메뉴 건너뛰기




Volumn 13, Issue 23, 2013, Pages 3001-3010

NAD+-Dependent Enzymes at the Endoplasmic Reticulum

Author keywords

ADP ribosyltransferase; ARTC; ARTD; Endoplasmic reticulum; Importin 1; NAD; Post translational modification; UPR

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; ADENOSINE TRIPHOSPHATE; CALNEXIN; CALRETICULIN; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; KARYOPHERIN BETA; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 16; NICOTINAMIDE NUCLEOTIDE; NICOTINAMIDE NUCLEOTIDE ADENYLYLTRANSFERASE; NICOTINAMIDE RIBOSIDE; NICOTINIC ACID; PEPTIDES AND PROTEINS; PROTEIN DISULFIDE ISOMERASE; PROTEIN IRE1; PROTEIN PERK; RYANODINE RECEPTOR; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; STRESS ACTIVATED PROTEIN KINASE; TRYPTOPHAN; UNCLASSIFIED DRUG; UNINDEXED DRUG; X BOX BINDING PROTEIN 1;

EID: 84888984794     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/15680266113136660214     Document Type: Article
Times cited : (15)

References (136)
  • 1
    • 0034023238 scopus 로고    scopus 로고
    • New functions of a long-known molecule. Emerging roles of NAD in cellular signaling
    • Ziegler, M. New functions of a long-known molecule. Emerging roles of NAD in cellular signaling. Eur. J. Biochem., 2000, 267(6), 1550-64.
    • (2000) Eur. J. Biochem , vol.267 , Issue.6 , pp. 1550-1564
    • Ziegler, M.1
  • 2
    • 1542346420 scopus 로고    scopus 로고
    • The new life of a centenarian: Signalling functions of NAD(P)
    • Berger, F.; Ramirez-Hernandez, M. H.; Ziegler, M. The new life of a centenarian: signalling functions of NAD(P). Trends. Biochem. Sci., 2004, 29(3), 111-8.
    • (2004) Trends. Biochem. Sci , vol.29 , Issue.3 , pp. 111-118
    • Berger, F.1    Ramirez-Hernandez, M.H.2    Ziegler, M.3
  • 3
    • 0142188258 scopus 로고    scopus 로고
    • NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor
    • Seman, M.; Adriouch, S.; Scheuplein, F.; Krebs, C.; Freese, D.; Glowacki, G.; Deterre, P.; Haag, F.; Koch-Nolte, F. NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor. Immunity, 2003, 19(4), 571-82.
    • (2003) Immunity , vol.19 , Issue.4 , pp. 571-582
    • Seman, M.1    Adriouch, S.2    Scheuplein, F.3    Krebs, C.4    Freese, D.5    Glowacki, G.6    Deterre, P.7    Haag, F.8    Koch-Nolte, F.9
  • 5
    • 25444495510 scopus 로고    scopus 로고
    • Physiological relevance of the endogenous mono-ADP-ribosylation of cellular proteins
    • Di Girolamo, M.; Dani, N.; Stilla, A.; Corda, D. Physiological relevance of the endogenous mono-ADP-ribosylation of cellular proteins. FEBS J., 2005, 272(18), 4565-75.
    • (2005) FEBS J , vol.272 , Issue.18 , pp. 4565-4575
    • Di Girolamo, M.1    Dani, N.2    Stilla, A.3    Corda, D.4
  • 7
    • 25144496904 scopus 로고    scopus 로고
    • The Sir 2 family of protein deacetylases
    • Denu, J. M. The Sir 2 family of protein deacetylases. Curr. Opin. Chem. Biol., 2005, 9(5), 431-40.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , Issue.5 , pp. 431-440
    • Denu, J.M.1
  • 11
    • 0037829279 scopus 로고    scopus 로고
    • Reconstructing eukaryotic NAD metabolism
    • Rongvaux, A.; Andris, F.; Van Gool, F.; Leo, O. Reconstructing eukaryotic NAD metabolism. Bioessays, 2003, 25(7), 683-90.
    • (2003) Bioessays , vol.25 , Issue.7 , pp. 683-690
    • Rongvaux, A.1    Andris, F.2    Van Gool, F.3    Leo, O.4
  • 12
    • 1942485497 scopus 로고    scopus 로고
    • Structure and enzymology of ADP-ribosyl cyclases: Conserved enzymes that produce multiple calcium mobilizing metabolites
    • Schuber, F.; Lund, F. E. Structure and enzymology of ADP-ribosyl cyclases: conserved enzymes that produce multiple calcium mobilizing metabolites. Curr. Mol. Med., 2004, 4(3), 249-61.
    • (2004) Curr. Mol. Med , vol.4 , Issue.3 , pp. 249-261
    • Schuber, F.1    Lund, F.E.2
  • 14
    • 77049143681 scopus 로고
    • Inhibition of spleen diphosphopyridine nucleotidase by nicotinamide, an exchange reaction
    • Zatman, L. J.; Kaplan, N. O.; Colowick, S. P. Inhibition of spleen diphosphopyridine nucleotidase by nicotinamide, an exchange reaction. J. Biol. Chem., 1953, 200(1), 197-212.
    • (1953) J. Biol. Chem , vol.200 , Issue.1 , pp. 197-212
    • Zatman, L.J.1    Kaplan, N.O.2    Colowick, S.P.3
  • 16
    • 70449212074 scopus 로고
    • Biosynthesis of diphosphopyridine nucleotide. I. Identification of intermediates
    • Preiss, J.; Handler, P. Biosynthesis of diphosphopyridine nucleotide. I. Identification of intermediates. J. Biol. Chem., 1958, 233(2), 488-92.
    • (1958) J. Biol. Chem , vol.233 , Issue.2 , pp. 488-492
    • Preiss, J.1    Handler, P.2
  • 17
    • 2342550554 scopus 로고    scopus 로고
    • + in fungi and humans
    • + in fungi and humans. Cell, 2004, 117(4), 495-502.
    • (2004) Cell , vol.117 , Issue.4 , pp. 495-502
    • Bieganowski, P.1    Brenner, C.2
  • 18
    • 27744501798 scopus 로고    scopus 로고
    • Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms
    • Berger, F.; Lau, C.; Dahlmann, M.; Ziegler, M. Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J. Biol. Chem., 2005, 280(43), 36334-41.
    • (2005) J. Biol. Chem , vol.280 , Issue.43 , pp. 36334-36341
    • Berger, F.1    Lau, C.2    Dahlmann, M.3    Ziegler, M.4
  • 19
    • 84876987935 scopus 로고    scopus 로고
    • Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2
    • Milde, S.; Gilley, J.; Coleman, M. P. Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2. PLoS Biol., 2013, 11(4), e1001539.
    • (2013) PLoS Biol , vol.11 , Issue.4
    • Milde, S.1    Gilley, J.2    Coleman, M.P.3
  • 20
    • 34247278118 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1
    • Berger, F.; Lau, C.; Ziegler, M. Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1. Proc. Natl. Acad. Sci. U S A, 2007, 104(10), 3765-70.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , Issue.10 , pp. 3765-3770
    • Berger, F.1    Lau, C.2    Ziegler, M.3
  • 24
    • 78650071674 scopus 로고    scopus 로고
    • Expression, localization, and biochemical characterization of nicotinamide mononucleotide adenylyltransferase 2
    • Mayer, P. R.; Huang, N.; Dewey, C. M.; Dries, D. R.; Zhang, H.; Yu, G. Expression, localization, and biochemical characterization of nicotinamide mononucleotide adenylyltransferase 2. J. Biol. Chem., 2010, 285(51), 40387-96.
    • (2010) J. Biol. Chem , vol.285 , Issue.51 , pp. 40387-40396
    • Mayer, P.R.1    Huang, N.2    Dewey, C.M.3    Dries, D.R.4    Zhang, H.5    Yu, G.6
  • 25
    • 75849118659 scopus 로고    scopus 로고
    • Visualization of subcellular NAD pools and intra-organellar protein localization by poly-ADP-ribose formation
    • Dolle, C.; Niere, M.; Lohndal, E.; Ziegler, M. Visualization of subcellular NAD pools and intra-organellar protein localization by poly-ADP-ribose formation. Cell. Mol. Life Sci., 2010, 67(3), 433-43.
    • (2010) Cell. Mol. Life Sci , vol.67 , Issue.3 , pp. 433-443
    • Dolle, C.1    Niere, M.2    Lohndal, E.3    Ziegler, M.4
  • 27
    • 79955505833 scopus 로고    scopus 로고
    • Peroxisome assembly: Matrix and membrane protein biogenesis
    • Ma, C.; Agrawal, G.; Subramani, S. Peroxisome assembly: matrix and membrane protein biogenesis. J. Cell. Biol., 2011, 193(1), 7-16.
    • (2011) J. Cell. Biol , vol.193 , Issue.1 , pp. 7-16
    • Ma, C.1    Agrawal, G.2    Subramani, S.3
  • 28
    • 0027225636 scopus 로고
    • Isolation and the complete amino acid sequence of lumenal endoplasmic reticulum glucose-6-phosphate dehydrogenase
    • Ozols, J. Isolation and the complete amino acid sequence of lumenal endoplasmic reticulum glucose-6-phosphate dehydrogenase. Proc. Natl. Acad. Sci. U S A, 1993, 90(11), 5302-6.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , Issue.11 , pp. 5302-5306
    • Ozols, J.1
  • 29
    • 77952527006 scopus 로고    scopus 로고
    • Contribution of hexose-6-phosphate dehydrogenase to NADPH content and redox environment in the endoplasmic reticulum
    • Rogoff, D.; Black, K.; McMillan, D. R.; White, P. C. Contribution of hexose-6-phosphate dehydrogenase to NADPH content and redox environment in the endoplasmic reticulum. Redox. Rep., 2010, 15(2), 64-70.
    • (2010) Redox. Rep , vol.15 , Issue.2 , pp. 64-70
    • Rogoff, D.1    Black, K.2    McMillan, D.R.3    White, P.C.4
  • 30
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann, O.; Walz, B. Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int. Rev. Cytol., 2001, 205, 149-214.
    • (2001) Int. Rev. Cytol , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 31
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz, G. K.; Rolls, M. M.; Rapoport, T. A. Structural organization of the endoplasmic reticulum. EMBO Rep., 2002, 3(10), 944-50.
    • (2002) EMBO Rep , vol.3 , Issue.10 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 32
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: Spatial organization of the endoplasmic reticulum-mitochondria relationship
    • de Brito, O. M.; Scorrano, L. An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. Embo J., 2010, 29(16), 2715-23.
    • (2010) Embo J , vol.29 , Issue.16 , pp. 2715-2723
    • de Brito, O.M.1    Scorrano, L.2
  • 34
    • 67649947773 scopus 로고    scopus 로고
    • Sizing up the nucleus: Nuclear shape, size and nuclear-envelope assembly
    • Webster, M.; Witkin, K. L.; Cohen-Fix, O. Sizing up the nucleus: nuclear shape, size and nuclear-envelope assembly. J. Cell. Sci., 2009, 122(Pt 10), 1477-86.
    • (2009) J. Cell. Sci , vol.122 , Issue.PART 10 , pp. 1477-1486
    • Webster, M.1    Witkin, K.L.2    Cohen-Fix, O.3
  • 35
    • 66349117317 scopus 로고    scopus 로고
    • Membrane phospholipid synthesis and endoplasmic reticulum function
    • Fagone, P.; Jackowski, S. Membrane phospholipid synthesis and endoplasmic reticulum function. J. Lipid Res., 2009, 50 Suppl, S311-6.
    • (2009) J. Lipid Res , vol.50 , Issue.SUPPL. , pp. 311-316
    • Fagone, P.1    Jackowski, S.2
  • 37
    • 75749134145 scopus 로고    scopus 로고
    • N-glycan structures: Recognition and processing in the ER
    • Aebi, M.; Bernasconi, R.; Clerc, S.; Molinari, M. N-glycan structures: recognition and processing in the ER. Trends Biochem. Sci., 2010, 35(2), 74-82.
    • (2010) Trends Biochem. Sci , vol.35 , Issue.2 , pp. 74-82
    • Aebi, M.1    Bernasconi, R.2    Clerc, S.3    Molinari, M.4
  • 38
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky, J. L. Cleaning up: ER-associated degradation to the rescue. Cell, 2012, 151(6), 1163-7.
    • (2012) Cell , vol.151 , Issue.6 , pp. 1163-1167
    • Brodsky, J.L.1
  • 39
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith, M. H.; Ploegh, H. L.; Weissman, J. S. Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science, 2011, 334(6059), 1086-90.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 40
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar, S. S.; Brodsky, J. L. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell. Biol., 2008, 9(12), 944-57.
    • (2008) Nat. Rev. Mol. Cell. Biol , vol.9 , Issue.12 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 41
    • 77951177952 scopus 로고    scopus 로고
    • The UPR and cell fate at a glance
    • Merksamer, P. I.; Papa, F. R. The UPR and cell fate at a glance. J. Cell. Sci., 2010, 123(Pt 7), 1003-6.
    • (2010) J. Cell. Sci , vol.123 , Issue.PART 7 , pp. 1003-1006
    • Merksamer, P.I.1    Papa, F.R.2
  • 42
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P.; Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science, 2011, 334(6059), 1081-6.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 43
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D.; Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell. Biol., 2007, 8(7), 519-29.
    • (2007) Nat. Rev. Mol. Cell. Biol , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 44
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A.; Zhang, Y.; Hendershot, L. M.; Harding, H. P.; Ron, D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol., 2000, 2(6), 326-32.
    • (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
  • 45
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P.; Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science, 2011, 334(6059), 1081-6.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 46
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P.; Zhang, Y.; Ron, D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature, 1999, 397(6716), 271-4.
    • (1999) Nature , vol.397 , Issue.6716 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 47
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding, H. P.; Zhang, Y.; Bertolotti, A.; Zeng, H.; Ron, D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell., 2000, 5(5), 897-904.
    • (2000) Mol. Cell , vol.5 , Issue.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 48
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer, J. W.; Diehl, J. A. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl. Acad. Sci. U S A, 2000, 97(23), 12625-30.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , Issue.23 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 49
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J.; Chen, X.; Hendershot, L.; Prywes, R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell., 2002, 3(1), 99-111.
    • (2002) Dev. Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 50
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H.; Matsui, T.; Yamamoto, A.; Okada, T.; Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell, 2001, 107(7), 881-91.
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 51
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M.; Zeng, H.; Urano, F.; Till, J. H.; Hubbard, S. R.; Harding, H. P.; Clark, S. G.; Ron, D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature, 2002, 415(6867), 92-6.
    • (2002) Nature , vol.415 , Issue.6867 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 52
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze, K.; Yoshida, H.; Yanagi, H.; Yura, T.; Mori, K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell, 1999, 10(11), 3787-99.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.11 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 53
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma, Y.; Brewer, J. W.; Diehl, J. A.; Hendershot, L. M. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol., 2002, 318(5), 1351-65.
    • (2002) J. Mol. Biol , vol.318 , Issue.5 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 55
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6ooand XBP1
    • Yamamoto, K.; Sato, T.; Matsui, T.; Sato, M.; Okada, T.; Yoshida, H.; Harada, A.; Mori, K. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6ooand XBP1. Dev. Cell, 2007, 13(3), 365-76.
    • (2007) Dev. Cell , vol.13 , Issue.3 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 57
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano, F.; Wang, X.; Bertolotti, A.; Zhang, Y.; Chung, P.; Harding, H. P.; Ron, D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science, 2000, 287(5453), 664-6.
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 58
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H.; Matsuzawa, A.; Tobiume, K.; Saegusa, K.; Takeda, K.; Inoue, K.; Hori, S.; Kakizuka, A.; Ichijo, H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev., 2002, 16(11), 1345-55.
    • (2002) Genes Dev , vol.16 , Issue.11 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 59
    • 0028110180 scopus 로고
    • BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum
    • Haas, I. G. BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum. Experientia, 1994, 50(11-12), 1012-20.
    • (1994) Experientia , vol.50 , Issue.11-12 , pp. 1012-1020
    • Haas, I.G.1
  • 60
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M.; Kaufman, R. J. The mammalian unfolded protein response. Annu. Rev. Biochem., 2005, 74, 739-89.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 61
    • 0032897211 scopus 로고    scopus 로고
    • The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing
    • Laitusis, A. L.; Brostrom, M. A.; Brostrom, C. O. The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing. J. Biol. Chem., 1999, 274(1), 486-93.
    • (1999) J. Biol. Chem , vol.274 , Issue.1 , pp. 486-493
    • Laitusis, A.L.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 62
    • 0028134743 scopus 로고
    • ADP-ribosylation of the molecular chaperone GRP78/BiP
    • Ledford, B. E.; Leno, G. H. ADP-ribosylation of the molecular chaperone GRP78/BiP. Mol. Cell. Biochem., 1994, 138(1-2), 141-8.
    • (1994) Mol. Cell. Biochem , vol.138 , Issue.1-2 , pp. 141-148
    • Ledford, B.E.1    Leno, G.H.2
  • 63
    • 0026567520 scopus 로고
    • Interconversion of three differentially modified and assembled forms of BiP
    • Freiden, P. J.; Gaut, J. R.; Hendershot, L. M. Interconversion of three differentially modified and assembled forms of BiP. Embo J., 1992, 11(1), 63-70.
    • (1992) Embo J , vol.11 , Issue.1 , pp. 63-70
    • Freiden, P.J.1    Gaut, J.R.2    Hendershot, L.M.3
  • 64
    • 0026487216 scopus 로고
    • Interconversion of GRP78/BiP. A novel event in the action of Pasteurella multocida toxin, bombesin, and platelet-derived growth factor
    • Staddon, J. M.; Bouzyk, M. M.; Rozengurt, E. Interconversion of GRP78/BiP. A novel event in the action of Pasteurella multocida toxin, bombesin, and platelet-derived growth factor. J. Biol. Chem., 1992, 267(35), 25239-45.
    • (1992) J. Biol. Chem , vol.267 , Issue.35 , pp. 25239-25245
    • Staddon, J.M.1    Bouzyk, M.M.2    Rozengurt, E.3
  • 65
    • 0025674402 scopus 로고
    • Reversible ADP-ribosylation of the 78 kDa glucose-regulated protein
    • Leno, G. H.; Ledford, B. E. Reversible ADP-ribosylation of the 78 kDa glucose-regulated protein. FEBS Lett., 1990, 276(1-2), 29-33.
    • (1990) FEBS Lett , vol.276 , Issue.1-2 , pp. 29-33
    • Leno, G.H.1    Ledford, B.E.2
  • 66
    • 0024846211 scopus 로고
    • ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress
    • Leno, G. H.; Ledford, B. E. ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress. Eur. J. Biochem., 1989, 186(1-2), 205-11.
    • (1989) Eur. J. Biochem , vol.186 , Issue.1-2 , pp. 205-211
    • Leno, G.H.1    Ledford, B.E.2
  • 67
    • 84866455655 scopus 로고    scopus 로고
    • ADP-ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load
    • Chambers, J. E.; Petrova, K.; Tomba, G.; Vendruscolo, M.; Ron, D. ADP-ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load. J. Cell. Biol., 2012, 198(3), 371-85.
    • (2012) J. Cell. Biol , vol.198 , Issue.3 , pp. 371-385
    • Chambers, J.E.1    Petrova, K.2    Tomba, G.3    Vendruscolo, M.4    Ron, D.5
  • 68
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt, G.; Ford, E.; Kurtev, M.; Guarente, L. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem., 2005, 280(22), 21313-20.
    • (2005) J. Biol. Chem , vol.280 , Issue.22 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 69
    • 84886686038 scopus 로고    scopus 로고
    • Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins
    • Feldman, J. L.; Baeza, J.; Denu, J. M. Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins. J. Biol. Chem., 2013, 288(43), 31350-6.
    • (2013) J. Biol. Chem , vol.288 , Issue.43 , pp. 31350-31356
    • Feldman, J.L.1    Baeza, J.2    Denu, J.M.3
  • 70
    • 0028981421 scopus 로고
    • The family of bacterial ADPribosylating exotoxins
    • Krueger, K. M.; Barbieri, J. T. The family of bacterial ADPribosylating exotoxins. Clin. Microbiol. Rev., 1995, 8(1), 34-47.
    • (1995) Clin. Microbiol. Rev , vol.8 , Issue.1 , pp. 34-47
    • Krueger, K.M.1    Barbieri, J.T.2
  • 72
    • 0032797983 scopus 로고    scopus 로고
    • Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases
    • Okazaki, I. J.; Moss, J. Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases. Annu. Rev. Nutr., 1999, 19, 485-509.
    • (1999) Annu. Rev. Nutr , vol.19 , pp. 485-509
    • Okazaki, I.J.1    Moss, J.2
  • 74
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages
    • Domenighini, M.; Rappuoli, R. Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Mol. Microbiol., 1996, 21(4), 667-74.
    • (1996) Mol. Microbiol , vol.21 , Issue.4 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 75
    • 0028138580 scopus 로고
    • Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins
    • Domenighini, M.; Magagnoli, C.; Pizza, M.; Rappuoli, R. Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins. Mol. Microbiol., 1994, 14(1), 41-50.
    • (1994) Mol. Microbiol , vol.14 , Issue.1 , pp. 41-50
    • Domenighini, M.1    Magagnoli, C.2    Pizza, M.3    Rappuoli, R.4
  • 77
    • 0031081726 scopus 로고    scopus 로고
    • Two novel human members of an emerging mammalian gene family related to mono-ADP-ribosylating bacterial toxins
    • Koch-Nolte, F.; Haag, F.; Braren, R.; Kuhl, M.; Hoovers, J.; Balasubramanian, S.; Bazan, F.; Thiele, H. G. Two novel human members of an emerging mammalian gene family related to mono-ADP-ribosylating bacterial toxins. Genomics, 1997, 39(3), 370-6.
    • (1997) Genomics , vol.39 , Issue.3 , pp. 370-376
    • Koch-Nolte, F.1    Haag, F.2    Braren, R.3    Kuhl, M.4    Hoovers, J.5    Balasubramanian, S.6    Bazan, F.7    Thiele, H.G.8
  • 79
    • 0027331555 scopus 로고
    • Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells
    • Zolkiewska, A.; Moss, J. Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem., 1993, 268(34), 25273-6.
    • (1993) J. Biol. Chem , vol.268 , Issue.34 , pp. 25273-25276
    • Zolkiewska, A.1    Moss, J.2
  • 80
    • 0032508689 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases
    • Okazaki, I. J.; Moss, J. Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases. J. Biol. Chem., 1998, 273(37), 23617-20.
    • (1998) J. Biol. Chem , vol.273 , Issue.37 , pp. 23617-23620
    • Okazaki, I.J.1    Moss, J.2
  • 81
    • 0037881920 scopus 로고    scopus 로고
    • Functional aspects of protein mono-ADP-ribosylation
    • Corda, D.; Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J., 2003, 22(9), 1953-8.
    • (2003) EMBO J , vol.22 , Issue.9 , pp. 1953-1958
    • Corda, D.1    Di Girolamo, M.2
  • 82
    • 0037126639 scopus 로고    scopus 로고
    • Mono-ADP-ribosylation: A tool for modulating immune response and cell signaling
    • Corda, D.; Di Girolamo, M. Mono-ADP-ribosylation: a tool for modulating immune response and cell signaling. Sci. STKE, 2002(163), PE53.
    • (2002) Sci. STKE , Issue.163
    • Corda, D.1    Di Girolamo, M.2
  • 83
    • 33749989623 scopus 로고    scopus 로고
    • Human alpha-defensins neutralize toxins of the mono-ADPribosyltransferase family
    • Kim, C.; Slavinskaya, Z.; Merrill, A. R.; Kaufmann, S. H. Human alpha-defensins neutralize toxins of the mono-ADPribosyltransferase family. Biochem. J., 2006, 399(2), 225-9.
    • (2006) Biochem. J , vol.399 , Issue.2 , pp. 225-229
    • Kim, C.1    Slavinskaya, Z.2    Merrill, A.R.3    Kaufmann, S.H.4
  • 84
    • 1842430537 scopus 로고    scopus 로고
    • Ecto-ADPribosyltransferases (ARTs): Emerging actors in cell communication and signaling
    • Seman, M.; Adriouch, S.; Haag, F.; Koch-Nolte, F. Ecto-ADPribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr. Med. Chem., 2004, 11(7), 857-72.
    • (2004) Curr. Med. Chem , vol.11 , Issue.7 , pp. 857-872
    • Seman, M.1    Adriouch, S.2    Haag, F.3    Koch-Nolte, F.4
  • 86
    • 63149116496 scopus 로고    scopus 로고
    • Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
    • Dani, N.; Stilla, A.; Marchegiani, A.; Tamburro, A.; Till, S.; Ladurner, A. G.; Corda, D.; Di Girolamo, M. Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proc. Natl. Acad. Sci. U S A, 2009, 106(11), 4243-8.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , Issue.11 , pp. 4243-4248
    • Dani, N.1    Stilla, A.2    Marchegiani, A.3    Tamburro, A.4    Till, S.5    Ladurner, A.G.6    Corda, D.7    Di Girolamo, M.8
  • 87
    • 0027198328 scopus 로고
    • Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase
    • Takada, T.; Iida, K.; Moss, J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem., 1993, 268(24), 17837-43.
    • (1993) J. Biol. Chem , vol.268 , Issue.24 , pp. 17837-17843
    • Takada, T.1    Iida, K.2    Moss, J.3
  • 88
    • 0031010494 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase
    • Lin, W.; Ame, J. C.; Aboul-Ela, N.; Jacobson, E. L.; Jacobson, M. K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem., 1997, 272(18), 11895-901.
    • (1997) J. Biol. Chem , vol.272 , Issue.18 , pp. 11895-11901
    • Lin, W.1    Ame, J.C.2    Aboul-Ela, N.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 89
    • 84860844237 scopus 로고    scopus 로고
    • ADP-Ribosylhydrolase 3 (ARH3), not Poly-ADP-Ribose Glycohydrolase (PARG) Isoforms, are Responsible for Degradation of Mitochondrial Matrix-Associated Poly-ADP-Ribose
    • Niere, M.; Mashimo, M.; Agledal, L.; Doelle, C.; Kasamatsu, A.; Kato, J.; Moss, J.; Ziegler, M. ADP-Ribosylhydrolase 3 (ARH3), not Poly-ADP-Ribose Glycohydrolase (PARG) Isoforms, are Responsible for Degradation of Mitochondrial Matrix-Associated Poly-ADP-Ribose. J. Biol. Chem., 2012, 287(20), 16088-16102.
    • (2012) J. Biol. Chem , vol.287 , Issue.20 , pp. 16088-16102
    • Niere, M.1    Mashimo, M.2    Agledal, L.3    Doelle, C.4    Kasamatsu, A.5    Kato, J.6    Moss, J.7    Ziegler, M.8
  • 91
    • 33750940806 scopus 로고    scopus 로고
    • The 39-kDa poly(ADPribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
    • Ono, T.; Kasamatsu, A.; Oka, S.; Moss, J. The 39-kDa poly(ADPribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases. Proc. Natl. Acad. Sci. U S A, 2006, 103(45), 16687-91.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , Issue.45 , pp. 16687-16691
    • Ono, T.1    Kasamatsu, A.2    Oka, S.3    Moss, J.4
  • 92
    • 84880324619 scopus 로고    scopus 로고
    • Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology
    • Feijs, K. L.; Verheugd, P.; Luscher, B. Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology. Febs J., 2013, 280(15), 3519-29.
    • (2013) Febs J , vol.280 , Issue.15 , pp. 3519-3529
    • Feijs, K.L.1    Verheugd, P.2    Luscher, B.3
  • 95
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson, B. A.; Kraus, W. L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell. Biol., 2012, 13(7), 411-24.
    • (2012) Nat. Rev. Mol. Cell. Biol , vol.13 , Issue.7 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 96
    • 34548183836 scopus 로고    scopus 로고
    • Poly-ADP-ribosylation and cancer
    • Miwa, M.; Masutani, M. Poly-ADP-ribosylation and cancer. Cancer Sci., 2007, 98(10), 1528-35.
    • (2007) Cancer Sci , vol.98 , Issue.10 , pp. 1528-1535
    • Miwa, M.1    Masutani, M.2
  • 97
    • 79953651847 scopus 로고    scopus 로고
    • PARP-3, a DNA-dependent PARP with emerging roles in double-strand break repair and mitotic progression
    • Boehler, C.; Dantzer, F. PARP-3, a DNA-dependent PARP with emerging roles in double-strand break repair and mitotic progression. Cell Cycle, 2011, 10(7), 1023-4.
    • (2011) Cell Cycle , vol.10 , Issue.7 , pp. 1023-1024
    • Boehler, C.1    Dantzer, F.2
  • 98
    • 85047693635 scopus 로고    scopus 로고
    • Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
    • Chang, P.; Coughlin, M.; Mitchison, T. J. Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function. Nat. Cell Biol., 2005, 7(11), 1133-9.
    • (2005) Nat. Cell Biol , vol.7 , Issue.11 , pp. 1133-1139
    • Chang, P.1    Coughlin, M.2    Mitchison, T.J.3
  • 99
    • 0037379179 scopus 로고    scopus 로고
    • Involvement of poly(ADP-Ribose) polymerase 1 and poly(ADP-Ribosyl)ation in regulation of centrosome function
    • Kanai, M.; Tong, W. M.; Sugihara, E.; Wang, Z. Q.; Fukasawa, K.; Miwa, M. Involvement of poly(ADP-Ribose) polymerase 1 and poly(ADP-Ribosyl)ation in regulation of centrosome function. Mol. Cell. Biol., 2003, 23(7), 2451-62.
    • (2003) Mol. Cell. Biol , vol.23 , Issue.7 , pp. 2451-2462
    • Kanai, M.1    Tong, W.M.2    Sugihara, E.3    Wang, Z.Q.4    Fukasawa, K.5    Miwa, M.6
  • 102
    • 77649129121 scopus 로고    scopus 로고
    • GSK3: A multifaceted kinase in Wnt signaling
    • Wu, D.; Pan, W. GSK3: a multifaceted kinase in Wnt signaling. Trends Biochem. Sci., 2010, 35(3), 161-8.
    • (2010) Trends Biochem. Sci , vol.35 , Issue.3 , pp. 161-168
    • Wu, D.1    Pan, W.2
  • 104
    • 84862233980 scopus 로고    scopus 로고
    • PARP16/ARTD15 Is a Novel Endoplasmic-Reticulum-Associated Mono-ADP-ribosyltransferase that interacts with, and modifies Karyopherinm1
    • Di Paola, S.; Micaroni, M.; Di Tullio, G.; Buccione, R.; Di Girolamo, M. PARP16/ARTD15 Is a Novel Endoplasmic-Reticulum-Associated Mono-ADP-ribosyltransferase that interacts with, and modifies Karyopherinm1. PLoS ONE, 2012, 7(6), e37352.
    • (2012) PLoS ONE , vol.7 , Issue.6
    • Di Paola, S.1    Micaroni, M.2    Di Tullio, G.3    Buccione, R.4    Di Girolamo, M.5
  • 105
    • 33645243011 scopus 로고    scopus 로고
    • Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor
    • Goenka, S.; Boothby, M. Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor. Proc. Natl. Acad. Sci. U S A, 2006, 103(11), 4210-5.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , Issue.11 , pp. 4210-4215
    • Goenka, S.1    Boothby, M.2
  • 106
    • 84880333963 scopus 로고    scopus 로고
    • A role of intracellular mono-ADP-ribosylation in cancer biology
    • Scarpa, E. S.; Fabrizio, G.; Di Girolamo, M. A role of intracellular mono-ADP-ribosylation in cancer biology. Febs J., 2013, 280(15), 3551-62.
    • (2013) Febs J , vol.280 , Issue.15 , pp. 3551-3562
    • Scarpa, E.S.1    Fabrizio, G.2    Di Girolamo, M.3
  • 107
    • 84869094697 scopus 로고    scopus 로고
    • PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK-and IRE1alpha-mediated unfolded protein response
    • Jwa, M.; Chang, P. PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK-and IRE1alpha-mediated unfolded protein response. Nat. Cell Biol., 2012, 14(11), 1223-30.
    • (2012) Nat. Cell Biol , vol.14 , Issue.11 , pp. 1223-1230
    • Jwa, M.1    Chang, P.2
  • 108
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried, H.; Kutay, U. Nucleocytoplasmic transport: taking an inventory. Cell Mol Life Sci, 2003, 60(8), 1659-88.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.8 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 109
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • Conti, E.; Izaurralde, E. Nucleocytoplasmic transport enters the atomic age. Curr. Opin. Cell Biol., 2001, 13(3), 310-9.
    • (2001) Curr. Opin. Cell Biol , vol.13 , Issue.3 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 110
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Gorlich, D.; Prehn, S.; Laskey, R. A.; Hartmann, E. Isolation of a protein that is essential for the first step of nuclear protein import. Cell, 1994, 79(5), 767-78.
    • (1994) Cell , vol.79 , Issue.5 , pp. 767-778
    • Gorlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 111
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • Harel, A.; Forbes, D. J. Importin beta: conducting a much larger cellular symphony. Mol. Cell, 2004, 16(3), 319-30.
    • (2004) Mol. Cell , vol.16 , Issue.3 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 112
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani, G.; Petosa, C.; Weis, K.; Muller, C. W. Structure of importin-beta bound to the IBB domain of importin-alpha. Nature, 1999, 399(6733), 221-9.
    • (1999) Nature , vol.399 , Issue.6733 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 113
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Gorlich, D.; Kostka, S.; Kraft, R.; Dingwall, C.; Laskey, R. A.; Hartmann, E.; Prehn, S. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr. Biol., 1995, 5(4), 383-92.
    • (1995) Curr. Biol , vol.5 , Issue.4 , pp. 383-392
    • Gorlich, D.1    Kostka, S.2    Kraft, R.3    Dingwall, C.4    Laskey, R.A.5    Hartmann, E.6    Prehn, S.7
  • 115
    • 0037268889 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic transport of proteins as a target for therapeutic drugs
    • Yashiroda, Y.; Yoshida, M. Nucleo-cytoplasmic transport of proteins as a target for therapeutic drugs. Curr. Med. Chem., 2003, 10(9), 741-8.
    • (2003) Curr. Med. Chem , vol.10 , Issue.9 , pp. 741-748
    • Yashiroda, Y.1    Yoshida, M.2
  • 116
    • 14544272335 scopus 로고    scopus 로고
    • Regulation of nuclear transport: Central role in development and transformation?
    • Poon, I. K.; Jans, D. A. Regulation of nuclear transport: central role in development and transformation? Traffic, 2005, 6(3), 173-86.
    • (2005) Traffic , vol.6 , Issue.3 , pp. 173-186
    • Poon, I.K.1    Jans, D.A.2
  • 117
    • 33845414955 scopus 로고    scopus 로고
    • Controlling protein compartmentalization to overcome disease
    • Davis, J. R.; Kakar, M.; Lim, C. S. Controlling protein compartmentalization to overcome disease. Pharm. Res., 2007, 24(1), 17-27.
    • (2007) Pharm. Res , vol.24 , Issue.1 , pp. 17-27
    • Davis, J.R.1    Kakar, M.2    Lim, C.S.3
  • 118
    • 0019377631 scopus 로고
    • Synthesis and processing of asparaginelinked oligosaccharides
    • Hubbard, S. C.; Ivatt, R. J. Synthesis and processing of asparaginelinked oligosaccharides. Annu. Rev. Biochem., 1981, 50, 555-83.
    • (1981) Annu. Rev. Biochem , vol.50 , pp. 555-583
    • Hubbard, S.C.1    Ivatt, R.J.2
  • 119
    • 0035675962 scopus 로고    scopus 로고
    • The action of molecular chaperones in the early secretory pathway
    • Fewell, S. W.; Travers, K. J.; Weissman, J. S.; Brodsky, J. L. The action of molecular chaperones in the early secretory pathway. Annu. Rev. Genet., 2001, 35, 149-91.
    • (2001) Annu. Rev. Genet , vol.35 , pp. 149-191
    • Fewell, S.W.1    Travers, K.J.2    Weissman, J.S.3    Brodsky, J.L.4
  • 120
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang, K.; Kaufman, R. J. From endoplasmic-reticulum stress to the inflammatory response. Nature, 2008, 454(7203), 455-62.
    • (2008) Nature , vol.454 , Issue.7203 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 121
    • 80053176398 scopus 로고    scopus 로고
    • ImportinMMInteracts with the Endoplasmic Reticulum-associated Degradation Machinery and Promotes Ubiq uitination and Degradation of Mutant u1-Antitrypsin
    • Zhong, Y.; Wang, Y.; Yang, H.; Ballar, P.; Lee, J. G.; Ye, Y.; Monteiro, M. J.; Fang, S. ImportinMMInteracts with the Endoplasmic Reticulum-associated Degradation Machinery and Promotes Ubiq uitination and Degradation of Mutant u1-Antitrypsin. J. Biol. Chem., 2011, 286(39), 33921-30.
    • (2011) J. Biol. Chem , vol.286 , Issue.39 , pp. 33921-33930
    • Zhong, Y.1    Wang, Y.2    Yang, H.3    Ballar, P.4    Lee, J.G.5    Ye, Y.6    Monteiro, M.J.7    Fang, S.8
  • 122
    • 58149109602 scopus 로고    scopus 로고
    • GRP78: A chaperone with diverse roles beyond the endoplasmic reticulum
    • Quinones, Q. J.; de Ridder, G. G.; Pizzo, S. V. GRP78: a chaperone with diverse roles beyond the endoplasmic reticulum. Histol. Histopathol., 2008, 23(11), 1409-16.
    • (2008) Histol. Histopathol , vol.23 , Issue.11 , pp. 1409-1416
    • Quinones, Q.J.1    de Ridder, G.G.2    Pizzo, S.V.3
  • 123
    • 33646171070 scopus 로고    scopus 로고
    • Stress induction of GRP78/BiP and its role in cancer
    • Li, J.; Lee, A. S. Stress induction of GRP78/BiP and its role in cancer. Curr. Mol. Med., 2006, 6(1), 45-54.
    • (2006) Curr. Mol. Med , vol.6 , Issue.1 , pp. 45-54
    • Li, J.1    Lee, A.S.2
  • 124
    • 20444399528 scopus 로고    scopus 로고
    • Expression of endoplasmic reticulum molecular chaperone Grp78 in human lung cancer and its clinical significance
    • Uramoto, H.; Sugio, K.; Oyama, T.; Nakata, S.; Ono, K.; Yoshimastu, T.; Morita, M.; Yasumoto, K. Expression of endoplasmic reticulum molecular chaperone Grp78 in human lung cancer and its clinical significance. Lung Cancer, 2005, 49(1), 55-62.
    • (2005) Lung Cancer , vol.49 , Issue.1 , pp. 55-62
    • Uramoto, H.1    Sugio, K.2    Oyama, T.3    Nakata, S.4    Ono, K.5    Yoshimastu, T.6    Morita, M.7    Yasumoto, K.8
  • 125
    • 77955474897 scopus 로고    scopus 로고
    • Roles of GRP78 in physiology and cancer
    • Zhang, L. H.; Zhang, X. Roles of GRP78 in physiology and cancer. J. Cell. Biochem., 2010, 110(6), 1299-305.
    • (2010) J. Cell. Biochem , vol.110 , Issue.6 , pp. 1299-1305
    • Zhang, L.H.1    Zhang, X.2
  • 126
    • 0036837864 scopus 로고    scopus 로고
    • Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha
    • Koumenis, C.; Naczki, C.; Koritzinsky, M.; Rastani, S.; Diehl, A.; Sonenberg, N.; Koromilas, A.; Wouters, B. G. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha. Mol. Cell. Biol., 2002, 22(21), 7405-16.
    • (2002) Mol. Cell. Biol , vol.22 , Issue.21 , pp. 7405-7416
    • Koumenis, C.1    Naczki, C.2    Koritzinsky, M.3    Rastani, S.4    Diehl, A.5    Sonenberg, N.6    Koromilas, A.7    Wouters, B.G.8
  • 128
    • 33751179210 scopus 로고    scopus 로고
    • Targeting XBP-1 as a novel anti-cancer strategy
    • Koong, A. C.; Chauhan, V.; Romero-Ramirez, L. Targeting XBP-1 as a novel anti-cancer strategy. Cancer Biol. Ther., 2006, 5(7), 756-9.
    • (2006) Cancer Biol. Ther , vol.5 , Issue.7 , pp. 756-759
    • Koong, A.C.1    Chauhan, V.2    Romero-Ramirez, L.3
  • 130
    • 84883614839 scopus 로고    scopus 로고
    • Why Proteasome Inhibitors Cannot ERADicate Multiple Myeloma
    • Orlowski, R. Z. Why Proteasome Inhibitors Cannot ERADicate Multiple Myeloma. Cancer Cell, 2013, 24(3), 275-7.
    • (2013) Cancer Cell , vol.24 , Issue.3 , pp. 275-277
    • Orlowski, R.Z.1
  • 131
    • 84883625365 scopus 로고    scopus 로고
    • Xbp1snegative tumor B cells and pre-plasmablasts mediate therapeutic proteasome inhibitor resistance in multiple myeloma
    • Leung-Hagesteijn, C.; Erdmann, N.; Cheung, G.; Keats, J. J.; Stewart, A. K.; Reece, D. E.; Chung, K. C.; Tiedemann, R. E. Xbp1snegative tumor B cells and pre-plasmablasts mediate therapeutic proteasome inhibitor resistance in multiple myeloma. Cancer Cell, 2013, 24(3), 289-304.
    • (2013) Cancer Cell , vol.24 , Issue.3 , pp. 289-304
    • Leung-Hagesteijn, C.1    Erdmann, N.2    Cheung, G.3    Keats, J.J.4    Stewart, A.K.5    Reece, D.E.6    Chung, K.C.7    Tiedemann, R.E.8
  • 132
    • 84876733507 scopus 로고    scopus 로고
    • ADPRibosylated Proteins as Old and New Drug Targets for Anticancer Therapy: The Example of ARF6
    • Dani, N.; Barbosa, A. J.; Del Rio, A.; Di Girolamo, M. ADPRibosylated Proteins as Old and New Drug Targets for Anticancer Therapy: the Example of ARF6. Curr. Pharm. Des., 2013, 19(4), 624-633.
    • (2013) Curr. Pharm. Des , vol.19 , Issue.4 , pp. 624-633
    • Dani, N.1    Barbosa, A.J.2    Del Rio, A.3    Di Girolamo, M.4
  • 133
    • 84878613097 scopus 로고    scopus 로고
    • Human sirtuins: An overview of an emerging drug target in age-related diseases and cancer
    • Donadini, A.; Rosano, C.; Felli, L.; Ponassi, M. Human sirtuins: an overview of an emerging drug target in age-related diseases and cancer. Curr. Drug Targets, 2013, 14(6), 653-61.
    • (2013) Curr. Drug Targets , vol.14 , Issue.6 , pp. 653-661
    • Donadini, A.1    Rosano, C.2    Felli, L.3    Ponassi, M.4
  • 135
    • 84870693696 scopus 로고    scopus 로고
    • Modulation of epigenetic targets for anticancer therapy: Clinicopathological relevance, structural data and drug discovery perspectives
    • Andreoli, F.; Barbosa, A. J.; Parenti, M. D.; Del Rio, A. Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives. Curr. Pharm. Des,., 2013, 19(4), 578-613.
    • (2013) Curr. Pharm. Des , vol.19 , Issue.4 , pp. 578-613
    • Andreoli, F.1    Barbosa, A.J.2    Parenti, M.D.3    Del Rio, A.4
  • 136
    • 84863804147 scopus 로고    scopus 로고
    • Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain
    • Karlberg, T.; Thorsell, A. G.; Kallas, A.; Schuler, H. Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain. J. Biol. Chem., 2012, 287(29), 24077-81.
    • (2012) J. Biol. Chem , vol.287 , Issue.29 , pp. 24077-24081
    • Karlberg, T.1    Thorsell, A.G.2    Kallas, A.3    Schuler, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.