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Volumn 1803, Issue 6, 2010, Pages 684-693

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum

Author keywords

Carbohydrates; Endoplasmic reticulum; Molecular chaperones; Protein folding; Quality control

Indexed keywords

CALNEXIN; CALRETICULIN; CHAPERONE; GLYCOPROTEIN; LECTIN; OXIDOREDUCTASE; PROTEIN ERP57; UNCLASSIFIED DRUG;

EID: 77953024704     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.10.008     Document Type: Review
Times cited : (63)

References (145)
  • 1
    • 0015859467 scopus 로고
    • 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
  • 4
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • Frydman J., Erdjument-Bromage H., Tempst P., Hartl F.U. Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat. Struct. Biol. 1999, 6:697-705.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Hartl, F.U.4
  • 5
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum
    • Chen W., Helenius J., Braakman I., Helenius A. Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:6229-6233.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 6
    • 0002006297 scopus 로고
    • 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
  • 7
    • 0037459073 scopus 로고    scopus 로고
    • Protein modulators: multi-functional mediators of protein translocation across membranes.
    • Schnell D.J., Hebert D.N. Protein modulators: multi-functional mediators of protein translocation across membranes. Cell 2003, 112:491-505.
    • (2003) Cell , vol.112 , pp. 491-505
    • Schnell, D.J.1    Hebert, D.N.2
  • 8
    • 4644285228 scopus 로고    scopus 로고
    • Protein folding in the cell: reshaping the folding funnel.
    • Clark P.L. Protein folding in the cell: reshaping the folding funnel. Trends. Biochem. Sci. 2004, 29:527-534.
    • (2004) Trends. Biochem. Sci. , vol.29 , pp. 527-534
    • Clark, P.L.1
  • 9
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Fedorov A.N., Baldwin T.O. Cotranslational protein folding. J. Biol. Chem. 1997, 272:32715-32718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32715-32718
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 10
    • 0027491725 scopus 로고
    • Structural argument for N-terminal initiation of protein folding
    • Alexandrov N. Structural argument for N-terminal initiation of protein folding. Protein Sci. 1993, 2:1989-1991.
    • (1993) Protein Sci. , vol.2 , pp. 1989-1991
    • Alexandrov, N.1
  • 11
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J., Nimmesgern E., Ohtsuka K., Hartl F.-U. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 1994, 370:111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.-U.4
  • 12
    • 0021474773 scopus 로고
    • Protein translocation across the endoplasmic reticulum
    • Walter P., Gilmore R., Blobel G. Protein translocation across the endoplasmic reticulum. Cell 1984, 38:5-8.
    • (1984) Cell , vol.38 , pp. 5-8
    • Walter, P.1    Gilmore, R.2    Blobel, G.3
  • 13
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: a dynamic gateway at the ER membrane.
    • Johnson A.E., van Waes M.A. The translocon: a dynamic gateway at the ER membrane. Annu. Rev. Cell Dev. Biol. 1999, 15:799-842.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 799-842
    • Johnson, A.E.1    van Waes, M.A.2
  • 14
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport T.A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 2007, 450:663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 15
    • 0033998246 scopus 로고    scopus 로고
    • 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
  • 16
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion inot the endoplasmic reticulum
    • Shaw A.S., Rottier P.J.M., Rose J.K. Evidence for the loop model of signal-sequence insertion inot the endoplasmic reticulum. Proc. Natl. Acad. Acad. USA 1988, 85:7592-7596.
    • (1988) Proc. Natl. Acad. Acad. USA , vol.85 , pp. 7592-7596
    • Shaw, A.S.1    Rottier, P.J.M.2    Rose, J.K.3
  • 17
    • 0035951866 scopus 로고    scopus 로고
    • Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum
    • Chen X., VanValkenburgh C., Liang H., Fang H., Green N. Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum. J. Biol. Chem. 2001, 276:2411-2416.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2411-2416
    • Chen, X.1    VanValkenburgh, C.2    Liang, H.3    Fang, H.4    Green, N.5
  • 18
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R., Kurowski B., Johnson A.E., Hebert D.N. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell. 2003, 11:79-90.
    • (2003) Mol. Cell. , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 19
    • 23044516246 scopus 로고    scopus 로고
    • The cotranslational maturation of the type I membrane glycoprotein tyrosinase: the heat shock protein 70 system hands off to the lectin-based chaperone system
    • Wang N., Daniels R., Hebert D.N. The cotranslational maturation of the type I membrane glycoprotein tyrosinase: the heat shock protein 70 system hands off to the lectin-based chaperone system. Mol. Biol. Cell. 2005, 16:3740-3752.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 3740-3752
    • Wang, N.1    Daniels, R.2    Hebert, D.N.3
  • 20
    • 0035794608 scopus 로고    scopus 로고
    • Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor
    • Rehm A., Stern P., Ploegh H.L., Tortorella D. Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor. EMBO. J. 2001, 20:1573-1582.
    • (2001) EMBO. J. , vol.20 , pp. 1573-1582
    • Rehm, A.1    Stern, P.2    Ploegh, H.L.3    Tortorella, D.4
  • 21
    • 0034608884 scopus 로고    scopus 로고
    • The HIV-1 Env protein signal sequence retards its cleavage and down-regulates the glycoprotein folding.
    • Li Y., Luo L., Thomas D.Y., Kang C.Y. The HIV-1 Env protein signal sequence retards its cleavage and down-regulates the glycoprotein folding. Virology 2000, 272:417-428.
    • (2000) Virology , vol.272 , pp. 417-428
    • Li, Y.1    Luo, L.2    Thomas, D.Y.3    Kang, C.Y.4
  • 22
    • 0041528498 scopus 로고    scopus 로고
    • Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen
    • Rutkowski D.T., Ott C.M., Polansky J.R., Lingappa V.R. Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen. J. Biol. Chem. 2003, 278:30365-30372.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30365-30372
    • Rutkowski, D.T.1    Ott, C.M.2    Polansky, J.R.3    Lingappa, V.R.4
  • 23
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead C.A., McCormick P.J., Johnson A.E. Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 2004, 116:725-736.
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 24
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum.
    • Kowarik M., Kung S., Martoglio B., Helenius A. Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol. Cell. 2002, 10:769-778.
    • (2002) Mol. Cell. , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 25
    • 5144234840 scopus 로고    scopus 로고
    • Structure acquisition of the T1 domain of Kv1.3 during biogenesis
    • Kosolapov A., Tu L., Wang J., Deutsch C. Structure acquisition of the T1 domain of Kv1.3 during biogenesis. Neuron 2004, 44:295-307.
    • (2004) Neuron , vol.44 , pp. 295-307
    • Kosolapov, A.1    Tu, L.2    Wang, J.3    Deutsch, C.4
  • 26
    • 0012249596 scopus 로고    scopus 로고
    • Different conformations of nascent polypeptides during translocation across the ER membrane
    • Mingarro I., Nilsson I., Whitley P., von Heijne G. Different conformations of nascent polypeptides during translocation across the ER membrane. BMC Cell Biol. 2000, 1:3.
    • (2000) BMC Cell Biol. , vol.1 , pp. 3
    • Mingarro, I.1    Nilsson, I.2    Whitley, P.3    von Heijne, G.4
  • 27
    • 0029983258 scopus 로고    scopus 로고
    • A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain
    • Whitley P., Nilsson I., von Heijne G. A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain. J. Biol. Chem. 1996, 271:6241-6244.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6241-6244
    • Whitley, P.1    Nilsson, I.2    von Heijne, G.3
  • 28
    • 0021891884 scopus 로고
    • 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
  • 29
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 2004, 73:1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 30
    • 35748948975 scopus 로고    scopus 로고
    • 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
  • 31
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol. Cell 2003, 12:101-111.
    • (2003) Mol. Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 32
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada C., Kelleher D.J., Gilmore R. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 2009, 136:272-283.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 34
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion
    • Allen S., Naim H.Y., Bulleid N.J. Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion. J. Biol. Chem. 1995, 270:4797-4804.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 35
    • 0029953675 scopus 로고    scopus 로고
    • Competition between folding and glycosylation in the endoplasmic reticulum.
    • Holst B., Bruun A.W., Kielland-Brandt M.C., Winther J.R. Competition between folding and glycosylation in the endoplasmic reticulum. EMBO J. 1996, 15:3538-3546.
    • (1996) EMBO J. , vol.15 , pp. 3538-3546
    • Holst, B.1    Bruun, A.W.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 36
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • Imperiali B., Rickert K.W. Conformational implications of asparagine-linked glycosylation. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:97-101.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 97-101
    • Imperiali, B.1    Rickert, K.W.2
  • 37
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali B., O'Connor S.E. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 1999, 3:643-649.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 38
    • 33644830238 scopus 로고    scopus 로고
    • N-linked oligosaccharides as outfitters for glycoprotein folding, form and function
    • Mitra N., Sinha S., Ramya T.N., Surolia A. N-linked oligosaccharides as outfitters for glycoprotein folding, form and function. Trends Biochem. Sci. 2006, 31:156-163.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 156-163
    • Mitra, N.1    Sinha, S.2    Ramya, T.N.3    Surolia, A.4
  • 39
    • 0036854512 scopus 로고    scopus 로고
    • Chaperone-like functions of high-mannose type and complex-type N-glycans and their molecular basis
    • Jitsuhara Y., Toyoda T., Itai T., Yamaguchi H. Chaperone-like functions of high-mannose type and complex-type N-glycans and their molecular basis. J. Biochem. 2002, 132:803-811.
    • (2002) J. Biochem. , vol.132 , pp. 803-811
    • Jitsuhara, Y.1    Toyoda, T.2    Itai, T.3    Yamaguchi, H.4
  • 41
    • 0037934610 scopus 로고    scopus 로고
    • The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment
    • Bosques C.J., Imperiali B. The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:7593-7598.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7593-7598
    • Bosques, C.J.1    Imperiali, B.2
  • 42
    • 0032742816 scopus 로고    scopus 로고
    • Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis
    • Kundra R., Kornfeld S. Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis. J. Biol. Chem. 1999, 274:31039-31046.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31039-31046
    • Kundra, R.1    Kornfeld, S.2
  • 45
    • 62549107841 scopus 로고    scopus 로고
    • The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability
    • Hanson S.R., Culyba E.K., Hsu T.L., Wong C.H., Kelly J.W., Powers E.T. The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:3131-3136.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 3131-3136
    • Hanson, S.R.1    Culyba, E.K.2    Hsu, T.L.3    Wong, C.H.4    Kelly, J.W.5    Powers, E.T.6
  • 47
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags
    • Hebert D.N., Garman S.C., Molinari M. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 2005, 15:364-370.
    • (2005) Trends Cell Biol. , vol.15 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 48
    • 22544467505 scopus 로고    scopus 로고
    • More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle
    • Deprez P., Gautschi M., Helenius A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol. Cell. 2005, 19:183-195.
    • (2005) Mol. Cell. , vol.19 , pp. 183-195
    • Deprez, P.1    Gautschi, M.2    Helenius, A.3
  • 49
    • 0018786795 scopus 로고
    • Synthesis and processing of protein-linked oligosaccharides in vivo
    • Hubbard S.C., Robbins P.W. Synthesis and processing of protein-linked oligosaccharides in vivo. J. Biol. Chem. 1979, 254:4568-4576.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4568-4576
    • Hubbard, S.C.1    Robbins, P.W.2
  • 50
    • 0035937852 scopus 로고    scopus 로고
    • Oligosaccharide-based information in the endoplasmic reticulum quality control and other biological systems.
    • Lehrman M.A. Oligosaccharide-based information in the endoplasmic reticulum quality control and other biological systems. J. Biol. Chem. 2001, 276:8623-8626.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8623-8626
    • Lehrman, M.A.1
  • 52
    • 24044432222 scopus 로고    scopus 로고
    • Large scale protein identification in intracellular aquaporin-2 vesicles from renal inner medullary collecting duct
    • Barile M., Pisitkun T., Yu M.J., Chou C.L., Verbalis M.J., Shen R.F., Knepper M.A. Large scale protein identification in intracellular aquaporin-2 vesicles from renal inner medullary collecting duct. Mol. Cell. Proteomics 2005, 4:1095-1106.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1095-1106
    • Barile, M.1    Pisitkun, T.2    Yu, M.J.3    Chou, C.L.4    Verbalis, M.J.5    Shen, R.F.6    Knepper, M.A.7
  • 53
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic Reticulum Glucosidase II, is Composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound non-catalytic HDEL-containing subunit
    • Trombetta E.S., Simons J.F., Helenius A. Endoplasmic Reticulum Glucosidase II, is Composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound non-catalytic HDEL-containing subunit. J. Biol. Chem 1996, 271:27509-27516.
    • (1996) J. Biol. Chem , vol.271 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 54
    • 33646591932 scopus 로고    scopus 로고
    • Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum
    • Wilkinson B.M., Purswani J., Stirling C.J. Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J. Biol. Chem. 2006, 281:6325-6333.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6325-6333
    • Wilkinson, B.M.1    Purswani, J.2    Stirling, C.J.3
  • 56
    • 0035807024 scopus 로고    scopus 로고
    • Quaternary and domain structure of glycoprotein processing glucosidase II
    • Trombetta E.S., Fleming K.G., Helenius A. Quaternary and domain structure of glycoprotein processing glucosidase II. Biochemistry 2001, 40:10717-10722.
    • (2001) Biochemistry , vol.40 , pp. 10717-10722
    • Trombetta, E.S.1    Fleming, K.G.2    Helenius, A.3
  • 57
    • 0025130561 scopus 로고
    • Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells
    • Kaushal G.P., Pastuszak I., Hatanaka K., Elbein A.D. Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells. J. Biol. Chem. 1990, 265:16271-16279.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16271-16279
    • Kaushal, G.P.1    Pastuszak, I.2    Hatanaka, K.3    Elbein, A.D.4
  • 58
    • 33845969527 scopus 로고    scopus 로고
    • Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans
    • Totani K., Ihara Y., Matsuo I., Ito Y. Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans. J. Biol. Chem. 2006, 281:31502-31508.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31502-31508
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Ito, Y.4
  • 59
    • 0030839727 scopus 로고    scopus 로고
    • The solution NMR, structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding
    • Petrescu A.J., Butters T.D., Reinkensmeier G., Petrescu S., Platt F.M., Dwek R.A., Wormald M.R. The solution NMR, structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 1997, 16:4302-4310.
    • (1997) EMBO J. , vol.16 , pp. 4302-4310
    • Petrescu, A.J.1    Butters, T.D.2    Reinkensmeier, G.3    Petrescu, S.4    Platt, F.M.5    Dwek, R.A.6    Wormald, M.R.7
  • 61
    • 0035838410 scopus 로고    scopus 로고
    • The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins
    • Munro S. The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins. Curr. Biol. 2001, 11:R499-501.
    • (2001) Curr. Biol. , vol.11
    • Munro, S.1
  • 62
    • 33744965386 scopus 로고    scopus 로고
    • The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition
    • Cruciat C.M., Hassler C., Niehrs C. The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition. J. Biol. Chem. 2006, 281:12986-12993.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12986-12993
    • Cruciat, C.M.1    Hassler, C.2    Niehrs, C.3
  • 63
    • 0019332339 scopus 로고
    • Substrate specificities of rat liver microsomal glucosidases which process glycoproteins.
    • Grinna L.S., Robbins P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 1980, 255:2255-2258.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2255-2258
    • Grinna, L.S.1    Robbins, P.W.2
  • 65
    • 67650162476 scopus 로고    scopus 로고
    • Genetic analysis of glucosidase II beta-subunit in trimming of high-mannose-type glycans
    • Watanabe T., Totani K., Matsuo I., Maruyama J., Kitamoto K., Ito Y. Genetic analysis of glucosidase II beta-subunit in trimming of high-mannose-type glycans. Glycobiology 2009, 19:834-840.
    • (2009) Glycobiology , vol.19 , pp. 834-840
    • Watanabe, T.1    Totani, K.2    Matsuo, I.3    Maruyama, J.4    Kitamoto, K.5    Ito, Y.6
  • 66
    • 0025863583 scopus 로고
    • From rat liver microsomes. Kinetic model for binding and hydrolysis
    • Alonso J.M., Santa-Cecilia A., Calvo P., Glucosidase II from rat liver microsomes. Kinetic model for binding and hydrolysis. Biochem. J. 1991, 278(Pt. 3):721-727.
    • (1991) Biochem. J. , vol.278 , Issue.PART. 3 , pp. 721-727
    • Alonso, J.M.1    Santa-Cecilia, A.2    Calvo, P.3    Glucosidase, I.I.4
  • 67
    • 0027295871 scopus 로고
    • 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
  • 68
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum
    • Hammond C., Braakman I., Helenius A. Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum. 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
  • 69
    • 0029024748 scopus 로고
    • 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
  • 70
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson J.R., Ora A., Nguyen Van P., Helenius A. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 1995, 6:1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Nguyen Van, P.3    Helenius, A.4
  • 71
    • 0029934119 scopus 로고    scopus 로고
    • 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
  • 72
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos A., Cohen-Doyle M.F., Peterson P.A., Jackson M.R., Williams D.B. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 1996, 15:1495-1506.
    • (1996) EMBO J. , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 73
    • 0031035644 scopus 로고    scopus 로고
    • Van, der, Wal, Fj, N.J. Bulleid, S. High, Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J.D. van, der, Wal, Fj, N.J. Bulleid, S. High, Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 1997, 275:86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1
  • 74
    • 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., 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
  • 75
  • 77
    • 0346727443 scopus 로고    scopus 로고
    • Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
    • Kapoor M., Ellgaard L., Gopalakrishnapai J., Schirra C., Gemma E., Oscarson S., Helenius A., Surolia A. Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry 2004, 43:97-106.
    • (2004) Biochemistry , vol.43 , pp. 97-106
    • Kapoor, M.1    Ellgaard, L.2    Gopalakrishnapai, J.3    Schirra, C.4    Gemma, E.5    Oscarson, S.6    Helenius, A.7    Surolia, A.8
  • 78
    • 0025788270 scopus 로고
    • Expression of calreticulin in Escherichia coli and identification of its Ca2+binding domains
    • Baksh S., Michalak M. Expression of calreticulin in Escherichia coli and identification of its Ca2+binding domains. J. Biol. Chem. 1991, 266:21458-21465.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21458-21465
    • Baksh, S.1    Michalak, M.2
  • 79
    • 0028205240 scopus 로고
    • Human, mouse, and rat calnexin cDNA cloning: idetnification of potential calcium binding motifs and gene localization to human chromosome 5
    • Tjoelker L.W., Seyfried C., Eddy R.L., Byers M.G. Human, mouse, and rat calnexin cDNA cloning: idetnification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry 1994, 33:3229-3236.
    • (1994) Biochemistry , vol.33 , pp. 3229-3236
    • Tjoelker, L.W.1    Seyfried, C.2    Eddy, R.L.3    Byers, M.G.4
  • 83
    • 0034646876 scopus 로고    scopus 로고
    • 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
  • 84
    • 0028076031 scopus 로고
    • Folding of VSV G protein: sequential interaction with BiP and calnexin
    • Hammond C., Helenius A. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 1994, 266:456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 85
    • 0029134004 scopus 로고
    • Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • Wada I., Imai S.-i., 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.-I.2    Kai, M.3    Sakane, F.4    Kanoh, H.5
  • 86
    • 0030667061 scopus 로고    scopus 로고
    • 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
  • 87
    • 0034724690 scopus 로고    scopus 로고
    • Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin
    • Danilczyk U.G., Cohen-Doyle M.F., Williams D.B. Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin. J. Biol. Chem. 2000, 275:13089-13097.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13089-13097
    • Danilczyk, U.G.1    Cohen-Doyle, M.F.2    Williams, D.B.3
  • 88
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott J.G., Oliver J.D., High S. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J. Biol. Chem. 1997, 272:13849-13855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 89
    • 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., High S. The transient association of ERp57 with N-glycosylated proteins is regulated by glucose trimming. Eur. J. Biochem. 1998, 256:51-59.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 51-59
    • Van der Wal, F.J.1    Oliver, J.D.2    High, S.3
  • 90
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Peaper D.R., Cresswell P. The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:10477-10482.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 91
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper D.R., Wearsch P.A., Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J. 2005, 24:3613-3623.
    • (2005) EMBO J. , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 92
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class I assembly and peptide binding
    • Peaper D.R., Cresswell P. Regulation of MHC class I assembly and peptide binding. Annu. Rev. Cell Dev. Biol. 2008, 24:343-368.
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 93
    • 33745861722 scopus 로고    scopus 로고
    • Conservation and diversity of the cellular disulfide bond formation pathways
    • Sevier C.S., Kaiser C.A. Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid. Redox Signal. 2006, 8:797-811.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 797-811
    • Sevier, C.S.1    Kaiser, C.A.2
  • 94
    • 0037147191 scopus 로고    scopus 로고
    • Coordinated nonvectorial folding in a newly synthesized multidomain protein
    • Jansens A., van Duijn E., Braakman I. Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science 2002, 298:2401-2403.
    • (2002) Science , vol.298 , pp. 2401-2403
    • Jansens, A.1    van Duijn, E.2    Braakman, I.3
  • 96
    • 0035890070 scopus 로고    scopus 로고
    • 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
  • 97
    • 11244319355 scopus 로고    scopus 로고
    • Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells
    • Jessop C.E., Bulleid N.J. Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. J. Biol. Chem. 2004, 279:55341-55347.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55341-55347
    • Jessop, C.E.1    Bulleid, N.J.2
  • 98
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop C.E., Chakravarthi S., Garbi N., Hammerling G.J., Lovell S., Bulleid N.J. ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J. 2007, 26:28-40.
    • (2007) EMBO J. , vol.26 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hammerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 99
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • Garbi N., Tanaka S., Momburg F., Hammerling G.J. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat. Immunol. 2006, 7:93-102.
    • (2006) Nat. Immunol. , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 100
    • 33646594461 scopus 로고    scopus 로고
    • 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
  • 101
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: versatility packed into a single fold
    • Appenzeller-Herzog C., Ellgaard L. The human PDI family: versatility packed into a single fold. Biochim. Biophys. Acta 2008, 1783:535-548.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 102
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo J.J., Parodi A.J. Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 2008, 283:10221-10225.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 103
    • 0029085605 scopus 로고
    • Retention of glucose units added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
    • Labriola C., Cazzulo J.J., Parodi A.J. Retention of glucose units added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum. J. Cell Biol. 1995, 130:771-779.
    • (1995) J. Cell Biol. , vol.130 , pp. 771-779
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 104
    • 0029126624 scopus 로고
    • 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
  • 105
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa M.C., Ferrero-Garcia M.A., Parodi A.J. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 1992, 31:97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 106
    • 0034689022 scopus 로고    scopus 로고
    • Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum
    • Trombetta E.S., Helenius A. Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum. J. Cell Biol. 2000, 148:1123-1129.
    • (2000) J. Cell Biol. , vol.148 , pp. 1123-1129
    • Trombetta, E.S.1    Helenius, A.2
  • 107
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan S., Xu Y., Brenner M.B. Retention of unassembled components of integral membrane proteins by calnexin. Science 1994, 263:387-390.
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 108
    • 0029934119 scopus 로고    scopus 로고
    • 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
  • 109
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin.
    • Oda Y., Hosokawa N., Wada I., Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 2003, 299:1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 110
    • 0034031279 scopus 로고    scopus 로고
    • Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase
    • Ritter C., Helenius A. Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase. Nat. Struct. Biol. 2000, 7:278-280.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 278-280
    • Ritter, C.1    Helenius, A.2
  • 111
    • 0037422614 scopus 로고    scopus 로고
    • UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates.
    • Caramelo J.J., Castro O.A., Alonso L.G., de Prat-Gay G., Parodi A.J. UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proc. Natl. Acad. Aca. Sci. U. S. A. 2003, 100:86-91.
    • (2003) Proc. Natl. Acad. Aca. Sci. U. S. A. , vol.100 , pp. 86-91
    • Caramelo, J.J.1    Castro, O.A.2    Alonso, L.G.3    de Prat-Gay, G.4    Parodi, A.J.5
  • 112
    • 0038779355 scopus 로고    scopus 로고
    • Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase
    • Taylor S.C., Thibault P., Tessier D.C., Bergeron J.J., Thomas D.Y. Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase. EMBO Rep. 2003, 4:405-411.
    • (2003) EMBO Rep. , vol.4 , pp. 405-411
    • Taylor, S.C.1    Thibault, P.2    Tessier, D.C.3    Bergeron, J.J.4    Thomas, D.Y.5
  • 113
    • 18944395787 scopus 로고    scopus 로고
    • 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
  • 114
    • 8544242762 scopus 로고    scopus 로고
    • 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
  • 115
    • 0742322956 scopus 로고    scopus 로고
    • The ER, protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation
    • Taylor S.C., Ferguson A.D., Bergeron J.J., Thomas D.Y. The ER, protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation. Nat. Struct. Mol. Biol. 2004, 11:128-134.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 128-134
    • Taylor, S.C.1    Ferguson, A.D.2    Bergeron, J.J.3    Thomas, D.Y.4
  • 116
    • 24044539202 scopus 로고    scopus 로고
    • Glycoprotein tertiary and quaternary structures are monitored by the same quality control mechanism
    • Keith N., Parodi A.J., Caramelo J.J. Glycoprotein tertiary and quaternary structures are monitored by the same quality control mechanism. J. Biol. Chem. 2005, 280:18138-18141.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18138-18141
    • Keith, N.1    Parodi, A.J.2    Caramelo, J.J.3
  • 117
    • 42449144739 scopus 로고    scopus 로고
    • A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein
    • Pearse B.R., Gabriel L., Wang N., Hebert D.N. A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein. J. Cell. Biol. 2008, 181:309-320.
    • (2008) J. Cell. Biol. , vol.181 , pp. 309-320
    • Pearse, B.R.1    Gabriel, L.2    Wang, N.3    Hebert, D.N.4
  • 118
    • 0242321979 scopus 로고    scopus 로고
    • The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain
    • Arnold S.M., Kaufman R.J. The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain. J. Biol. Chem. 2003, 278:43320-43328.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43320-43328
    • Arnold, S.M.1    Kaufman, R.J.2
  • 119
    • 0037743618 scopus 로고    scopus 로고
    • The UDP-glucose:Glycoprotein glucosyltransferase is organized in at least two tightly bound domains from yeast to mammals
    • Guerin M., Parodi A.J. The UDP-glucose:Glycoprotein glucosyltransferase is organized in at least two tightly bound domains from yeast to mammals. J. Biol. Chem. 2003, 278:20540-20546.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20540-20546
    • Guerin, M.1    Parodi, A.J.2
  • 120
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammlian, plant, fungal and trypanosomatid protozoa microsomal membranes
    • Trombetta S., Bosch M., Parodi A.J. Glucosylation of glycoproteins by mammlian, plant, fungal and trypanosomatid protozoa microsomal membranes. Biochemistry 1989, 28:8108-8116.
    • (1989) Biochemistry , vol.28 , pp. 8108-8116
    • Trombetta, S.1    Bosch, M.2    Parodi, A.J.3
  • 121
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
    • Wiggins C.A., Munro S. Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:7945-7950.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7945-7950
    • Wiggins, C.A.1    Munro, S.2
  • 122
    • 0034026441 scopus 로고    scopus 로고
    • Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme
    • Tessier D.C., Dignard D., Zapun A., Radominska-Pandya A., Parodi A.J., Bergeron J.J., Thomas D.Y. Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme. Glycobiology 2000, 10:403-412.
    • (2000) Glycobiology , vol.10 , pp. 403-412
    • Tessier, D.C.1    Dignard, D.2    Zapun, A.3    Radominska-Pandya, A.4    Parodi, A.J.5    Bergeron, J.J.6    Thomas, D.Y.7
  • 123
    • 0012784535 scopus 로고    scopus 로고
    • Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
    • Pedersen L.C., Dong J., Taniguchi F., Kitagawa H., Krahn J.M., Pedersen L.G., Sugahara K., Negishi M. Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. J. Biol. Chem. 2003, 278:14420-14428.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14420-14428
    • Pedersen, L.C.1    Dong, J.2    Taniguchi, F.3    Kitagawa, H.4    Krahn, J.M.5    Pedersen, L.G.6    Sugahara, K.7    Negishi, M.8
  • 124
    • 65249184983 scopus 로고    scopus 로고
    • The recognition motif of the glycoprotein-folding sensor enzyme, UDP-Glc: glycoprotein glucosyltransferase
    • Totani K., Ihara Y., Matsuo I., Tsujimoto T., Ito Y. The recognition motif of the glycoprotein-folding sensor enzyme, UDP-Glc: glycoprotein glucosyltransferase. Biochemistry 2009, 48:2933-2940.
    • (2009) Biochemistry , vol.48 , pp. 2933-2940
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Tsujimoto, T.4    Ito, Y.5
  • 125
    • 0034010855 scopus 로고    scopus 로고
    • Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity
    • Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J. Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity. Biochemistry 2000, 39:2149-2163.
    • (2000) Biochemistry , vol.39 , pp. 2149-2163
    • Arnold, S.M.1    Fessler, L.I.2    Fessler, J.H.3    Kaufman, R.J.4
  • 126
    • 0035845484 scopus 로고    scopus 로고
    • Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
    • Zuber C., Fan J.Y., Guhl B., Parodi A., Fessler J.H., Parker C., Roth J. Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:10710-10715.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10710-10715
    • Zuber, C.1    Fan, J.Y.2    Guhl, B.3    Parodi, A.4    Fessler, J.H.5    Parker, C.6    Roth, J.7
  • 128
    • 33847008259 scopus 로고    scopus 로고
    • The Sep15 protein family: roles in disulfide bond formation and quality control in the endoplasmic reticulum
    • Labunskyy V.M., Hatfield D.L., Gladyshev V.N. The Sep15 protein family: roles in disulfide bond formation and quality control in the endoplasmic reticulum. IUBMB Life 2007, 59:1-5.
    • (2007) IUBMB Life , vol.59 , pp. 1-5
    • Labunskyy, V.M.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 130
    • 27844454857 scopus 로고    scopus 로고
    • A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase
    • Labunskyy V.M., Ferguson A.D., Fomenko D.E., Chelliah Y., Hatfield D.L., Gladyshev V.N. A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase. J. Biol. Chem. 2005, 280:37839-37845.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37839-37845
    • Labunskyy, V.M.1    Ferguson, A.D.2    Fomenko, D.E.3    Chelliah, Y.4    Hatfield, D.L.5    Gladyshev, V.N.6
  • 132
    • 27944464985 scopus 로고    scopus 로고
    • 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
  • 133
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisae
    • Fernandez F.S., Trombetta S.E., Hellman U., Parodi A.J. Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisae. J. Biol. Chem. 1994, 269:30701-30706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30701-30706
    • Fernandez, F.S.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 134
    • 0035478934 scopus 로고    scopus 로고
    • Dissecting glycoprotein quality control in the secretory pathway.
    • Cabral C.M., Liu Y., Sifers R.N. Dissecting glycoprotein quality control in the secretory pathway. Tren. Biochem. Sci. 2001, 26:619-624.
    • (2001) Tren. Biochem. Sci. , vol.26 , pp. 619-624
    • Cabral, C.M.1    Liu, Y.2    Sifers, R.N.3
  • 135
    • 20444429745 scopus 로고    scopus 로고
    • A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins
    • Lederkremer G.Z., Glickman M.H. A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem. Sci. 2005, 30:297-303.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 297-303
    • Lederkremer, G.Z.1    Glickman, M.H.2
  • 136
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro R.G., Zhu Q., Bhoyroo V., Soling H.D. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 1996, 271:11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.D.4
  • 137
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperone calnexin and calreticulin
    • Vassilakos A., Michalak M., Lehrman M.A., Williams D.B. Oligosaccharide binding characteristics of the molecular chaperone 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
  • 138
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1?SEL1L ubiquitin ligase complex for ERAD
    • Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1?SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 2008, 10:272-282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 140
    • 66449136067 scopus 로고    scopus 로고
    • EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex.
    • Cormier J.H., Tamura T., Sunryd J.C., Hebert D.N. EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex. Mol. Cell 2009, 34:627-633.
    • (2009) Mol. Cell , vol.34 , pp. 627-633
    • Cormier, J.H.1    Tamura, T.2    Sunryd, J.C.3    Hebert, D.N.4
  • 141
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • Bhamidipati A., Denic V., Quan E.M., Weissman J.S. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol. Cell 2005, 19:741-751.
    • (2005) Mol. Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 142
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • Szathmary R., Bielmann R., Nita-Lazar M., Burda P., Jakob C.A. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol. Cell 2005, 19:765-775.
    • (2005) Mol. Cell , vol.19 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 143
    • 57749083532 scopus 로고    scopus 로고
    • Defining the glycan destruction signal for endoplasmic reticulum-associated degradation
    • Quan E.M., Kamiya Y., Kamiya D., Denic V., Weibezahn J., Kato K., Weissman J.S. Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol. Cell 2008, 32:870-877.
    • (2008) Mol. Cell , vol.32 , pp. 870-877
    • Quan, E.M.1    Kamiya, Y.2    Kamiya, D.3    Denic, V.4    Weibezahn, J.5    Kato, K.6    Weissman, J.S.7
  • 144
    • 17644414638 scopus 로고    scopus 로고
    • Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation
    • Spear E.D., Ng D.T. Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation. J. Cell Biol. 2005, 169:73-82.
    • (2005) J. Cell Biol. , vol.169 , pp. 73-82
    • Spear, E.D.1    Ng, D.T.2
  • 145
    • 53749105805 scopus 로고    scopus 로고
    • Consequences of individual N-glycan deletions and of proteasomal inhibition on secretion of active BACE
    • Vanoni O., Paganetti P., Molinari M. Consequences of individual N-glycan deletions and of proteasomal inhibition on secretion of active BACE. Mol. Biol. Cell 2008, 19:4086-4098.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4086-4098
    • Vanoni, O.1    Paganetti, P.2    Molinari, M.3


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