메뉴 건너뛰기




Volumn 463, Issue 4, 2015, Pages 881-887

A highly sensitive assay of IRE1 activity using the small luciferase NanoLuc: Evaluation of ALS-related genetic and pathological factors

Author keywords

ER stress; IRE1; NanoLuc; XBP1

Indexed keywords

FIREFLY LUCIFERASE; GREEN FLUORESCENT PROTEIN; HOMOCYSTEINE; MUTANT PROTEIN; PROTEIN IRE1; SAR1 PROTEIN; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1; DNA BINDING PROTEIN; ERN1 PROTEIN, HUMAN; PRIMER DNA; PROTEIN SERINE THREONINE KINASE; REGULATORY FACTOR X TRANSCRIPTION FACTORS; RIBONUCLEASE; TRANSCRIPTION FACTOR;

EID: 84936890798     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.05.132     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • M.J. Gething, and J. Sambrook Protein folding in the cell Nature 355 1992 33 45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 2
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein-folding compartment
    • A. Helenius, T. Marquardt, and I. Braakman The endoplasmic reticulum as a protein-folding compartment Trends Cell. Biol. 2 1992 227 231
    • (1992) Trends Cell. Biol. , vol.2 , pp. 227-231
    • Helenius, A.1    Marquardt, T.2    Braakman, I.3
  • 3
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • H.P. Harding, Y. Zhang, and D. Ron Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase Nature 397 1999 271 274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 5
    • 0030850013 scopus 로고    scopus 로고
    • Interaction of ATF6 and serum response factor
    • C. Zhu, F.E. Johansen, and R. Prywes Interaction of ATF6 and serum response factor Mol. Cell. Biol. 17 1997 4957-496
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4957-5496
    • Zhu, C.1    Johansen, F.E.2    Prywes, R.3
  • 6
    • 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
    • K. Haze, H. Yoshida, H. Yanagi, T. Yura, and K. Mori Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress Mol. Biol. Cell. 10 1999 3787 3799
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 8
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • S. Oyadomari, and M. Mori Roles of CHOP/GADD153 in endoplasmic reticulum stress Cell. Death Differ. 11 2004 381 389
    • (2004) Cell. Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 9
    • 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
    • H. Yoshida, T. Matsui, A. Yamamoto, T. Okada, and K. Mori XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor Cell 107 2001 881 891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 10
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • A.H. Lee, N.N. Iwakoshi, and L.H. Glimcher XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response Mol. Cell. Biol. 23 2003 7448 7459
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 12
    • 29244448729 scopus 로고    scopus 로고
    • XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands
    • A.H. Lee, G.C. Chu, N.N. Iwakoshi, and L.H. Glimcher XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands EMBO J. 24 2005 4368 4380
    • (2005) EMBO J. , vol.24 , pp. 4368-4380
    • Lee, A.H.1    Chu, G.C.2    Iwakoshi, N.N.3    Glimcher, L.H.4
  • 13
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • A.H. Lee, E.F. Scapa, D.E. Cohen, and L.H. Glimcher Regulation of hepatic lipogenesis by the transcription factor XBP1 Science 320 2008 1492 1496
    • (2008) Science , vol.320 , pp. 1492-1496
    • Lee, A.H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 14
    • 33749624512 scopus 로고    scopus 로고
    • Analysis of the XBP1 splicing mechanism using endoplasmic reticulum stress-indicators
    • T. Iwawaki, and R. Akai Analysis of the XBP1 splicing mechanism using endoplasmic reticulum stress-indicators Biochem. Biophys. Res. Commun. 350 2006 709 715
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , pp. 709-715
    • Iwawaki, T.1    Akai, R.2
  • 15
    • 1842612402 scopus 로고    scopus 로고
    • A transgenic mouse model for monitoring endoplasmic reticulum stress
    • T. Iwawaki, R. Akai, K. Kohno, and M. Miura A transgenic mouse model for monitoring endoplasmic reticulum stress Nat. Med. 10 2004 98 102
    • (2004) Nat. Med. , vol.10 , pp. 98-102
    • Iwawaki, T.1    Akai, R.2    Kohno, K.3    Miura, M.4
  • 19
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • S. Boillee, V.C. Vande, and D.W. Cleveland ALS: A disease of motor neurons and their nonneuronal neighbors Neuron 52 2006 39 59
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    Vande, V.C.2    Cleveland, D.W.3
  • 22
    • 85040709233 scopus 로고    scopus 로고
    • Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments
    • Y.J. Zhang, T.F. Gendron, Y.F. Xu, L.W. Ko, S.H. Yen, and L. Petrucelli Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments Mol. Neurodegener. 5 2010 33
    • (2010) Mol. Neurodegener. , vol.5 , pp. 33
    • Zhang, Y.J.1    Gendron, T.F.2    Xu, Y.F.3    Ko, L.W.4    Yen, S.H.5    Petrucelli, L.6
  • 25
    • 33845926059 scopus 로고    scopus 로고
    • Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking
    • D.J. Dupré, M. Robitaille, N. Éthier, L.R. Villeneuve, A.M. Mamarbachi, and T.E. Hébert Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking J. Biol. Chem. 281 2006 34561 34573
    • (2006) J. Biol. Chem. , vol.281 , pp. 34561-34573
    • Dupré, D.J.1    Robitaille, M.2    Éthier, N.3    Villeneuve, L.R.4    Mamarbachi, A.M.5    Hébert, T.E.6
  • 28
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • M.P. Mattson, and S.L. Chan Neuronal and glial calcium signaling in Alzheimer's disease Cell. Calcium 34 2003 385 397
    • (2003) Cell. Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 29
    • 0034666267 scopus 로고    scopus 로고
    • Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity
    • I.J. Kruman, C. Culmsee, S.L. Chan, Y. Kruman, Z. Guo, L. Penix, and M.P. Mattson Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity J. Neurosci. 20 2000 6920 6926
    • (2000) J. Neurosci. , vol.20 , pp. 6920-6926
    • Kruman, I.J.1    Culmsee, C.2    Chan, S.L.3    Kruman, Y.4    Guo, Z.5    Penix, L.6    Mattson, M.P.7
  • 30
    • 0037382957 scopus 로고    scopus 로고
    • H2O2 and 4-hydroxynonenal mediate amyloid beta-induced neuronal apoptosis by activating JNKs and p38MAPK
    • E. Tamagno, G. Robino, A. Obbili, P. Bardini, M. Aragno, M. Parola, and O. Danni H2O2 and 4-hydroxynonenal mediate amyloid beta-induced neuronal apoptosis by activating JNKs and p38MAPK Exp. Neurol. 180 2003 144 155
    • (2003) Exp. Neurol. , vol.180 , pp. 144-155
    • Tamagno, E.1    Robino, G.2    Obbili, A.3    Bardini, P.4    Aragno, M.5    Parola, M.6    Danni, O.7
  • 32
    • 33646747001 scopus 로고    scopus 로고
    • Mechanisms of homocysteine neurotoxicity in neurodegenerative diseases with special reference to dementia
    • R. Obeid, and W. Herrmann Mechanisms of homocysteine neurotoxicity in neurodegenerative diseases with special reference to dementia FEBS Lett. 580 2006 2994 3005
    • (2006) FEBS Lett. , vol.580 , pp. 2994-3005
    • Obeid, R.1    Herrmann, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.