메뉴 건너뛰기




Volumn 42, Issue , 2015, Pages 3-18

INS-gene mutations: From genetics and beta cell biology to clinical disease

Author keywords

Diabetes; Endoplasmic reticulum stress; Insulin biosynthesis; Insulin gene mutation; Pancreatic beta cell; Proinsulin misfolding

Indexed keywords

INSULIN; INSULIN RECEPTOR; PREPROINSULIN; PROINSULIN; PROTEIN PRECURSOR;

EID: 84940009221     PISSN: 00982997     EISSN: 18729452     Source Type: Journal    
DOI: 10.1016/j.mam.2014.12.001     Document Type: Review
Times cited : (110)

References (173)
  • 1
    • 0027418977 scopus 로고
    • The biosynthesis of the subtilisin-related proprotein convertase PC3, but no that of the PC2 convertase, is regulated by glucose in parallel to proinsulin biosynthesis in rat pancreatic islets
    • Alarcón C., Lincoln B., and Rhodes C.J. The biosynthesis of the subtilisin-related proprotein convertase PC3, but no that of the PC2 convertase, is regulated by glucose in parallel to proinsulin biosynthesis in rat pancreatic islets J. Biol. Chem 268 6 1993 4276 4280
    • (1993) J. Biol. Chem , vol.268 , Issue.6 , pp. 4276-4280
    • Alarcón, C.1    Lincoln, B.2    Rhodes, C.J.3
  • 2
    • 0028912883 scopus 로고
    • Increased secretory demand rather than a defect in the proinsulin conversion mechanism causes hyperproinsulinemia in a glucose-infusion rat model of non-insulin-dependent diabetes mellitus
    • Alarcon C., Leahy J.L., Schuppin G.T., and Rhodes C.J. Increased secretory demand rather than a defect in the proinsulin conversion mechanism causes hyperproinsulinemia in a glucose-infusion rat model of non-insulin-dependent diabetes mellitus J. Clin. Invest 95 3 1995 1032 1039
    • (1995) J. Clin. Invest , vol.95 , Issue.3 , pp. 1032-1039
    • Alarcon, C.1    Leahy, J.L.2    Schuppin, G.T.3    Rhodes, C.J.4
  • 4
    • 0025013749 scopus 로고
    • Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism
    • Arnold A., Horst S.A., Gardella T.J., Baba H., Levine M.A., and Kronenberg H.M. Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism J. Clin. Invest 86 4 1990 1084 1087
    • (1990) J. Clin. Invest , vol.86 , Issue.4 , pp. 1084-1087
    • Arnold, A.1    Horst, S.A.2    Gardella, T.J.3    Baba, H.4    Levine, M.A.5    Kronenberg, H.M.6
  • 5
    • 0020183413 scopus 로고
    • [LeuB24]insulin and [AlaB24]insulin: Altered structures and cellular processing of B24-substituted insulin analogs
    • Assoian R.K., Thomas N.E., Kaiser E.T., and Tager H.S. [LeuB24]insulin and [AlaB24]insulin: altered structures and cellular processing of B24-substituted insulin analogs Proc. Natl. Acad. Sci. U.S.A. 79 17 1982 5147 5151
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , Issue.17 , pp. 5147-5151
    • Assoian, R.K.1    Thomas, N.E.2    Kaiser, E.T.3    Tager, H.S.4
  • 7
    • 84875416620 scopus 로고    scopus 로고
    • Stimulation of autophagy improves endoplasmic reticulum stress-induced diabetes
    • Bachar-Wikstrom E., Wikstrom J.D., Ariav Y., Tirosh B., Kaiser N., and Cerasi E. Stimulation of autophagy improves endoplasmic reticulum stress-induced diabetes Diabetes 62 4 2013 1227 1237
    • (2013) Diabetes , vol.62 , Issue.4 , pp. 1227-1237
    • Bachar-Wikstrom, E.1    Wikstrom, J.D.2    Ariav, Y.3    Tirosh, B.4    Kaiser, N.5    Cerasi, E.6
  • 8
    • 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., and Hutton J.C. A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase Biochem. J. 285 2 1992 391 394
    • (1992) Biochem. J. , 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
  • 9
    • 0025314601 scopus 로고
    • Two unrelated patients with familial hyperproinsulinemia due to a mutation substituting histidine for arginine at position 65 in the proinsulin molecule: Identification of the mutation by direct sequencing of genomic deoxyribonucleic acid amplified by polymerase chain reaction
    • Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., and Gabbay K.H. Two unrelated patients with familial hyperproinsulinemia due to a mutation substituting histidine for arginine at position 65 in the proinsulin molecule: identification of the mutation by direct sequencing of genomic deoxyribonucleic acid amplified by polymerase chain reaction J. Clin. Endocrinol. Metab 71 1 1990 164 169
    • (1990) J. Clin. Endocrinol. Metab , vol.71 , Issue.1 , pp. 164-169
    • Barbetti, F.1    Raben, N.2    Kadowaki, T.3    Cama, A.4    Accili, D.5    Gabbay, K.H.6
  • 10
    • 84876387069 scopus 로고    scopus 로고
    • Secretory protein biogenesis and traffic in the early secretory pathway
    • Barlowe C.K., and Miller E.A. Secretory protein biogenesis and traffic in the early secretory pathway Genetics 193 2 2013 383 410
    • (2013) Genetics , vol.193 , Issue.2 , pp. 383-410
    • Barlowe, C.K.1    Miller, E.A.2
  • 11
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S., Papa F.R., and Walter P. Intracellular signaling by the unfolded protein response Annu. Rev. Cell Dev. Biol 22 1 2006 487 508
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , Issue.1 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 12
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein
    • Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein Nat. Cell Biol 2 6 2000 326 332
    • (2000) Nat. Cell Biol , vol.2 , Issue.6 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 13
    • 0025360748 scopus 로고
    • The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity
    • Bird P., Gething M.J., and Sambrook J. The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity J. Biol. Chem 265 15 1990 8420 8425
    • (1990) J. Biol. Chem , vol.265 , Issue.15 , pp. 8420-8425
    • Bird, P.1    Gething, M.J.2    Sambrook, J.3
  • 14
    • 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., and Lauenborg J. Further evidence that mutations in INS can be a rare cause of Maturity-Onset Diabetes of the Young (MODY) BMC Med. Genet 11 1 2010 42
    • (2010) BMC Med. Genet , vol.11 , Issue.1 , pp. 42
    • Boesgaard, T.1    Pruhova, S.2    Andersson, E.3    Cinek, O.4    Obermannova, B.5    Lauenborg, J.6
  • 15
    • 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., and Iafusco D. Insulin gene mutations as cause of diabetes in children negative for five type 1 diabetes autoantibodies Diabetes Care 32 1 2009 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
  • 16
    • 84868574593 scopus 로고    scopus 로고
    • Disulfide bond formation in the mammalian endoplasmic reticulum
    • Bulleid N.J. Disulfide bond formation in the mammalian endoplasmic reticulum Cold Spring Harbor Perspect. Biol 4 11 2012
    • (2012) Cold Spring Harbor Perspect. Biol , vol.4 , Issue.11
    • Bulleid, N.J.1
  • 17
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess T.L., and Kelly R.B. Constitutive and regulated secretion of proteins Annu. Rev. Cell Biol 3 1 1987 243 293
    • (1987) Annu. Rev. Cell Biol , vol.3 , Issue.1 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 19
  • 20
    • 0035896588 scopus 로고    scopus 로고
    • Aberrant signal peptide cleavage of collagen X in schmid metaphyseal chondrodysplasia. Implications for the molecular basis of the disease
    • Chan D., Ho M.S.P., and Cheah K.S.E. Aberrant signal peptide cleavage of collagen X in schmid metaphyseal chondrodysplasia. Implications for the molecular basis of the disease J. Biol. Chem 276 11 2001 7992 7997
    • (2001) J. Biol. Chem , vol.276 , Issue.11 , pp. 7992-7997
    • Chan, D.1    Ho, M.S.P.2    Cheah, K.S.E.3
  • 21
    • 0343853015 scopus 로고
    • A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia
    • Chan S.J., Seino S., Gruppuso P.A., Schwartz R., and Steiner D.F. A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia Proc. Natl Acad. Sci. U.S.A. 84 8 1987 2194 2197
    • (1987) Proc. Natl Acad. Sci. U.S.A. , vol.84 , Issue.8 , pp. 2194-2197
    • Chan, S.J.1    Seino, S.2    Gruppuso, P.A.3    Schwartz, R.4    Steiner, D.F.5
  • 22
    • 45749104374 scopus 로고    scopus 로고
    • Seven mutations in the human insulin gene linked to permanent neonatal/infancy-onset diabetes mellitus
    • Colombo C., Porzio O., Liu M., Massa O., Vasta M., and Salardi S. Seven mutations in the human insulin gene linked to permanent neonatal/infancy-onset diabetes mellitus J. Clin. Invest 118 6 2008 2148 2156
    • (2008) J. Clin. Invest , vol.118 , Issue.6 , pp. 2148-2156
    • Colombo, C.1    Porzio, O.2    Liu, M.3    Massa, O.4    Vasta, M.5    Salardi, S.6
  • 23
    • 38049180869 scopus 로고    scopus 로고
    • Signal sequence mutation in autosomal dominant form of hypoparathyroidism induces apoptosis that is corrected by a chemical chaperone
    • Datta R., Waheed A., Shah G.N., and Sly W.S. Signal sequence mutation in autosomal dominant form of hypoparathyroidism induces apoptosis that is corrected by a chemical chaperone Proc. Natl Acad. Sci. U.S.A. 104 50 2007 19989 19994
    • (2007) Proc. Natl Acad. Sci. U.S.A. , vol.104 , Issue.50 , pp. 19989-19994
    • Datta, R.1    Waheed, A.2    Shah, G.N.3    Sly, W.S.4
  • 24
    • 0023655547 scopus 로고
    • The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing
    • Davidson H.W., and Hutton J.C. The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing Biochem. J. 245 2 1987 575 582
    • (1987) Biochem. J. , vol.245 , Issue.2 , pp. 575-582
    • Davidson, H.W.1    Hutton, J.C.2
  • 25
    • 0042887445 scopus 로고    scopus 로고
    • Intracellular clusterin causes juxtanuclear aggregate formation and mitochondrial alteration
    • Debure L., Vayssière J.-L., Rincheval V., Loison F., Le Dréan Y., and Michel D. Intracellular clusterin causes juxtanuclear aggregate formation and mitochondrial alteration J. Cell Sci 116 15 2003 3109 3121
    • (2003) J. Cell Sci , vol.116 , Issue.15 , pp. 3109-3121
    • Debure, L.1    Vayssière, J.-L.2    Rincheval, V.3    Loison, F.4    Le Dréan, Y.5    Michel, D.6
  • 26
    • 0027398295 scopus 로고
    • Differential expression of the two nonallelic proinsulin genes in the developing mouse embryo
    • Deltour L., Leduque P., Blume N., Madsen O., Dubois P., and Jami J. Differential expression of the two nonallelic proinsulin genes in the developing mouse embryo Proc. Natl Acad. Sci. U.S.A. 90 2 1993 527 531
    • (1993) Proc. Natl Acad. Sci. U.S.A. , vol.90 , Issue.2 , pp. 527-531
    • Deltour, L.1    Leduque, P.2    Blume, N.3    Madsen, O.4    Dubois, P.5    Jami, J.6
  • 27
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • Dodson G., and Steiner D.F. The role of assembly in insulin's biosynthesis Curr. Opin. Struct. Biol 8 2 1998 189 194
    • (1998) Curr. Opin. Struct. Biol , vol.8 , Issue.2 , pp. 189-194
    • Dodson, G.1    Steiner, D.F.2
  • 28
    • 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 18 4 2005 295 303
    • (2005) Biometals , vol.18 , Issue.4 , pp. 295-303
    • Dunn, M.1
  • 30
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard L., and Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties EMBO Rep 6 1 2005 28 32
    • (2005) EMBO Rep , vol.6 , Issue.1 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 31
    • 57649225887 scopus 로고    scopus 로고
    • The importance of RNA binding proteins in preproinsulin mRNA stability
    • Fred R.G., and Welsh N. The importance of RNA binding proteins in preproinsulin mRNA stability Mol. Cell. Endocrinol 297 1-2 2009 28 33
    • (2009) Mol. Cell. Endocrinol , vol.297 , Issue.12 , pp. 28-33
    • Fred, R.G.1    Welsh, N.2
  • 32
    • 0022519470 scopus 로고
    • Cloning and sequence analysis of cDNA for bovine carboxypeptidase e
    • Fricker L.D., Evans C.J., Esch F.S., and Herbert E. Cloning and sequence analysis of cDNA for bovine carboxypeptidase E Nature 323 6087 1986 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
  • 33
    • 77953517920 scopus 로고    scopus 로고
    • Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon
    • Fujita H., Kida Y., Hagiwara M., Morimoto F., and Sakaguchi M. Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon Mol. Biol. Cell 21 12 2010 2045 2056
    • (2010) Mol. Biol. Cell , vol.21 , Issue.12 , pp. 2045-2056
    • Fujita, H.1    Kida, Y.2    Hagiwara, M.3    Morimoto, F.4    Sakaguchi, M.5
  • 34
    • 0018913424 scopus 로고
    • The insulinopathies
    • Gabbay K.H. The insulinopathies NEJM 302 3 1980 165 167
    • (1980) NEJM , vol.302 , Issue.3 , pp. 165-167
    • Gabbay, K.H.1
  • 36
    • 0018769250 scopus 로고
    • Familial hyperproinsulinemia: Partial characterization of circulating proinsulin-like material
    • Gabbay K.H., Bergenstal R.M., Wolff J., Mako M.E., and Rubenstein A.H. Familial hyperproinsulinemia: partial characterization of circulating proinsulin-like material Proc. Natl Acad. Sci. U.S.A. 76 6 1979 2881 2885
    • (1979) Proc. Natl Acad. Sci. U.S.A. , vol.76 , Issue.6 , pp. 2881-2885
    • Gabbay, K.H.1    Bergenstal, R.M.2    Wolff, J.3    Mako, M.E.4    Rubenstein, A.H.5
  • 37
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner B.M., and Walter P. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response Science 333 6051 2011 1891 1894
    • (2011) Science , vol.333 , Issue.6051 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 38
    • 77649262569 scopus 로고    scopus 로고
    • Recessive mutations in the INS gene result in neonatal diabetes through reduced insulin biosynthesis
    • Garin I., Edghill E., Akerman I., Rubio-Cabezas O., Rica I., and Locke J.M. Recessive mutations in the INS gene result in neonatal diabetes through reduced insulin biosynthesis Proc. Natl. Acad. Sci. U.S.A. 107 7 2010 3105 3110
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.7 , pp. 3105-3110
    • Garin, I.1    Edghill, E.2    Akerman, I.3    Rubio-Cabezas, O.4    Rica, I.5    Locke, J.M.6
  • 41
    • 0035979713 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins: Determinants and dynamics
    • Goder V., and Spiess M. Topogenesis of membrane proteins: determinants and dynamics FEBS Lett 504 3 2001 87 93
    • (2001) FEBS Lett , vol.504 , Issue.3 , pp. 87-93
    • Goder, V.1    Spiess, M.2
  • 42
    • 1542313960 scopus 로고    scopus 로고
    • Sec61p contributes to signal sequence orientation according to the positive-inside rule
    • Goder V., Junne T., and Spiess M. Sec61p contributes to signal sequence orientation according to the positive-inside rule Mol. Biol. Cell 15 3 2004 1470 1478
    • (2004) Mol. Biol. Cell , vol.15 , Issue.3 , pp. 1470-1478
    • Goder, V.1    Junne, T.2    Spiess, M.3
  • 43
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins Nature 426 6968 2003 895 899
    • (2003) Nature , vol.426 , Issue.6968 , pp. 895-899
    • Goldberg, A.L.1
  • 44
    • 0024368808 scopus 로고
    • Partial diversion of a mutant proinsulin (B10 aspartic acid) from the regulated to the constitutive secretory pathway in transfected AtT-20 cells
    • Gross D.J., Halban P.A., Kahn C.R., Weir G.C., and Villa-Komaroff L. Partial diversion of a mutant proinsulin (B10 aspartic acid) from the regulated to the constitutive secretory pathway in transfected AtT-20 cells Proc. Natl Acad. Sci. U.S.A. 86 11 1989 4107 4111
    • (1989) Proc. Natl Acad. Sci. U.S.A. , vol.86 , Issue.11 , pp. 4107-4111
    • Gross, D.J.1    Halban, P.A.2    Kahn, C.R.3    Weir, G.C.4    Villa-Komaroff, L.5
  • 45
    • 0021214250 scopus 로고
    • Familial hyperproinsulinemia due to a proposed defect in conversion of proinsulin to insulin
    • Gruppuso P.A., Gorden P., Kahn C.R., Cornblath M., Zeller W.P., and Schwartz R. Familial hyperproinsulinemia due to a proposed defect in conversion of proinsulin to insulin N. Engl. J. Med 311 10 1984 629 634
    • (1984) N. Engl. J. Med , vol.311 , Issue.10 , pp. 629-634
    • Gruppuso, P.A.1    Gorden, P.2    Kahn, C.R.3    Cornblath, M.4    Zeller, W.P.5    Schwartz, R.6
  • 46
    • 0025979251 scopus 로고
    • Insulin secretory granule biogenesis. Co-ordinate regulation of the biosynthesis of the majority of constituent proteins
    • Guest P.C., Bailyes E.M., Rutherford N.G., and Hutton J.C. Insulin secretory granule biogenesis. Co-ordinate regulation of the biosynthesis of the majority of constituent proteins Biochem. J. 274 1 1991 73 78
    • (1991) Biochem. J. , vol.274 , Issue.1 , pp. 73-78
    • Guest, P.C.1    Bailyes, E.M.2    Rutherford, N.G.3    Hutton, J.C.4
  • 47
    • 84902188979 scopus 로고    scopus 로고
    • Inefficient translocation of preproinsulin contributes to pancreatic beta cell failure and late onset diabetes
    • Guo H., Xiong Y., Witkowski P., Wang L.-J., Cui J., and Lara-Lemus R. Inefficient translocation of preproinsulin contributes to pancreatic beta cell failure and late onset diabetes J. Biol. Chem 289 23 2014 16290 16302
    • (2014) J. Biol. Chem , vol.289 , Issue.23 , pp. 16290-16302
    • Guo, H.1    Xiong, Y.2    Witkowski, P.3    Wang, L.-J.4    Cui, J.5    Lara-Lemus, R.6
  • 48
    • 77955383087 scopus 로고    scopus 로고
    • PERK (EIF2AK3) regulates proinsulin trafficking and quality control in the secretory pathway
    • Gupta S., McGrath B., and Cavener D.R. PERK (EIF2AK3) regulates proinsulin trafficking and quality control in the secretory pathway Diabetes 59 8 2010 1937 1947
    • (2010) Diabetes , vol.59 , Issue.8 , pp. 1937-1947
    • Gupta, S.1    McGrath, B.2    Cavener, D.R.3
  • 49
    • 84872721533 scopus 로고    scopus 로고
    • Proinsulin intermolecular interactions during secretory trafficking in pancreatic β cells
    • Haataja L., Snapp E., Wright J., Liu M., Hardy A.B., and Wheeler M.B. Proinsulin intermolecular interactions during secretory trafficking in pancreatic β cells J. Biol. Chem 288 3 2013 1896 1906
    • (2013) J. Biol. Chem , vol.288 , Issue.3 , pp. 1896-1906
    • Haataja, L.1    Snapp, E.2    Wright, J.3    Liu, M.4    Hardy, A.B.5    Wheeler, M.B.6
  • 50
    • 0024556674 scopus 로고
    • A tripartite structure of the signals that determine protein insertion into the endoplasmic reticulum membrane
    • Haeuptle M.T., Flint N., Gough N.M., and Dobberstein B. A tripartite structure of the signals that determine protein insertion into the endoplasmic reticulum membrane J. Cell Biol 108 4 1989 1227 1236
    • (1989) J. Cell Biol , vol.108 , Issue.4 , pp. 1227-1236
    • Haeuptle, M.T.1    Flint, N.2    Gough, N.M.3    Dobberstein, B.4
  • 51
    • 84901374066 scopus 로고    scopus 로고
    • The pathogenic mechanism of the mycobacterium ulcerans virulence factor, mycolactone, depends on blockade of protein translocation into the ER
    • Hall B.S., Hill K., McKenna M., Ogbechi J., High S., and Willis A.E. The pathogenic mechanism of the mycobacterium ulcerans virulence factor, mycolactone, depends on blockade of protein translocation into the ER PLoS Pathog 10 4 2014 e1004061
    • (2014) PLoS Pathog , vol.10 , Issue.4 , pp. e1004061
    • Hall, B.S.1    Hill, K.2    McKenna, M.3    Ogbechi, J.4    High, S.5    Willis, A.E.6
  • 52
    • 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., and Volchuk A. Endoplasmic reticulum stress response in an INS-1 pancreatic beta-cell line with inducible expression of a folding-deficient proinsulin BMC Cell Biol 11 1 2010 59
    • (2010) BMC Cell Biol , vol.11 , Issue.1 , pp. 59
    • Hartley, T.1    Siva, M.2    Lai, E.3    Teodoro, T.4    Zhang, L.5    Volchuk, A.6
  • 53
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann E., Rapoport T.A., and Lodish H.F. Predicting the orientation of eukaryotic membrane-spanning proteins Proc. Natl Acad. Sci. U.S.A. 86 15 1989 5786 5790
    • (1989) Proc. Natl Acad. Sci. U.S.A. , vol.86 , Issue.15 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 54
    • 33845544522 scopus 로고    scopus 로고
    • Comparative analysis of insulin gene promoters: Implications for diabetes research
    • Hay C.W., and Docherty K. Comparative analysis of insulin gene promoters: implications for diabetes research Diabetes 55 12 2006 3201 3213
    • (2006) Diabetes , vol.55 , Issue.12 , pp. 3201-3213
    • Hay, C.W.1    Docherty, K.2
  • 55
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert D.N., and Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases Physiol. Rev 87 4 2007 1377 1408 10.1152/physrev.00050
    • (2007) Physiol. Rev , vol.87 , Issue.4 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 56
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot L. The ER function BiP is a master regulator of ER function Mt Sinai J. Med 71 5 2004 289 297
    • (2004) Mt Sinai J. Med , vol.71 , Issue.5 , pp. 289-297
    • Hendershot, L.1
  • 57
    • 34248187585 scopus 로고    scopus 로고
    • Dominant-negative effects of a novel mutated Ins2 allele causes early-onset diabetes and severe {beta}-cell loss in Munich Ins2C95S mutant mice
    • Herbach N., Rathkolb B., Kemter E., Pichl L., Klaften M., and de Angelis M.H. Dominant-negative effects of a novel mutated Ins2 allele causes early-onset diabetes and severe {beta}-cell loss in Munich Ins2C95S mutant mice Diabetes 56 5 2007 1268 1276
    • (2007) Diabetes , vol.56 , Issue.5 , pp. 1268-1276
    • Herbach, N.1    Rathkolb, B.2    Kemter, E.3    Pichl, L.4    Klaften, M.5    De Angelis, M.H.6
  • 58
    • 73649115634 scopus 로고    scopus 로고
    • Misfolded proinsulin affects bystander proinsulin in neonatal diabetes
    • Hodish I., Liu M., Rajpal G., Larkin D., Holz R.W., and Adams A. Misfolded proinsulin affects bystander proinsulin in neonatal diabetes J. Biol. Chem 285 1 2010 685 694
    • (2010) J. Biol. Chem , vol.285 , Issue.1 , pp. 685-694
    • Hodish, I.1    Liu, M.2    Rajpal, G.3    Larkin, D.4    Holz, R.W.5    Adams, A.6
  • 59
    • 80052843122 scopus 로고    scopus 로고
    • In vivo misfolding of proinsulin below the threshold of frank diabetes
    • Hodish I., Absood A., Liu L., Liu M., Haataja L., and Larkin D. In vivo misfolding of proinsulin below the threshold of frank diabetes Diabetes 60 8 2011 2092 2101
    • (2011) Diabetes , vol.60 , Issue.8 , pp. 2092-2101
    • Hodish, I.1    Absood, A.2    Liu, L.3    Liu, M.4    Haataja, L.5    Larkin, D.6
  • 60
    • 33748785712 scopus 로고    scopus 로고
    • The folding nucleus of the insulin superfamily: A flexible peptide model foreshadows the native state
    • Hua Q.-X., Mayer J.P., Jia W., Zhang J., and Weiss M.A. The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state J. Biol. Chem 281 38 2006 28131 28142
    • (2006) J. Biol. Chem , vol.281 , Issue.38 , pp. 28131-28142
    • Hua, Q.-X.1    Mayer, J.P.2    Jia, W.3    Zhang, J.4    Weiss, M.A.5
  • 61
    • 0027458937 scopus 로고
    • Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus
    • Hua Q.X., Shoelson S.E., Inouye K., and Weiss M.A. Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus Proc. Natl Acad. Sci. U.S.A. 90 2 1993 582 586
    • (1993) Proc. Natl Acad. Sci. U.S.A. , vol.90 , Issue.2 , pp. 582-586
    • Hua, Q.X.1    Shoelson, S.E.2    Inouye, K.3    Weiss, M.A.4
  • 62
    • 33747641643 scopus 로고    scopus 로고
    • A conserved histidine in insulin is required for the foldability of human proinsulin: Structure and function of an ALAB5 analog
    • Hua Q.X., Liu M., Hu S.Q., Jia W., Arvan P., and Weiss M.A. A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog J. Biol. Chem 281 34 2006 24889 24899
    • (2006) J. Biol. Chem , vol.281 , Issue.34 , pp. 24889-24899
    • Hua, Q.X.1    Liu, M.2    Hu, S.Q.3    Jia, W.4    Arvan, P.5    Weiss, M.A.6
  • 63
    • 0028074665 scopus 로고
    • Formation of the insulin-containing secretory granule core occurs within immature beta-granules
    • Huang X.F., and Arvan P. Formation of the insulin-containing secretory granule core occurs within immature beta-granules J. Biol. Chem 269 33 1994 20838 20844
    • (1994) J. Biol. Chem , vol.269 , Issue.33 , pp. 20838-20844
    • Huang, X.F.1    Arvan, P.2
  • 64
    • 0029133141 scopus 로고
    • Intracellular transport of proinsulin in pancreatic β-cells: Structural maturation probed by disulfide accessibility
    • Huang X.F., and Arvan P. Intracellular transport of proinsulin in pancreatic β-cells: structural maturation probed by disulfide accessibility J. Biol. Chem 270 35 1995 20417 20423
    • (1995) J. Biol. Chem , vol.270 , Issue.35 , pp. 20417-20423
    • Huang, X.F.1    Arvan, P.2
  • 65
    • 84878223129 scopus 로고    scopus 로고
    • Permanent neonatal diabetes due to a novel insulin signal peptide mutation
    • Hussain S., Ali J.M., Jalaludin M.Y., and Harun F. Permanent neonatal diabetes due to a novel insulin signal peptide mutation Pediatr. Diabetes 14 4 2013 299 303
    • (2013) Pediatr. Diabetes , vol.14 , Issue.4 , pp. 299-303
    • Hussain, S.1    Ali, J.M.2    Jalaludin, M.Y.3    Harun, F.4
  • 66
    • 0023664453 scopus 로고
    • Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli
    • Iino T., Takahashi M., and Sako T. Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli J. Biol. Chem 262 15 1987 7412 7417
    • (1987) J. Biol. Chem , vol.262 , Issue.15 , pp. 7412-7417
    • Iino, T.1    Takahashi, M.2    Sako, T.3
  • 67
    • 0018831212 scopus 로고
    • Translational control of proinsulin synthesis by glucose
    • Itoh N., and Okamoto H. Translational control of proinsulin synthesis by glucose Nature 283 1980 100 102
    • (1980) Nature , vol.283 , pp. 100-102
    • Itoh, N.1    Okamoto, H.2
  • 68
    • 0037312881 scopus 로고    scopus 로고
    • Dominant negative pathogenesis by mutant proinsulin in the akita diabetic mouse
    • Izumi T., Yokota-Hashimoto H., Zhao S., Wang J., Halban P.A., and Takeuchi T. Dominant negative pathogenesis by mutant proinsulin in the akita diabetic mouse Diabetes 52 2 2003 409 416
    • (2003) Diabetes , vol.52 , Issue.2 , pp. 409-416
    • Izumi, T.1    Yokota-Hashimoto, H.2    Zhao, S.3    Wang, J.4    Halban, P.A.5    Takeuchi, T.6
  • 69
    • 77953025666 scopus 로고    scopus 로고
    • Recognition of a signal peptide by the signal recognition particle
    • Janda C.Y., Li J., Oubridge C., Hernandez H., Robinson C.V., and Nagai K. Recognition of a signal peptide by the signal recognition particle Nature 465 7297 2010 507 510
    • (2010) Nature , vol.465 , Issue.7297 , pp. 507-510
    • Janda, C.Y.1    Li, J.2    Oubridge, C.3    Hernandez, H.4    Robinson, C.V.5    Nagai, K.6
  • 71
    • 84863900755 scopus 로고    scopus 로고
    • TRC40 can deliver short secretory proteins to the Sec61 translocon
    • Johnson N., Vilardi F., Lang S., Leznicki P., Zimmermann R., and High S. TRC40 can deliver short secretory proteins to the Sec61 translocon J. Cell Sci 125 15 2012 3612 3620
    • (2012) J. Cell Sci , vol.125 , Issue.15 , pp. 3612-3620
    • Johnson, N.1    Vilardi, F.2    Lang, S.3    Leznicki, P.4    Zimmermann, R.5    High, S.6
  • 72
    • 84880643959 scopus 로고    scopus 로고
    • Post-translational translocation into the endoplasmic reticulum
    • Johnson N., Powis K., and High S. Post-translational translocation into the endoplasmic reticulum Biochim. Biophys. Acta Mol. Cell Res 1833 11 2013 2403 2409
    • (2013) Biochim. Biophys. Acta Mol. Cell Res , vol.1833 , Issue.11 , pp. 2403-2409
    • Johnson, N.1    Powis, K.2    High, S.3
  • 73
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., and Frydman J. Misfolded proteins partition between two distinct quality control compartments Nature 454 7208 2008 1088 1095
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 74
    • 84874833124 scopus 로고    scopus 로고
    • DNAJ proteins and protein aggregation diseases
    • Kakkar V., Prins L., and LKampinga H. DNAJ proteins and protein aggregation diseases Curr. Top. Med. Chem 12 22 2012 2479 2490
    • (2012) Curr. Top. Med. Chem , vol.12 , Issue.22 , pp. 2479-2490
    • Kakkar, V.1    Prins, L.2    Lkampinga, H.3
  • 75
    • 0028919333 scopus 로고
    • Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein
    • Karaplis A.C., Lim S.-K., Baba H., Arnold A., and Kronenberg H.M. Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein J. Biol. Chem 270 4 1995 1629 1635
    • (1995) J. Biol. Chem , vol.270 , Issue.4 , pp. 1629-1635
    • Karaplis, A.C.1    Lim, S.-K.2    Baba, H.3    Arnold, A.4    Kronenberg, H.M.5
  • 76
    • 35348967427 scopus 로고    scopus 로고
    • Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins
    • Kimata Y., Ishiwata-Kimata Y., Ito T., Hirata A., Suzuki T., and Oikawa D. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins J. Cell Biol 179 1 2007 75 86
    • (2007) J. Cell Biol , vol.179 , Issue.1 , pp. 75-86
    • Kimata, Y.1    Ishiwata-Kimata, Y.2    Ito, T.3    Hirata, A.4    Suzuki, T.5    Oikawa, D.6
  • 77
    • 84869215749 scopus 로고    scopus 로고
    • Orientation of internal signal-anchor sequences at the Sec61 translocon
    • Kocik L., Junne T., and Spiess M. Orientation of internal signal-anchor sequences at the Sec61 translocon J. Mol. Biol 424 5 2012 368 378
    • (2012) J. Mol. Biol , vol.424 , Issue.5 , pp. 368-378
    • Kocik, L.1    Junne, T.2    Spiess, M.3
  • 78
    • 0026695156 scopus 로고
    • Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment
    • Kuliawat R., and Arvan P. Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment J. Cell Biol 118 3 1992 521 529
    • (1992) J. Cell Biol , vol.118 , Issue.3 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 79
    • 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., and Strub K. Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation Mol. Biol. Cell 23 14 2012 2712 2722
    • (2012) Mol. Biol. 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
  • 80
    • 0034730756 scopus 로고    scopus 로고
    • Glucose-stimulated insulin biosynthesis depends on insulin-stimulated insulin gene transcription
    • Leibiger B., Wåhlander K., Berggren P.-O., and Leibiger I.B. Glucose-stimulated insulin biosynthesis depends on insulin-stimulated insulin gene transcription J. Biol. Chem 275 39 2000 30153 30156
    • (2000) J. Biol. Chem , vol.275 , Issue.39 , pp. 30153-30156
    • Leibiger, B.1    Wåhlander, K.2    Berggren, P.-O.3    Leibiger, I.B.4
  • 82
    • 0038446405 scopus 로고    scopus 로고
    • The unfolded protein response
    • Liu C.Y., and Kaufman R.J. The unfolded protein response J. Cell Sci 116 10 2003 1861 1862 10.1242/jcs.00408
    • (2003) J. Cell Sci , vol.116 , Issue.10 , pp. 1861-1862
    • Liu, C.Y.1    Kaufman, R.J.2
  • 83
    • 17144365015 scopus 로고    scopus 로고
    • Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum
    • Liu M., Li Y., Cavener D., and Arvan P. Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum J. Biol. Chem 280 14 2005 13209 13212
    • (2005) J. Biol. Chem , vol.280 , Issue.14 , pp. 13209-13212
    • Liu, M.1    Li, Y.2    Cavener, D.3    Arvan, P.4
  • 84
    • 35648957233 scopus 로고    scopus 로고
    • Proinsulin maturation, misfolding, and proteotoxicity
    • Liu M., Hodish I., Rhodes C.J., and Arvan P. Proinsulin maturation, misfolding, and proteotoxicity Proc. Natl Acad. Sci. U.S.A. 104 40 2007 15841 15846
    • (2007) Proc. Natl Acad. Sci. U.S.A. , vol.104 , Issue.40 , pp. 15841-15846
    • Liu, M.1    Hodish, I.2    Rhodes, C.J.3    Arvan, P.4
  • 85
    • 71749116066 scopus 로고    scopus 로고
    • Crystal structure of a "nonfoldable" insulin impaired folding efficiency despite native activity
    • Liu M., Wan Z.L., Chu Y.C., Aladdin H., Klaproth B., and Choquette M. Crystal structure of a "nonfoldable" insulin impaired folding efficiency despite native activity J. Biol. Chem 284 50 2009 35259 35272
    • (2009) J. Biol. Chem , vol.284 , Issue.50 , pp. 35259-35272
    • Liu, M.1    Wan, Z.L.2    Chu, Y.C.3    Aladdin, H.4    Klaproth, B.5    Choquette, M.6
  • 86
    • 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., and Phillips N.F. Mutant INS-gene induced diabetes of youth: proinsulin cysteine residues impose dominant-negative inhibition on wild-type proinsulin transport PLoS ONE 5 10 2010 e13333
    • (2010) PLoS ONE , vol.5 , Issue.10 , pp. e13333
    • Liu, M.1    Haataja, L.2    Wright, J.3    Wickramasinghe, N.P.4    Hua, Q.X.5    Phillips, N.F.6
  • 88
    • 77957262631 scopus 로고    scopus 로고
    • Deciphering the hidden informational content of protein sequences
    • Liu M., Hua Q.-X., Hu S.-Q., Jia W., Yang Y., and Saith S.E. Deciphering the hidden informational content of protein sequences J. Biol. Chem 285 40 2010 30989 31001
    • (2010) J. Biol. Chem , vol.285 , Issue.40 , pp. 30989-31001
    • Liu, M.1    Hua, Q.-X.2    Hu, S.-Q.3    Jia, W.4    Yang, Y.5    Saith, S.E.6
  • 89
    • 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., and Barbetti F. Impaired cleavage of preproinsulin signal peptide linked to autosomal-dominant diabetes Diabetes 61 4 2012 828 837
    • (2012) Diabetes , vol.61 , Issue.4 , pp. 828-837
    • Liu, M.1    Lara-Lemus, R.2    Shan, S.-O.3    Wright, J.4    Haataja, L.5    Barbetti, F.6
  • 90
    • 84894046601 scopus 로고    scopus 로고
    • Chapter two - Proinsulin entry and transit through the endoplasmic reticulum in pancreatic beta cells
    • Gerald L. Academic Press
    • Liu M., Wright J., Guo H., Xiong Y., and Arvan P. Chapter two - proinsulin entry and transit through the endoplasmic reticulum in pancreatic beta cells Gerald L. Vitamins & Hormones 2014 Academic Press 35 62
    • (2014) Vitamins & Hormones , pp. 35-62
    • Liu, M.1    Wright, J.2    Guo, H.3    Xiong, Y.4    Arvan, P.5
  • 92
    • 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.L., and Bonnefond A.L. Insulin gene mutations resulting in early-onset diabetes: marked differences in clinical presentation, metabolic status, and pathogenic effect through endoplasmic reticulum retention Diabetes 59 3 2010 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.L.5    Bonnefond, A.L.6
  • 94
    • 42449127920 scopus 로고    scopus 로고
    • Mutations in the insulin gene can cause MODY and autoantibody-negative type 1 diabetes
    • Molven A., Ringdal M., Nordbã A.M., Rãder H., Stãy J., and Lipkind G.M. Mutations in the insulin gene can cause MODY and autoantibody-negative type 1 diabetes Diabetes 57 4 2008 1131 1135
    • (2008) Diabetes , vol.57 , Issue.4 , pp. 1131-1135
    • Molven, A.1    Ringdal, M.2    Nordbã, A.M.3    Rãder, H.4    Stãy, J.5    Lipkind, G.M.6
  • 95
    • 84874494804 scopus 로고    scopus 로고
    • Identification of INS and KCNJ11 gene mutations in type 1B diabetes in Japanese children with onset of diabetes before 5 yr of age
    • Moritani M., Yokota I., Tsubouchi K., Takaya R., Takemoto K., and Minamitani K. Identification of INS and KCNJ11 gene mutations in type 1B diabetes in Japanese children with onset of diabetes before 5 yr of age Pediatr. Diabetes 14 2 2013 112 120
    • (2013) Pediatr. Diabetes , vol.14 , Issue.2 , pp. 112-120
    • Moritani, M.1    Yokota, I.2    Tsubouchi, K.3    Takaya, R.4    Takemoto, K.5    Minamitani, K.6
  • 96
    • 0035173051 scopus 로고    scopus 로고
    • Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway
    • Mutka S.C., and Walter P. Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway Mol. Biol. Cell 12 3 2001 577 588
    • (2001) Mol. Biol. Cell , vol.12 , Issue.3 , pp. 577-588
    • Mutka, S.C.1    Walter, P.2
  • 97
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y., Hosokawa N., Wada I., and Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin Science 299 5611 2003 1394 1397
    • (2003) Science , vol.299 , Issue.5611 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 98
  • 99
    • 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., and Perrelet A. Direct identification of prohormone conversion site in insulin-secreting cells Cell 42 2 1985 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
  • 100
    • 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., and Vassalli J.D. Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles J. Cell Biol 103 6 1986 2273 2281
    • (1986) J. Cell Biol , 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
  • 101
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari S., Koizumi A., Takeda K., Gotoh T., Akira S., and Araki E. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes J. Clin. Invest 109 4 2002 525 532
    • (2002) J. Clin. Invest , vol.109 , Issue.4 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5    Araki, E.6
  • 102
    • 84907181828 scopus 로고    scopus 로고
    • Neonatal diabetes in an infant of diabetic mother: Same novel INS missense mutation in the mother and her offspring
    • Ozturk Mehmet A., Kurtoglu S., Bastug O., Korkmaz L., Daar G., and Memur S. Neonatal diabetes in an infant of diabetic mother: same novel INS missense mutation in the mother and her offspring J. Pediatr. Endocrinol. Metab 27 7-8 2014 745
    • (2014) J. Pediatr. Endocrinol. Metab , vol.27 , Issue.78 , pp. 745
    • Ozturk Mehmet, A.1    Kurtoglu, S.2    Bastug, O.3    Korkmaz, L.4    Daar, G.5    Memur, S.6
  • 103
    • 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., and Bell G.I. Mutant proinsulin proteins associated with neonatal diabetes are retained in the endoplasmic reticulum and not efficiently secreted Biochem. Biophys. Res. Commun 391 3 2010 1449 1454
    • (2010) Biochem. Biophys. Res. Commun , vol.391 , Issue.3 , pp. 1449-1454
    • Park, S.-Y.1    Ye, H.2    Steiner, D.F.3    Bell, G.I.4
  • 104
    • 0025970881 scopus 로고
    • Topology of eukaryotic type II membrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain
    • Parks G.D., and Lamb R.A. Topology of eukaryotic type II membrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain Cell 64 4 1991 777 787
    • (1991) Cell , vol.64 , Issue.4 , pp. 777-787
    • Parks, G.D.1    Lamb, R.A.2
  • 105
    • 0242412456 scopus 로고    scopus 로고
    • Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle
    • Peterson J.H., Woolhead C., and Bernstein H.D. Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle J. Biol. Chem 278 46 2003 46155 46162
    • (2003) J. Biol. Chem , vol.278 , Issue.46 , pp. 46155-46162
    • Peterson, J.H.1    Woolhead, C.2    Bernstein, H.D.3
  • 106
    • 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., and Schekman R. Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane Mol. Biol. Cell 9 12 1998 3455 3473
    • (1998) Mol. Biol. Cell , vol.9 , Issue.12 , pp. 3455-3473
    • Pilon, M.1    Romisch, K.2    Quach, D.3    Schekman, R.4
  • 107
    • 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., and Rapoport T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane Cell 94 6 1998 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
  • 108
    • 42449102605 scopus 로고    scopus 로고
    • Heterozygous missense mutations in the insulin gene are linked to permanent diabetes appearing in the neonatal period or in early infancy
    • Polak M., Dechaume A., Cavé H., Nimri R., Crosnier H., and Sulmont V. Heterozygous missense mutations in the insulin gene are linked to permanent diabetes appearing in the neonatal period or in early infancy Diabetes 57 4 2008 1115 1119
    • (2008) Diabetes , vol.57 , Issue.4 , pp. 1115-1119
    • Polak, M.1    Dechaume, A.2    Cavé, H.3    Nimri, R.4    Crosnier, H.5    Sulmont, V.6
  • 109
    • 0025786795 scopus 로고
    • Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers
    • Quinn D., Orci L., Ravazzola M., and Moore H. Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers J. Cell Biol 113 5 1991 987 996
    • (1991) J. Cell Biol , vol.113 , Issue.5 , pp. 987-996
    • Quinn, D.1    Orci, L.2    Ravazzola, M.3    Moore, H.4
  • 110
    • 79960198707 scopus 로고    scopus 로고
    • Diabetes caused by insulin gene (INS) deletion: Clinical characteristics of homozygous and heterozygous individuals
    • Raile K., O'Connell M., Galler A., Werther G., Khnen P., and Krude H. Diabetes caused by insulin gene (INS) deletion: clinical characteristics of homozygous and heterozygous individuals Eur. J. Endocrinol 165 2 2011 255 260
    • (2011) Eur. J. Endocrinol , vol.165 , Issue.2 , pp. 255-260
    • Raile, K.1    O'Connell, M.2    Galler, A.3    Werther, G.4    Khnen, P.5    Krude, H.6
  • 111
    • 77349112160 scopus 로고    scopus 로고
    • In vitro processing and secretion of mutant insulin proteins that cause permanent neonatal diabetes
    • Rajan S., Eames S.C., Park S.-Y., Labno C., Bell G.I., and Prince V.E. In vitro processing and secretion of mutant insulin proteins that cause permanent neonatal diabetes Am. J. Physiol. Endocrinol. Metab 298 3 2010 E403 E410
    • (2010) Am. J. Physiol. Endocrinol. Metab , vol.298 , Issue.3 , pp. E403-E410
    • Rajan, S.1    Eames, S.C.2    Park, S.-Y.3    Labno, C.4    Bell, G.I.5    Prince, V.E.6
  • 112
    • 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., and Arvan P. Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β cells J. Biol. Chem 287 1 2012 43 47
    • (2012) J. Biol. Chem , vol.287 , Issue.1 , pp. 43-47
    • Rajpal, G.1    Schuiki, I.2    Liu, M.3    Volchuk, A.4    Arvan, P.5
  • 113
    • 77149179440 scopus 로고    scopus 로고
    • Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein
    • Rane N.S., Chakrabarti O., Feigenbaum L., and Hegde R.S. Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein J. Cell Biol 188 4 2010 515 526
    • (2010) J. Cell Biol , vol.188 , Issue.4 , pp. 515-526
    • Rane, N.S.1    Chakrabarti, O.2    Feigenbaum, L.3    Hegde, R.S.4
  • 114
    • 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 450 7170 2007 663 669
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 115
    • 79961244260 scopus 로고    scopus 로고
    • Accurate measurement of pancreatic islet b-cell mass using a second-generation fluorescent exendin-4 analog
    • Reiner T., Thurber G., Gaglia J., Vinegoni C., Liew C.W., and Upadhyay R. Accurate measurement of pancreatic islet b-cell mass using a second-generation fluorescent exendin-4 analog Proce. Natl Acad. Sci. U.S.A. 108 31 2011 12815 12820
    • (2011) Proce. Natl Acad. Sci. U.S.A. , vol.108 , Issue.31 , pp. 12815-12820
    • Reiner, T.1    Thurber, G.2    Gaglia, J.3    Vinegoni, C.4    Liew, C.W.5    Upadhyay, R.6
  • 117
    • 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., and 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 J. Cell Biol 105 1 1987 145 153
    • (1987) J. Cell Biol , vol.105 , Issue.1 , pp. 145-153
    • Rhodes, C.J.1    Halban, P.A.2
  • 118
    • 0036175125 scopus 로고    scopus 로고
    • Proteotoxicity in the endoplasmic reticulum: Lessons from the Akita diabetic mouse
    • Ron D. Proteotoxicity in the endoplasmic reticulum: lessons from the Akita diabetic mouse J. Clin. Invest 109 4 2002 443 445
    • (2002) J. Clin. Invest , vol.109 , Issue.4 , pp. 443-445
    • Ron, D.1
  • 119
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • 787
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration Nature 443 7113 2006 780 787
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780
    • Rubinsztein, D.C.1
  • 120
    • 70349490955 scopus 로고    scopus 로고
    • Testing for monogenic diabetes among children and adolescents with antibody-negative clinically defined Type 1 diabetes
    • Rubio-Cabezas O., Edghill E., Argente J., and Hattersley A. Testing for monogenic diabetes among children and adolescents with antibody-negative clinically defined Type 1 diabetes Diabetic Med 26 10 2009 1070 1074
    • (2009) Diabetic Med , vol.26 , Issue.10 , pp. 1070-1074
    • Rubio-Cabezas, O.1    Edghill, E.2    Argente, J.3    Hattersley, A.4
  • 121
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • Saibil H. Chaperone machines for protein folding, unfolding and disaggregation Nat. Rev. Mol. Cell Biol 14 10 2013 630 642
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , Issue.10 , pp. 630-642
    • Saibil, H.1
  • 122
    • 0026501551 scopus 로고
    • Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge
    • Sakaguchi M., Tomiyoshi R., Kuroiwa T., Mihara K., and Omura T. Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge Proc. Natl Acad. Sci. U.S.A. 89 1 1992 16 19
    • (1992) Proc. Natl Acad. Sci. U.S.A. , vol.89 , Issue.1 , pp. 16-19
    • Sakaguchi, M.1    Tomiyoshi, R.2    Kuroiwa, T.3    Mihara, K.4    Omura, T.5
  • 123
    • 0022849922 scopus 로고
    • Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val - -Leu) isolated from the pancreas
    • Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., and Hirata H. Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val - -Leu) isolated from the pancreas J. Clin. Invest 78 6 1986 1666 1672
    • (1986) J. Clin. Invest , vol.78 , Issue.6 , pp. 1666-1672
    • Sakura, H.1    Iwamoto, Y.2    Sakamoto, Y.3    Kuzuya, T.4    Hirata, H.5
  • 124
    • 0025262033 scopus 로고
    • In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli
    • Sasaki S., Matsuyama S., and Mizushima S. In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli J. Biol. Chem 265 8 1990 4358 4363
    • (1990) J. Biol. Chem , vol.265 , Issue.8 , pp. 4358-4363
    • Sasaki, S.1    Matsuyama, S.2    Mizushima, S.3
  • 125
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation
    • Schaffar G., Breuer P., Boteva R., Behrends C., Tzvetkov N., and Strippel N. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation Mol. Cell 15 1 2004 95 105
    • (2004) Mol. Cell , vol.15 , Issue.1 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3    Behrends, C.4    Tzvetkov, N.5    Strippel, N.6
  • 126
    • 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., and Tsukamoto K. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis Nat. Med 11 7 2005 757 764
    • (2005) Nat. Med , 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
  • 127
    • 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., and Herzog V. In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER EMBO J. 14 6 1995 1091 1098
    • (1995) EMBO J. , vol.14 , Issue.6 , pp. 1091-1098
    • Schmitz, A.1    Maintz, M.2    Kehle, T.3    Herzog, V.4
  • 128
    • 0030605859 scopus 로고    scopus 로고
    • A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type IIs
    • Seppen J., Steenken E., Lindhout D., Bosma P.J., and Oude Elferink R.P.J. A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type IIs FEBS Lett 390 3 1996 294 298
    • (1996) FEBS Lett , vol.390 , Issue.3 , pp. 294-298
    • Seppen, J.1    Steenken, E.2    Lindhout, D.3    Bosma, P.J.4    Oude Elferink, R.P.J.5
  • 129
    • 77949754469 scopus 로고    scopus 로고
    • New insights into oxidative folding
    • Sevier C.S. New insights into oxidative folding J. Cell Biol 188 6 2010 757 758
    • (2010) J. Cell Biol , vol.188 , Issue.6 , pp. 757-758
    • Sevier, C.S.1
  • 130
    • 84455178968 scopus 로고    scopus 로고
    • A calmodulin-dependent translocation pathway for small secretory proteins
    • Shao S., and Hegde R.S. A calmodulin-dependent translocation pathway for small secretory proteins Cell 147 7 2011 1576 1588
    • (2011) Cell , vol.147 , Issue.7 , pp. 1576-1588
    • Shao, S.1    Hegde, R.S.2
  • 131
    • 0028127761 scopus 로고
    • Glucose-induced transcription of the insulin gene is mediated by factors required for beta-cell-type-specific expression
    • Sharma A., and Stein R. Glucose-induced transcription of the insulin gene is mediated by factors required for beta-cell-type-specific expression Mol. Cell. Biol 14 2 1994 871 879
    • (1994) Mol. Cell. Biol , vol.14 , Issue.2 , pp. 871-879
    • Sharma, A.1    Stein, R.2
  • 132
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response
    • Shen J., Snapp E.L., Lippincott-Schwartz J., and Prywes R. Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response Mol. Cell. Biol 25 3 2005 921 932
    • (2005) Mol. Cell. Biol , vol.25 , Issue.3 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 133
    • 0021045564 scopus 로고
    • Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution
    • Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., and Kaiser E. Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution Proc. Natl. Acad. Sci. U.S.A. 80 24 1983 7390 7394
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , Issue.24 , pp. 7390-7394
    • Shoelson, S.1    Fickova, M.2    Haneda, M.3    Nahum, A.4    Musso, G.5    Kaiser, E.6
  • 135
    • 0021341053 scopus 로고
    • Human insulin B24 (Phe - -Ser). Secretion and metabolic clearance of the abnormal insulin in man and in a dog model
    • Shoelson S.E., Polonsky K., Zeidler A., Rubenstein A.H., and Tager H.S. Human insulin B24 (Phe - -Ser). Secretion and metabolic clearance of the abnormal insulin in man and in a dog model J. Clin. Invest 73 5 1984 1351 1358
    • (1984) J. Clin. Invest , vol.73 , Issue.5 , pp. 1351-1358
    • Shoelson, S.E.1    Polonsky, K.2    Zeidler, A.3    Rubenstein, A.H.4    Tager, H.S.5
  • 136
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith M.H., Ploegh H.L., and Weissman J.S. Road to ruin: targeting proteins for degradation in the endoplasmic reticulum Science 334 6059 2011 1086 1090
    • (2011) Science , vol.334 , Issue.6059 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 137
    • 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., and Whittaker J. 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 J. Biol. Chem 285 7 2010 5040 5055
    • (2010) J. Biol. Chem , 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
  • 138
    • 80054731388 scopus 로고    scopus 로고
    • On the discovery of precursor processing
    • Mbikay M. Seidah N.G. Humana Press
    • Steiner D. On the discovery of precursor processing Mbikay M. Seidah N.G. Proprotein Convertases 2011 Humana Press 3 11
    • (2011) Proprotein Convertases , pp. 3-11
    • Steiner, D.1
  • 139
    • 0000962628 scopus 로고
    • The biosynthesis of insulin and a probable precursor of insulin by a human islet cell adenoma
    • Steiner D., and Oyer P. The biosynthesis of insulin and a probable precursor of insulin by a human islet cell adenoma Proc. Natl. Acad. Sci. U.S.A. 57 2 1967 473 480
    • (1967) Proc. Natl. Acad. Sci. U.S.A. , vol.57 , Issue.2 , pp. 473-480
    • Steiner, D.1    Oyer, P.2
  • 140
    • 0031995477 scopus 로고    scopus 로고
    • The proprotein convertases
    • Steiner D.F. The proprotein convertases Curr. Opin. Chem. Biol 2 1 1998 31 39
    • (1998) Curr. Opin. Chem. Biol , vol.2 , Issue.1 , pp. 31-39
    • Steiner, D.F.1
  • 141
    • 0014200189 scopus 로고
    • Insulin biosynthesis: Evidence for a precursor
    • Steiner D.F., Cunningham D., Spigelman L., and Aten B. Insulin biosynthesis: evidence for a precursor Science 157 3789 1967 697 700
    • (1967) Science , vol.157 , Issue.3789 , pp. 697-700
    • Steiner, D.F.1    Cunningham, D.2    Spigelman, L.3    Aten, B.4
  • 145
    • 78650581726 scopus 로고    scopus 로고
    • Clinical and molecular genetics of neonatal diabetes due to mutations in the insulin gene
    • Støy J., Steiner D., Park S.-Y., Ye H., Philipson L., and Bell G. Clinical and molecular genetics of neonatal diabetes due to mutations in the insulin gene Rev. Endocr. Metab. Disord 11 3 2010 205 215
    • (2010) Rev. Endocr. Metab. Disord , vol.11 , Issue.3 , pp. 205-215
    • Støy, J.1    Steiner, D.2    Park, S.-Y.3    Ye, H.4    Philipson, L.5    Bell, G.6
  • 146
    • 33847232980 scopus 로고    scopus 로고
    • Pronounced cytosolic aggregation of cellular prion protein in pancreatic [beta]-cells in response to hyperglycemia
    • Strom A., Wang G.-S., Reimer R., Finegood D.T., and Scott F.W. Pronounced cytosolic aggregation of cellular prion protein in pancreatic [beta]-cells in response to hyperglycemia Lab. Invest 87 2 2006 139 149
    • (2006) Lab. Invest , vol.87 , Issue.2 , pp. 139-149
    • Strom, A.1    Wang, G.-S.2    Reimer, R.3    Finegood, D.T.4    Scott, F.W.5
  • 147
    • 0021167455 scopus 로고
    • Lilly lecture 1983. Abnormal products of the human insulin gene
    • Tager H. Lilly lecture 1983. Abnormal products of the human insulin gene Diabetes 33 7 1984 693 699
    • (1984) Diabetes , vol.33 , Issue.7 , pp. 693-699
    • Tager, H.1
  • 149
    • 0037059772 scopus 로고    scopus 로고
    • Control of insulin mRNA stability in rat pancreatic islets: Regulatory role of a 3′-untranslated region pyrimidine-rich sequence
    • Tillmar L., Carlsson C., and Welsh N. Control of insulin mRNA stability in rat pancreatic islets: regulatory role of a 3′-untranslated region pyrimidine-rich sequence J. Biol. Chem 277 2 2002 1099 1106
    • (2002) J. Biol. Chem , vol.277 , Issue.2 , pp. 1099-1106
    • Tillmar, L.1    Carlsson, C.2    Welsh, N.3
  • 150
    • 0024499153 scopus 로고
    • Anomalies in the translocation and processing of glycophorin precursors in murine erythroleukemia cells
    • Ulmer J.B., and Palade G.E. Anomalies in the translocation and processing of glycophorin precursors in murine erythroleukemia cells J. Biol. Chem 264 2 1989 1084 1091
    • (1989) J. Biol. Chem , vol.264 , Issue.2 , pp. 1084-1091
    • Ulmer, J.B.1    Palade, G.E.2
  • 151
    • 0009746027 scopus 로고
    • Targeting and processing of glycophorins in murine erythroleukemia cells: Use of brefeldin A as a perturbant of intracellular traffic
    • Ulmer J.B., and Palade G.E. Targeting and processing of glycophorins in murine erythroleukemia cells: use of brefeldin A as a perturbant of intracellular traffic Proc. Natl Acad. Sci. U.S.A. 86 18 1989 6992 6996
    • (1989) Proc. Natl Acad. Sci. U.S.A. , vol.86 , Issue.18 , pp. 6992-6996
    • Ulmer, J.B.1    Palade, G.E.2
  • 152
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., and Nagata K. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER Science 321 5888 2008 569 572
    • (2008) Science , vol.321 , Issue.5888 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 153
    • 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 J. Mol. Biol 192 2 1986 287 290
    • (1986) J. Mol. Biol , vol.192 , Issue.2 , pp. 287-290
    • Von Heijne, G.1
  • 154
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • vonHeijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues Nature 341 6241 1989 456 458
    • (1989) Nature , vol.341 , Issue.6241 , pp. 456-458
    • Vonheijne, G.1
  • 155
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar S.S., and Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation Nat. Rev. Mol. Cell Biol 9 12 2008 944 957
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , Issue.12 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 156
    • 0023846720 scopus 로고
    • Mutant insulin syndromes
    • Vinik A., and Bell G. Mutant insulin syndromes Horm. Metab. Res 20 1 1988 1 10
    • (1988) Horm. Metab. Res , vol.20 , Issue.1 , pp. 1-10
    • Vinik, A.1    Bell, G.2
  • 157
    • 79751480230 scopus 로고    scopus 로고
    • Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation
    • Viswanathan J., Haapasalo A., Böttcher C., Miettinen R., Kurkinen K.M.A., and Lu A. Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation Traffic 12 3 2011 330 348
    • (2011) Traffic , vol.12 , Issue.3 , pp. 330-348
    • Viswanathan, J.1    Haapasalo, A.2    Böttcher, C.3    Miettinen, R.4    Kurkinen, K.M.A.5    Lu, A.6
  • 158
    • 77957301909 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response in the pancreatic β-cell
    • Volchuk A., and Ron D. The endoplasmic reticulum stress response in the pancreatic β-cell Diabetes Obes. Metab 12 2010 48 57
    • (2010) Diabetes Obes. Metab , vol.12 , pp. 48-57
    • Volchuk, A.1    Ron, D.2
  • 159
    • 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., and Spiess M. Multiple determinants direct the orientation of signal,Äìanchor proteins: the topogenic role of the hydrophobic signal domain J. Cell Biol 137 3 1997 555 562
    • (1997) J. Cell Biol , vol.137 , Issue.3 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 160
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P., and Ron D. The unfolded protein response: from stress pathway to homeostatic regulation Science 334 6059 2011 1081 1086
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 161
    • 0032918044 scopus 로고    scopus 로고
    • A mutation in the insulin 2 gene induces diabetes with severe pancreatic ß-cell dysfunction in the Mody mouse
    • Wang J., Takeuchi T., Tanaka S., Kubo S.-K., Kayo T., and Lu D. A mutation in the insulin 2 gene induces diabetes with severe pancreatic ß-cell dysfunction in the Mody mouse J. Clin. Invest 103 1 1999 27 37
    • (1999) J. Clin. Invest , vol.103 , Issue.1 , pp. 27-37
    • Wang, J.1    Takeuchi, T.2    Tanaka, S.3    Kubo, S.-K.4    Kayo, T.5    Lu, D.6
  • 162
    • 76749151327 scopus 로고    scopus 로고
    • Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis
    • Wang M., Ye R., Barron E., Baumeister P., Mao C., and Luo S. Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis Cell Death Differ 17 3 2009 488 498
    • (2009) Cell Death Differ , vol.17 , Issue.3 , pp. 488-498
    • Wang, M.1    Ye, R.2    Barron, E.3    Baumeister, P.4    Mao, C.5    Luo, S.6
  • 163
    • 77952913087 scopus 로고    scopus 로고
    • Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer
    • Wang X., Lee J., Di Jeso B., Treglia A.S., Comoletti D., and Dubi N. Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer J. Biol. Chem 285 23 2010 17564 17573
    • (2010) J. Biol. Chem , vol.285 , Issue.23 , pp. 17564-17573
    • Wang, X.1    Lee, J.2    Di Jeso, B.3    Treglia, A.S.4    Comoletti, D.5    Dubi, N.6
  • 165
    • 67749096213 scopus 로고    scopus 로고
    • Proinsulin and the genetics of diabetes mellitus
    • Weiss M.A. Proinsulin and the genetics of diabetes mellitus J. Biol. Chem 284 29 2009 19159 19163
    • (2009) J. Biol. Chem , vol.284 , Issue.29 , pp. 19159-19163
    • Weiss, M.A.1
  • 166
    • 0035933884 scopus 로고    scopus 로고
    • Cooperativity between the preproinsulin mRNA untranslated regions is necessary for glucose-stimulated translation
    • Wicksteed B., Herbert T.P., Alarcon C., Lingohr M.K., Moss L.G., and Rhodes C.J. Cooperativity between the preproinsulin mRNA untranslated regions is necessary for glucose-stimulated translation J. Biol. Chem 276 25 2001 22553 22558
    • (2001) J. Biol. Chem , vol.276 , Issue.25 , pp. 22553-22558
    • Wicksteed, B.1    Herbert, T.P.2    Alarcon, C.3    Lingohr, M.K.4    Moss, L.G.5    Rhodes, C.J.6
  • 167
    • 84886672340 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin-1α (Ero1α) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress
    • Wright J., Birk J., Haataja L., Liu M., Ramming T., and Weiss M.A. Endoplasmic reticulum oxidoreductin-1α (Ero1α) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress J. Biol. Chem 288 43 2013 31010 31018
    • (2013) J. Biol. Chem , vol.288 , Issue.43 , pp. 31010-31018
    • Wright, J.1    Birk, J.2    Haataja, L.3    Liu, M.4    Ramming, T.5    Weiss, M.A.6
  • 168
    • 84879658402 scopus 로고    scopus 로고
    • Dominant protein interactions that influence the pathogenesis of conformational diseases
    • Wright J., Wang X., Haataja L., Kellogg A.P., Lee J., and Liu M. Dominant protein interactions that influence the pathogenesis of conformational diseases J. Clin. Invest 123 7 2013 3124 3134
    • (2013) J. Clin. Invest , vol.123 , Issue.7 , pp. 3124-3134
    • Wright, J.1    Wang, X.2    Haataja, L.3    Kellogg, A.P.4    Lee, J.5    Liu, M.6
  • 169
    • 3142579218 scopus 로고    scopus 로고
    • Diabetes-associated mutations in insulin: Consecutive residues in the B chain contact distinct domains of the insulin receptor
    • Xu B., Hu S.-Q., Chu Y.-C., Huang K., Nakagawa S.H., and Whittaker J. Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor Biochemistry 43 26 2004 8356 8372
    • (2004) Biochemistry , vol.43 , Issue.26 , pp. 8356-8372
    • Xu, B.1    Hu, S.-Q.2    Chu, Y.-C.3    Huang, K.4    Nakagawa, S.H.5    Whittaker, J.6
  • 170
    • 0026688937 scopus 로고
    • A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto)
    • Yano H., Kitano N., Morimoto M., Polonsky K., Imura H., and Seino Y. A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto) J. Clin. Invest 89 6 1992 1902 1907
    • (1992) J. Clin. Invest , vol.89 , Issue.6 , pp. 1902-1907
    • Yano, H.1    Kitano, N.2    Morimoto, M.3    Polonsky, K.4    Imura, H.5    Seino, Y.6
  • 172
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K., and Kaufman R.J. From endoplasmic-reticulum stress to the inflammatory response Nature 454 7203 2008 455 462
    • (2008) Nature , vol.454 , Issue.7203 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.