메뉴 건너뛰기




Volumn 95, Issue , 2014, Pages 35-62

Proinsulin entry and transit through the endoplasmic reticulum in pancreatic beta cells

Author keywords

Diabetes; Endoplasmic reticulum; Pancreatic beta cells; Preproinsulin; Proinsulin; Protein folding; Protein translocation

Indexed keywords

INSULIN; PREPROINSULIN; PROINSULIN; PROTEIN PRECURSOR; SIGNAL PEPTIDE;

EID: 84894046601     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-800174-5.00002-8     Document Type: Chapter
Times cited : (71)

References (147)
  • 3
    • 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. Biochimica et Biophysica Acta 2008, 1783(4):535-548.
    • (2008) Biochimica et Biophysica Acta , vol.1783 , Issue.4 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 4
    • 1942489824 scopus 로고    scopus 로고
    • Endoplasmic reticulum export site formation and function in dendrites
    • Aridor M., Guzik A.K., Bielli A., Fish K.N. Endoplasmic reticulum export site formation and function in dendrites. The Journal of Neuroscience 2004, 24(15):3770-3776.
    • (2004) The Journal of Neuroscience , vol.24 , Issue.15 , pp. 3770-3776
    • Aridor, M.1    Guzik, A.K.2    Bielli, A.3    Fish, K.N.4
  • 5
    • 0026693483 scopus 로고
    • A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase
    • Bailyes E.M., Shennan K.I., Seal A.J., Smeekens S.P., Steiner D.F., Hutton J.C., et al. A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase. The Biochemical Journal 1992, 285(2):391-394.
    • (1992) The Biochemical Journal , vol.285 , Issue.2 , pp. 391-394
    • Bailyes, E.M.1    Shennan, K.I.2    Seal, A.J.3    Smeekens, S.P.4    Steiner, D.F.5    Hutton, J.C.6
  • 6
    • 0029040080 scopus 로고
    • Differences between the catalytic properties of recombinant human PC2 and endogenous rat PC2
    • Bailyes E.M., Shennan K.I., Usac E.F., Arden S.D., Guest P.C., Docherty K., et al. Differences between the catalytic properties of recombinant human PC2 and endogenous rat PC2. The Biochemical Journal 1995, 309(2):587-594.
    • (1995) The Biochemical Journal , vol.309 , Issue.2 , pp. 587-594
    • Bailyes, E.M.1    Shennan, K.I.2    Usac, E.F.3    Arden, S.D.4    Guest, P.C.5    Docherty, K.6
  • 7
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4Å resolution. Science 2000, 289(5481):905-920.
    • (2000) Science , vol.289 , Issue.5481 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 9
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. The Journal of Cell Biology 1975, 67(3):835-851.
    • (1975) The Journal of Cell Biology , vol.67 , Issue.3 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 10
    • 77949449300 scopus 로고    scopus 로고
    • Further evidence that mutations in INS can be a rare cause of maturity-onset diabetes of the young (MODY)
    • Boesgaard T., Pruhova S., Andersson E., Cinek O., Obermannova B., Lauenborg J., et al. Further evidence that mutations in INS can be a rare cause of maturity-onset diabetes of the young (MODY). BMC Medical Genetics 2010, 11(1):42.
    • (2010) BMC Medical Genetics , vol.11 , Issue.1 , pp. 42
    • Boesgaard, T.1    Pruhova, S.2    Andersson, E.3    Cinek, O.4    Obermannova, B.5    Lauenborg, J.6
  • 11
    • 64549146740 scopus 로고    scopus 로고
    • Insulin gene mutations as cause of diabetes in children negative for five type 1 diabetes autoantibodies
    • Bonfanti R., Colombo C., Nocerino V., Massa O., Lampasona V., Iafusco D., et al. Insulin gene mutations as cause of diabetes in children negative for five type 1 diabetes autoantibodies. Diabetes Care 2009, 32(1):123-125.
    • (2009) Diabetes Care , vol.32 , Issue.1 , pp. 123-125
    • Bonfanti, R.1    Colombo, C.2    Nocerino, V.3    Massa, O.4    Lampasona, V.5    Iafusco, D.6
  • 12
    • 0028786868 scopus 로고
    • CDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: Characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase
    • Bourdi M., Demady D., Martin J.L., Jabbour S.K., Martin B.M., George J.W., et al. cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: Characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase. Archives of Biochemistry and Biophysics 1995, 323(2):397-403.
    • (1995) Archives of Biochemistry and Biophysics , vol.323 , Issue.2 , pp. 397-403
    • Bourdi, M.1    Demady, D.2    Martin, J.L.3    Jabbour, S.K.4    Martin, B.M.5    George, J.W.6
  • 16
    • 0032580247 scopus 로고    scopus 로고
    • Carboxypeptidase E is a sorting receptor for prohormones: Binding and kinetic studies
    • Cool D.R., Loh Y.P. Carboxypeptidase E is a sorting receptor for prohormones: Binding and kinetic studies. Molecular and Cellular Endocrinology 1998, 139(1-2):7-13.
    • (1998) Molecular and Cellular Endocrinology , vol.139 , Issue.1-2 , pp. 7-13
    • Cool, D.R.1    Loh, Y.P.2
  • 17
    • 0030976604 scopus 로고    scopus 로고
    • Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpefat mice
    • Cool D.R., Normant E., Shen F.-S., Chen H.-C., Pannell L., Zhang Y., et al. Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpefat mice. Cell 1997, 88(1):73-83.
    • (1997) Cell , vol.88 , Issue.1 , pp. 73-83
    • Cool, D.R.1    Normant, E.2    Shen, F.-S.3    Chen, H.-C.4    Pannell, L.5    Zhang, Y.6
  • 20
    • 0023655547 scopus 로고
    • The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing
    • Davidson H.W., Hutton J.C. The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing. The Biochemical Journal 1987, 245(2):575-582.
    • (1987) The Biochemical Journal , vol.245 , Issue.2 , pp. 575-582
    • Davidson, H.W.1    Hutton, J.C.2
  • 23
    • 0032977203 scopus 로고    scopus 로고
    • Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E based on comparative distribution studies in the rat central nervous system
    • Dong W., Fricker L.D., Day R. Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E based on comparative distribution studies in the rat central nervous system. Neuroscience 1999, 89(4):1301-1317.
    • (1999) Neuroscience , vol.89 , Issue.4 , pp. 1301-1317
    • Dong, W.1    Fricker, L.D.2    Day, R.3
  • 24
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen A.J.M., Nouwen N. Protein translocation across the bacterial cytoplasmic membrane. Annual Review of Biochemistry 2008, 77(1):643-667.
    • (2008) Annual Review of Biochemistry , vol.77 , Issue.1 , pp. 643-667
    • Driessen, A.J.M.1    Nouwen, N.2
  • 25
    • 24744439439 scopus 로고    scopus 로고
    • Zinc, ligand interactions modulate assembly and stability of the insulin hexamer
    • Dunn M. Zinc, ligand interactions modulate assembly and stability of the insulin hexamer. Biometals 2005, 18(4):295-303.
    • (2005) Biometals , vol.18 , Issue.4 , pp. 295-303
    • Dunn, M.1
  • 30
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L., Molinari M., Helenius A. Setting the standards: Quality control in the secretory pathway. Science 1999, 286(5446):1882-1888.
    • (1999) Science , vol.286 , Issue.5446 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 31
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard L., Ruddock L.W. The human protein disulphide isomerase family: Substrate interactions and functional properties. EMBO Reports 2005, 6(1):28-32.
    • (2005) EMBO Reports , vol.6 , Issue.1 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 32
    • 0020544575 scopus 로고
    • Cell-free processing and segregation of insulin precursors
    • Eskridge E., Shields D. Cell-free processing and segregation of insulin precursors. The Journal of Biological Chemistry 1983, 258(19):11487-11491.
    • (1983) The Journal of Biological Chemistry , vol.258 , Issue.19 , pp. 11487-11491
    • Eskridge, E.1    Shields, D.2
  • 33
    • 84862576004 scopus 로고    scopus 로고
    • Novel standards in the measurement of rat insulin granules combining electron microscopy, high-content image analysis and in silico modelling
    • Fava E., Dehghany J., Ouwendijk J., Muller A., Niederlein A., Verkade P., et al. Novel standards in the measurement of rat insulin granules combining electron microscopy, high-content image analysis and in silico modelling. Diabetologia 2012, 55(4):1013-1023.
    • (2012) Diabetologia , vol.55 , Issue.4 , pp. 1013-1023
    • Fava, E.1    Dehghany, J.2    Ouwendijk, J.3    Muller, A.4    Niederlein, A.5    Verkade, P.6
  • 35
    • 0025216609 scopus 로고
    • Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site
    • Fikes J.D., Barkocy-Gallagher G.A., Klapper D.G., Bassford P.J. Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site. Journal of Biological Chemistry 1990, 265(6):3417-3423.
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.6 , pp. 3417-3423
    • Fikes, J.D.1    Barkocy-Gallagher, G.A.2    Klapper, D.G.3    Bassford, P.J.4
  • 36
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annual Review of Biochemistry 2009, 78:477-513.
    • (2009) Annual Review of Biochemistry , vol.78 , pp. 477-513
    • Finley, D.1
  • 37
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn G.C., Pohl J., Flocco M.T., Rothman J.E. Peptide-binding specificity of the molecular chaperone BiP. Nature 1991, 353(6346):726-730. 10.1038/353726a0.
    • (1991) Nature , vol.353 , Issue.6346 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 38
  • 40
    • 0029825451 scopus 로고    scopus 로고
    • Carboxypeptidase E activity is deficient in mice with the fat mutation: Effect on peptide processing
    • Fricker L.D., Berman Y.L., Leiter E.H., Devi L.A. Carboxypeptidase E activity is deficient in mice with the fat mutation: Effect on peptide processing. Journal of Biological Chemistry 1996, 271(48):30619-30624.
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.48 , pp. 30619-30624
    • Fricker, L.D.1    Berman, Y.L.2    Leiter, E.H.3    Devi, L.A.4
  • 41
    • 0022519470 scopus 로고
    • Cloning and sequence analysis of cDNA for bovine carboxypeptidase E
    • Fricker L.D., Evans C.J., Esch F.S., Herbert E. Cloning and sequence analysis of cDNA for bovine carboxypeptidase E. Nature 1986, 323(6087):461-464.
    • (1986) Nature , vol.323 , Issue.6087 , pp. 461-464
    • Fricker, L.D.1    Evans, C.J.2    Esch, F.S.3    Herbert, E.4
  • 42
    • 0032488981 scopus 로고    scopus 로고
    • Incomplete processing of proinsulin to insulin accompanied by elevation of Des-31,32 proinsulin intermediates in islets of mice lacking active PC2
    • Furuta M., Carroll R., Martin S., Swift H.H., Ravazzola M., Orci L., et al. Incomplete processing of proinsulin to insulin accompanied by elevation of Des-31,32 proinsulin intermediates in islets of mice lacking active PC2. Journal of Biological Chemistry 1998, 273(6):3431-3437.
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3431-3437
    • Furuta, M.1    Carroll, R.2    Martin, S.3    Swift, H.H.4    Ravazzola, M.5    Orci, L.6
  • 43
    • 84875499653 scopus 로고    scopus 로고
    • The human protein disulfide isomerase gene family
    • Galligan J.J., Petersen D.R. The human protein disulfide isomerase gene family. Human Genomics 2012, 6:6.
    • (2012) Human Genomics , vol.6 , pp. 6
    • Galligan, J.J.1    Petersen, D.R.2
  • 45
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch L.M. Signal sequences. Biochemistry 1989, 28(3):923-930.
    • (1989) Biochemistry , vol.28 , Issue.3 , pp. 923-930
    • Gierasch, L.M.1
  • 46
    • 1542313960 scopus 로고    scopus 로고
    • Sec61p contributes to signal sequence orientation according to the positive-inside rule
    • Goder V., Junne T., Spiess M. Sec61p contributes to signal sequence orientation according to the positive-inside rule. Molecular Biology of the Cell 2004, 15(3):1470-1478.
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1470-1478
    • Goder, V.1    Junne, T.2    Spiess, M.3
  • 47
    • 84857218845 scopus 로고    scopus 로고
    • Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates
    • Grubb S., Guo L., Fisher E.A., Brodsky J.L. Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Molecular Biology of the Cell 2012, 23(4):520-532.
    • (2012) Molecular Biology of the Cell , vol.23 , Issue.4 , pp. 520-532
    • Grubb, S.1    Guo, L.2    Fisher, E.A.3    Brodsky, J.L.4
  • 48
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • Guerriero C.J., Brodsky J.L. The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiological Reviews 2012, 92(2):537-576.
    • (2012) Physiological Reviews , vol.92 , Issue.2 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 50
    • 0037148535 scopus 로고    scopus 로고
    • A new role for BiP: Closing the aqueous translocon pore during protein integration into the ER membrane
    • Haigh N.G., Johnson A.E. A new role for BiP: Closing the aqueous translocon pore during protein integration into the ER membrane. The Journal of Cell Biology 2002, 156(2):261-270.
    • (2002) The Journal of Cell Biology , vol.156 , Issue.2 , pp. 261-270
    • Haigh, N.G.1    Johnson, A.E.2
  • 51
    • 0025951092 scopus 로고
    • Structural domains and molecular lifestyles of insulin and its precursors in the pancreatic beta cell
    • Halban P.A. Structural domains and molecular lifestyles of insulin and its precursors in the pancreatic beta cell. Diabetologia 1991, 34(11):767-778.
    • (1991) Diabetologia , vol.34 , Issue.11 , pp. 767-778
    • Halban, P.A.1
  • 52
    • 0019311577 scopus 로고
    • Intracellular degradation of insulin stores by rat pancreatic islets in vitro. An alternative pathway for homeostasis of pancreatic insulin content
    • Halban P.A., Wollheim C.B. Intracellular degradation of insulin stores by rat pancreatic islets in vitro. An alternative pathway for homeostasis of pancreatic insulin content. Journal of Biological Chemistry 1980, 255(13):6003-6006.
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.13 , pp. 6003-6006
    • Halban, P.A.1    Wollheim, C.B.2
  • 53
    • 13844266603 scopus 로고    scopus 로고
    • The signal recognition particle and its interactions during protein targeting
    • Halic M., Beckmann R. The signal recognition particle and its interactions during protein targeting. Current Opinion in Structural Biology 2005, 15(1):116-125.
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.1 , pp. 116-125
    • Halic, M.1    Beckmann, R.2
  • 54
    • 77954872755 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response in an INS-1 pancreatic beta-cell line with inducible expression of a folding-deficient proinsulin
    • Hartley T., Siva M., Lai E., Teodoro T., Zhang L., Volchuk A. Endoplasmic reticulum stress response in an INS-1 pancreatic beta-cell line with inducible expression of a folding-deficient proinsulin. BMC Cell Biology 2010, 11(1):59.
    • (2010) BMC Cell Biology , vol.11 , Issue.1 , pp. 59
    • Hartley, T.1    Siva, M.2    Lai, E.3    Teodoro, T.4    Zhang, L.5    Volchuk, A.6
  • 56
    • 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. Physiological Reviews 2007, 87(4):1377-1408. 10.1152/physrev.00050.2006.
    • (2007) Physiological Reviews , vol.87 , Issue.4 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 57
  • 58
    • 0029133141 scopus 로고
    • Intracellular transport of proinsulin in pancreatic beta-cells. Structural maturation probed by disulfide accessibility
    • Huang X.F., Arvan P. Intracellular transport of proinsulin in pancreatic beta-cells. Structural maturation probed by disulfide accessibility. The Journal of Biological Chemistry 1995, 270(35):20417-20423.
    • (1995) The Journal of Biological Chemistry , vol.270 , Issue.35 , pp. 20417-20423
    • Huang, X.F.1    Arvan, P.2
  • 59
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley S.M., Helenius A. Protein oligomerization in the endoplasmic reticulum. Annual Review of Cell Biology 1989, 5:277-307.
    • (1989) Annual Review of Cell Biology , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 60
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A., Lodish H. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257(5076):1496-1502.
    • (1992) Science , vol.257 , Issue.5076 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.2    Lodish, H.3
  • 61
    • 0014118370 scopus 로고
    • Intracellular transport of secretory proteins in the pancreatic exocrine cell: I. Role of the peripheral elements of the Golgi complex
    • Jamieson J.D., Palade G.E. Intracellular transport of secretory proteins in the pancreatic exocrine cell: I. Role of the peripheral elements of the Golgi complex. The Journal of Cell Biology 1967, 34(2):577-596.
    • (1967) The Journal of Cell Biology , vol.34 , Issue.2 , pp. 577-596
    • Jamieson, J.D.1    Palade, G.E.2
  • 64
    • 0015887937 scopus 로고
    • Studies on the conversion of proinsulin to insulin: III. Studies in vitro with a crude secretion granule fraction isolated from rat Islets of Langerhans
    • Kemmler W., Steiner D.F., Borg J. Studies on the conversion of proinsulin to insulin: III. Studies in vitro with a crude secretion granule fraction isolated from rat Islets of Langerhans. Journal of Biological Chemistry 1973, 248(13):4544-4551.
    • (1973) Journal of Biological Chemistry , vol.248 , Issue.13 , pp. 4544-4551
    • Kemmler, W.1    Steiner, D.F.2    Borg, J.3
  • 65
    • 79959405694 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin-1-like beta (ero1l{beta}) regulates susceptibility to endoplasmic reticulum stress and is induced by insulin flux in {beta}-cells
    • Khoo C., Yang J., Rajpal G., Wang Y., Liu J., Arvan P., et al. Endoplasmic reticulum oxidoreductin-1-like beta (ero1l{beta}) regulates susceptibility to endoplasmic reticulum stress and is induced by insulin flux in {beta}-cells. Endocrinology 2011, 152(7):2599-2608.
    • (2011) Endocrinology , vol.152 , Issue.7 , pp. 2599-2608
    • Khoo, C.1    Yang, J.2    Rajpal, G.3    Wang, Y.4    Liu, J.5    Arvan, P.6
  • 66
    • 0024414469 scopus 로고
    • Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs
    • Kozak M. Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs. Molecular and Cellular Biology 1989, 9(11):5134-5142.
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.11 , pp. 5134-5142
    • Kozak, M.1
  • 67
    • 0026695156 scopus 로고
    • Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment
    • Kuliawat R., Arvan P. Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment. The Journal of Cell Biology 1992, 118(3):521-529.
    • (1992) The Journal of Cell Biology , vol.118 , Issue.3 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 68
    • 84863934536 scopus 로고    scopus 로고
    • Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation
    • Lakkaraju A.K.K., Thankappan R., Mary C., Garrison J.L., Taunton J., Strub K. Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation. Molecular Biology of the Cell 2012, 23(14):2712-2722.
    • (2012) Molecular Biology of the Cell , vol.23 , Issue.14 , pp. 2712-2722
    • Lakkaraju, A.K.K.1    Thankappan, R.2    Mary, C.3    Garrison, J.L.4    Taunton, J.5    Strub, K.6
  • 71
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous er translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao S., Lin J., Do H., Johnson A.E. Both lumenal and cytosolic gating of the aqueous er translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 1997, 90(1):31-41.
    • (1997) Cell , vol.90 , Issue.1 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 72
    • 78149445119 scopus 로고    scopus 로고
    • Mutant INS-gene induced diabetes of youth: Proinsulin cysteine residues impose dominant-negative inhibition on wild-type proinsulin transport
    • Liu M., Haataja L., Wright J., Wickramasinghe N.P., Hua Q.X., Phillips N.F., et al. Mutant INS-gene induced diabetes of youth: Proinsulin cysteine residues impose dominant-negative inhibition on wild-type proinsulin transport. PLoS One 2010, 5(10):e13333.
    • (2010) PLoS One , vol.5 , Issue.10
    • Liu, M.1    Haataja, L.2    Wright, J.3    Wickramasinghe, N.P.4    Hua, Q.X.5    Phillips, N.F.6
  • 76
    • 84859550168 scopus 로고    scopus 로고
    • Impaired cleavage of preproinsulin signal peptide linked to autosomal-dominant diabetes
    • Liu M., Lara-Lemus R., Shan S.-O., Wright J., Haataja L., Barbetti F., et al. Impaired cleavage of preproinsulin signal peptide linked to autosomal-dominant diabetes. Diabetes 2012, 61:828-837.
    • (2012) Diabetes , vol.61 , pp. 828-837
    • Liu, M.1    Lara-Lemus, R.2    Shan, S.-O.3    Wright, J.4    Haataja, L.5    Barbetti, F.6
  • 77
    • 17144365015 scopus 로고    scopus 로고
    • Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum
    • Liu M., Li Y., Cavener D., Arvan P. Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum. Journal of Biological Chemistry 2005, 280(14):13209-13212.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13209-13212
    • Liu, M.1    Li, Y.2    Cavener, D.3    Arvan, P.4
  • 79
    • 0023838784 scopus 로고
    • Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. A rate-limiting step in protein maturation and secretion
    • Lodish H.F. Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. A rate-limiting step in protein maturation and secretion. Journal of Biological Chemistry 1988, 263(5):2107-2110.
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.5 , pp. 2107-2110
    • Lodish, H.F.1
  • 80
    • 0028955427 scopus 로고
    • The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane
    • Matlack K.E.S., Walter P. The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane. Journal of Biological Chemistry 1995, 270(11):6170-6180.
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.11 , pp. 6170-6180
    • Matlack, K.E.S.1    Walter, P.2
  • 81
    • 77950348445 scopus 로고    scopus 로고
    • Insulin gene mutations resulting in early-onset diabetes: Marked differences in clinical presentation, metabolic status, and pathogenic effect through endoplasmic reticulum retention
    • Meur G., Simon A., Harun N., Virally M., Dechaume A., Bonnefond A., et al. Insulin gene mutations resulting in early-onset diabetes: Marked differences in clinical presentation, metabolic status, and pathogenic effect through endoplasmic reticulum retention. Diabetes 2010, 59(3):653-661.
    • (2010) Diabetes , vol.59 , Issue.3 , pp. 653-661
    • Meur, G.1    Simon, A.2    Harun, N.3    Virally, M.4    Dechaume, A.5    Bonnefond, A.6
  • 82
    • 33750580851 scopus 로고    scopus 로고
    • Co- and post-translational translocation through the protein-conducting channel: Analogous mechanisms at work?
    • Mitra K., Frank J., Driessen A. Co- and post-translational translocation through the protein-conducting channel: Analogous mechanisms at work?. Nature Structural & Molecular Biology 2006, 13(11):957-964. 10.1038/nsmb1166.
    • (2006) Nature Structural & Molecular Biology , vol.13 , Issue.11 , pp. 957-964
    • Mitra, K.1    Frank, J.2    Driessen, A.3
  • 83
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M., Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 1999, 402(6757):90-93.
    • (1999) Nature , vol.402 , Issue.6757 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 84
    • 77950642050 scopus 로고    scopus 로고
    • The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin
    • Moore P., Bernardi K.M., Tsai B. The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin. Molecular Biology of the Cell 2010, 21(7):1305-1313.
    • (2010) Molecular Biology of the Cell , vol.21 , Issue.7 , pp. 1305-1313
    • Moore, P.1    Bernardi, K.M.2    Tsai, B.3
  • 85
    • 0029040210 scopus 로고
    • Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity
    • Naggert J.K., Fricker L.D., Varlamov O., Nishina P.M., Rouille Y., Steiner D.F., et al. Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity. Nature Genetics 1995, 10(2):135-142.
    • (1995) Nature Genetics , vol.10 , Issue.2 , pp. 135-142
    • Naggert, J.K.1    Fricker, L.D.2    Varlamov, O.3    Nishina, P.M.4    Rouille, Y.5    Steiner, D.F.6
  • 87
    • 0025305255 scopus 로고
    • Truncations of a secretory protein define minimum lengths required for binding to signal recognition particle and translocation across the endoplasmic reticulum membrane
    • Okun M.M., Eskridge E.M., Shields D. Truncations of a secretory protein define minimum lengths required for binding to signal recognition particle and translocation across the endoplasmic reticulum membrane. Journal of Biological Chemistry 1990, 265(13):7478-7484.
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.13 , pp. 7478-7484
    • Okun, M.M.1    Eskridge, E.M.2    Shields, D.3
  • 88
    • 0026701014 scopus 로고
    • Translocation of preproinsulin across the endoplasmic reticulum membrane. The relationship between nascent polypeptide size and extent of signal recognition particle-mediated inhibition of protein synthesis
    • Okun M., Shields D. Translocation of preproinsulin across the endoplasmic reticulum membrane. The relationship between nascent polypeptide size and extent of signal recognition particle-mediated inhibition of protein synthesis. The Journal of Biological Chemistry 1992, 267(16):11476-11482.
    • (1992) The Journal of Biological Chemistry , vol.267 , Issue.16 , pp. 11476-11482
    • Okun, M.1    Shields, D.2
  • 89
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J.D., van der Wal F.J., Bulleid N.J., High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 1997, 275(5296):86-88.
    • (1997) Science , vol.275 , Issue.5296 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 90
    • 0022979193 scopus 로고
    • Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles
    • Orci L., Ravazzola M., Amherdt M., Madsen O., Perrelet A., Vassalli J.D., et al. Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles. The Journal of Cell Biology 1986, 103(6):2273-2281.
    • (1986) The Journal of Cell Biology , vol.103 , Issue.6 , pp. 2273-2281
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Perrelet, A.5    Vassalli, J.D.6
  • 91
    • 0022129515 scopus 로고
    • Direct identification of prohormone conversion site in insulin-secreting cells
    • Orci L., Ravazzola M., Amherdt M.N., Madsen O., Vassalli J.-D., Perrelet A. Direct identification of prohormone conversion site in insulin-secreting cells. Cell 1985, 42(2):671-681.
    • (1985) Cell , vol.42 , Issue.2 , pp. 671-681
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.N.3    Madsen, O.4    Vassalli, J.-D.5    Perrelet, A.6
  • 93
    • 0027980035 scopus 로고
    • Selection of functional signal peptide cleavage sites from a library of random sequences
    • Palzkill T., Le Q.Q., Wong A., Botstein D. Selection of functional signal peptide cleavage sites from a library of random sequences. Journal of Bacteriology 1994, 176(3):563-568.
    • (1994) Journal of Bacteriology , vol.176 , Issue.3 , pp. 563-568
    • Palzkill, T.1    Le, Q.Q.2    Wong, A.3    Botstein, D.4
  • 94
    • 73949154312 scopus 로고    scopus 로고
    • Mutant proinsulin proteins associated with neonatal diabetes are retained in the endoplasmic reticulum and not efficiently secreted
    • Park S.-Y., Ye H., Steiner D.F., Bell G.I. Mutant proinsulin proteins associated with neonatal diabetes are retained in the endoplasmic reticulum and not efficiently secreted. Biochemical and Biophysical Research Communications 2010, 391(3):1449-1454.
    • (2010) Biochemical and Biophysical Research Communications , vol.391 , Issue.3 , pp. 1449-1454
    • Park, S.-Y.1    Ye, H.2    Steiner, D.F.3    Bell, G.I.4
  • 95
    • 0025970881 scopus 로고
    • Topology of eukaryotic type II membrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain
    • Parks G.D., Lamb R.A. Topology of eukaryotic type II membrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain. Cell 1991, 64(4):777-787.
    • (1991) Cell , vol.64 , Issue.4 , pp. 777-787
    • Parks, G.D.1    Lamb, R.A.2
  • 97
    • 0031770876 scopus 로고    scopus 로고
    • Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane
    • Pilon M., Romisch K., Quach D., Schekman R. Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane. Molecular Biology of the Cell 1998, 9(12):3455-3473.
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.12 , pp. 3455-3473
    • Pilon, M.1    Romisch, K.2    Quach, D.3    Schekman, R.4
  • 98
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon M., Schekman R., Romisch K. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. The EMBO Journal 1997, 16(15):4540-4548.
    • (1997) The EMBO Journal , vol.16 , Issue.15 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Romisch, K.3
  • 99
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath K., Mothes W., Wilkinson B.M., Stirling C.J., Rapoport T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 1998, 94(6):795-807.
    • (1998) Cell , vol.94 , Issue.6 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 100
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper R.K., Bohmler S., Bordallo J., Sommer T., Wolf D.H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 1997, 388(6645):891-895.
    • (1997) Nature , vol.388 , Issue.6645 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 101
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A., Gilbert H.F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. Journal of Biological Chemistry 1994, 269(10):7764-7771.
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 102
    • 0025786795 scopus 로고
    • Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers
    • Quinn D., Orci L., Ravazzola M., Moore H. Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers. The Journal of Cell Biology 1991, 113(5):987-996.
    • (1991) The Journal of Cell Biology , vol.113 , Issue.5 , pp. 987-996
    • Quinn, D.1    Orci, L.2    Ravazzola, M.3    Moore, H.4
  • 104
    • 84855289267 scopus 로고    scopus 로고
    • Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells
    • Rajpal G., Schuiki I., Liu M., Volchuk A., Arvan P. Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells. Journal of Biological Chemistry 2012, 287(1):43-47.
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.1 , pp. 43-47
    • Rajpal, G.1    Schuiki, I.2    Liu, M.3    Volchuk, A.4    Arvan, P.5
  • 105
    • 77149179440 scopus 로고    scopus 로고
    • Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein
    • Rane N.S., Chakrabarti O., Feigenbaum L., Hegde R.S. Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein. The Journal of Cell Biology 2010, 188(4):515-526.
    • (2010) The Journal of Cell Biology , vol.188 , Issue.4 , pp. 515-526
    • Rane, N.S.1    Chakrabarti, O.2    Feigenbaum, L.3    Hegde, R.S.4
  • 106
    • 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(7170):663-669.
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 107
    • 0023257123 scopus 로고
    • Newly synthesized proinsulin/insulin and stored insulin are released from pancreatic B cells predominantly via a regulated, rather than a constitutive, pathway
    • Rhodes C.J., Halban P.A. Newly synthesized proinsulin/insulin and stored insulin are released from pancreatic B cells predominantly via a regulated, rather than a constitutive, pathway. The Journal of Cell Biology 1987, 105(1):145-153.
    • (1987) The Journal of Cell Biology , vol.105 , Issue.1 , pp. 145-153
    • Rhodes, C.J.1    Halban, P.A.2
  • 108
    • 0026475382 scopus 로고
    • Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing
    • Rhodes C.J., Lincoln B., Shoelson S.E. Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing. Journal of Biological Chemistry 1992, 267(32):22719-22727.
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.32 , pp. 22719-22727
    • Rhodes, C.J.1    Lincoln, B.2    Shoelson, S.E.3
  • 109
    • 84873670723 scopus 로고    scopus 로고
    • Regulation of insulin secretion in human pancreatic islets
    • Rorsman P., Braun M. Regulation of insulin secretion in human pancreatic islets. Annual Review of Physiology 2013, 75(1):155-179.
    • (2013) Annual Review of Physiology , vol.75 , Issue.1 , pp. 155-179
    • Rorsman, P.1    Braun, M.2
  • 110
    • 0042879951 scopus 로고    scopus 로고
    • Insulin granule dynamics in pancreatic beta cells
    • Rorsman P., Renstrom E. Insulin granule dynamics in pancreatic beta cells. Diabetologia 2003, 46(8):1029-1045.
    • (2003) Diabetologia , vol.46 , Issue.8 , pp. 1029-1045
    • Rorsman, P.1    Renstrom, E.2
  • 111
    • 79953752538 scopus 로고    scopus 로고
    • Molecular mechanism of co-translational protein targeting by the signal recognition particle
    • Saraogi I., Shan S.-O. Molecular mechanism of co-translational protein targeting by the signal recognition particle. Traffic 2011, 12(5):535-542.
    • (2011) Traffic , vol.12 , Issue.5 , pp. 535-542
    • Saraogi, I.1    Shan, S.-O.2
  • 112
    • 43549105167 scopus 로고    scopus 로고
    • The unfolded protein response: A pathway that links insulin demand with {beta}-cell failure and diabetes
    • Scheuner D., Kaufman R.J. The unfolded protein response: A pathway that links insulin demand with {beta}-cell failure and diabetes. Endocrine Reviews 2008, 29(3):317-333.
    • (2008) Endocrine Reviews , vol.29 , Issue.3 , pp. 317-333
    • Scheuner, D.1    Kaufman, R.J.2
  • 113
    • 22544444513 scopus 로고    scopus 로고
    • Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis
    • Scheuner D., Vander Mierde D., Song B., Flamez D., Creemers J.W., Tsukamoto K., et al. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Nature Medicine 2005, 11(7):757-764.
    • (2005) Nature Medicine , vol.11 , Issue.7 , pp. 757-764
    • Scheuner, D.1    Vander Mierde, D.2    Song, B.3    Flamez, D.4    Creemers, J.W.5    Tsukamoto, K.6
  • 114
    • 0028927425 scopus 로고
    • In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER
    • Schmitz A., Maintz M., Kehle T., Herzog V. In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER. The EMBO Journal 1995, 14(6):1091-1098.
    • (1995) The EMBO Journal , vol.14 , Issue.6 , pp. 1091-1098
    • Schmitz, A.1    Maintz, M.2    Kehle, T.3    Herzog, V.4
  • 115
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Antón L.C., Gibbs J., Norbury C.C., Yewdell J.W., Bennink J.R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000, 404(6779):770-774.
    • (2000) Nature , vol.404 , Issue.6779 , pp. 770-774
    • Schubert, U.1    Antón, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 116
    • 46249094620 scopus 로고    scopus 로고
    • Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins
    • Scott D.C., Schekman R. Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins. The Journal of Cell Biology 2008, 181(7):1095-1105.
    • (2008) The Journal of Cell Biology , vol.181 , Issue.7 , pp. 1095-1105
    • Scott, D.C.1    Schekman, R.2
  • 117
    • 77949754469 scopus 로고    scopus 로고
    • New insights into oxidative folding
    • Sevier C.S. New insights into oxidative folding. The Journal of Cell Biology 2010, 188(6):757-758.
    • (2010) The Journal of Cell Biology , vol.188 , Issue.6 , pp. 757-758
    • Sevier, C.S.1
  • 118
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide-bond formation and the Er redox environment by feedback regulation of Ero1
    • Sevier C.S., Qu H., Heldman N., Gross E., Fass D., Kaiser C.A. Modulation of cellular disulfide-bond formation and the Er redox environment by feedback regulation of Ero1. Cell 2007, 129(2):333-344.
    • (2007) Cell , vol.129 , Issue.2 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 119
    • 84455178968 scopus 로고    scopus 로고
    • A calmodulin-dependent translocation pathway for small secretory proteins
    • Shao S., Hegde R.S. A calmodulin-dependent translocation pathway for small secretory proteins. Cell 2011, 147(7):1576-1588.
    • (2011) Cell , vol.147 , Issue.7 , pp. 1576-1588
    • Shao, S.1    Hegde, R.S.2
  • 120
    • 77951191473 scopus 로고    scopus 로고
    • Contribution of residue B5 to the folding and function of insulin and IGF-I: Constraints and fine-tuning in the evolution of a protein family
    • Sohma Y., Hua Q.X., Liu M., Phillips N.B., Hu S.Q., Whittaker J., et al. Contribution of residue B5 to the folding and function of insulin and IGF-I: Constraints and fine-tuning in the evolution of a protein family. The Journal of Biological Chemistry 2010, 285(7):5040-5055.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.7 , pp. 5040-5055
    • Sohma, Y.1    Hua, Q.X.2    Liu, M.3    Phillips, N.B.4    Hu, S.Q.5    Whittaker, J.6
  • 121
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro R.G. Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002, 12(4):43R-56R.
    • (2002) Glycobiology , vol.12 , Issue.4
    • Spiro, R.G.1
  • 122
    • 0023227779 scopus 로고
    • Stimulation of insulin secretion reveals heterogeneity of pancreatic B cells in vivo
    • Stefan Y., Meda P., Neufeld M., Orci L. Stimulation of insulin secretion reveals heterogeneity of pancreatic B cells in vivo. The Journal of Clinical Investigation 1987, 80(1):175-183.
    • (1987) The Journal of Clinical Investigation , vol.80 , Issue.1 , pp. 175-183
    • Stefan, Y.1    Meda, P.2    Neufeld, M.3    Orci, L.4
  • 123
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., Dobson C.M. Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. Journal of Molecular Medicine (Berlin) 2003, 81(11):678-699.
    • (2003) Journal of Molecular Medicine (Berlin) , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 127
    • 33751202431 scopus 로고    scopus 로고
    • ER targeting signals: More than meets the eye?
    • Swanton E., High S. ER targeting signals: More than meets the eye?. Cell 2006, 127(5):877-879.
    • (2006) Cell , vol.127 , Issue.5 , pp. 877-879
    • Swanton, E.1    High, S.2
  • 129
    • 0025372089 scopus 로고
    • The insulin A and B chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase
    • Tang J.G., Tsou C.L. The insulin A and B chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase. The Biochemical Journal 1990, 268(2):429-435.
    • (1990) The Biochemical Journal , vol.268 , Issue.2 , pp. 429-435
    • Tang, J.G.1    Tsou, C.L.2
  • 130
    • 0023683192 scopus 로고
    • Formation of native insulin from the scrambled molecule by protein disulphide-isomerase
    • Tang J.G., Wang C.C., Tsou C.L. Formation of native insulin from the scrambled molecule by protein disulphide-isomerase. The Biochemical Journal 1988, 255(2):451-455.
    • (1988) The Biochemical Journal , vol.255 , Issue.2 , pp. 451-455
    • Tang, J.G.1    Wang, C.C.2    Tsou, C.L.3
  • 132
    • 0030782386 scopus 로고    scopus 로고
    • β-Cell lines derived from transgenic Cpefat/Cpefat mice are defective in carboxypeptidase e and proinsulin processing
    • Varlamov O., Fricker L.D., Furukawa H., Steiner D.F., Langley S.H., Leiter E.H. β-Cell lines derived from transgenic Cpefat/Cpefat mice are defective in carboxypeptidase e and proinsulin processing. Endocrinology 1997, 138(11):4883-4892.
    • (1997) Endocrinology , vol.138 , Issue.11 , pp. 4883-4892
    • Varlamov, O.1    Fricker, L.D.2    Furukawa, H.3    Steiner, D.F.4    Langley, S.H.5    Leiter, E.H.6
  • 133
    • 0023036920 scopus 로고
    • Net N-C charge imbalance may be important for signal sequence function in bacteria
    • von Heijne G. Net N-C charge imbalance may be important for signal sequence function in bacteria. Journal of Molecular Biology 1986, 192(2):287-290.
    • (1986) Journal of Molecular Biology , vol.192 , Issue.2 , pp. 287-290
    • von Heijne, G.1
  • 134
    • 0032511879 scopus 로고    scopus 로고
    • Protein transport: Life and death of a signal peptide
    • von Heijne G. Protein transport: Life and death of a signal peptide. Nature 1998, 396(6707):111-113.
    • (1998) Nature , vol.396 , Issue.6707 , pp. 111-113
    • von Heijne, G.1
  • 135
    • 0030919649 scopus 로고    scopus 로고
    • Multiple determinants direct the orientation of signal'äìanchor proteins: The topogenic role of the hydrophobic signal domain
    • Wahlberg J.M., Spiess M. Multiple determinants direct the orientation of signal'äìanchor proteins: The topogenic role of the hydrophobic signal domain. The Journal of Cell Biology 1997, 137(3):555-562.
    • (1997) The Journal of Cell Biology , vol.137 , Issue.3 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 136
    • 84857620109 scopus 로고    scopus 로고
    • Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry
    • Walczak C.P., Bernardi K.M., Tsai B. Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry. Antioxidants & Redox Signaling 2012, 16(8):809-818.
    • (2012) Antioxidants & Redox Signaling , vol.16 , Issue.8 , pp. 809-818
    • Walczak, C.P.1    Bernardi, K.M.2    Tsai, B.3
  • 137
    • 0021016938 scopus 로고
    • Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe
    • Walter P., Blobel G. Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe. The Journal of Cell Biology 1983, 97(6):1693-1699.
    • (1983) The Journal of Cell Biology , vol.97 , Issue.6 , pp. 1693-1699
    • Walter, P.1    Blobel, G.2
  • 138
    • 79955773190 scopus 로고    scopus 로고
    • Control of precursor maturation and disposal is an early regulative mechanism in the normal insulin production of pancreatic beta-cells
    • Wang J., Chen Y., Yuan Q., Tang W., Zhang X., Osei K. Control of precursor maturation and disposal is an early regulative mechanism in the normal insulin production of pancreatic beta-cells. PLoS One 2011, 6(4):e19446.
    • (2011) PLoS One , vol.6 , Issue.4
    • Wang, J.1    Chen, Y.2    Yuan, Q.3    Tang, W.4    Zhang, X.5    Osei, K.6
  • 139
    • 79960565850 scopus 로고    scopus 로고
    • Proinsulin maturation disorder is a contributor to the defect of subsequent conversion to insulin in beta-cells
    • Wang J., Osei K. Proinsulin maturation disorder is a contributor to the defect of subsequent conversion to insulin in beta-cells. Biochemical and Biophysical Research Communications 2011, 411(1):150-155.
    • (2011) Biochemical and Biophysical Research Communications , vol.411 , Issue.1 , pp. 150-155
    • Wang, J.1    Osei, K.2
  • 140
    • 0037016671 scopus 로고    scopus 로고
    • Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
    • Winter J., Klappa P., Freedman R.B., Lilie H., Rudolph R. Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. The Journal of Biological Chemistry 2002, 277(1):310-317.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 310-317
    • Winter, J.1    Klappa, P.2    Freedman, R.B.3    Lilie, H.4    Rudolph, R.5
  • 141
    • 0027189824 scopus 로고
    • Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes
    • Wolin S.L., Walter P. Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes. The Journal of Cell Biology 1993, 121(6):1211-1219.
    • (1993) The Journal of Cell Biology , vol.121 , Issue.6 , pp. 1211-1219
    • Wolin, S.L.1    Walter, P.2
  • 142
    • 0037423397 scopus 로고    scopus 로고
    • Behavior in the eukaryotic secretory pathway of insulin-containing fusion proteins and single-chain insulins bearing various B-chain mutations
    • Zhang B.-Y., Liu M., Arvan P. Behavior in the eukaryotic secretory pathway of insulin-containing fusion proteins and single-chain insulins bearing various B-chain mutations. The Journal of Biological Chemistry 2003, 278(6):3687-3693.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 3687-3693
    • Zhang, B.-Y.1    Liu, M.2    Arvan, P.3
  • 143
    • 77952127782 scopus 로고    scopus 로고
    • Sequential checkpoints govern substrate selection during cotranslational protein targeting
    • Zhang X., Rashid R., Wang K., Shan S.-O. Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science 2010, 328(5979):757-760.
    • (2010) Science , vol.328 , Issue.5979 , pp. 757-760
    • Zhang, X.1    Rashid, R.2    Wang, K.3    Shan, S.-O.4
  • 144
    • 0030595327 scopus 로고    scopus 로고
    • Signal sequences: The same yet different
    • Zheng N., Gierasch L.M. Signal sequences: The same yet different. Cell 1996, 86(6):849-852.
    • (1996) Cell , vol.86 , Issue.6 , pp. 849-852
    • Zheng, N.1    Gierasch, L.M.2
  • 145
    • 0036678101 scopus 로고    scopus 로고
    • Severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3
    • Zhu X., Orci L., Carroll R., Norrbom C., Ravazzola M., Steiner D.F. Severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3. Proceedings of the National Academy of Sciences of the United States of America 2002, 99(16):10299-10304.
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.16 , pp. 10299-10304
    • Zhu, X.1    Orci, L.2    Carroll, R.3    Norrbom, C.4    Ravazzola, M.5    Steiner, D.F.6
  • 147
    • 77949716997 scopus 로고    scopus 로고
    • ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
    • Zito E., Chin K.T., Blais J., Harding H.P., Ron D. ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis. The Journal of Cell Biology 2010, 188(6):821-832.
    • (2010) The Journal of Cell Biology , vol.188 , Issue.6 , pp. 821-832
    • Zito, E.1    Chin, K.T.2    Blais, J.3    Harding, H.P.4    Ron, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.