메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

KDEL receptor 1 regulates T-cell homeostasis via PP1 that is a key phosphatase for ISR

Author keywords

[No Author keywords available]

Indexed keywords

BIM PROTEIN; ETHYLNITROSOUREA; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; INITIATION FACTOR 2ALPHA; KDEL RECEPTOR 1; PHOSPHOPROTEIN PHOSPHATASE 1; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; VASCULOTROPIN A; APOPTOSIS REGULATORY PROTEIN; BCL2L11 PROTEIN, MOUSE; INITIATION FACTOR 2; KDELR1 PROTEIN, MOUSE; MEMBRANE PROTEIN; ONCOPROTEIN; RECEPTOR;

EID: 84935871697     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8474     Document Type: Article
Times cited : (34)

References (63)
  • 1
    • 0030450784 scopus 로고    scopus 로고
    • The dynamic organisation of the secretory pathway
    • Pelham, H. R. B. The dynamic organisation of the secretory pathway. Cell Struct. Funct. 21, 413-419 (1996).
    • (1996) Cell Struct. Funct. , vol.21 , pp. 413-419
    • Pelham, H.R.B.1
  • 2
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard, L., Molinari, M. & Helenius, A. Setting the standards: quality control in the secretory pathway. Science 286, 1882-1888 (1999).
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 3
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis, M. J. & Pelham, H. R. A human homologue of the yeast HDEL receptor. Nature 348, 162-163 (1990).
    • (1990) Nature , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.2
  • 4
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J. C., Hardwick, K. G., Dean, N. & Pelham, H. R. 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
  • 5
    • 0141594939 scopus 로고    scopus 로고
    • The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen-activated protein kinase signaling cascades
    • Yamamoto, K. et al. The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen-activated protein kinase signaling cascades. J. Biol. Chem. 278, 34525-34532 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34525-34532
    • Yamamoto, K.1
  • 6
    • 48649101763 scopus 로고    scopus 로고
    • A traffic-activated golgi-based signalling circuit coordinates the secretory pathway
    • Pulvirenti, T. et al. A traffic-activated Golgi-based signalling circuit coordinates the secretory pathway. Nat. Cell Biol. 10, 912-922 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 912-922
    • Pulvirenti, T.1
  • 7
    • 70450227413 scopus 로고    scopus 로고
    • The KDEL receptor: New functions for an old protein
    • Capitani, M. & Sallese, M. The KDEL receptor: new functions for an old protein. FEBS Lett. 583, 3863-3871 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 3863-3871
    • Capitani, M.1    Sallese, M.2
  • 8
    • 0033230617 scopus 로고    scopus 로고
    • PKR; A sentinel kinase for cellular stress
    • Williams, B. R. PKR; a sentinel kinase for cellular stress. Oncogene 18, 6112-6120 (1999).
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 9
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H. P. et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6, 1099-1108 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1
  • 10
    • 0035166679 scopus 로고    scopus 로고
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses
    • Lu, L., Han, A. P. & Chen, J. J. Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses. Mol. Cell. Biol. 21, 7971-7980 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7971-7980
    • Lu, L.1    Han, A.P.2    Chen, J.J.3
  • 11
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding, H. P., Calfon, M., Urano, F., Novoa, I. & Ron, D. Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18, 575-599 (2002).
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 12
    • 1442264796 scopus 로고    scopus 로고
    • The protein kinase PKR: A molecular clock that sequentially activates survival and death programs
    • Donze, O. et al. The protein kinase PKR: a molecular clock that sequentially activates survival and death programs. EMBO J. 23, 564-571 (2004).
    • (2004) EMBO J. , vol.23 , pp. 564-571
    • Donze, O.1
  • 13
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration
    • Moreno, J. A. et al. Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration. Nature 485, 507-511 (2012).
    • (2012) Nature , vol.485 , pp. 507-511
    • Moreno, J.A.1
  • 14
    • 60549114848 scopus 로고    scopus 로고
    • Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development
    • Harding, H. P. et al. Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development. Proc. Natl Acad. Sci. USA 106, 1832-1837 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1832-1837
    • Harding, H.P.1
  • 15
    • 0345465663 scopus 로고    scopus 로고
    • Integration of endoplasmic reticulum signaling in health and disease
    • Aridor, M. & Balch, W. E. 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
  • 16
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang, P. et al. The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol. Cell. Biol. 22, 3864-3874 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3864-3874
    • Zhang, P.1
  • 17
    • 0037147666 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor-2alpha (eIF2alpha) is associated with neuronal degeneration in alzheimer's disease
    • Chang, R. C., Wong, A. K., Ng, H. K. & Hugon, J. Phosphorylation of eukaryotic initiation factor-2alpha (eIF2alpha) is associated with neuronal degeneration in Alzheimer's disease. Neuroreport 13, 2429-2432 (2002).
    • (2002) Neuroreport , vol.13 , pp. 2429-2432
    • Chang, R.C.1    Wong, A.K.2    Ng, H.K.3    Hugon, J.4
  • 18
    • 33744465772 scopus 로고    scopus 로고
    • Activation of the integrated stress response during T helper cell differentiation
    • Scheu, S. et al. Activation of the integrated stress response during T helper cell differentiation. Nat. Immunol. 7, 644-651 (2006).
    • (2006) Nat. Immunol. , vol.7 , pp. 644-651
    • Scheu, S.1
  • 19
    • 54049110990 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress regulator XBP-1 contributes to effector CD8+ T cell differentiation during acute infection
    • Kamimura, D. & Bevan, M. J. Endoplasmic reticulum stress regulator XBP-1 contributes to effector CD8+ T cell differentiation during acute infection. J Immunol. 181, 5433-5441 (2008).
    • (2008) J Immunol. , vol.181 , pp. 5433-5441
    • Kamimura, D.1    Bevan, M.J.2
  • 20
    • 0034698825 scopus 로고    scopus 로고
    • Homeostatic T cell proliferation: How far can T cells be activated to self-ligands?
    • Surh, C. D. & Sprent, J. Homeostatic T cell proliferation: how far can T cells be activated to self-ligands? J Exp Med. 192, F9-F14 (2000).
    • (2000) J Exp Med. , vol.192 , pp. F9-F14
    • Surh, C.D.1    Sprent, J.2
  • 21
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic bcl-2 relative bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • Bouillet, P. et al. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 286, 1735-1738 (1999).
    • (1999) Science , vol.286 , pp. 1735-1738
    • Bouillet, P.1
  • 22
    • 0036069819 scopus 로고    scopus 로고
    • Activated T cell death in vivo mediated by proapoptotic bcl-2 family member bim
    • Hildeman, D. A. et al. Activated T cell death in vivo mediated by proapoptotic bcl-2 family member bim. Immunity 16, 759-767 (2002).
    • (2002) Immunity , vol.16 , pp. 759-767
    • Hildeman, D.A.1
  • 23
  • 24
    • 34447258837 scopus 로고    scopus 로고
    • Bim/Bcl-2 balance is critical for maintaining naive and memory T cell homeostasis
    • Wojciechowski, S. et al. Bim/Bcl-2 balance is critical for maintaining naive and memory T cell homeostasis. J. Exp. Med. 204, 1665-1675 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 1665-1675
    • Wojciechowski, S.1
  • 25
    • 34250758642 scopus 로고    scopus 로고
    • ER stress triggers apoptosis by activating BH3-only protein bim
    • Puthalakath, H. et al. ER stress triggers apoptosis by activating BH3-only protein Bim. Cell 129, 1337-1349 (2007).
    • (2007) Cell , vol.129 , pp. 1337-1349
    • Puthalakath, H.1
  • 26
    • 0022369586 scopus 로고
    • Dose-repetition increases the mutagenic effectiveness of N-ethyl-N-nitrosourea in mouse spermatogonia
    • Hitotsumachi, S., Carpenter, D. A. & Russell, W. L. Dose-repetition increases the mutagenic effectiveness of N-ethyl-N-nitrosourea in mouse spermatogonia. Proc. Natl Acad. Sci. USA 82, 6619-6621 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 6619-6621
    • Hitotsumachi, S.1    Carpenter, D.A.2    Russell, W.L.3
  • 27
    • 33745042388 scopus 로고    scopus 로고
    • Autoimmune arthritis associated with mutated interleukin (IL)-6 receptor gp130 is driven by STAT3/IL-7-dependent homeostatic proliferation of CD4+ T cells
    • Sawa, S. et al. Autoimmune arthritis associated with mutated interleukin (IL)-6 receptor gp130 is driven by STAT3/IL-7-dependent homeostatic proliferation of CD4+ T cells. J. Exp. Med. 12, 1459-1470 (2006).
    • (2006) J. Exp. Med. , vol.12 , pp. 1459-1470
    • Sawa, S.1
  • 28
    • 33748988988 scopus 로고    scopus 로고
    • CD1d-restricted NKT cell activation enhanced homeostatic proliferation of CD8+ T cells in a manner dependent on IL-4
    • Ueda, N. et al. CD1d-restricted NKT cell activation enhanced homeostatic proliferation of CD8+ T cells in a manner dependent on IL-4. Int. Immunol. 18, 1397-1404 (2006).
    • (2006) Int. Immunol. , vol.18 , pp. 1397-1404
    • Ueda, N.1
  • 29
    • 3242882807 scopus 로고    scopus 로고
    • Enforcing order within a complex locus: Current perspectives on the control of V(D)J recombination at the murine T-cell receptor alpha/delta locus
    • Krangel, M. S., Carabana, J., Abbarategui, I., Schlimgen, R. & Hawwari, A. Enforcing order within a complex locus: current perspectives on the control of V(D)J recombination at the murine T-cell receptor alpha/delta locus. Immunol. Rev. 200, 224-232 (2004).
    • (2004) Immunol. Rev. , vol.200 , pp. 224-232
    • Krangel, M.S.1    Carabana, J.2    Abbarategui, I.3    Schlimgen, R.4    Hawwari, A.5
  • 30
    • 33645064260 scopus 로고    scopus 로고
    • Turning T-cell receptor beta recombination on and off: More questions than answers
    • Jackson, A. M. & Krangel, M. S. Turning T-cell receptor beta recombination on and off: more questions than answers. Immunol. Rev. 209, 129-141 (2006).
    • (2006) Immunol. Rev. , vol.209 , pp. 129-141
    • Jackson, A.M.1    Krangel, M.S.2
  • 32
    • 79956209348 scopus 로고    scopus 로고
    • Bcl-2 allows effector and memory CD8+ T cells to tolerate higher expression of bim
    • Kurtulus, S. et al. Bcl-2 allows effector and memory CD8+ T cells to tolerate higher expression of Bim. J. Immunol. 186, 5729-5737 (2011).
    • (2011) J. Immunol. , vol.186 , pp. 5729-5737
    • Kurtulus, S.1
  • 33
    • 0037009521 scopus 로고    scopus 로고
    • A mitochondrial specific stress response in mammalian cells
    • Zhao, Q. et al. A mitochondrial specific stress response in mammalian cells. EMBO J. 21, 4411-4419 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4411-4419
    • Zhao, Q.1
  • 34
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund, A. M., Pellegrino, M. W., Fiorese, C. J., Baker, B. M. & Haynes, C. M. Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337, 587-590 (2012).
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 35
    • 0033056848 scopus 로고    scopus 로고
    • RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling
    • Ito, T., Yang, M. & May, W. S. RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J. Biol. Chem. 274, 15427-15432 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 15427-15432
    • Ito, T.1    Yang, M.2    May, W.S.3
  • 36
    • 17944362905 scopus 로고    scopus 로고
    • Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency
    • Han, A. P. et al. Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency. EMBO J. 20, 6909-6918 (2001).
    • (2001) EMBO J. , vol.20 , pp. 6909-6918
    • Han, A.P.1
  • 37
    • 1642326675 scopus 로고    scopus 로고
    • Glucose insufficiency alters neuronal viability and increases susceptibility to glutamate toxicity
    • Ioudina, M., Uemura, E. & Greenlee, H. W. Glucose insufficiency alters neuronal viability and increases susceptibility to glutamate toxicity. Brain Res. 1004, 188-192 (2004).
    • (2004) Brain Res. , vol.1004 , pp. 188-192
    • Ioudina, M.1    Uemura, E.2    Greenlee, H.W.3
  • 38
    • 77956706423 scopus 로고    scopus 로고
    • Phosphorylation of eIF2alpha at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency
    • Muaddi, H. et al. Phosphorylation of eIF2alpha at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency. Mol. Biol. Cell. 21, 3220-3231 (2010).
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 3220-3231
    • Muaddi, H.1
  • 39
    • 84870984470 scopus 로고    scopus 로고
    • PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress
    • Verfaillie, T. et al. PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress. Cell Death Differ. 19, 1880-1891 (2012).
    • (2012) Cell Death Differ. , vol.19 , pp. 1880-1891
    • Verfaillie, T.1
  • 40
    • 13644256191 scopus 로고    scopus 로고
    • A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress
    • Boyce, M. et al. A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 307, 935-939 (2005).
    • (2005) Science , vol.307 , pp. 935-939
    • Boyce, M.1
  • 41
    • 0035399464 scopus 로고    scopus 로고
    • Combinatorial control of protein phosphatase-1
    • Bollen, M. Combinatorial control of protein phosphatase-1. Trends Biochem. Sci. 26, 426-431 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 426-431
    • Bollen, M.1
  • 42
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff, M. P. et al. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16, 1876-1887 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1876-1887
    • Egloff, M.P.1
  • 43
    • 0031464540 scopus 로고    scopus 로고
    • The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1
    • Aoe, T. et al. The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1. EMBO J. 16, 7305-7316 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7305-7316
    • Aoe, T.1
  • 44
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J. et al. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745-753 (1995).
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1
  • 45
    • 0031953138 scopus 로고    scopus 로고
    • Identification of amino acids in the binding pocket of the human KDEL receptor
    • Scheel, A. A. & Pelham, H. R. Identification of amino acids in the binding pocket of the human KDEL receptor. J. Biol. Chem. 273, 2467-2472 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2467-2472
    • Scheel, A.A.1    Pelham, H.R.2
  • 46
    • 0035999828 scopus 로고    scopus 로고
    • Regulation of the TCRalpha repertoire by the survival window of CD4(+)CD8(+) thymocytes
    • Guo, J. et al. Regulation of the TCRalpha repertoire by the survival window of CD4(+)CD8(+) thymocytes. Nat. Immunol. 3, 469-476 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 469-476
    • Guo, J.1
  • 47
    • 0033532594 scopus 로고    scopus 로고
    • Role of the 78-kDa glucose-regulated protein as an activity modulator of protein phosphatase1gamma2
    • Chun, Y. S. et al. Role of the 78-kDa glucose-regulated protein as an activity modulator of protein phosphatase1gamma2. Biochem. Biophys. Res. Commun. 259, 300-304 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 300-304
    • Chun, Y.S.1
  • 48
    • 35448981358 scopus 로고    scopus 로고
    • Regulatory proteins of eukaryotic initiation factor 2-alpha subunit (eIF2 alpha) phosphatase, under ischemic reperfusion and tolerance
    • Garcia-Bonilla, L. et al. Regulatory proteins of eukaryotic initiation factor 2-alpha subunit (eIF2 alpha) phosphatase, under ischemic reperfusion and tolerance. J. Neurochem. 103, 1368-1380 (2007).
    • (2007) J. Neurochem. , vol.103 , pp. 1368-1380
    • Garcia-Bonilla, L.1
  • 49
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. & Pelham, H. R. 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
  • 50
    • 0037317592 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2
    • Brush, M. H., Weiser, D. C. & Shenolikar, S. Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Mol. Cell. Biol. 23, 1292-1303 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1292-1303
    • Brush, M.H.1    Weiser, D.C.2    Shenolikar, S.3
  • 51
    • 77952557954 scopus 로고    scopus 로고
    • PD-1 regulates germinal center B cell survival and the formation and affinity of long-lived plasma cells
    • Good-Jacobson, K. L. et al. PD-1 regulates germinal center B cell survival and the formation and affinity of long-lived plasma cells. Nat. Immunol. 11, 535-542 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 535-542
    • Good-Jacobson, K.L.1
  • 52
    • 84880752273 scopus 로고    scopus 로고
    • Repression of the transcription factor bach2 contributes to predisposition of IgG1 memory B cells toward plasma cell differentiation
    • Kometani, K. et al. Repression of the transcription factor Bach2 contributes to predisposition of IgG1 memory B cells toward plasma cell differentiation. Immunity 39, 136-147 (2013).
    • (2013) Immunity , vol.39 , pp. 136-147
    • Kometani, K.1
  • 53
    • 2942729856 scopus 로고    scopus 로고
    • A series of maturity onset diabetes of the young, type 2 (MODY2) mouse models generated by a large-scale ENU mutagenesis program
    • Inoue, M. et al. A series of maturity onset diabetes of the young, type 2 (MODY2) mouse models generated by a large-scale ENU mutagenesis program. Hum. Mol. Genet. 13, 1147-1157 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1147-1157
    • Inoue, M.1
  • 54
    • 77953993126 scopus 로고    scopus 로고
    • Zinc suppresses Th17 development via inhibition of STAT3 activation
    • Kitabayashi, C. et al. Zinc suppresses Th17 development via inhibition of STAT3 activation. Int. Immunol. 22, 375-386 (2010).
    • (2010) Int. Immunol. , vol.22 , pp. 375-386
    • Kitabayashi, C.1
  • 55
    • 38449087590 scopus 로고    scopus 로고
    • The surprising kinetics of the T cell response to live antigenic cells
    • Tyznik, A. J. & Bevan, M. J. The surprising kinetics of the T cell response to live antigenic cells. J. Immunol. 179, 4988-4995 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 4988-4995
    • Tyznik, A.J.1    Bevan, M.J.2
  • 56
    • 34547824186 scopus 로고    scopus 로고
    • Naive CD8+ T cells differentiate into protective memory-like cells after IL-2 anti IL-2 complex treatment in vivo
    • Kamimura, D. & Bevan, M. J. Naive CD8+ T cells differentiate into protective memory-like cells after IL-2 anti IL-2 complex treatment in vivo. J. Exp. Med. 204, 1803-1812 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 1803-1812
    • Kamimura, D.1    Bevan, M.J.2
  • 57
    • 63949084607 scopus 로고    scopus 로고
    • SUnSET, a nonradioactive method to monitor protein synthesis
    • Schmidt, E. K., Clavarino, G., Ceppi, M. & Pierre, P. SUnSET, a nonradioactive method to monitor protein synthesis. Nat Methods. 6, 275-277 (2009).
    • (2009) Nat Methods. , vol.6 , pp. 275-277
    • Schmidt, E.K.1    Clavarino, G.2    Ceppi, M.3    Pierre, P.4
  • 58
    • 79954618679 scopus 로고    scopus 로고
    • Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique
    • Goodman, C. A. et al. Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique. FASEB J. 25, 1028-1039 (2011).
    • (2011) FASEB J. , vol.25 , pp. 1028-1039
    • Goodman, C.A.1
  • 59
    • 18244406271 scopus 로고    scopus 로고
    • Regulation of T cell receptor alpha gene assembly by a complex hierarchy of germline jalpha promoters
    • Hawwari, A., Bock, C. & Krangel, M. S. Regulation of T cell receptor alpha gene assembly by a complex hierarchy of germline Jalpha promoters. Nat. Immunol. 6, 481-489 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 481-489
    • Hawwari, A.1    Bock, C.2    Krangel, M.S.3
  • 60
    • 0032476606 scopus 로고    scopus 로고
    • Requirement of CD3 complex-associated signaling functions for expression of rearranged T cell receptor beta VDJ genes in early thymic development
    • Würch, A. et al. Requirement of CD3 complex-associated signaling functions for expression of rearranged T cell receptor beta VDJ genes in early thymic development. J. Exp. Med. 188, 166-1678 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 166-1678
    • Würch, A.1
  • 61
    • 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 397, 271-274 (1999).
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 62
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa, I., Zeng, H., Harding, H. P. & Ron, D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J. Cell Biol. 153, 1011-1022 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 63
    • 0344875071 scopus 로고    scopus 로고
    • Red blood cells upregulate cytoprotective proteins and the labile iron pool in dividing human T cells despite a reduction in oxidative stress
    • Fonseca, A. M., Pereira, C. F., Porto, G. & Arosa, F. A. Red blood cells upregulate cytoprotective proteins and the labile iron pool in dividing human T cells despite a reduction in oxidative stress. Free Radic. Biol. Med. 35, 1404-1416 (2003).
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 1404-1416
    • Fonseca, A.M.1    Pereira, C.F.2    Porto, G.3    Arosa, F.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.