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Volumn 245, Issue , 2005, Pages 91-121

Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57

Author keywords

Adhesion; Calcium homeostasis; Calnexin; Calreticulin; ERp57; Protein folding

Indexed keywords

CALNEXIN; CALRETICULIN; GLYCOPROTEIN; PROTEASOME; PROTEIN P57; CALCIUM ION; CHAPERONE; HEAT SHOCK PROTEIN; PDIA3 PROTEIN, HUMAN; PROTEIN DISULFIDE ISOMERASE;

EID: 23944438373     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(05)45004-4     Document Type: Review
Times cited : (133)

References (159)
  • 1
    • 0034810825 scopus 로고    scopus 로고
    • Endoplasmic reticulum retention and prolonged association of a von Willebrand's disease-causing von Willebrand factor variant with ERp57 and calnexin
    • Allen S., Goodeve A.C., Peake I.R., and Daly M.E.N. Endoplasmic reticulum retention and prolonged association of a von Willebrand's disease-causing von Willebrand factor variant with ERp57 and calnexin Biochem. Biophys. Res. Commun. 280 2001 448 453
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 448-453
    • Allen, S.1    Goodeve, A.C.2    Peake, I.R.3    Daly, M.E.N.4
  • 2
    • 0037195869 scopus 로고    scopus 로고
    • Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria
    • Arnaudeau S., Frieden M., Nakamura K., Castelbou C., Michalak M., and Demaurex N. Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria J. Biol. Chem. 277 2002 46696 46705
    • (2002) J. Biol. Chem. , vol.277 , pp. 46696-46705
    • Arnaudeau, S.1    Frieden, M.2    Nakamura, K.3    Castelbou, C.4    Michalak, M.5    Demaurex, N.6
  • 3
    • 0028888054 scopus 로고
    • Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin
    • Arunachalam B., and Cresswell P. Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin J. Biol. Chem. 270 1995 2784 2790
    • (1995) J. Biol. Chem. , vol.270 , pp. 2784-2790
    • Arunachalam, B.1    Cresswell, P.2
  • 4
    • 0035133393 scopus 로고    scopus 로고
    • ER calcium and the functions of intracellular organelles
    • Ashby M.C., and Tepikin A.V. ER calcium and the functions of intracellular organelles Semin. Cell Dev. Biol. 12 2001 11 17
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 11-17
    • Ashby, M.C.1    Tepikin, A.V.2
  • 6
    • 0025788270 scopus 로고
    • Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains
    • Baksh S., and Michalak M. Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains J. Biol. Chem. 266 1991 21458 21465
    • (1991) J. Biol. Chem. , vol.266 , pp. 21458-21465
    • Baksh, S.1    Michalak, M.2
  • 7
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh S., Burns K., Andrin C., and Michalak M. Interaction of calreticulin with protein disulfide isomerase J. Biol. Chem. 270 1995 31338 31344
    • (1995) J. Biol. Chem. , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 8
    • 0036852135 scopus 로고    scopus 로고
    • Calcium-binding proteins and calcium-release channels in human maturing oocytes, pronuclear zygotes and early preimplantation embryos
    • Balakier H., Dziak E., Sojecki A., Librach C., Michalak M., and Opas M. Calcium-binding proteins and calcium-release channels in human maturing oocytes, pronuclear zygotes and early preimplantation embryos Hum. Reprod. 11 2002 2938 2947
    • (2002) Hum. Reprod. , vol.11 , pp. 2938-2947
    • Balakier, H.1    Dziak, E.2    Sojecki, A.3    Librach, C.4    Michalak, M.5    Opas, M.6
  • 10
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu S., Binder R.J., Ramalingam T., and Srivastava P.K. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin Immunity 14 2001 303 313
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 12
    • 0038710918 scopus 로고    scopus 로고
    • Identification of calreticulin as a nuclear matrix protein associated with human colon cancer
    • Brunagel G., Shah U., Schoen R.E., and Getzenberg R.H. Identification of calreticulin as a nuclear matrix protein associated with human colon cancer J. Cell. Biochem. 89 2003 238 243
    • (2003) J. Cell. Biochem. , vol.89 , pp. 238-243
    • Brunagel, G.1    Shah, U.2    Schoen, R.E.3    Getzenberg, R.H.4
  • 13
    • 1542345448 scopus 로고    scopus 로고
    • Cytoskeletal network in colon cancer: From genes to clinical application
    • Buda A., and Pignatelli M. Cytoskeletal network in colon cancer: From genes to clinical application Int. J. Biochem. Cell Biol. 36 2004 759 765
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 759-765
    • Buda, A.1    Pignatelli, M.2
  • 15
    • 0029156597 scopus 로고
    • Calreticulin inhibits repetitive intracellular Ca2+ waves
    • Camacho P., and Lechleiter J.D. Calreticulin inhibits repetitive intracellular Ca2+ waves Cell 82 1995 765 771
    • (1995) Cell , vol.82 , pp. 765-771
    • Camacho, P.1    Lechleiter, J.D.2
  • 16
    • 0028239790 scopus 로고
    • Class I histocompatibility molecule association with phosphorylated calnexin. Implications for rates of intracellular transport
    • Capps G.G., and Zuniga M.C. Class I histocompatibility molecule association with phosphorylated calnexin. Implications for rates of intracellular transport J. Biol. Chem. 269 1994 11634 11639
    • (1994) J. Biol. Chem. , vol.269 , pp. 11634-11639
    • Capps, G.G.1    Zuniga, M.C.2
  • 17
    • 0029073719 scopus 로고
    • Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class I-connecting peptide segment in calnexin association
    • Carreno B.M., Schreiber K.L., McKean D.J., Stroynowski I., and Hansen T.H. Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class I-connecting peptide segment in calnexin association J. Immunol. 154 1995 5173 5180
    • (1995) J. Immunol. , vol.154 , pp. 5173-5180
    • Carreno, B.M.1    Schreiber, K.L.2    McKean, D.J.3    Stroynowski, I.4    Hansen, T.H.5
  • 18
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen W., Helenius J., Braakman I., and Helenius A. Cotranslational folding and calnexin binding during glycoprotein synthesis Proc. Natl. Acad. Sci. USA 92 1995 6229 6233
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 23
    • 0034537052 scopus 로고    scopus 로고
    • Caveolae from canine airway smooth muscle contain the necessary components for a role in Ca(2+) handling
    • Darby P.J., Kwan C.Y., and Daniel E.E. Caveolae from canine airway smooth muscle contain the necessary components for a role in Ca(2+) handling Am. J. Physiol. Lung Cell Mol. Physiol. 279 2000 L1226 L1235
    • (2000) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.279
    • Darby, P.J.1    Kwan, C.Y.2    Daniel, E.E.3
  • 24
    • 0028240392 scopus 로고
    • Novel functions of calreticulin: Interaction with integrins and modulation of gene expression
    • Dedhar S. Novel functions of calreticulin: Interaction with integrins and modulation of gene expression Trends Biochem. Sci. 19 1994 269 271
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 269-271
    • Dedhar, S.1
  • 25
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning G.M., Anderson M.P., Amara J.F., Marshall J., Smith A.E., and Welsh M.J. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive Nature 358 1992 761 764
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 28
    • 0035253721 scopus 로고    scopus 로고
    • A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum
    • Diedrich G., Bangia N., Pan M., and Cresswell P. A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum J. Immunol. 166 2001 1703 1709
    • (2001) J. Immunol. , vol.166 , pp. 1703-1709
    • Diedrich, G.1    Bangia, N.2    Pan, M.3    Cresswell, P.4
  • 30
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • Drickamer K., and Taylor M.E. Evolving views of protein glycosylation Trends Biochem. Sci. 23 1998 321 324
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 321-324
    • Drickamer, K.1    Taylor, M.E.2
  • 31
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek R.A. Glycobiology: Toward understanding the function of sugars Chem. Rev. 96 1996 683 720
    • (1996) Chem. Rev. , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 32
    • 0141539469 scopus 로고    scopus 로고
    • Stress protein-polypeptide complexes acting as autoimmune triggers
    • Eggleton P. Stress protein-polypeptide complexes acting as autoimmune triggers Clin. Exp. Immunol. 134 2003 6 8
    • (2003) Clin. Exp. Immunol. , vol.134 , pp. 6-8
    • Eggleton, P.1
  • 33
    • 0030930662 scopus 로고    scopus 로고
    • Clinical relevance of calreticulin in systemic lupus erythematosus
    • Eggleton P., Reid K.B.M., Kishore U., and Sontheimer R.D. Clinical relevance of calreticulin in systemic lupus erythematosus Lupus 6 1997 564 571
    • (1997) Lupus , vol.6 , pp. 564-571
    • Eggleton, P.1    Reid, K.B.M.2    Kishore, U.3    Sontheimer, R.D.4
  • 34
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott J.G., Oliver J.D., and High S. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins J. Biol. Chem. 272 1997 13849 13855
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 35
    • 0033591411 scopus 로고    scopus 로고
    • Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion
    • Fadel M.P., Dziak E., Lo C.M., Ferrier J., Mesaeli N., Michalak M., and Opas M. Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion J. Biol. Chem. 274 1999 15085 15094
    • (1999) J. Biol. Chem. , vol.274 , pp. 15085-15094
    • Fadel, M.P.1    Dziak, E.2    Lo, C.M.3    Ferrier, J.4    Mesaeli, N.5    Michalak, M.6    Opas, M.7
  • 37
    • 0031843044 scopus 로고    scopus 로고
    • Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells
    • Fasolato C., Pizzo P., and Pozzan T. Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells Mol. Biol. Cell 9 1998 1513 1522
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1513-1522
    • Fasolato, C.1    Pizzo, P.2    Pozzan, T.3
  • 38
    • 0038756766 scopus 로고    scopus 로고
    • Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule
    • Ghiran I., Klickstein L.B., and Nicholson-Weller A. Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule J. Biol. Chem. 278 2003 21024 21031
    • (2003) J. Biol. Chem. , vol.278 , pp. 21024-21031
    • Ghiran, I.1    Klickstein, L.B.2    Nicholson-weller, A.3
  • 39
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea S., Orr A.W., Pallero M.A., Eggleton P., and Murphy-Ullrich J.E. Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin J. Biol. Chem. 275 2000 36358 36368
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-ullrich, J.E.5
  • 40
    • 0037020093 scopus 로고    scopus 로고
    • The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin
    • Goicoechea S., Pallero M.A., Eggleton P., Michalak M., and Murphy-Ullrich J.E. The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin J. Biol. Chem. 277 2002 37219 37228
    • (2002) J. Biol. Chem. , vol.277 , pp. 37219-37228
    • Goicoechea, S.1    Pallero, M.A.2    Eggleton, P.3    Michalak, M.4    Murphy-ullrich, J.E.5
  • 41
    • 0037184931 scopus 로고    scopus 로고
    • Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse
    • Guo L., Nakamura K., Lynch J., Opas M., Olson E.N., Agellon L.B., and Michalak M. Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse J. Biol. Chem. 277 2002 50776 50779
    • (2002) J. Biol. Chem. , vol.277 , pp. 50776-50779
    • Guo, L.1    Nakamura, K.2    Lynch, J.3    Opas, M.4    Olson, E.N.5    Agellon, L.B.6    Michalak, M.7
  • 42
    • 0034705048 scopus 로고    scopus 로고
    • Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism
    • Halaban R., Svedine S., Cheng E., Smicun Y., Aron R., and Hebert D.N. Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism Proc. Natl. Acad. Sci. USA 97 2000 5889 5894
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5889-5894
    • Halaban, R.1    Svedine, S.2    Cheng, E.3    Smicun, Y.4    Aron, R.5    Hebert, D.N.6
  • 43
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C., Braakman I., and Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control Proc. Natl. Acad. Sci. USA 91 1994 913 917
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 44
    • 0032886702 scopus 로고    scopus 로고
    • Calcium as a versatile second messenger in the control of gene expression
    • Hardingham G.E., and Bading H. Calcium as a versatile second messenger in the control of gene expression Microsc. Res. Tech. 46 1999 348 355
    • (1999) Microsc. Res. Tech. , vol.46 , pp. 348-355
    • Hardingham, G.E.1    Bading, H.2
  • 45
    • 0031019855 scopus 로고    scopus 로고
    • Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression
    • Hardingham G.E., Chawla S., and Johnson C.M. Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression Nature 385 1997 260 265
    • (1997) Nature , vol.385 , pp. 260-265
    • Hardingham, G.E.1    Chawla, S.2    Johnson, C.M.3
  • 46
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • Haynes C.M., Titus E.A., and Cooper A.A. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death Mol. Cell 15 2004 767 776
    • (2004) Mol. Cell , vol.15 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 47
    • 0028198111 scopus 로고
    • 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. 5 1994 253 265
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 253-265
    • Helenius, A.1
  • 48
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A., and Aebi M.N. Intracellular functions of N-linked glycans Science 291 2001 2364 2369
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.N.2
  • 49
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., and Aebi M. Roles of N-linked glycans in the endoplasmic reticulum Annu. Rev. Biochem. 73 2004 1019 1049
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 53
    • 0345327702 scopus 로고    scopus 로고
    • Presence of the inositol 1,4,5-triphosphate receptor isoforms in the nucleoplasm
    • Huh Y.H., and Yoo S.H. Presence of the inositol 1,4,5-triphosphate receptor isoforms in the nucleoplasm FEBS Lett. 555 2003 411 418
    • (2003) FEBS Lett. , vol.555 , pp. 411-418
    • Huh, Y.H.1    Yoo, S.H.2
  • 54
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • Hutzfeld M. The armadillo family of structural proteins Int. Rev. Cytol. 186 1999 179 224
    • (1999) Int. Rev. Cytol. , vol.186 , pp. 179-224
    • Hutzfeld, M.1
  • 55
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara Y., Cohen-Doyle M.F., Saito Y., and Williams D.B. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro Mol. Cell. 4 1999 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
  • 56
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson M.R., Cohen-Doyle M.F., Peterson P.A., and Williams D.B. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90) Science 263 1994 384 387
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 57
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • Jakob C.A., Burda P., Roth J., and Aebi M. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure J. Cell. Biol. 142 1998 1223 1233
    • (1998) J. Cell. Biol. , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 59
    • 0035122051 scopus 로고    scopus 로고
    • Increased sensitivity of melanocytes to oxidative stress and abnormal expression of tyrosinase-related protein in vitiligo
    • Jimbow K., Chen H., Park J.S., and Thomas P.D. Increased sensitivity of melanocytes to oxidative stress and abnormal expression of tyrosinase-related protein in vitiligo Br. J. Dermatol. 144 2001 55 65
    • (2001) Br. J. Dermatol. , vol.144 , pp. 55-65
    • Jimbow, K.1    Chen, H.2    Park, J.S.3    Thomas, P.D.4
  • 60
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: From the ER lumen to the extracellular space
    • Johnson S., Michalak M., Opas M., and Eggleton P. The ins and outs of calreticulin: From the ER lumen to the extracellular space Trends Cell Biol. 11 2001 122 129
    • (2001) Trends Cell Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 61
    • 0029099030 scopus 로고
    • Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes
    • Jouaville L.S., Ichas F., Holmuhamedov E.L., Camacho P., and Lechleiter J.D. Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes Nature 377 1995 438 441
    • (1995) Nature , vol.377 , pp. 438-441
    • Jouaville, L.S.1    Ichas, F.2    Holmuhamedov, E.L.3    Camacho, P.4    Lechleiter, J.D.5
  • 62
    • 0027993624 scopus 로고
    • Persistence of glucose residues on core oligosaccharides prevents association of TCR alpha and TCR beta proteins with calnexin and results specifically in accelerated degradation of nascent TCR alpha proteins within the endoplasmic reticulum
    • Kearse K.P., Williams D.B., and Singer A. Persistence of glucose residues on core oligosaccharides prevents association of TCR alpha and TCR beta proteins with calnexin and results specifically in accelerated degradation of nascent TCR alpha proteins within the endoplasmic reticulum EMBO J. 13 1994 3678 3686
    • (1994) EMBO J. , vol.13 , pp. 3678-3686
    • Kearse, K.P.1    Williams, D.B.2    Singer, A.3
  • 65
    • 0034830616 scopus 로고    scopus 로고
    • Adhesion of epithelial cells to fibronectin or collagen I induces alterations in gene expression via a protein kinase C-dependent mechanism
    • Lam K., Zhang L., Yamada K.M., and Lafrenie R.M. Adhesion of epithelial cells to fibronectin or collagen I induces alterations in gene expression via a protein kinase C-dependent mechanism J. Cell Physiol. 189 2001 79 90
    • (2001) J. Cell Physiol. , vol.189 , pp. 79-90
    • Lam, K.1    Zhang, L.2    Yamada, K.M.3    Lafrenie, R.M.4
  • 66
    • 0028341304 scopus 로고
    • Association between calnexin and a secretion-incompetent variant of human alpha 1-antitrypsin
    • Le A., Steiner J.L., Ferrell G.A., Shaker J.C., and Sifers R.N. Association between calnexin and a secretion-incompetent variant of human alpha 1-antitrypsin J. Biol. Chem. 269 1994 7514 7519
    • (1994) J. Biol. Chem. , vol.269 , pp. 7514-7519
    • Le, A.1    Steiner, J.L.2    Ferrell, G.A.3    Shaker, J.C.4    Sifers, R.N.5
  • 67
    • 0028180208 scopus 로고
    • The integrin chains beta 1 and alpha 6 associate with the chaperone calnexin prior to integrin assembly
    • Lenter M., and Vestweber D. The integrin chains beta 1 and alpha 6 associate with the chaperone calnexin prior to integrin assembly J. Biol. Chem. 269 1994 12263 12268
    • (1994) J. Biol. Chem. , vol.269 , pp. 12263-12268
    • Lenter, M.1    Vestweber, D.2
  • 68
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin-subunit-binding protein
    • Leung-Hagesteijn C.Y., Milankov K., Michalak M., Wilkins J., and Dedhar S. Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin-subunit-binding protein J. Cell Sci. 107 1994 589 600
    • (1994) J. Cell Sci. , vol.107 , pp. 589-600
    • Leung-hagesteijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 71
    • 0347753252 scopus 로고    scopus 로고
    • 2+-dependent redox modulation of SERCA 2b by ERp57
    • 2+-dependent redox modulation of SERCA 2b by ERp57 J. Cell Biol. 164 2004 35 46
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 72
    • 0028020123 scopus 로고
    • 2+ response to bradykinin and increases sensitivity to ionomycin in NG-108-15 cells
    • 2+ response to bradykinin and increases sensitivity to ionomycin in NG-108-15 cells J. Biol. Chem. 269 1994 28635 28639
    • (1994) J. Biol. Chem. , vol.269 , pp. 28635-28639
    • Liu, N.1    Fine, R.E.2    Simons, E.3    Johnson, R.J.4
  • 73
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • Liu Y., Choudhury P., Cabral C.M., and Sifers R.N. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome J. Biol. Chem. 274 1999 5861 5867
    • (1999) J. Biol. Chem. , vol.274 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 74
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains
    • Lockwich T.P., Liu X., Singh B.B., Jadlowiec J., Weiland S., and Ambudkar I.S. Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains J. Biol. Chem. 275 2000 11934 11942
    • (2000) J. Biol. Chem. , vol.275 , pp. 11934-11942
    • Lockwich, T.P.1    Liu, X.2    Singh, B.B.3    Jadlowiec, J.4    Weiland, S.5    Ambudkar, I.S.6
  • 75
    • 0035834716 scopus 로고    scopus 로고
    • Stabilization of cortical actin induces internalization of Trp3-associated caveolar Ca2+ signaling complex and loss of Ca2+ influx without disruption of Trp3-IP3R association
    • Lockwich T.P., Singh B.B., Liu X., and Ambudkar I.S. Stabilization of cortical actin induces internalization of Trp3-associated caveolar Ca2+ signaling complex and loss of Ca2+ influx without disruption of Trp3-IP3R association J. Biol. Chem. 276 2001 42401 42408
    • (2001) J. Biol. Chem. , vol.276 , pp. 42401-42408
    • Lockwich, T.P.1    Singh, B.B.2    Liu, X.3    Ambudkar, I.S.4
  • 76
    • 0021280849 scopus 로고
    • Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex
    • Lodish H.F., and Kong N. Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex J. Cell Biol. 98 1984 1720 1729
    • (1984) J. Cell Biol. , vol.98 , pp. 1720-1729
    • Lodish, H.F.1    Kong, N.2
  • 78
    • 0031925211 scopus 로고    scopus 로고
    • The role of calnexin in NK-target cell interaction
    • Malyguine A.M., Scott J.E., and Dawson J.R. The role of calnexin in NK-target cell interaction Immunol. Lett. 61 1998 67 71
    • (1998) Immunol. Lett. , vol.61 , pp. 67-71
    • Malyguine, A.M.1    Scott, J.E.2    Dawson, J.R.3
  • 79
    • 0027304377 scopus 로고
    • Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90)
    • Margolese L., Waneck G.L., Suzuki C.K., Degen E., Flavell R.A., and Williams D.B. Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90) J. Biol. Chem. 268 1993 17959 17966
    • (1993) J. Biol. Chem. , vol.268 , pp. 17959-17966
    • Margolese, L.1    Waneck, G.L.2    Suzuki, C.K.3    Degen, E.4    Flavell, R.A.5    Williams, D.B.6
  • 80
    • 0036864199 scopus 로고    scopus 로고
    • Structure-function studies of the receptors for complement C1q
    • McGreal E., and Gasque P. Structure-function studies of the receptors for complement C1q Biochem. Soc. Trans 30 2001 1010 1014
    • (2001) Biochem. Soc. Trans , vol.30 , pp. 1010-1014
    • McGreal, E.1    Gasque, P.2
  • 81
    • 0032555788 scopus 로고    scopus 로고
    • 2+ stores has a key role in nonmuscle cell signaling and function
    • 2+ stores has a key role in nonmuscle cell signaling and function J. Cell Biol. 142 1998 1395 1398
    • (1998) J. Cell Biol. , vol.142 , pp. 1395-1398
    • Meldolesi, J.1    Pozzan, T.2
  • 82
    • 0032169935 scopus 로고    scopus 로고
    • Mitochondrial impairment as an early event in the process of apoptosis induced by glutathione depletion in neuronal cells: Relevance to Parkinson's disease
    • Merad-Boudia M., Nicole A., Santiard-Baron D., Saille C., and Ceballos-Picot I. Mitochondrial impairment as an early event in the process of apoptosis induced by glutathione depletion in neuronal cells: Relevance to Parkinson's disease Biochem. Pharmacol. 56 1998 645 655
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 645-655
    • Merad-boudia, M.1    Nicole, A.2    Santiard-baron, D.3    Saille, C.4    Ceballos-picot, I.5
  • 84
    • 1642546248 scopus 로고    scopus 로고
    • Impaired p53 expression, function, and nuclear localization in calreticulin-deficient cells
    • Mesaeli N., and Phillipson C. Impaired p53 expression, function, and nuclear localization in calreticulin-deficient cells Mol. Biol. Cell 15 2004 1862 1870
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1862-1870
    • Mesaeli, N.1    Phillipson, C.2
  • 86
  • 87
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum Cell Calcium 32 2002 269 278
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Parker, J.M.R.2    Opas, M.3
  • 88
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M., and Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells Nature 402 1999 90 93
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 89
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari M., Calanca V., Galli C., Lucca P., and Paganetti P. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle Science 299 2003 1397 1400
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 93
    • 0035803473 scopus 로고    scopus 로고
    • Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis
    • Muller-Taubenberger A., Lupas A.N., Li H., Ecke M., Simmeth E., and Gerisch G. Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis EMBO J. 20 2001 6772 6782
    • (2001) EMBO J. , vol.20 , pp. 6772-6782
    • Muller-taubenberger, A.1    Lupas, A.N.2    Li, H.3    Ecke, M.4    Simmeth, E.5    Gerisch, G.6
  • 94
    • 0035058769 scopus 로고    scopus 로고
    • The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state?
    • Murphy-Ullrich J.E. The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state? J. Clin. Invest. 107 2001 785 790
    • (2001) J. Clin. Invest. , vol.107 , pp. 785-790
    • Murphy-ullrich, J.E.1
  • 95
    • 0033152788 scopus 로고    scopus 로고
    • Calreticulin displays in vivo peptide-binding activity and can elicit CTL response against bound peptide
    • Nair S., Wearsch P.A., Mitchell D.A., Wassenberg J.J., Gilboa E., and Nicchitta C.V. Calreticulin displays in vivo peptide-binding activity and can elicit CTL response against bound peptide J. Immunol. 162 1999 6426 6432
    • (1999) J. Immunol. , vol.162 , pp. 6426-6432
    • Nair, S.1    Wearsch, P.A.2    Mitchell, D.A.3    Wassenberg, J.J.4    Gilboa, E.5    Nicchitta, C.V.6
  • 99
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef W.M., McCormick S.J., and Clark R.A. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase J. Biol. Chem. 270 1995 4741 4747
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 100
    • 0027957793 scopus 로고
    • A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily
    • Nigam S.K., Goldberg A.L., Ho S., Rohde M.F., Bush K.T., and Sherman M. A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily J. Biol. Chem. 269 1994 1744 1749
    • (1994) J. Biol. Chem. , vol.269 , pp. 1744-1749
    • Nigam, S.K.1    Goldberg, A.L.2    Ho, S.3    Rohde, M.F.4    Bush, K.T.5    Sherman, M.6
  • 101
    • 0033210414 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
    • Noiva R. Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum Semin. Cell Dev. Biol. 10 1999 481 493
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 481-493
    • Noiva, R.1
  • 102
    • 0030267033 scopus 로고    scopus 로고
    • Modulation of protein structure and function by asparagine-linked glycosylation
    • O'Connor S.E., and Imperiali B. Modulation of protein structure and function by asparagine-linked glycosylation Chem. Biol. 3 1996 803 812
    • (1996) Chem. Biol. , vol.3 , pp. 803-812
    • O'Connor, S.E.1    Imperiali, B.2
  • 103
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y., Hosokawa N., Wada I., and Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin Science 299 2003 1394 1397
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 104
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and cd91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden C.A., deCathelineau A., Hoffmann P.R., Bratton D., Ghebrehiwet B., Fadok V.A., and Henson P.M. C1q and mannose binding lectin engagement of cell surface calreticulin and cd91 initiates macropinocytosis and uptake of apoptotic cells J. Exp. Med. 194 2001 781 796
    • (2001) J. Exp. Med. , vol.194 , pp. 781-796
    • Ogden, C.A.1    Decathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 105
    • 0034680917 scopus 로고    scopus 로고
    • Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum
    • Okazaki Y., Ohno H., Takase K., Ochiai T., and Saito T. Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum J. Biol. Chem. 275 2000 35751 35758
    • (2000) J. Biol. Chem. , vol.275 , pp. 35751-35758
    • Okazaki, Y.1    Ohno, H.2    Takase, K.3    Ochiai, T.4    Saito, T.5
  • 107
    • 0037036434 scopus 로고    scopus 로고
    • Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent ERK activation
    • Orr A.W., Pallero M.A., and Murphy-Ullrich J.E. Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent ERK activation J. Biol. Chem. 277 2002 20453 20460
    • (2002) J. Biol. Chem. , vol.277 , pp. 20453-20460
    • Orr, A.W.1    Pallero, M.A.2    Murphy-ullrich, J.E.3
  • 109
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken A., and Moss B. Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin J. Biol. Chem. 271 1996 97 103
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 110
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou W.J., Cameron P.H., Thomas D.Y., and Bergeron J.J. Association of folding intermediates of glycoproteins with calnexin during protein maturation Nature 364 1993 771 776
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 111
    • 0037450789 scopus 로고    scopus 로고
    • Is all of the endoplasmic reticulum created equal? the effect of the heterogeneous distribution of endoplasmic reticulum Ca2+-handling protein
    • Papp S., Dziak E., Michalak M., and Opas M. Is all of the endoplasmic reticulum created equal? The effect of the heterogeneous distribution of endoplasmic reticulum Ca2+-handling protein J. Cell. Biol. 160 2003 475 479
    • (2003) J. Cell. Biol. , vol.160 , pp. 475-479
    • Papp, S.1    Dziak, E.2    Michalak, M.3    Opas, M.4
  • 112
    • 0029006125 scopus 로고
    • The calnexin homologue cnx1+ in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain
    • Parlati F., Dignard D., Bergeron J.J.M., and Thomas D.Y. The calnexin homologue cnx1+ in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain EMBO J. 14 1995 3064 3072
    • (1995) EMBO J. , vol.14 , pp. 3064-3072
    • Parlati, F.1    Dignard, D.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 113
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson J.R., Ora A., Van P.N., and Helenius A. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins Mol. Biol. Cell 6 1995 1173 1184
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 118
    • 0033215397 scopus 로고    scopus 로고
    • "kissin' cousins": Intimate plasma membrane-ER interactions underlie capacitative calcium entry
    • Putney J.W. Jr. "Kissin' cousins": Intimate plasma membrane-ER interactions underlie capacitative calcium entry Cell 99 1999 5 8
    • (1999) Cell , vol.99 , pp. 5-8
    • Putney Jr., J.W.1
  • 119
    • 0028221225 scopus 로고
    • Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum
    • Rajagopalan S., and Brenner M.B. Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum J. Exp. Med. 180 1994 407 412
    • (1994) J. Exp. Med. , vol.180 , pp. 407-412
    • Rajagopalan, S.1    Brenner, M.B.2
  • 120
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan S., Xu Y., and Brenner M.B. Retention of unassembled components of integral membrane proteins by calnexin Science 263 1994 387 390
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 121
    • 0029019816 scopus 로고
    • Enhanced expression of calreticulin in the nucleus of radioresistant squamos carcinoma cells in response to ionizing radiation
    • Ramsamooj P., Notario V., and Dritschilo A. Enhanced expression of calreticulin in the nucleus of radioresistant squamos carcinoma cells in response to ionizing radiation Cancer Res. 55 1995 3016 3021
    • (1995) Cancer Res. , vol.55 , pp. 3016-3021
    • Ramsamooj, P.1    Notario, V.2    Dritschilo, A.3
  • 123
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNAse with calnexin and calreticulin
    • Rodan A.R., Simons J.F., Trombetta E.S., and Helenius A. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNAse with calnexin and calreticulin EMBO J. 15 1996 6921 6930
    • (1996) EMBO J. , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 124
    • 0030964828 scopus 로고    scopus 로고
    • Nuclear localization of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors
    • Roderick H.L., Campbell A.K., and Llewellyn D.H. Nuclear localization of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors FEBS Lett. 405 1997 181 185
    • (1997) FEBS Lett. , vol.405 , pp. 181-185
    • Roderick, H.L.1    Campbell, A.K.2    Llewellyn, D.H.3
  • 125
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b
    • Roderick H.L., Lechleiter J.D., and Camacho P.N. Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b J. Cell Biol. 149 2000 1235 1248
    • (2000) J. Cell Biol. , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.N.3
  • 126
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits
    • Rojiani M.V., Finlay B.B., Gray V., and Dedhar S. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits Biochemistry 30 1991 9859 9866
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 128
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan B., Lehner P.J., Ortmann B., Spies T., and Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP Immunity 5 1996 103 114
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 129
    • 0030806695 scopus 로고    scopus 로고
    • Calcium signaling in the cell nucleus
    • Santella L., and Carafoli E. Calcium signaling in the cell nucleus FASEB J. 11 1997 1091 1109
    • (1997) FASEB J. , vol.11 , pp. 1091-1109
    • Santella, L.1    Carafoli, E.2
  • 130
    • 0022368666 scopus 로고
    • Castanospermine inhibits glucosidase I and glycoprotein secretion in human hepatoma cells
    • Sasak V.W., Ordovas J.M., Elbein A.D., and Berninger R.W. Castanospermine inhibits glucosidase I and glycoprotein secretion in human hepatoma cells Biochem. J. 232 1985 759 766
    • (1985) Biochem. J. , vol.232 , pp. 759-766
    • Sasak, V.W.1    Ordovas, J.M.2    Elbein, A.D.3    Berninger, R.W.4
  • 131
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato S., Ward C.L., Krouse M.E., Wine J.J., and Kopito R.R. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation J. Biol. Chem. 271 1996 635 638
    • (1996) J. Biol. Chem. , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 132
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag J.D., Bergeron J.J., Li Y., Borisova S., Hahn M., Thomas D.Y., and Cygler M. The structure of calnexin, an ER chaperone involved in quality control of protein folding Mol. Cell 8 2001 633 644
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 133
    • 0029009565 scopus 로고
    • MHC class I expression and transport in a calnexin-deficient cell line
    • Scott J.E., and Dawson J.R. MHC class I expression and transport in a calnexin-deficient cell line J. Immunol. 155 1995 143 148
    • (1995) J. Immunol. , vol.155 , pp. 143-148
    • Scott, J.E.1    Dawson, J.R.2
  • 134
    • 0033984014 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor associated with focal contact cytoskeletal proteins
    • Sugiyama T., Matsuda Y., and Mikoshiba K. Inositol 1,4,5-trisphosphate receptor associated with focal contact cytoskeletal proteins FEBS Lett. 466 2000 29 34
    • (2000) FEBS Lett. , vol.466 , pp. 29-34
    • Sugiyama, T.1    Matsuda, Y.2    Mikoshiba, K.3
  • 135
    • 0037082133 scopus 로고    scopus 로고
    • Chaperone interactions of the metalloproteinase meprin a in the secretory or proteasomal-degradative pathway
    • Tsukuba T., Kadowaki T., Hengst J.A., and Bond J.S. Chaperone interactions of the metalloproteinase meprin A in the secretory or proteasomal-degradative pathway Arch. Biochem. Biophys. 397 2002 191 198
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 191-198
    • Tsukuba, T.1    Kadowaki, T.2    Hengst, J.A.3    Bond, J.S.4
  • 137
    • 0032529113 scopus 로고    scopus 로고
    • The transient association of ERp57 with N-glycosylated proteins is regulated by glucose trimming
    • Van der Wal F.J., Oliver J.D., and High S. The transient association of ERp57 with N-glycosylated proteins is regulated by glucose trimming Eur. J. Biochem. 256 1998 51 59
    • (1998) Eur. J. Biochem. , vol.256 , pp. 51-59
    • Van Der Wal, F.J.1    Oliver, J.D.2    High, S.3
  • 138
    • 0036785571 scopus 로고    scopus 로고
    • Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: Calreticulin and CD91 as a common collectin receptor complex
    • Vandivier R.W., Ogden C.A., Fadok V.A., Hoffmann P.R., Brown K.K., Botto M., Walport M.J., Fisher J.H., Henson P.M., and Greene K.E. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: Calreticulin and CD91 as a common collectin receptor complex J. Immunol. 169 2002 3978 3986
    • (2002) J. Immunol. , vol.169 , pp. 3978-3986
    • Vandivier, R.W.1    Ogden, C.A.2    Fadok, V.A.3    Hoffmann, P.R.4    Brown, K.K.5    Botto, M.6    Walport, M.J.7    Fisher, J.H.8    Henson, P.M.9    Greene, K.E.10
  • 139
    • 0029993522 scopus 로고    scopus 로고
    • Calnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes
    • van Leeuwen J.E., and Kearse K.P. Calnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes J. Biol. Chem. 271 1996 9660 9665
    • (1996) J. Biol. Chem. , vol.271 , pp. 9660-9665
    • Van Leeuwen, J.E.1    Kearse, K.P.2
  • 140
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos A., Michalak M., Lehrman M.A., and Williams D.B. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin Biochemistry 37 1998 3480 3490
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 141
  • 142
    • 0035896560 scopus 로고    scopus 로고
    • Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr14) via activation of p38 mitogen-activated protein kinase and c-Src kinase - Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress
    • Volonté D., Galbiati F., Pestell R.G., and Lisanti M.P. Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr14) via activation of p38 mitogen-activated protein kinase and c-Src kinase - Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress J. Biol. Chem. 276 2001 8094 8103
    • (2001) J. Biol. Chem. , vol.276 , pp. 8094-8103
    • Volonté, D.1    Galbiati, F.2    Pestell, R.G.3    Lisanti, M.P.4
  • 145
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware F.E., Vassilakos A., Peterson P.A., Jackson M.R., Lehrman M.A., and Williams D.B. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins J. Biol. Chem. 270 1995 4697 4704
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697-4704
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 146
    • 0344507516 scopus 로고    scopus 로고
    • A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling
    • Wei Y., Yang X.W., Liu Q.M., Wilkins J.A., and Chapman H.A. A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling J. Cell Biol. 144 1999 1285 1294
    • (1999) J. Cell Biol. , vol.144 , pp. 1285-1294
    • Wei, Y.1    Yang, X.W.2    Liu, Q.M.3    Wilkins, J.A.4    Chapman, H.A.5
  • 147
    • 2142804719 scopus 로고    scopus 로고
    • Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic
    • Westphal V., Xiao M., Kwok P.Y., and Freeze H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic Hum. Mutat. 22 2003 420 421
    • (2003) Hum. Mutat. , vol.22 , pp. 420-421
    • Westphal, V.1    Xiao, M.2    Kwok, P.Y.3    Freeze, H.H.4
  • 148
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White T.K., Zhu Q., and Tanzer M.L. Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading J. Biol. Chem. 270 1995 15926 15929
    • (1995) J. Biol. Chem. , vol.270 , pp. 15926-15929
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 149
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: Glycan presentation and protein-fold stability
    • Wormald M.R., and Dwek R.A. Glycoproteins: Glycan presentation and protein-fold stability Structure Fold Des. 7 1999 R155 R160
    • (1999) Structure Fold Des. , vol.7
    • Wormald, M.R.1    Dwek, R.A.2
  • 150
    • 0036462598 scopus 로고    scopus 로고
    • Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling
    • Wormald M.R., Petrescu A.J., Pao Y.L., Glithero A., Elliott T., and Dwek R.A. Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling Chem. Rev. 102 2002 371 386
    • (2002) Chem. Rev. , vol.102 , pp. 371-386
    • Wormald, M.R.1    Petrescu, A.J.2    Pao, Y.L.3    Glithero, A.4    Elliott, T.5    Dwek, R.A.6
  • 153
    • 0031559803 scopus 로고    scopus 로고
    • The expression of the molecular chaperone calnexin is decreased in cancer cells grown as colonies compared to monolayer
    • Yeates L.C., and Powis G. The expression of the molecular chaperone calnexin is decreased in cancer cells grown as colonies compared to monolayer Biochem. Biophys. Res. Commun. 238 1997 66 70
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 66-70
    • Yeates, L.C.1    Powis, G.2
  • 154
  • 155
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun A., Petrescu S.M., Rudd P.M., Dwek R.A., Thomas D.Y., and Bergeron J.J. Conformation-independent binding of monoglucosylated ribonuclease B to calnexin Cell 88 1997 29 38
    • (1997) Cell , vol.88 , pp. 29-38
    • Zapun, A.1    Petrescu, S.M.2    Rudd, P.M.3    Dwek, R.A.4    Thomas, D.Y.5    Bergeron, J.J.6
  • 156
    • 0032513212 scopus 로고    scopus 로고
    • 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., and Thomas D.Y. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57 J. Biol. Chem. 273 1998 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
  • 157
    • 0028906481 scopus 로고
    • Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
    • Zhang Q., Tector M., and Salter R.D. Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules J. Biol. Chem. 270 1995 3944 3948
    • (1995) J. Biol. Chem. , vol.270 , pp. 3944-3948
    • Zhang, Q.1    Tector, M.2    Salter, R.D.3


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