
-
-
52449103780
-
Amyloid oligomer conformation in a group of natively folded proteins
-
Yoshiike Y., Minai R., Matsuo Y., Chen Y.R., Kimura T., Takashima A. Amyloid oligomer conformation in a group of natively folded proteins. PLoS One 2008, 3:e3235.
-
(2008)
PLoS One
, vol.3
-
-
Yoshiike, Y.1
Minai, R.2
Matsuo, Y.3
Chen, Y.R.4
Kimura, T.5
Takashima, A.6
-
122
-
-
27744445135
-
BIP co-chaperone MTJ1/ERDJ1 interacts with inter-alpha-trypsin inhibitor heavy chain 4
-
Kroczynska B., King-Simmons L., Alloza L., Alava M.A., Elguindi E.C., Blond S.Y. BIP co-chaperone MTJ1/ERDJ1 interacts with inter-alpha-trypsin inhibitor heavy chain 4. Biochem. Biophys. Res. Commun. 2005, 338:1467-1477.
-
(2005)
Biochem. Biophys. Res. Commun.
, vol.338
, pp. 1467-1477
-
-
Kroczynska, B.1
King-Simmons, L.2
Alloza, L.3
Alava, M.A.4
Elguindi, E.C.5
Blond, S.Y.6
-
123
-
-
72449129195
-
Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland
-
Hosoda A., Tokuda M., Akai R., Kohno K., Iwawaki T. Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland. Biochem. J. 2009, 425:117-125.
-
(2009)
Biochem. J.
, vol.425
, pp. 117-125
-
-
Hosoda, A.1
Tokuda, M.2
Akai, R.3
Kohno, K.4
Iwawaki, T.5
-
124
-
-
20144386666
-
Pancreatic beta-cell failure and diabetes in mice with a deletion mutation of the endoplasmic reticulum molecular chaperone gene P58IPK
-
Ladiges W.C., Knoblaugh S.E., Morton J.F., Korth M.J., Sopher B.L., Baskin C.R., MacAuley A., Goodman A.G., LeBoeuf R.C., Katze M.G. Pancreatic beta-cell failure and diabetes in mice with a deletion mutation of the endoplasmic reticulum molecular chaperone gene P58IPK. Diabetes 2005, 54:1074-1081.
-
(2005)
Diabetes
, vol.54
, pp. 1074-1081
-
-
Ladiges, W.C.1
Knoblaugh, S.E.2
Morton, J.F.3
Korth, M.J.4
Sopher, B.L.5
Baskin, C.R.6
MacAuley, A.7
Goodman, A.G.8
LeBoeuf, R.C.9
Katze, M.G.10
-
125
-
-
0036275663
-
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
-
Kabani M., Beckerich J.M., Brodsky J.L. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 2002, 22:4677-4689.
-
(2002)
Mol. Cell. Biol.
, vol.22
, pp. 4677-4689
-
-
Kabani, M.1
Beckerich, J.M.2
Brodsky, J.L.3
-
126
-
-
28444474185
-
The gene disrupted in Marinesco-Sjogren syndrome encodes SIL1, an HSPA5 cochaperone
-
Anttonen A.K., Mahjneh I., Hamalainen R.H., Lagier-Tourenne C., Kopra O., Waris L., Anttonen M., Joensuu T., Kalimo H., Paetau A., Tranebjaerg L., Chaigne D., Koenig M., Eeg-Olofsson O., Udd B., Somer M., Somer H., Lehesjoki A.E. The gene disrupted in Marinesco-Sjogren syndrome encodes SIL1, an HSPA5 cochaperone. Nat. Genet. 2005, 37:1309-1311.
-
(2005)
Nat. Genet.
, vol.37
, pp. 1309-1311
-
-
Anttonen, A.K.1
Mahjneh, I.2
Hamalainen, R.H.3
Lagier-Tourenne, C.4
Kopra, O.5
Waris, L.6
Anttonen, M.7
Joensuu, T.8
Kalimo, H.9
Paetau, A.10
Tranebjaerg, L.11
Chaigne, D.12
Koenig, M.13
Eeg-Olofsson, O.14
Udd, B.15
Somer, M.16
Somer, H.17
Lehesjoki, A.E.18
-
127
-
-
28444497039
-
Mutations in SIL1 cause Marinesco-Sjogren syndrome, a cerebellar ataxia with cataract and myopathy
-
Senderek J., Krieger M., Stendel C., Bergmann C., Moser M., Breitbach-Faller N., Rudnik-Schoneborn S., Blaschek A., Wolf N.I., Harting I., North K., Smith J., Muntoni F., Brockington M., Quijano-Roy S., Renault F., Herrmann R., Hendershot L.M., Schroder J.M., Lochmuller H., Topaloglu H., Voit T., Weis J., Ebinger F., Zerres K. Mutations in SIL1 cause Marinesco-Sjogren syndrome, a cerebellar ataxia with cataract and myopathy. Nat. Genet. 2005, 37:1312-1314.
-
(2005)
Nat. Genet.
, vol.37
, pp. 1312-1314
-
-
Senderek, J.1
Krieger, M.2
Stendel, C.3
Bergmann, C.4
Moser, M.5
Breitbach-Faller, N.6
Rudnik-Schoneborn, S.7
Blaschek, A.8
Wolf, N.I.9
Harting, I.10
North, K.11
Smith, J.12
Muntoni, F.13
Brockington, M.14
Quijano-Roy, S.15
Renault, F.16
Herrmann, R.17
Hendershot, L.M.18
Schroder, J.M.19
Lochmuller, H.20
Topaloglu, H.21
Voit, T.22
Weis, J.23
Ebinger, F.24
Zerres, K.25
more..
-
128
-
-
25144520251
-
Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
-
Zhao L., Longo-Guess C., Harris B.S., Lee J.W., Ackerman S.L. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 2005, 37:974-979.
-
(2005)
Nat. Genet.
, vol.37
, pp. 974-979
-
-
Zhao, L.1
Longo-Guess, C.2
Harris, B.S.3
Lee, J.W.4
Ackerman, S.L.5
-
129
-
-
0346727523
-
Coordinated activation of Hsp70 chaperones
-
Steel G.J., Fullerton D.M., Tyson J.R., Stirling C.J. Coordinated activation of Hsp70 chaperones. Science 2004, 303:98-101.
-
(2004)
Science
, vol.303
, pp. 98-101
-
-
Steel, G.J.1
Fullerton, D.M.2
Tyson, J.R.3
Stirling, C.J.4
-
130
-
-
77649314881
-
Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco-Sjogren syndrome
-
Zhao L., Rosales C., Seburn K., Ron D., Ackerman S.L. Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco-Sjogren syndrome. Hum. Mol. Genet. 2009, 19:25-35.
-
(2009)
Hum. Mol. Genet.
, vol.19
, pp. 25-35
-
-
Zhao, L.1
Rosales, C.2
Seburn, K.3
Ron, D.4
Ackerman, S.L.5
-
131
-
-
34548512233
-
The role of p58IPK in protecting the stressed endoplasmic reticulum
-
Rutkowski D.T., Kang S.W., Goodman A.G., Garrison J.L., Taunton J., Katze M.G., Kaufman R.J., Hegde R.S. The role of p58IPK in protecting the stressed endoplasmic reticulum. Mol. Biol. Cell 2007, 18:3681-3691.
-
(2007)
Mol. Biol. Cell
, vol.18
, pp. 3681-3691
-
-
Rutkowski, D.T.1
Kang, S.W.2
Goodman, A.G.3
Garrison, J.L.4
Taunton, J.5
Katze, M.G.6
Kaufman, R.J.7
Hegde, R.S.8
-
132
-
-
84875076497
-
A SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machinery
-
Kyostila K., Cizinauskas S., Seppala E.H., Suhonen E., Jeserevics J., Sukura A., Syrja P., Lohi H. A SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machinery. PLoS Genet. 2012, 8:e1002759.
-
(2012)
PLoS Genet.
, vol.8
-
-
Kyostila, K.1
Cizinauskas, S.2
Seppala, E.H.3
Suhonen, E.4
Jeserevics, J.5
Sukura, A.6
Syrja, P.7
Lohi, H.8
-
133
-
-
33748432548
-
Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
-
Lee J.W., Beebe K., Nangle L.A., Jang J., Longo-Guess C.M., Cook S.A., Davisson M.T., Sundberg J.P., Schimmel P., Ackerman S.L. Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration. Nature 2006, 443:50-55.
-
(2006)
Nature
, vol.443
, pp. 50-55
-
-
Lee, J.W.1
Beebe, K.2
Nangle, L.A.3
Jang, J.4
Longo-Guess, C.M.5
Cook, S.A.6
Davisson, M.T.7
Sundberg, J.P.8
Schimmel, P.9
Ackerman, S.L.10
-
134
-
-
77952589171
-
GRP94 in ER quality control and stress responses
-
Eletto D., Dersh D., Argon Y. GRP94 in ER quality control and stress responses. Semin. Cell Dev. Biol. 2010, 21:479-485.
-
(2010)
Semin. Cell Dev. Biol.
, vol.21
, pp. 479-485
-
-
Eletto, D.1
Dersh, D.2
Argon, Y.3
-
135
-
-
0026808864
-
The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
-
Melnick J., Aviel S., Argon Y. The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J. Biol. Chem. 1992, 267:21303-21306.
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 21303-21306
-
-
Melnick, J.1
Aviel, S.2
Argon, Y.3
-
136
-
-
0028923597
-
Molecular chaperones and the biosynthesis of antigen receptors
-
Melnick J., Argon Y. Molecular chaperones and the biosynthesis of antigen receptors. Immunol. Today 1995, 16:243-250.
-
(1995)
Immunol. Today
, vol.16
, pp. 243-250
-
-
Melnick, J.1
Argon, Y.2
-
137
-
-
0026656520
-
Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP
-
Kim P.S., Bole D., Arvan P. Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP. J. Cell Biol. 1992, 118:541-549.
-
(1992)
J. Cell Biol.
, vol.118
, pp. 541-549
-
-
Kim, P.S.1
Bole, D.2
Arvan, P.3
-
138
-
-
0030666195
-
Thyroglobulin transport along the secretory pathway. Investigation of the role of molecular chaperone, GRP94, in protein export from the endoplasmic reticulum [published erratum appears in J Biol Chem 1997 Nov 28;272(48):30590]
-
Muresan Z., Arvan P. Thyroglobulin transport along the secretory pathway. Investigation of the role of molecular chaperone, GRP94, in protein export from the endoplasmic reticulum [published erratum appears in J Biol Chem 1997 Nov 28;272(48):30590]. J. Biol. Chem. 1997, 272:26095-26102.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 26095-26102
-
-
Muresan, Z.1
Arvan, P.2
-
139
-
-
67650882756
-
An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells
-
Ostrovsky O., Makarewich C., Snapp E.L., Argon Y. An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:11600-11605.
-
(2009)
Proc. Natl. Acad. Sci. U. S. A.
, vol.106
, pp. 11600-11605
-
-
Ostrovsky, O.1
Makarewich, C.2
Snapp, E.L.3
Argon, Y.4
-
140
-
-
84857475033
-
Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone
-
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Hao B., Bona R., Han D., Li Z. Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Nat. Commun. 2010, 1:79.
-
(2010)
Nat. Commun.
, vol.1
, pp. 79
-
-
Liu, B.1
Yang, Y.2
Qiu, Z.3
Staron, M.4
Hong, F.5
Li, Y.6
Wu, S.7
Hao, B.8
Bona, R.9
Han, D.10
Li, Z.11
-
141
-
-
31344453190
-
Substrate transfer from the chaperone Hsp70 to Hsp90
-
Wegele H., Wandinger S.K., Schmid A.B., Reinstein J., Buchner J. Substrate transfer from the chaperone Hsp70 to Hsp90. J. Mol. Biol. 2006, 356:802-811.
-
(2006)
J. Mol. Biol.
, vol.356
, pp. 802-811
-
-
Wegele, H.1
Wandinger, S.K.2
Schmid, A.B.3
Reinstein, J.4
Buchner, J.5
-
142
-
-
84872194587
-
Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response
-
(Epub)
-
Eletto D., Maganty A., Eletto D., Dersh D., Makarewich C., Biswas C., Doroudgar S., Glembotski C.C., Argon Y. Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response. J. Cell Sci. August 1 2012, (Epub).
-
(2012)
J. Cell Sci.
-
-
Eletto, D.1
Maganty, A.2
Eletto, D.3
Dersh, D.4
Makarewich, C.5
Biswas, C.6
Doroudgar, S.7
Glembotski, C.C.8
Argon, Y.9
-
143
-
-
34948853214
-
GRP94 is essential for mesoderm induction and muscle development because it regulates IGF secretion
-
Wanderling S., Simen B.B., Ostrovsky O., Ahmed N.T., Vogen S., Gidalevitz T., Argon Y. GRP94 is essential for mesoderm induction and muscle development because it regulates IGF secretion. Mol. Biol. Cell 2007, 18:3764-3775.
-
(2007)
Mol. Biol. Cell
, vol.18
, pp. 3764-3775
-
-
Wanderling, S.1
Simen, B.B.2
Ostrovsky, O.3
Ahmed, N.T.4
Vogen, S.5
Gidalevitz, T.6
Argon, Y.7
-
144
-
-
51649117657
-
Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin
-
Liu B., Li Z. Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin. Blood 2008, 112:1223-1230.
-
(2008)
Blood
, vol.112
, pp. 1223-1230
-
-
Liu, B.1
Li, Z.2
-
145
-
-
84865788752
-
Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production
-
Barton E., Park S., James J.K., Makarewich C.A., Eletto D., Philippou A., Lei H., Brisson B., Ostrovsky O., Li Z., Argon Y. Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production. FASEB J. 2012, 26:3691-3702.
-
(2012)
FASEB J.
, vol.26
, pp. 3691-3702
-
-
Barton, E.1
Park, S.2
James, J.K.3
Makarewich, C.A.4
Eletto, D.5
Philippou, A.6
Lei, H.7
Brisson, B.8
Ostrovsky, O.9
Li, Z.10
Argon, Y.11
-
146
-
-
79959825676
-
Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex
-
Staron M., Wu S., Hong F., Stojanovic A., Du X., Bona R., Liu B., Li Z. Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex. Blood 2011, 117:7136-7144.
-
(2011)
Blood
, vol.117
, pp. 7136-7144
-
-
Staron, M.1
Wu, S.2
Hong, F.3
Stojanovic, A.4
Du, X.5
Bona, R.6
Liu, B.7
Li, Z.8
-
147
-
-
0034795208
-
Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
-
Randow F., Seed B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat. Cell Biol. 2001, 3:891-896.
-
(2001)
Nat. Cell Biol.
, vol.3
, pp. 891-896
-
-
Randow, F.1
Seed, B.2
-
148
-
-
84865165609
-
Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition
-
Widmer C., Gebauer J.M., Brunstein E., Rosenbaum S., Zaucke F., Drogemuller C., Leeb T., Baumann U. Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:13243-13247.
-
(2012)
Proc. Natl. Acad. Sci. U. S. A.
, vol.109
, pp. 13243-13247
-
-
Widmer, C.1
Gebauer, J.M.2
Brunstein, E.3
Rosenbaum, S.4
Zaucke, F.5
Drogemuller, C.6
Leeb, T.7
Baumann, U.8
-
149
-
-
33744956370
-
Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins
-
Koide T., Nishikawa Y., Asada S., Yamazaki C.M., Takahara Y., Homma D.L., Otaka A., Ohtani K., Wakamiya N., Nagata K., Kitagawa K. Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins. J. Biol. Chem. 2006, 281:11177-11185.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 11177-11185
-
-
Koide, T.1
Nishikawa, Y.2
Asada, S.3
Yamazaki, C.M.4
Takahara, Y.5
Homma, D.L.6
Otaka, A.7
Ohtani, K.8
Wakamiya, N.9
Nagata, K.10
Kitagawa, K.11
-
150
-
-
0037144491
-
Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47
-
Tasab M., Jenkinson L., Bulleid N.J. Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47. J. Biol. Chem. 2002, 277:35007-35012.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 35007-35012
-
-
Tasab, M.1
Jenkinson, L.2
Bulleid, N.J.3
-
151
-
-
0034683570
-
Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
-
Nagai N., Hosokawa M., Itohara S., Adachi E., Matsushita T., Hosokawa N., Nagata K. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J. Cell Biol. 2000, 150:1499-1506.
-
(2000)
J. Cell Biol.
, vol.150
, pp. 1499-1506
-
-
Nagai, N.1
Hosokawa, M.2
Itohara, S.3
Adachi, E.4
Matsushita, T.5
Hosokawa, N.6
Nagata, K.7
-
152
-
-
77952583297
-
Protein quality control in the ER: the recognition of misfolded proteins
-
Maattanen P., Gehring K., Bergeron J.J., Thomas D.Y. Protein quality control in the ER: the recognition of misfolded proteins. Semin. Cell Dev. Biol. 2010, 21:500-511.
-
(2010)
Semin. Cell Dev. Biol.
, vol.21
, pp. 500-511
-
-
Maattanen, P.1
Gehring, K.2
Bergeron, J.J.3
Thomas, D.Y.4
-
153
-
-
0029024748
-
Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
-
Hebert D.N., Foellmer B., Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 1995, 81:425-433.
-
(1995)
Cell
, vol.81
, pp. 425-433
-
-
Hebert, D.N.1
Foellmer, B.2
Helenius, A.3
-
154
-
-
33751508817
-
N-glycan processing in ER quality control
-
Ruddock L.W., Molinari M. N-glycan processing in ER quality control. J. Cell Sci. 2006, 119:4373-4380.
-
(2006)
J. Cell Sci.
, vol.119
, pp. 4373-4380
-
-
Ruddock, L.W.1
Molinari, M.2
-
155
-
-
0032502282
-
Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
-
Vassilakos A., Michalak M., Lehrman M.A., Williams D.B. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 1998, 37:3480-3490.
-
(1998)
Biochemistry
, vol.37
, pp. 3480-3490
-
-
Vassilakos, A.1
Michalak, M.2
Lehrman, M.A.3
Williams, D.B.4
-
156
-
-
0029134004
-
Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
-
Wada I., Imai S., Kai M., Sakane F., Kanoh H. Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 1995, 270:20298-20304.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 20298-20304
-
-
Wada, I.1
Imai, S.2
Kai, M.3
Sakane, F.4
Kanoh, H.5
-
157
-
-
0032101943
-
Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I
-
Harris M.R., Yu Y.Y., Kindle C.S., Hansen T.H., Solheim J.C. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J. Immunol. 1998, 160:5404-5409.
-
(1998)
J. Immunol.
, vol.160
, pp. 5404-5409
-
-
Harris, M.R.1
Yu, Y.Y.2
Kindle, C.S.3
Hansen, T.H.4
Solheim, J.C.5
-
158
-
-
0033197741
-
Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
-
Ihara Y., Cohen-Doyle M.F., Saito Y., Williams D.B. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol. Cell 1999, 4:331-341.
-
(1999)
Mol. Cell
, vol.4
, pp. 331-341
-
-
Ihara, Y.1
Cohen-Doyle, M.F.2
Saito, Y.3
Williams, D.B.4
-
159
-
-
0032101943
-
Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I
-
Harris M.R., Yu Y.Y., Kindle C.S., Hansen T.H., Solheim J.C. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J. Immunol. 1998, 160:5404-5409.
-
(1998)
J. Immunol.
, vol.160
, pp. 5404-5409
-
-
Harris, M.R.1
Yu, Y.Y.2
Kindle, C.S.3
Hansen, T.H.4
Solheim, J.C.5
-
160
-
-
0021891884
-
Assembly of asparagine-linked oligosaccharides
-
Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 1985, 54:631-664.
-
(1985)
Annu. Rev. Biochem.
, vol.54
, pp. 631-664
-
-
Kornfeld, R.1
Kornfeld, S.2
-
161
-
-
0027156495
-
Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)
-
David V., Hochstenbach F., Rajagopalan S., Brenner M.B. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J. Biol. Chem. 1993, 268:9585-9592.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 9585-9592
-
-
David, V.1
Hochstenbach, F.2
Rajagopalan, S.3
Brenner, M.B.4
-
162
-
-
0027295871
-
Association of folding intermediates of glycoproteins with calnexin during protein maturation
-
Ou W.-J., Cameron P.H., Thomas D.Y., Bergeron J.J.M. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 1993, 364:771-776.
-
(1993)
Nature
, vol.364
, pp. 771-776
-
-
Ou, W.-J.1
Cameron, P.H.2
Thomas, D.Y.3
Bergeron, J.J.M.4
-
163
-
-
0028103695
-
Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
-
Hammond C., Braakman I., Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:913-917.
-
(1994)
Proc. Natl. Acad. Sci. U. S. A.
, vol.91
, pp. 913-917
-
-
Hammond, C.1
Braakman, I.2
Helenius, A.3
-
164
-
-
20744441520
-
Subunits of the translocon interact with components of the oligosaccharyl transferase complex
-
Chavan M., Yan A., Lennarz W.J. Subunits of the translocon interact with components of the oligosaccharyl transferase complex. J. Biol. Chem. 2005, 280:22917-22924.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 22917-22924
-
-
Chavan, M.1
Yan, A.2
Lennarz, W.J.3
-
165
-
-
77950639519
-
Organization of the Sec61 translocon, studied by high resolution native electrophoresis
-
Dejgaard K., Theberge J.F., Heath-Engel H., Chevet E., Tremblay M.L., Thomas D.Y. Organization of the Sec61 translocon, studied by high resolution native electrophoresis. J. Proteome Res. 2010, 9:1763-1771.
-
(2010)
J. Proteome Res.
, vol.9
, pp. 1763-1771
-
-
Dejgaard, K.1
Theberge, J.F.2
Heath-Engel, H.3
Chevet, E.4
Tremblay, M.L.5
Thomas, D.Y.6
-
166
-
-
0034646876
-
Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
-
Molinari M., Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 2000, 288:331-333.
-
(2000)
Science
, vol.288
, pp. 331-333
-
-
Molinari, M.1
Helenius, A.2
-
167
-
-
0032513212
-
Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
-
Zapun A., Darby N.J., Tessier D.C., Michalak M., Bergeron J.J., Thomas D.Y. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 1998, 273:6009-6012.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 6009-6012
-
-
Zapun, A.1
Darby, N.J.2
Tessier, D.C.3
Michalak, M.4
Bergeron, J.J.5
Thomas, D.Y.6
-
168
-
-
0032807338
-
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
-
Oliver J.D., Roderick H.L., Llewellyn D.H., High S. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell 1999, 10:2573-2582.
-
(1999)
Mol. Biol. Cell
, vol.10
, pp. 2573-2582
-
-
Oliver, J.D.1
Roderick, H.L.2
Llewellyn, D.H.3
High, S.4
-
169
-
-
0033523910
-
Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
-
Molinari M., Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 1999, 402:90-93.
-
(1999)
Nature
, vol.402
, pp. 90-93
-
-
Molinari, M.1
Helenius, A.2
-
170
-
-
0037133347
-
TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain
-
Frickel E.M., Riek R., Jelesarov I., Helenius A., Wuthrich K., Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:1954-1959.
-
(2002)
Proc. Natl. Acad. Sci. U. S. A.
, vol.99
, pp. 1954-1959
-
-
Frickel, E.M.1
Riek, R.2
Jelesarov, I.3
Helenius, A.4
Wuthrich, K.5
Ellgaard, L.6
-
171
-
-
0028198111
-
How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
-
Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 1994, 5:253-265.
-
(1994)
Mol. Biol. Cell
, vol.5
, pp. 253-265
-
-
Helenius, A.1
-
172
-
-
0030765016
-
+ disturbances, and cell death in renal epithelial cells
-
+ disturbances, and cell death in renal epithelial cells. J. Biol. Chem. 1997, 272:21751-21759.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 21751-21759
-
-
Liu, H.1
Bowes, R.2
van de Water, B.3
Sillence, C.4
Nagelkerke, J.F.5
Stevens, J.L.6
-
173
-
-
0345253853
-
Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response
-
de Virgilio M., Kitzmuller C., Schwaiger E., Klein M., Kreibich G., Ivessa N.E. Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response. Mol. Biol. Cell 1999, 10:4059-4073.
-
(1999)
Mol. Biol. Cell
, vol.10
, pp. 4059-4073
-
-
de Virgilio, M.1
Kitzmuller, C.2
Schwaiger, E.3
Klein, M.4
Kreibich, G.5
Ivessa, N.E.6
-
174
-
-
33748795800
-
EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
-
Olivari S., Cali T., Salo K.E., Paganetti P., Ruddock L.W., Molinari M. EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem. Biophys. Res. Commun. 2006, 349:1278-1284.
-
(2006)
Biochem. Biophys. Res. Commun.
, vol.349
, pp. 1278-1284
-
-
Olivari, S.1
Cali, T.2
Salo, K.E.3
Paganetti, P.4
Ruddock, L.W.5
Molinari, M.6
-
175
-
-
33646928455
-
EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming
-
Hirao K., Natsuka Y., Tamura T., Wada I., Morito D., Natsuka S., Romero P., Sleno B., Tremblay L.O., Herscovics A., Nagata K., Hosokawa N. EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming. J. Biol. Chem. 2006, 281:9650-9658.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 9650-9658
-
-
Hirao, K.1
Natsuka, Y.2
Tamura, T.3
Wada, I.4
Morito, D.5
Natsuka, S.6
Romero, P.7
Sleno, B.8
Tremblay, L.O.9
Herscovics, A.10
Nagata, K.11
Hosokawa, N.12
-
176
-
-
0036838084
-
Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression
-
Denzel A., Molinari M., Trigueros C., Martin J.E., Velmurgan S., Brown S., Stamp G., Owen M.J. Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression. Mol. Cell. Biol. 2002, 22:7398-7404.
-
(2002)
Mol. Cell. Biol.
, vol.22
, pp. 7398-7404
-
-
Denzel, A.1
Molinari, M.2
Trigueros, C.3
Martin, J.E.4
Velmurgan, S.5
Brown, S.6
Stamp, G.7
Owen, M.J.8
-
178
-
-
0020713174
-
Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
-
Bause E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem. J. 1983, 209:331-336.
-
(1983)
Biochem. J.
, vol.209
, pp. 331-336
-
-
Bause, E.1
-
179
-
-
8544242762
-
The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates
-
Caramelo J.J., Castro O.A., de Prat-Gay G., Parodi A.J. The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates. J. Biol. Chem. 2004, 279:46280-46285.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 46280-46285
-
-
Caramelo, J.J.1
Castro, O.A.2
de Prat-Gay, G.3
Parodi, A.J.4
-
180
-
-
0029126624
-
The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
-
Sousa M., Parodi A.J. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 1995, 14:4196-4203.
-
(1995)
EMBO J.
, vol.14
, pp. 4196-4203
-
-
Sousa, M.1
Parodi, A.J.2
-
181
-
-
18944395787
-
Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT
-
Ritter C., Quirin K., Kowarik M., Helenius A. Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT. EMBO J. 2005, 24:1730-1738.
-
(2005)
EMBO J.
, vol.24
, pp. 1730-1738
-
-
Ritter, C.1
Quirin, K.2
Kowarik, M.3
Helenius, A.4
-
182
-
-
34250346376
-
Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control
-
Jin H., Yan Z., Nam K.H., Li J. Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control. Mol. Cell 2007, 26:821-830.
-
(2007)
Mol. Cell
, vol.26
, pp. 821-830
-
-
Jin, H.1
Yan, Z.2
Nam, K.H.3
Li, J.4
-
183
-
-
54249136020
-
Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation
-
Schallus T., Jaeckh C., Feher K., Palma A.S., Liu Y., Simpson J.C., Mackeen M., Stier G., Gibson T.J., Feizi T., Pieler T., Muhle-Goll C. Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Mol. Biol. Cell 2008, 19:3404-3414.
-
(2008)
Mol. Biol. Cell
, vol.19
, pp. 3404-3414
-
-
Schallus, T.1
Jaeckh, C.2
Feher, K.3
Palma, A.S.4
Liu, Y.5
Simpson, J.C.6
Mackeen, M.7
Stier, G.8
Gibson, T.J.9
Feizi, T.10
Pieler, T.11
Muhle-Goll, C.12
-
184
-
-
79551532382
-
Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER
-
Galli C., Bernasconi R., Solda T., Calanca V., Molinari M. Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER. PLoS One 2011, 6:e16304.
-
(2011)
PLoS One
, vol.6
-
-
Galli, C.1
Bernasconi, R.2
Solda, T.3
Calanca, V.4
Molinari, M.5
-
185
-
-
0029934119
-
Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
-
Hebert D.N., Foellmer B., Helenius A. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 1996, 15:2961-2968.
-
(1996)
EMBO J.
, vol.15
, pp. 2961-2968
-
-
Hebert, D.N.1
Foellmer, B.2
Helenius, A.3
-
186
-
-
35748948975
-
In and out of the ER: protein folding, quality control, degradation, and related human diseases
-
Hebert D.N., Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 2007, 87:1377-1408.
-
(2007)
Physiol. Rev.
, vol.87
, pp. 1377-1408
-
-
Hebert, D.N.1
Molinari, M.2
-
187
-
-
0034677754
-
Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control
-
Branza-Nichita N., Negroiu G., Petrescu A.J., Garman E.F., Platt F.M., Wormald M.R., Dwek R.A., Petrescu S.M. Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control. J. Biol. Chem. 2000, 275:8169-8175.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 8169-8175
-
-
Branza-Nichita, N.1
Negroiu, G.2
Petrescu, A.J.3
Garman, E.F.4
Platt, F.M.5
Wormald, M.R.6
Dwek, R.A.7
Petrescu, S.M.8
-
188
-
-
0033671867
-
Stabilization of human recombinant erythropoietin through interactions with the highly branched N-glycans
-
Toyoda T., Itai T., Arakawa T., Aoki K.H., Yamaguchi H. Stabilization of human recombinant erythropoietin through interactions with the highly branched N-glycans. J. Biochem. 2000, 128:731-737.
-
(2000)
J. Biochem.
, vol.128
, pp. 731-737
-
-
Toyoda, T.1
Itai, T.2
Arakawa, T.3
Aoki, K.H.4
Yamaguchi, H.5
-
189
-
-
0343607059
-
Solution structure of the alpha-subunit of human chorionic gonadotropin
-
Erbel P.J., Karimi-Nejad Y., De Beer T., Boelens R., Kamerling J.P., Vliegenthart J.F. Solution structure of the alpha-subunit of human chorionic gonadotropin. Eur. J. Biochem. 1999, 260:490-498.
-
(1999)
Eur. J. Biochem.
, vol.260
, pp. 490-498
-
-
Erbel, P.J.1
Karimi-Nejad, Y.2
De Beer, T.3
Boelens, R.4
Kamerling, J.P.5
Vliegenthart, J.F.6
-
190
-
-
0029009565
-
MHC class I expression and transport in a calnexin-deficient cell line
-
Scott J.E., Dawson J.R. MHC class I expression and transport in a calnexin-deficient cell line. J. Immunol. 1995, 155:143-148.
-
(1995)
J. Immunol.
, vol.155
, pp. 143-148
-
-
Scott, J.E.1
Dawson, J.R.2
-
191
-
-
77953296950
-
Calnexin deficiency leads to dysmyelination
-
Kraus A., Groenendyk J., Bedard K., Baldwin T.A., Krause K.H., Dubois-Dauphin M., Dyck J., Rosenbaum E.E., Korngut L., Colley N.J., Gosgnach S., Zochodne D., Todd K., Agellon L.B., Michalak M. Calnexin deficiency leads to dysmyelination. J. Biol. Chem. 2010, 285:18928-18938.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 18928-18938
-
-
Kraus, A.1
Groenendyk, J.2
Bedard, K.3
Baldwin, T.A.4
Krause, K.H.5
Dubois-Dauphin, M.6
Dyck, J.7
Rosenbaum, E.E.8
Korngut, L.9
Colley, N.J.10
Gosgnach, S.11
Zochodne, D.12
Todd, K.13
Agellon, L.B.14
Michalak, M.15
-
192
-
-
0033535353
-
Calreticulin is essential for cardiac development
-
Mesaeli N., Nakamura K., Zvaritch E., Dickie P., Dziak E., Krause K.H., Opas M., MacLennan D.H., Michalak M. Calreticulin is essential for cardiac development. J. Cell Biol. 1999, 144:857-868.
-
(1999)
J. Cell Biol.
, vol.144
, pp. 857-868
-
-
Mesaeli, N.1
Nakamura, K.2
Zvaritch, E.3
Dickie, P.4
Dziak, E.5
Krause, K.H.6
Opas, M.7
MacLennan, D.H.8
Michalak, M.9
-
193
-
-
84875499653
-
The human protein disulfide isomerase gene family
-
Galligan J.J., Petersen D.R. The human protein disulfide isomerase gene family. Hum. Genomics 2012, 6:6.
-
(2012)
Hum. Genomics
, vol.6
, pp. 6
-
-
Galligan, J.J.1
Petersen, D.R.2
-
194
-
-
0023303619
-
Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
-
Pihlajaniemi T., Helaakoski T., Tasanen K., Myllyla R., Huhtala M.L., Koivu J., Kivirikko K.I. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 1987, 6:643-649.
-
(1987)
EMBO J.
, vol.6
, pp. 643-649
-
-
Pihlajaniemi, T.1
Helaakoski, T.2
Tasanen, K.3
Myllyla, R.4
Huhtala, M.L.5
Koivu, J.6
Kivirikko, K.I.7
-
195
-
-
77957312329
-
From antibodies to adiponectin: role of ERp44 in sizing and timing protein secretion
-
Cortini M., Sitia R. From antibodies to adiponectin: role of ERp44 in sizing and timing protein secretion. Diabetes Obes. Metab. 2010, 12(Suppl. 2):39-47.
-
(2010)
Diabetes Obes. Metab.
, vol.12
, Issue.SUPPL. 2
, pp. 39-47
-
-
Cortini, M.1
Sitia, R.2
-
196
-
-
77956684691
-
Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
-
Rutkevich L.A., Cohen-Doyle M.F., Brockmeier U., Williams D.B. Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol. Biol. Cell 2010, 21:3093-3105.
-
(2010)
Mol. Biol. Cell
, vol.21
, pp. 3093-3105
-
-
Rutkevich, L.A.1
Cohen-Doyle, M.F.2
Brockmeier, U.3
Williams, D.B.4
-
197
-
-
34547670979
-
Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans
-
Winter A.D., McCormack G., Page A.P. Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans. Dev. Biol. 2007, 308:449-461.
-
(2007)
Dev. Biol.
, vol.308
, pp. 449-461
-
-
Winter, A.D.1
McCormack, G.2
Page, A.P.3
-
198
-
-
59049105293
-
Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
-
Jessop C.E., Tavender T.J., Watkins R.H., Chambers J.E., Bulleid N.J. Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J. Biol. Chem. 2009, 284:2194-2202.
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 2194-2202
-
-
Jessop, C.E.1
Tavender, T.J.2
Watkins, R.H.3
Chambers, J.E.4
Bulleid, N.J.5
-
199
-
-
33646594461
-
Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
-
Solda T., Garbi N., Hammerling G.J., Molinari M. Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. J. Biol. Chem. 2006, 281:6219-6226.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 6219-6226
-
-
Solda, T.1
Garbi, N.2
Hammerling, G.J.3
Molinari, M.4
-
200
-
-
70849101711
-
Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
-
Jessop C.E., Watkins R.H., Simmons J.J., Tasab M., Bulleid N.J. Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J. Cell Sci. 2009, 122:4287-4295.
-
(2009)
J. Cell Sci.
, vol.122
, pp. 4287-4295
-
-
Jessop, C.E.1
Watkins, R.H.2
Simmons, J.J.3
Tasab, M.4
Bulleid, N.J.5
-
201
-
-
34250372166
-
Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf
-
Menon S., Lee J., Abplanalp W.A., Yoo S.E., Agui T., Furudate S., Kim P.S., Arvan P. Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf. J. Biol. Chem. 2007, 282:6183-6191.
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 6183-6191
-
-
Menon, S.1
Lee, J.2
Abplanalp, W.A.3
Yoo, S.E.4
Agui, T.5
Furudate, S.6
Kim, P.S.7
Arvan, P.8
-
202
-
-
79551714334
-
A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection
-
Walczak C.P., Tsai B. A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. J. Virol. 2010, 85:2386-2396.
-
(2010)
J. Virol.
, vol.85
, pp. 2386-2396
-
-
Walczak, C.P.1
Tsai, B.2
-
203
-
-
70350129433
-
PERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin
-
Shimizu Y., Meunier L., Hendershot L.M. pERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:17013-17018.
-
(2009)
Proc. Natl. Acad. Sci. U. S. A.
, vol.106
, pp. 17013-17018
-
-
Shimizu, Y.1
Meunier, L.2
Hendershot, L.M.3
-
204
-
-
70350130802
-
Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1
-
van Anken E., Pena F., Hafkemeijer N., Christis C., Romijn E.P., Grauschopf U., Oorschot V.M., Pertel T., Engels S., Ora A., Lastun V., Glockshuber R., Klumperman J., Heck A.J., Luban J., Braakman I. Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:17019-17024.
-
(2009)
Proc. Natl. Acad. Sci. U. S. A.
, vol.106
, pp. 17019-17024
-
-
van Anken, E.1
Pena, F.2
Hafkemeijer, N.3
Christis, C.4
Romijn, E.P.5
Grauschopf, U.6
Oorschot, V.M.7
Pertel, T.8
Engels, S.9
Ora, A.10
Lastun, V.11
Glockshuber, R.12
Klumperman, J.13
Heck, A.J.14
Luban, J.15
Braakman, I.16
-
205
-
-
0018143763
-
Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization
-
Schmid F.X., Baldwin R.L. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proc. Natl. Acad. Sci. U. S. A. 1978, 75:4764-4768.
-
(1978)
Proc. Natl. Acad. Sci. U. S. A.
, vol.75
, pp. 4764-4768
-
-
Schmid, F.X.1
Baldwin, R.L.2
-
206
-
-
0027267916
-
Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum
-
Nigam S.K., Jin Y.J., Jin M.J., Bush K.T., Bierer B.E., Burakoff S.J. Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum. Biochem. J. 1993, 294:511-515.
-
(1993)
Biochem. J.
, vol.294
, pp. 511-515
-
-
Nigam, S.K.1
Jin, Y.J.2
Jin, M.J.3
Bush, K.T.4
Bierer, B.E.5
Burakoff, S.J.6
-
207
-
-
0025916166
-
Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum
-
Lodish H.F., Kong N. Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J. Biol. Chem. 1991, 266:14835-14838.
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 14835-14838
-
-
Lodish, H.F.1
Kong, N.2
-
208
-
-
77958543957
-
Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation
-
Bernasconi R., Solda T., Galli C., Pertel T., Luban J., Molinari M. Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation. PLoS One 2010, 5:e13008.
-
(2010)
PLoS One
, vol.5
-
-
Bernasconi, R.1
Solda, T.2
Galli, C.3
Pertel, T.4
Luban, J.5
Molinari, M.6
-
209
-
-
0032567714
-
Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway
-
Davis E.C., Broekelmann T.J., Ozawa Y., Mecham R.P. Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway. J. Cell Biol. 1998, 140:295-303.
-
(1998)
J. Cell Biol.
, vol.140
, pp. 295-303
-
-
Davis, E.C.1
Broekelmann, T.J.2
Ozawa, Y.3
Mecham, R.P.4
-
210
-
-
80955179560
-
Osteoblast-enriched membrane protein IFITM5 regulates the association of CD9 with an FKBP11-CD81-FPRP complex and stimulates expression of interferon-induced genes
-
Hanagata N., Li X. Osteoblast-enriched membrane protein IFITM5 regulates the association of CD9 with an FKBP11-CD81-FPRP complex and stimulates expression of interferon-induced genes. Biochem. Biophys. Res. Commun. 2011, 409:378-384.
-
(2011)
Biochem. Biophys. Res. Commun.
, vol.409
, pp. 378-384
-
-
Hanagata, N.1
Li, X.2
-
211
-
-
84862780507
-
Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss
-
Baumann M., Giunta C., Krabichler B., Ruschendorf F., Zoppi N., Colombi M., Bittner R.E., Quijano-Roy S., Muntoni F., Cirak S., Schreiber G., Zou Y., Hu Y., Romero N.B., Carlier R.Y., Amberger A., Deutschmann A., Straub V., Rohrbach M., Steinmann B., Rostasy K., Karall D., Bonnemann C.G., Zschocke J., Fauth C. Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss. Am. J. Hum. Genet. 2012, 90:201-216.
-
(2012)
Am. J. Hum. Genet.
, vol.90
, pp. 201-216
-
-
Baumann, M.1
Giunta, C.2
Krabichler, B.3
Ruschendorf, F.4
Zoppi, N.5
Colombi, M.6
Bittner, R.E.7
Quijano-Roy, S.8
Muntoni, F.9
Cirak, S.10
Schreiber, G.11
Zou, Y.12
Hu, Y.13
Romero, N.B.14
Carlier, R.Y.15
Amberger, A.16
Deutschmann, A.17
Straub, V.18
Rohrbach, M.19
Steinmann, B.20
Rostasy, K.21
Karall, D.22
Bonnemann, C.G.23
Zschocke, J.24
Fauth, C.25
more..
-
212
-
-
74249109599
-
Severe osteogenesis imperfecta in cyclophilin B-deficient mice
-
Choi J.W., Sutor S.L., Lindquist L., Evans G.L., Madden B.J., Bergen H.R., Hefferan T.E., Yaszemski M.J., Bram R.J. Severe osteogenesis imperfecta in cyclophilin B-deficient mice. PLoS Genet. 2009, 5:e1000750.
-
(2009)
PLoS Genet.
, vol.5
-
-
Choi, J.W.1
Sutor, S.L.2
Lindquist, L.3
Evans, G.L.4
Madden, B.J.5
Bergen, H.R.6
Hefferan, T.E.7
Yaszemski, M.J.8
Bram, R.J.9
-
213
-
-
84867455169
-
Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix
-
Barnes A.M., Cabral W.A., Weis M., Makareeva E., Mertz E.L., Leikin S., Eyre D., Trujillo C., Marini J.C. Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix. Hum. Mutat. 2012, 33:1589-1598.
-
(2012)
Hum. Mutat.
, vol.33
, pp. 1589-1598
-
-
Barnes, A.M.1
Cabral, W.A.2
Weis, M.3
Makareeva, E.4
Mertz, E.L.5
Leikin, S.6
Eyre, D.7
Trujillo, C.8
Marini, J.C.9
-
214
-
-
84865722729
-
An interaction map of endoplasmic reticulum chaperones and foldases
-
Jansen G., Maattanen P., Denisov A.Y., Scarffe L., Schade B., Balghi H., Dejgaard K., Chen L.Y., Muller W.J., Gehring K., Thomas D.Y. An interaction map of endoplasmic reticulum chaperones and foldases. Mol. Cell. Proteomics 2012, 11:710-723.
-
(2012)
Mol. Cell. Proteomics
, vol.11
, pp. 710-723
-
-
Jansen, G.1
Maattanen, P.2
Denisov, A.Y.3
Scarffe, L.4
Schade, B.5
Balghi, H.6
Dejgaard, K.7
Chen, L.Y.8
Muller, W.J.9
Gehring, K.10
Thomas, D.Y.11
-
215
-
-
34250364576
-
Loss of secretory pathway FK506-binding proteins results in cold-sensitive lethality and associate extracellular matrix defects in the nematode Caenorhabditis elegans
-
Winter A.D., Eschenlauer S.C., McCormack G., Page A.P. Loss of secretory pathway FK506-binding proteins results in cold-sensitive lethality and associate extracellular matrix defects in the nematode Caenorhabditis elegans. J. Biol. Chem. 2007, 282:12813-12821.
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 12813-12821
-
-
Winter, A.D.1
Eschenlauer, S.C.2
McCormack, G.3
Page, A.P.4
-
216
-
-
34247324294
-
Neurospora crassa FKBP22 is a novel ER chaperone and functionally cooperates with BiP
-
Tremmel D., Tropschug M. Neurospora crassa FKBP22 is a novel ER chaperone and functionally cooperates with BiP. J. Mol. Biol. 2007, 369:55-68.
-
(2007)
J. Mol. Biol.
, vol.369
, pp. 55-68
-
-
Tremmel, D.1
Tropschug, M.2
-
217
-
-
33846444710
-
The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity
-
Wang Y., Han R., Wu D., Li J., Chen C., Ma H., Mi H. The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity. Biochem. Biophys. Res. Commun. 2007, 354:315-320.
-
(2007)
Biochem. Biophys. Res. Commun.
, vol.354
, pp. 315-320
-
-
Wang, Y.1
Han, R.2
Wu, D.3
Li, J.4
Chen, C.5
Ma, H.6
Mi, H.7
-
218
-
-
79956224178
-
Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization
-
Feng M., Gu C., Ma S., Wang Y., Liu H., Han R., Gao J., Long Y., Mi H. Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization. Biochem. Biophys. Res. Commun. 2011, 408:537-540.
-
(2011)
Biochem. Biophys. Res. Commun.
, vol.408
, pp. 537-540
-
-
Feng, M.1
Gu, C.2
Ma, S.3
Wang, Y.4
Liu, H.5
Han, R.6
Gao, J.7
Long, Y.8
Mi, H.9
-
219
-
-
0036740693
-
The chaperone activity of protein disulfide isomerase is affected by cyclophilin B and cyclosporin A in vitro
-
Horibe T., Yosho C., Okada S., Tsukamoto M., Nagai H., Hagiwara Y., Tujimoto Y., Kikuchi M. The chaperone activity of protein disulfide isomerase is affected by cyclophilin B and cyclosporin A in vitro. J. Biochem. 2002, 132:401-407.
-
(2002)
J. Biochem.
, vol.132
, pp. 401-407
-
-
Horibe, T.1
Yosho, C.2
Okada, S.3
Tsukamoto, M.4
Nagai, H.5
Hagiwara, Y.6
Tujimoto, Y.7
Kikuchi, M.8
-
220
-
-
0041856169
-
Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity
-
Motohashi K., Koyama F., Nakanishi Y., Ueoka-Nakanishi H., Hisabori T. Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity. J. Biol. Chem. 2003, 278:31848-31852.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 31848-31852
-
-
Motohashi, K.1
Koyama, F.2
Nakanishi, Y.3
Ueoka-Nakanishi, H.4
Hisabori, T.5
-
221
-
-
78149238000
-
Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain
-
Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K. Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. J. Biol. Chem. 2010, 285:35551-35557.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 35551-35557
-
-
Kozlov, G.1
Bastos-Aristizabal, S.2
Maattanen, P.3
Rosenauer, A.4
Zheng, F.5
Killikelly, A.6
Trempe, J.F.7
Thomas, D.Y.8
Gehring, K.9
-
222
-
-
0036911213
-
A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
-
Meunier L., Usherwood Y.K., Chung K.T., Hendershot L.M. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 2002, 13:4456-4469.
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 4456-4469
-
-
Meunier, L.1
Usherwood, Y.K.2
Chung, K.T.3
Hendershot, L.M.4
-
223
-
-
0037470139
-
Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B
-
Zhang J., Herscovitz H. Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B. J. Biol. Chem. 2003, 278:7459-7468.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 7459-7468
-
-
Zhang, J.1
Herscovitz, H.2
-
224
-
-
27644436010
-
Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase
-
Di Jeso B., Park Y.N., Ulianich L., Treglia A.S., Urbanas M.L., High S., Arvan P. Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase. Mol. Cell. Biol. 2005, 25:9793-9805.
-
(2005)
Mol. Cell. Biol.
, vol.25
, pp. 9793-9805
-
-
Di Jeso, B.1
Park, Y.N.2
Ulianich, L.3
Treglia, A.S.4
Urbanas, M.L.5
High, S.6
Arvan, P.7
-
226
-
-
0028801931
-
Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
-
Kim P.S., Arvan P. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 1995, 128:29-38.
-
(1995)
J. Cell Biol.
, vol.128
, pp. 29-38
-
-
Kim, P.S.1
Arvan, P.2
-
227
-
-
0033782030
-
Dynamics and retention of misfolded proteins in native ER membranes
-
Nehls S., Snapp E.L., Cole N.B., Zaal K.J., Kenworthy A.K., Roberts T.H., Ellenberg J., Presley J.F., Siggia E., Lippincott-Schwartz J. Dynamics and retention of misfolded proteins in native ER membranes. Nat. Cell Biol. 2000, 2:288-295.
-
(2000)
Nat. Cell Biol.
, vol.2
, pp. 288-295
-
-
Nehls, S.1
Snapp, E.L.2
Cole, N.B.3
Zaal, K.J.4
Kenworthy, A.K.5
Roberts, T.H.6
Ellenberg, J.7
Presley, J.F.8
Siggia, E.9
Lippincott-Schwartz, J.10
-
228
-
-
33646238977
-
Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells
-
Snapp E.L., Sharma A., Lippincott-Schwartz J., Hegde R.S. Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:6536-6541.
-
(2006)
Proc. Natl. Acad. Sci. U. S. A.
, vol.103
, pp. 6536-6541
-
-
Snapp, E.L.1
Sharma, A.2
Lippincott-Schwartz, J.3
Hegde, R.S.4
-
229
-
-
77953501690
-
BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells
-
Lai C.W., Aronson D.E., Snapp E.L. BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells. Mol. Biol. Cell 2010, 21:1909-1921.
-
(2010)
Mol. Biol. Cell
, vol.21
, pp. 1909-1921
-
-
Lai, C.W.1
Aronson, D.E.2
Snapp, E.L.3
-
230
-
-
79960182560
-
Allostery in protein domains reflects a balance of steric and hydrophobic effects
-
England J.L. Allostery in protein domains reflects a balance of steric and hydrophobic effects. Structure 2011, 19:967-975.
-
(2011)
Structure
, vol.19
, pp. 967-975
-
-
England, J.L.1
-
231
-
-
76949097340
-
Quantitative proteomics reveals subset-specific viral recognition in dendritic cells
-
Luber C.A., Cox J., Lauterbach H., Fancke B., Selbach M., Tschopp J., Akira S., Wiegand M., Hochrein H., O'Keeffe M., Mann M. Quantitative proteomics reveals subset-specific viral recognition in dendritic cells. Immunity 2010, 32:279-289.
-
(2010)
Immunity
, vol.32
, pp. 279-289
-
-
Luber, C.A.1
Cox, J.2
Lauterbach, H.3
Fancke, B.4
Selbach, M.5
Tschopp, J.6
Akira, S.7
Wiegand, M.8
Hochrein, H.9
O'Keeffe, M.10
Mann, M.11
-
232
-
-
84872685287
-
Extensive quantitative remodeling of the proteome between normal colon tissue and adenocarcinoma
-
Wisniewski J.R., Ostasiewicz P., Dus K., Zielinska D.F., Gnad F., Mann M. Extensive quantitative remodeling of the proteome between normal colon tissue and adenocarcinoma. Mol. Syst. Biol. 2012, 8:611.
-
(2012)
Mol. Syst. Biol.
, vol.8
, pp. 611
-
-
Wisniewski, J.R.1
Ostasiewicz, P.2
Dus, K.3
Zielinska, D.F.4
Gnad, F.5
Mann, M.6
-
233
-
-
84857963102
-
A quantitative spatial proteomics analysis of proteome turnover in human cells
-
(M111 011429)
-
Boisvert F.M., Ahmad Y., Gierlinski M., Charriere F., Lamont D., Scott M., Barton G., Lamond A.I. A quantitative spatial proteomics analysis of proteome turnover in human cells. Mol. Cell. Proteomics 2012, 11. (M111 011429).
-
(2012)
Mol. Cell. Proteomics
, vol.11
-
-
Boisvert, F.M.1
Ahmad, Y.2
Gierlinski, M.3
Charriere, F.4
Lamont, D.5
Scott, M.6
Barton, G.7
Lamond, A.I.8
-
234
-
-
67649562565
-
Functions and pathologies of BiP and its interaction partners
-
Dudek J., Benedix J., Cappel S., Greiner M., Jalal C., Muller L., Zimmermann R. Functions and pathologies of BiP and its interaction partners. Cell. Mol. Life Sci. 2009, 66:1556-1569.
-
(2009)
Cell. Mol. Life Sci.
, vol.66
, pp. 1556-1569
-
-
Dudek, J.1
Benedix, J.2
Cappel, S.3
Greiner, M.4
Jalal, C.5
Muller, L.6
Zimmermann, R.7
-
235
-
-
33645065115
-
Tyrosinase maturation through the mammalian secretory pathway: bringing color to life
-
Wang N., Hebert D.N. Tyrosinase maturation through the mammalian secretory pathway: bringing color to life. Pigment Cell Res. 2006, 19:3-18.
-
(2006)
Pigment Cell Res.
, vol.19
, pp. 3-18
-
-
Wang, N.1
Hebert, D.N.2
-
236
-
-
79956195134
-
C-terminus glycans with critical functional role in the maturation of secretory glycoproteins
-
Cioaca D., Ghenea S., Spiridon L.N., Marin M., Petrescu A.J., Petrescu S.M. C-terminus glycans with critical functional role in the maturation of secretory glycoproteins. PLoS One 2011, 6:e19979.
-
(2011)
PLoS One
, vol.6
-
-
Cioaca, D.1
Ghenea, S.2
Spiridon, L.N.3
Marin, M.4
Petrescu, A.J.5
Petrescu, S.M.6
-
237
-
-
0017622587
-
Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation
-
Parham P., Alpert B.N., Orr H.T., Strominger J.L. Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation. J. Biol. Chem. 1977, 252:7555-7567.
-
(1977)
J. Biol. Chem.
, vol.252
, pp. 7555-7567
-
-
Parham, P.1
Alpert, B.N.2
Orr, H.T.3
Strominger, J.L.4
-
238
-
-
84870522502
-
Gain of glycosylation in integrin alpha3 causes lung disease and nephrotic syndrome
-
Nicolaou N., Margadant C., Kevelam S.H., Lilien M.R., Oosterveld M.J., Kreft M., van Eerde A.M., Pfundt R., Terhal P.A., van der Zwaag B., Nikkels P.G., Sachs N., Goldschmeding R., Knoers N.V., Renkema K.Y., Sonnenberg A. Gain of glycosylation in integrin alpha3 causes lung disease and nephrotic syndrome. J. Clin. Invest. 2012, 122:4375-4387.
-
(2012)
J. Clin. Invest.
, vol.122
, pp. 4375-4387
-
-
Nicolaou, N.1
Margadant, C.2
Kevelam, S.H.3
Lilien, M.R.4
Oosterveld, M.J.5
Kreft, M.6
van Eerde, A.M.7
Pfundt, R.8
Terhal, P.A.9
van der Zwaag, B.10
Nikkels, P.G.11
Sachs, N.12
Goldschmeding, R.13
Knoers, N.V.14
Renkema, K.Y.15
Sonnenberg, A.16
-
239
-
-
0035929552
-
N-glycosylation and residues Asn805 and Asn890 are involved in the functional properties of type VI adenylyl cyclase
-
Wu G.C., Lai H.L., Lin Y.W., Chu Y.T., Chern Y. N-glycosylation and residues Asn805 and Asn890 are involved in the functional properties of type VI adenylyl cyclase. J. Biol. Chem. 2001, 276:35450-35457.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 35450-35457
-
-
Wu, G.C.1
Lai, H.L.2
Lin, Y.W.3
Chu, Y.T.4
Chern, Y.5
-
240
-
-
84880622367
-
N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2)
-
Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D. N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2). FEBS J. 2012.
-
(2012)
FEBS J.
-
-
Walker, A.K.1
Soo, K.Y.2
Levina, V.3
Talbo, G.H.4
Atkin, J.D.5
-
241
-
-
84857373175
-
Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5
-
Ohgomori T., Nanao T., Morita A., Ikekita M. Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5. Glycoconj. J. 2011, 29:47-55.
-
(2011)
Glycoconj. J.
, vol.29
, pp. 47-55
-
-
Ohgomori, T.1
Nanao, T.2
Morita, A.3
Ikekita, M.4
-
242
-
-
80255130597
-
Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity
-
Bence M., Sahin-Toth M. Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity. FEBS J. 2011, 278:4338-4350.
-
(2011)
FEBS J.
, vol.278
, pp. 4338-4350
-
-
Bence, M.1
Sahin-Toth, M.2
|