메뉴 건너뛰기




Volumn 416, Issue 3-4, 2011, Pages 362-366

Endoplasmic reticulum stress enhances γ-secretase activity

Author keywords

Secretase; Amyloid ; ATF4; Diabetes; Endoplasmic reticulum stress; Obesity; Quercetin

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; GAMMA SECRETASE; NOTCH1 RECEPTOR; PRESENILIN 1; QUERCETIN; TUNICAMYCIN;

EID: 84855896629     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.11.042     Document Type: Article
Times cited : (45)

References (34)
  • 1
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 1999, 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 2
    • 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, 8:519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 3
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T., Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 2000, 150:887-894.
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 4
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000, 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 5
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430:631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 6
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 2007, 8:101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 9
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe M.S., Xia W., Ostaszewski B.L., Diehl T.S., Kimberly W.T., Selkoe D.J. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 1999, 398:513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 15
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010, 140:900-917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 16
    • 0036895383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the development of diabetes: a review
    • Harding H.P., Ron D. Endoplasmic reticulum stress and the development of diabetes: a review. Diabetes 2002, 51(Suppl. 3):S455-S461.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 3
    • Harding, H.P.1    Ron, D.2
  • 17
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival
    • Harding H.P., Zeng H., Zhang Y., Jungries R., Chung P., Plesken H., Sabatini D.D., Ron D. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol. Cell 2001, 7:1153-1163.
    • (2001) Mol. Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 19
    • 77950523710 scopus 로고    scopus 로고
    • The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation
    • Park S.W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nat. Med. 2010, 16:429-437.
    • (2010) Nat. Med. , vol.16 , pp. 429-437
    • Park, S.W.1    Zhou, Y.2    Lee, J.3    Lu, A.4    Sun, C.5    Chung, J.6    Ueki, K.7    Ozcan, U.8
  • 20
    • 77950537400 scopus 로고    scopus 로고
    • A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response
    • Winnay J.N., Boucher J., Mori M.A., Ueki K., Kahn C.R. A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response. Nat. Med. 2010, 16:438-445.
    • (2010) Nat. Med. , vol.16 , pp. 438-445
    • Winnay, J.N.1    Boucher, J.2    Mori, M.A.3    Ueki, K.4    Kahn, C.R.5
  • 23
    • 67749135249 scopus 로고    scopus 로고
    • The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis
    • Wang Y., Vera L., Fischer W.H., Montminy M. The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis. Nature 2009, 460:534-537.
    • (2009) Nature , vol.460 , pp. 534-537
    • Wang, Y.1    Vera, L.2    Fischer, W.H.3    Montminy, M.4
  • 28
    • 0020974133 scopus 로고
    • Effect of tunicamycin, an inhibitor of protein glycosylation, on division of tumor cells in vitro
    • Savage K.E., Baur P.S. Effect of tunicamycin, an inhibitor of protein glycosylation, on division of tumor cells in vitro. J. Cell Sci. 1983, 64:295-306.
    • (1983) J. Cell Sci. , vol.64 , pp. 295-306
    • Savage, K.E.1    Baur, P.S.2
  • 29
    • 0030003538 scopus 로고    scopus 로고
    • Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain
    • Kopan R., Schroeter E.H., Weintraub H., Nye J.S. Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain. Proc. Natl. Acad. Sci. USA 1996, 93:1683-1688.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1683-1688
    • Kopan, R.1    Schroeter, E.H.2    Weintraub, H.3    Nye, J.S.4
  • 30
    • 80052166441 scopus 로고    scopus 로고
    • Quercetin. Monograph
    • Kelly G.S. Quercetin. Monograph. Altern. Med. Rev. 2011, 16:172-194.
    • (2011) Altern. Med. Rev. , vol.16 , pp. 172-194
    • Kelly, G.S.1
  • 32
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1
    • Wiseman R.L., Zhang Y., Lee K.P., Harding H.P., Haynes C.M., Price J., Sicheri F., Ron D. Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol. Cell 2010, 38:291-304.
    • (2010) Mol. Cell , vol.38 , pp. 291-304
    • Wiseman, R.L.1    Zhang, Y.2    Lee, K.P.3    Harding, H.P.4    Haynes, C.M.5    Price, J.6    Sicheri, F.7    Ron, D.8
  • 33
    • 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. 2001, 153:1011-1022.
    • (2001) J. Cell Biol. , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.