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Volumn 8, Issue 3-4, 2006, Pages 325-337

ERp29, an unusual redox-inactive member of the thioredoxin family

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERP29; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 33646687533     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.325     Document Type: Review
Times cited : (51)

References (105)
  • 2
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, and Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J 21: 835-844, 2002.
    • (2002) EMBO J , vol.21 , pp. 835-844
    • Anelli, T.1    Alessio, M.2    Mezghrani, A.3    Simmen, T.4    Talamo, F.5    Bachi, A.6    Sitia, R.7
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 181: 223-230, 1973.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0345465663 scopus 로고    scopus 로고
    • Integration of endoplasmic reticulum signaling in health and disease
    • Aridor M and Balch WE. Integration of endoplasmic reticulum signaling in health and disease. Nat Med 5: 745-751, 1999.
    • (1999) Nat Med , vol.5 , pp. 745-751
    • Aridor, M.1    Balch, W.E.2
  • 5
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong RN. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 10: 2-18, 1997.
    • (1997) Chem Res Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 6
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner ES and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267: 6102-6109, 2000.
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 7
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein
    • Arrigo AP, Suhan JP, and Welch WJ. Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol Cell Biol 8: 5059-5071, 1988.
    • (1988) Mol Cell Biol , vol.8 , pp. 5059-5071
    • Arrigo, A.P.1    Suhan, J.P.2    Welch, W.J.3
  • 8
    • 0030981967 scopus 로고    scopus 로고
    • Intracellular protein transport to the thyrocyte plasma membrane: Potential implications for thyroid physiology
    • Arvan P, Kim PS, Kuliawat R, Prabakaran D, Muresan Z, Yoo SE, and Abu Hossain S. Intracellular protein transport to the thyrocyte plasma membrane: potential implications for thyroid physiology. Thyroid 7: 89-105, 1997.
    • (1997) Thyroid , vol.7 , pp. 89-105
    • Arvan, P.1    Kim, P.S.2    Kuliawat, R.3    Prabakaran, D.4    Muresan, Z.5    Yoo, S.E.6    Abu Hossain, S.7
  • 9
    • 0030973847 scopus 로고    scopus 로고
    • The early emergence of platyhelminths is contradicted by the agreement between 18S rRNA and Hox genes data
    • Balavoine G. The early emergence of platyhelminths is contradicted by the agreement between 18S rRNA and Hox genes data. C R Acad Sci III 320: 83-94, 1997.
    • (1997) C R Acad Sci III , vol.320 , pp. 83-94
    • Balavoine, G.1
  • 10
    • 4544371124 scopus 로고    scopus 로고
    • Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure
    • Barnewitz K, Guo C, Sevvana M, Ma Q, Sheldrick GM, Soling HD, and Ferrari DM. Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure. J Biol Chem 279: 39829-39837, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 39829-39837
    • Barnewitz, K.1    Guo, C.2    Sevvana, M.3    Ma, Q.4    Sheldrick, G.M.5    Soling, H.D.6    Ferrari, D.M.7
  • 11
    • 29644440061 scopus 로고    scopus 로고
    • ERp29 is an essential endoplasmic reticulum factor regulating secretion of thyroglobulin
    • Baryshev M, Sargsyan E, and Mkrtchian S. ERp29 is an essential endoplasmic reticulum factor regulating secretion of thyroglobulin. Biochem Biophys Res Commun 340: 617-624, 2006.
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 617-624
    • Baryshev, M.1    Sargsyan, E.2    Mkrtchian, S.3
  • 12
    • 3042771829 scopus 로고    scopus 로고
    • Unfolded protein response is involved in the pathology of human congenital hypothyroid goiter and rat non-goitrous congenital hypothyroidism
    • Baryshev M, Sargsyan E, Wallin G, Lejnieks A, Furudate S, Hishinuma A, and Mkrtchian S. Unfolded protein response is involved in the pathology of human congenital hypothyroid goiter and rat non-goitrous congenital hypothyroidism. J Mol Endocrinol 32: 903-920, 2004.
    • (2004) J Mol Endocrinol , vol.32 , pp. 903-920
    • Baryshev, M.1    Sargsyan, E.2    Wallin, G.3    Lejnieks, A.4    Furudate, S.5    Hishinuma, A.6    Mkrtchian, S.7
  • 13
    • 0026623463 scopus 로고
    • Examining the function and regulation of hsp 70 in cells subjected to metabolic stress
    • Beckmann RP, Lovett M, and Welch WJ. Examining the function and regulation of hsp 70 in cells subjected to metabolic stress. J Cell Biol 117: 1137-1150, 1992.
    • (1992) J Cell Biol , vol.117 , pp. 1137-1150
    • Beckmann, R.P.1    Lovett, M.2    Welch, W.J.3
  • 14
    • 0034470157 scopus 로고    scopus 로고
    • Role of rap in the biogenesis of lipoprotein receptors
    • Bu G and Marzolo MP. Role of rap in the biogenesis of lipoprotein receptors. Trends Cardiovasc Med 10: 148-155, 2000.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 148-155
    • Bu, G.1    Marzolo, M.P.2
  • 15
    • 0026523153 scopus 로고
    • Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: Multiple species and disaggregation
    • Carlino A, Toledo H, Skaleris D, DeLisio R, Weissbach H, and Brot N. Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation. Proc Natl Acad Sci USA 89: 2081-2085, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2081-2085
    • Carlino, A.1    Toledo, H.2    Skaleris, D.3    DeLisio, R.4    Weissbach, H.5    Brot, N.6
  • 17
    • 2542430403 scopus 로고    scopus 로고
    • Structural basis of Redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA
    • Crow A, Acheson RM, Le Brun NE, and Oubric A. Structural basis of Redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA. J Biol Chem 279: 23654-23660, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 23654-23660
    • Crow, A.1    Acheson, R.M.2    Le Brun, N.E.3    Oubric, A.4
  • 18
    • 0031054441 scopus 로고    scopus 로고
    • Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum
    • Demmer J, Zhou C, and Hubbard MJ. Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum. FEBS Lett 402: 145-150, 1997.
    • (1997) FEBS Lett , vol.402 , pp. 145-150
    • Demmer, J.1    Zhou, C.2    Hubbard, M.J.3
  • 20
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson CM and Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr Opin Struct Biol 9: 92-101, 1999.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 21
    • 0022587320 scopus 로고
    • Transcription factor Sp1 recognizes a DNA sequence in the mouse dihydrofolate reductase promoter
    • Dynan WS, Sazer S, Tjian R, and Schimke RT. Transcription factor Sp1 recognizes a DNA sequence in the mouse dihydrofolate reductase promoter. Nature 319: 246-248, 1986.
    • (1986) Nature , vol.319 , pp. 246-248
    • Dynan, W.S.1    Sazer, S.2    Tjian, R.3    Schimke, R.T.4
  • 22
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L and Helenius A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4: 181-191, 2003.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 23
    • 0030792377 scopus 로고    scopus 로고
    • Combination of direct DNA sequencing with degenerate primer-mediated PCR and 5′-/3′-RACE to screen novel cDNA sequences
    • Fang C, Mkrtchian S, and Ingelman-Sundberg M. Combination of direct DNA sequencing with degenerate primer-mediated PCR and 5′-/3′-RACE to screen novel cDNA sequences. Biotechniques 23: 52, 54, 56, 58, 1997.
    • (1997) Biotechniques , vol.23 , pp. 52
    • Fang, C.1    Mkrtchian, S.2    Ingelman-Sundberg, M.3
  • 24
    • 0036186384 scopus 로고    scopus 로고
    • Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
    • Fassio A and Sitia R. Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum. Histochem Cell Biol 117: 151-157, 2002.
    • (2002) Histochem Cell Biol , vol.117 , pp. 151-157
    • Fassio, A.1    Sitia, R.2
  • 25
    • 0032146759 scopus 로고    scopus 로고
    • ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif
    • Ferrari DM, Nguyen Van P, Kratzin HD, and Soling HD. ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif. Eur J Biochem 255: 570-579, 1998.
    • (1998) Eur J Biochem , vol.255 , pp. 570-579
    • Ferrari, D.M.1    Van Nguyen, P.2    Kratzin, H.D.3    Soling, H.D.4
  • 26
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari DM and Soling HD. The protein disulphide-isomerase family: unravelling a string of folds. Biochem J 339: 1-10, 1999.
    • (1999) Biochem J , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 27
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman RB, Hirst TR, and Tuite MF. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19: 331-336, 1994.
    • (1994) Trends Biochem Sci , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 28
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70: 603-647, 2001.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 29
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin
    • Gaudet R, Bohm A, and Sigler PB. Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. Cell 87: 577-588, 1996.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 30
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10: 465-472, 1999.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 31
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ and Sambrook J. Protein folding in the cell. Nature 355: 33-45, 1992.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 32
    • 0034734041 scopus 로고    scopus 로고
    • Lectins and traffic in the secretory pathway
    • Hauri H, Appenzeller C, Kuhn F, and Nufer O. Lectins and traffic in the secretory pathway. FEBS Lett 476: 32-37, 2000.
    • (2000) FEBS Lett , vol.476 , pp. 32-37
    • Hauri, H.1    Appenzeller, C.2    Kuhn, F.3    Nufer, O.4
  • 33
    • 17144367645 scopus 로고    scopus 로고
    • Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125
    • Hermann VM, Cutfield JF, and Hubbard MJ. Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125. J Biol Chem 280: 13529-13537, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 13529-13537
    • Hermann, V.M.1    Cutfield, J.F.2    Hubbard, M.J.3
  • 36
    • 9144252641 scopus 로고    scopus 로고
    • Purification and biochemical characterization of native ERp29 from rat liver
    • Hubbard MJ, Mangum JE, and McHugh NJ. Purification and biochemical characterization of native ERp29 from rat liver. Biochem J 3 83: 589-597, 2004.
    • (2004) Biochem J , vol.383 , pp. 589-597
    • Hubbard, M.J.1    Mangum, J.E.2    McHugh, N.J.3
  • 37
    • 0034108939 scopus 로고    scopus 로고
    • Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis
    • Hubbard MJ, McHugh NJ, and Carne DL. Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis. Eur J Biochem 267: 1945-1957, 2000.
    • (2000) Eur J Biochem , vol.267 , pp. 1945-1957
    • Hubbard, M.J.1    McHugh, N.J.2    Carne, D.L.3
  • 38
    • 0023665337 scopus 로고
    • Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates
    • Huber HE, Tabor S, and Richardson CC. Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates. J Biol Chem 262: 16224-16232, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 16224-16232
    • Huber, H.E.1    Tabor, S.2    Richardson, C.C.3
  • 40
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman RJ. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev 13: 1211-1233, 1999.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 41
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink J, Darby NJ, Dijkstra K, Nilges M, and Creighton TE. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr Biol 7: 239-245, 1997.
    • (1997) Curr Biol , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 43
    • 0037716929 scopus 로고    scopus 로고
    • Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)
    • Kim JH, Kim SJ, Jeong DG, Son JH, and Ryu SE. Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1). FEBS Lett 543: 164-169, 2003.
    • (2003) FEBS Lett , vol.543 , pp. 164-169
    • Kim, J.H.1    Kim, S.J.2    Jeong, D.G.3    Son, J.H.4    Ryu, S.E.5
  • 45
    • 0032432673 scopus 로고    scopus 로고
    • Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: Disorders of protein trafficking and the role of ER molecular chaperones
    • Kim PS and Arvan P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones. Endocr Rev 19: 173-202, 1998.
    • (1998) Endocr Rev , vol.19 , pp. 173-202
    • Kim, P.S.1    Arvan, P.2
  • 46
    • 0029941327 scopus 로고    scopus 로고
    • An endoplasmic reticulum storage disease causing congenital goiter with hypothyroidism
    • Kim PS, Kwon OY, and Arvan P. An endoplasmic reticulum storage disease causing congenital goiter with hypothyroidism. J Cell Biol 133: 517-527, 1996.
    • (1996) J Cell Biol , vol.133 , pp. 517-527
    • Kim, P.S.1    Kwon, O.Y.2    Arvan, P.3
  • 47
    • 0031882304 scopus 로고    scopus 로고
    • Windbeutel, a gene required for dorsoventral patterning in Drosophila, encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum
    • Konsolaki M and Schupbach T. Windbeutel, a gene required for dorsoventral patterning in Drosophila, encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum. Genes Dev 12: 120-131, 1998.
    • (1998) Genes Dev , vol.12 , pp. 120-131
    • Konsolaki, M.1    Schupbach, T.2
  • 48
    • 0034625576 scopus 로고    scopus 로고
    • TSH regulates a gene expression encoding ERp29, an endoplasmic reticulum stress protein, in the thyrocytes of FRTL-5 cells
    • Kwon OY, Park S, Lee W, You KH, Kim H, and Shong M. TSH regulates a gene expression encoding ERp29, an endoplasmic reticulum stress protein, in the thyrocytes of FRTL-5 cells. FEBS Lett 475: 27-30, 2000.
    • (2000) FEBS Lett , vol.475 , pp. 27-30
    • Kwon, O.Y.1    Park, S.2    Lee, W.3    You, K.H.4    Kim, H.5    Shong, M.6
  • 49
    • 0026742792 scopus 로고
    • CpG islands as gene markers in the human genome
    • Larsen F, Gundersen G, Lopez R, and Prydz H. CpG islands as gene markers in the human genome. Genomics 13: 1095-1107, 1992.
    • (1992) Genomics , vol.13 , pp. 1095-1107
    • Larsen, F.1    Gundersen, G.2    Lopez, R.3    Prydz, H.4
  • 50
    • 0034989106 scopus 로고    scopus 로고
    • Thioredoxin fold as homodimerization module in the putative chaperone ERp29. NMR structures of the domains and experimental model of the 51 kDa dimer
    • Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, and Mkrtchian S. Thioredoxin fold as homodimerization module in the putative chaperone ERp29. NMR structures of the domains and experimental model of the 51 kDa dimer. Structure 9: 457-471, 2001.
    • (2001) Structure , vol.9 , pp. 457-471
    • Liepinsh, E.1    Baryshev, M.2    Sharipo, A.3    Ingelman-Sundberg, M.4    Otting, G.5    Mkrtchian, S.6
  • 51
    • 0242497806 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein
    • Ma Q, Guo C, Barnewitz K, Sheldrick GM, Soling HD, Uson I, and Ferrari DM. Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein. J Biol Chem 278: 44600-44607, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 44600-44607
    • Ma, Q.1    Guo, C.2    Barnewitz, K.3    Sheldrick, G.M.4    Soling, H.D.5    Uson, I.6    Ferrari, D.M.7
  • 52
    • 3843070861 scopus 로고    scopus 로고
    • ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain
    • MacLeod JC, Sayer RJ, Lucocq JM, and Hubbard MJ. ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain. J Comp Neurol 477: 29-42, 2004.
    • (2004) J Comp Neurol , vol.477 , pp. 29-42
    • MacLeod, J.C.1    Sayer, R.J.2    Lucocq, J.M.3    Hubbard, M.J.4
  • 53
    • 26944450514 scopus 로고    scopus 로고
    • ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • Magnuson B, Rainey EK, Benjamin T, Baryshev M, Mkrtchian S, and Tsai B. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol Cell 20: 289-300, 2005.
    • (2005) Mol Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3    Baryshev, M.4    Mkrtchian, S.5    Tsai, B.6
  • 54
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin JL. Thioredoxin-a fold for all reasons. Structure 3: 245-250, 1995.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 55
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin JL, Bardwell JC, and Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365: 464-468, 1993.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 57
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, and Hendershot LM. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 59
    • 0032518585 scopus 로고    scopus 로고
    • A stress-inducible rat liver endoplasmic reticulum protein, ERp29
    • Mkrtchian S, Fang C, Hellman U, and Ingelman-Sundberg M. A stress-inducible rat liver endoplasmic reticulum protein, ERp29. Eur J Biochem 251: 304-313, 1998.
    • (1998) Eur J Biochem , vol.251 , pp. 304-313
    • Mkrtchian, S.1    Fang, C.2    Hellman, U.3    Ingelman-Sundberg, M.4
  • 60
    • 0033782873 scopus 로고    scopus 로고
    • Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase
    • Monnat J, Neuhaus EM, Pop MS, Ferrari DM, Kramer B, and Soldati T. Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase. Mol Biol Cell 11: 3469-3484, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 3469-3484
    • Monnat, J.1    Neuhaus, E.M.2    Pop, M.S.3    Ferrari, D.M.4    Kramer, B.5    Soldati, T.6
  • 61
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori K. Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101: 451-454, 2000.
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 63
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S and Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48: 899-907, 1987.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 64
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano N, Orengo CA, and Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J Mol Biol 321: 741-765, 2002.
    • (2002) J Mol Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 66
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, and Sitia R. Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275: 23685-23692, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 67
    • 0034650343 scopus 로고    scopus 로고
    • Crystal structure of RNA 3′-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology
    • Palm GJ, Billy E, Filipowicz W, and Wlodawer A. Crystal structure of RNA 3′-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology. Structure 8: 13-23, 2000.
    • (2000) Structure , vol.8 , pp. 13-23
    • Palm, G.J.1    Billy, E.2    Filipowicz, W.3    Wlodawer, A.4
  • 68
    • 0028977988 scopus 로고
    • Mutant (delta F508) cystic fibrosis transmembrane conductance regulator Cl- channel is functional when retained in endoplasmic reticulum of mammalian cells
    • Pasyk EA and Foskett JK. Mutant (delta F508) cystic fibrosis transmembrane conductance regulator Cl- channel is functional when retained in endoplasmic reticulum of mammalian cells. J Biol Chem 270: 12347-12350, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 12347-12350
    • Pasyk, E.A.1    Foskett, J.K.2
  • 69
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil C and Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13: 349-355, 2001.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 70
    • 0023303619 scopus 로고
    • Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi T, Helaakoski T, Tasanen K, Myllyla R, Huhtala ML, Koivu J, and Kivirikko KI. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J 6: 643-649, 1987.
    • (1987) EMBO J , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 72
    • 0037274724 scopus 로고    scopus 로고
    • Beta-propellers: Associated functions and their role in human diseases
    • Pons T, Gomez R, Chinea G, and Valencia A. Beta-propellers: associated functions and their role in human diseases. Curr Med Chem 10: 505-524, 2003.
    • (2003) Curr Med Chem , vol.10 , pp. 505-524
    • Pons, T.1    Gomez, R.2    Chinea, G.3    Valencia, A.4
  • 73
    • 0025986514 scopus 로고
    • Transcription from a TATA-less promoter requires a multisubunit TFIID complex
    • Pugh BF and Tjian R. Transcription from a TATA-less promoter requires a multisubunit TFIID complex. Genes Dev 5: 1935-1945, 1991.
    • (1991) Genes Dev , vol.5 , pp. 1935-1945
    • Pugh, B.F.1    Tjian, R.2
  • 74
    • 0027468652 scopus 로고
    • Contribution of sequences downstream of the TATA element to a protein-DNA complex containing the TATA-binding protein
    • Purnell BA and Gilmour DS. Contribution of sequences downstream of the TATA element to a protein-DNA complex containing the TATA-binding protein. Mol Cell Biol 13: 2593-2603, 1993.
    • (1993) Mol Cell Biol , vol.13 , pp. 2593-2603
    • Purnell, B.A.1    Gilmour, D.S.2
  • 75
    • 0030585150 scopus 로고    scopus 로고
    • The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal
    • Qin J, Clore GM, Kennedy WP, Kuszewski J, and Gronenborn AM. The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure 4: 613-620, 1996.
    • (1996) Structure , vol.4 , pp. 613-620
    • Qin, J.1    Clore, G.M.2    Kennedy, W.P.3    Kuszewski, J.4    Gronenborn, A.M.5
  • 76
    • 0031816805 scopus 로고    scopus 로고
    • A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
    • Ren B, Tibbelin G, de Pascale D, Rossi M, Bartolucci S, and Ladenstein R. A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units. Nat Struct Biol 5: 602-611, 1998.
    • (1998) Nat Struct Biol , vol.5 , pp. 602-611
    • Ren, B.1    Tibbelin, G.2    De Pascale, D.3    Rossi, M.4    Bartolucci, S.5    Ladenstein, R.6
  • 77
    • 0033607476 scopus 로고    scopus 로고
    • Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein
    • Reuter K, Nottrott S, Fabrizio P, Luhrmann R, and Ficner R. Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein. J Mol Biol 294: 515-525, 1999.
    • (1999) J Mol Biol , vol.294 , pp. 515-525
    • Reuter, K.1    Nottrott, S.2    Fabrizio, P.3    Luhrmann, R.4    Ficner, R.5
  • 78
    • 0037018773 scopus 로고    scopus 로고
    • Endoplasmic reticulum storage diseases
    • Rutishauser J and Spiess M. Endoplasmic reticulum storage diseases. Swiss Med Wkly 132: 211-222, 2002.
    • (2002) Swiss Med Wkly , vol.132 , pp. 211-222
    • Rutishauser, J.1    Spiess, M.2
  • 79
    • 0029645581 scopus 로고
    • Crystal structure of thioredoxin-2 from Anabaena
    • Saarinen M, Gleason FK, and Eklund H. Crystal structure of thioredoxin-2 from Anabaena. Structure 3: 1097-1108, 1995.
    • (1995) Structure , vol.3 , pp. 1097-1108
    • Saarinen, M.1    Gleason, F.K.2    Eklund, H.3
  • 80
    • 0037138390 scopus 로고    scopus 로고
    • Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29
    • Sargsyan E, Baryshev M, Backlund M, Sharipo A, and Mkrtchian S. Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29. Gene 285: 127-139, 2002.
    • (2002) Gene , vol.285 , pp. 127-139
    • Sargsyan, E.1    Baryshev, M.2    Backlund, M.3    Sharipo, A.4    Mkrtchian, S.5
  • 81
    • 6044255043 scopus 로고    scopus 로고
    • The physiological unfolded protein response in the thyroid epithelial cells
    • Sargsyan E, Baryshev M, and Mkrtchian S. The physiological unfolded protein response in the thyroid epithelial cells. Biochem Biophys Res Commun 322: 570-576, 2004.
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 570-576
    • Sargsyan, E.1    Baryshev, M.2    Mkrtchian, S.3
  • 82
    • 0037053397 scopus 로고    scopus 로고
    • Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex
    • Sargsyan E, Baryshev M, Szekely L, Sharipo A, and Mkrtchian S. Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex. J Biol Chem 277: 17009-17015, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 17009-17015
    • Sargsyan, E.1    Baryshev, M.2    Szekely, L.3    Sharipo, A.4    Mkrtchian, S.5
  • 83
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman DM, Schmid SL, Braell WA, and Rothman JE. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 99: 723-733, 1984.
    • (1984) J Cell Biol , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 84
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza JC, Hardwick KG, Dean N, and Pelham HR. ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61: 1349-1357, 1990.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 85
    • 0034524031 scopus 로고    scopus 로고
    • Windbeutel is required for function and correct subcellular localization of the Drosophila patterning protein Pipe
    • Sen J, Goltz JS, Konsolaki M, Schupbach T, and Stein D. Windbeutel is required for function and correct subcellular localization of the Drosophila patterning protein Pipe. Development 127: 5541-5550, 2000.
    • (2000) Development , vol.127 , pp. 5541-5550
    • Sen, J.1    Goltz, J.S.2    Konsolaki, M.3    Schupbach, T.4    Stein, D.5
  • 86
    • 0036200181 scopus 로고    scopus 로고
    • ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production
    • Shnyder SD and Hubbard MJ. ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production. J Histochem Cytochem 50: 557-566, 2002.
    • (2002) J Histochem Cytochem , vol.50 , pp. 557-566
    • Shnyder, S.D.1    Hubbard, M.J.2
  • 87
    • 19244365393 scopus 로고    scopus 로고
    • Stress, protein (mis)folding, and signaling: The redox onnection
    • Sitia R and Molteni SN. Stress, protein (mis)folding, and signaling: the redox onnection. Sci STKE 2004: pe27, 2004.
    • (2004) Sci STKE , vol.2004
    • Sitia, R.1    Molteni, S.N.2
  • 89
    • 0022536553 scopus 로고
    • Stress protein systems of mammalian cells
    • Subjeck JR and Shyy TT. Stress protein systems of mammalian cells. Am J Physiol 250: C1-C17, 1986.
    • (1986) Am J Physiol , vol.250
    • Subjeck, J.R.1    Shyy, T.T.2
  • 90
    • 0023815684 scopus 로고
    • Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase
    • Tasanen K, Parkkonen T, Chow LT, Kivirikko KI, and Pihlajaniemi T. Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. J Biol Chem 263: 16218-16224, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 16218-16224
    • Tasanen, K.1    Parkkonen, T.2    Chow, L.T.3    Kivirikko, K.I.4    Pihlajaniemi, T.5
  • 92
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai B, Rodighiero C, Lencer WI, and Rapoport TA. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104: 937-948, 2001.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 94
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu BP, Ho-Schleyer SC, Travers KJ, and Weissman JS. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290: 1571-1574, 2000.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 95
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken E, Romijn EP, Maggioni C, Mezghrani A, Sitia R, Braakman I, and Heck AJ. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 18: 243-253, 2003.
    • (2003) Immunity , vol.18 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.7
  • 96
    • 0032432034 scopus 로고    scopus 로고
    • Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone
    • Wang CC. Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone. Ann NY Acad Sci 864: 9-13, 1998.
    • (1998) Ann NY Acad Sci , vol.864 , pp. 9-13
    • Wang, C.C.1
  • 97
    • 0027136018 scopus 로고
    • Protein disulfide isomerase is both an enzyme and a chaperone
    • Wang CC and Tsou CL. Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J 7: 1515-1517, 1993.
    • (1993) FASEB J , vol.7 , pp. 1515-1517
    • Wang, C.C.1    Tsou, C.L.2
  • 98
    • 0031779532 scopus 로고    scopus 로고
    • Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
    • Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, and Kang CH. Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nat Struct Biol 5: 476-483, 1998.
    • (1998) Nat Struct Biol , vol.5 , pp. 476-483
    • Wang, S.1    Trumble, W.R.2    Liao, H.3    Wesson, C.R.4    Dunker, A.K.5    Kang, C.H.6
  • 99
    • 0030460813 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain
    • Wearsch PA and Nicchitta CV. Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain. Biochemistry 35: 16760-16769, 1996.
    • (1996) Biochemistry , vol.35 , pp. 16760-16769
    • Wearsch, P.A.1    Nicchitta, C.V.2
  • 100
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • Weichsel A, Gasdaska JR, Powis G, and Montfort WR. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4: 735-751, 1996.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 101
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau JR, Combs KA, Spinner SN, and Joiner BJ. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 265: 9801-9807, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 9801-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 103
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain
    • Witte S, Villalba M, Bi K, Liu Y, Isakov N, and Altman A. Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. J Biol Chem 275: 1902-1909, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 104
    • 0033769564 scopus 로고    scopus 로고
    • Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells
    • Wu CC, Howell KE, Neville MC, Yates JR, 3rd, and McManaman JL. Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells. Electrophoresis 21: 3470-3482, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 3470-3482
    • Wu, C.C.1    Howell, K.E.2    Neville, M.C.3    Yates III, J.R.4    McManaman, J.L.5
  • 105


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