메뉴 건너뛰기




Volumn 53, Issue 9, 2012, Pages 1932-1943

Molecular characterization of proprotein convertase subtilisin/kexin type 9-mediated degradation of the LDLR

Author keywords

Autophagy; Cholesterol; Endosomes; Low density lipoprotein receptor; Lysosomes

Indexed keywords

CLATHRIN HEAVY CHAIN; ESCRT PROTEIN; HEPATOCYTE GROWTH FACTOR REGULATED TYROSINE KINASE SUBSTRATE; KEXIN; LOW DENSITY LIPOPROTEIN RECEPTOR; PROPROTEIN CONVERTASE SUBTILISIN KEXIN TYPE 9; PROTEASOME; PROTEIN TYROSINE KINASE; SCATTER FACTOR; SMALL INTERFERING RNA; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 84864851760     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M028563     Document Type: Article
Times cited : (93)

References (61)
  • 1
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein. 1986. A receptor-mediated pathway for cholesterol homeostasis. Science. 232: 34-47. (Pubitemid 16037973)
    • (1986) Science , vol.232 , Issue.4746 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 3
    • 9644266673 scopus 로고    scopus 로고
    • Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver
    • Park, S. W., Y. A. Moon, and J. D. Horton. 2004. Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver. J. Biol. Chem. 279: 50630-50638.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50630-50638
    • Park, S.W.1    Moon, Y.A.2    Horton, J.D.3
  • 8
    • 13944265645 scopus 로고    scopus 로고
    • Low LDL cholesterol in individuals of African descent resulting from frequent nonsense mutations in PCSK9
    • Cohen, J., A. Pertsemlidis, I. K. Kotowski, R. Graham, C. K. Garcia, and H. H. Hobbs. 2005. Low LDL cholesterol in individuals of African descent resulting from frequent nonsense mutations in PCSK9. Nat. Genet. 37: 161-165.
    • (2005) Nat. Genet. , vol.37 , pp. 161-165
    • Cohen, J.1    Pertsemlidis, A.2    Kotowski, I.K.3    Graham, R.4    Garcia, C.K.5    Hobbs, H.H.6
  • 11
    • 66349126280 scopus 로고    scopus 로고
    • PCSK9: A convertase that coordinates LDL catabolism
    • Horton, J. D., J. C. Cohen, and H. H. Hobbs. 2009. PCSK9: a convertase that coordinates LDL catabolism. J. Lipid Res. 50 (Suppl): S172-S177.
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Horton, J.D.1    Cohen, J.C.2    Hobbs, H.H.3
  • 12
    • 0037147281 scopus 로고    scopus 로고
    • Structure of the LDL receptor extracellular domain at endosomal pH
    • DOI 10.1126/science.1078124
    • Rudenko, G., L. Henry, K. Henderson, K. Ichtchenko, M. S. Brown, J. L. Goldstein, and J. Deisenhofer. 2002. Structure of the LDL receptor extracellular domain at endosomal pH. Science. 298: 2353-2358. (Pubitemid 36014201)
    • (2002) Science , vol.298 , Issue.5602 , pp. 2353-2358
    • Rudenko, G.1    Henry, L.2    Henderson, K.3    Ichtchenko, K.4    Brown, M.S.5    Goldstein, J.L.6    Deisenhofer, J.7
  • 13
    • 34547108600 scopus 로고    scopus 로고
    • Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation
    • DOI 10.1074/jbc.M702027200
    • Zhang, D. W., T. A. Lagace, R. Garuti, Z. Zhao, M. McDonald, J. D. Horton, J. C. Cohen, and H. H. Hobbs. 2007. Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation. J. Biol. Chem. 282: 18602-18612. (Pubitemid 47100234)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18602-18612
    • Zhang, D.-W.1    Lagace, T.A.2    Garuti, R.3    Zhao, Z.4    McDonald, M.5    Horton, J.D.6    Cohen, J.C.7    Hobbs, H.H.8
  • 14
    • 51349161358 scopus 로고    scopus 로고
    • Structural requirements for PCSK9-mediated degradation of the low-density lipoprotein receptor
    • Zhang, D. W., R. Garuti, W. J. Tang, J. C. Cohen, and H. H. Hobbs. 2008. Structural requirements for PCSK9-mediated degradation of the low-density lipoprotein receptor. Proc. Natl. Acad. Sci. USA. 105: 13045-13050.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13045-13050
    • Zhang, D.W.1    Garuti, R.2    Tang, W.J.3    Cohen, J.C.4    Hobbs, H.H.5
  • 18
    • 84857684478 scopus 로고    scopus 로고
    • Interaction between the ligand-binding domain of the LDL receptor and the C-terminal domain of PCSK9 is required for PCSK9 to remain bound to the LDL receptor during endosomal acidification
    • Tveten, K., O. L. Holla, J. Cameron, T. B. Strom, K. E. Berge, J. K. Laerdahl, and T. P. Leren. 2012. Interaction between the ligand-binding domain of the LDL receptor and the C-terminal domain of PCSK9 is required for PCSK9 to remain bound to the LDL receptor during endosomal acidification. Hum. Mol. Genet. 21: 1402-1409.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1402-1409
    • Tveten, K.1    Holla, O.L.2    Cameron, J.3    Strom, T.B.4    Berge, K.E.5    Laerdahl, J.K.6    Leren, T.P.7
  • 19
    • 79953136043 scopus 로고    scopus 로고
    • A two-step binding model of PCSK9 interaction with the low density lipoprotein receptor
    • Yamamoto, T., C. Lu, and R. O. Ryan. 2011. A two-step binding model of PCSK9 interaction with the low density lipoprotein receptor. J. Biol. Chem. 286: 5464-5470.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5464-5470
    • Yamamoto, T.1    Lu, C.2    Ryan, R.O.3
  • 21
    • 0021215312 scopus 로고
    • Domain map of the LDL receptor: Sequence homology with the epidermal growth factor precursor
    • Russell, D. W., W. J. Schneider, T. Yamamamoto, K. L. Luskey, M. S. Brown, and J. L. Goldstein. 1984. Domain map of the LDL receptor: sequence homology with the epidermal growth factor precursor. Cell. 37: 577-585. (Pubitemid 14079052)
    • (1984) Cell , vol.37 , Issue.2 , pp. 577-585
    • Russell, D.W.1    Schneider, W.J.2    Yamamoto, T.3
  • 23
    • 0021099685 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl Coenzyme A reductase and its mRNA in rat liver as studied with a monoclonal antibody and a cDNA probe
    • Liscum, L., K. L. Luskey, D. J. Chin, Y. K. Ho, J. L. Goldstein, and M. S. Brown. 1983. Regulation of 3-hydroxy-3-methylglutaryl Coenzyme A reductase and its mRNA in rat liver as studied with a monoclonal antibody and a cDNA probe. J. Biol. Chem. 258: 8450-8455.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8450-8455
    • Liscum, L.1    Luskey, K.L.2    Chin, D.J.3    Ho, Y.K.4    Goldstein, J.L.5    Brown, M.S.6
  • 24
    • 4043105580 scopus 로고    scopus 로고
    • The modular adaptor protein ARH is required for low density lipoprotein (LDL) binding and internalization but not for LDL receptor clustering in coated pits
    • DOI 10.1074/jbc.M405242200
    • Michaely, P., W. P. Li, R. G. Anderson, J. C. Cohen, and H. H. Hobbs. 2004. The modular adaptor protein ARH Is required for low density lipoprotein (LDL) binding and internalization but not for LDL receptor clustering in coated pits. J. Biol. Chem. 279: 34023-34031. (Pubitemid 39063054)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 34023-34031
    • Michaely, P.1    Li, W.-P.2    Anderson, R.G.W.3    Cohen, J.C.4    Hobbs, H.H.5
  • 25
    • 0030961960 scopus 로고    scopus 로고
    • Differential expression of exons 1a and 1c in mRNAs for sterol regulatory element binding protein-1 in human and mouse organs and cultured cells
    • Shimomura, I., H. Shimano, J. D. Horton, J. L. Goldstein, and M. S. Brown. 1997. Differential expression of exons 1a and 1c in mRNAs for sterol regulatory element binding protein-1 in human and mouse organs and cultured cells. J. Clin. Invest. 99: 838-845. (Pubitemid 27123619)
    • (1997) Journal of Clinical Investigation , vol.99 , Issue.5 , pp. 838-845
    • Shimomura, I.1    Shimano, H.2    Horton, J.D.3    Goldstein, J.L.4    Brown, M.S.5
  • 26
    • 33847404337 scopus 로고    scopus 로고
    • Autophagy Gene-Dependent Clearance of Apoptotic Cells during Embryonic Development
    • DOI 10.1016/j.cell.2006.12.044, PII S009286740700178X
    • Qu, X., Z. Zou, Q. Sun, K. Luby-Phelps, P. Cheng, R. N. Hogan, C. Gilpin, and B. Levine. 2007. Autophagy gene-dependent clearance of apoptotic cells during embryonic development. Cell. 128: 931-946. (Pubitemid 46341412)
    • (2007) Cell , vol.128 , Issue.5 , pp. 931-946
    • Qu, X.1    Zou, Z.2    Sun, Q.3    Luby-Phelps, K.4    Cheng, P.5    Hogan, R.N.6    Gilpin, C.7    Levine, B.8
  • 28
    • 33846679386 scopus 로고    scopus 로고
    • Molecular biology of PCSK9: its role in LDL metabolism
    • DOI 10.1016/j.tibs.2006.12.008, PII S096800040600332X
    • Horton, J. D., J. C. Cohen, and H. H. Hobbs. 2007. Molecular biology of PCSK9: its role in LDL metabolism. Trends Biochem. Sci. 32: 71-77. (Pubitemid 46199197)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.2 , pp. 71-77
    • Horton, J.D.1    Cohen, J.C.2    Hobbs, H.H.3
  • 29
    • 0017246512 scopus 로고
    • Analysis of a mutant strain of human fibroblasts with a defect in the internalization of receptor-bound low density lipoprotein
    • Brown, M. S., and J. L. Goldstein. 1976. Analysis of a mutant strain of human fibroblasts with a defect in the internalization of receptor-bound low density lipoprotein. Cell. 9: 663-674.
    • (1976) Cell , vol.9 , pp. 663-674
    • Brown, M.S.1    Goldstein, J.L.2
  • 30
    • 0017661852 scopus 로고
    • Genetics of the LDL receptor: evidence that the mutations affecting binding and internalization are allelic
    • Goldstein, J. L., M. S. Brown, and N. J. Stone. 1977. Genetics of the LDL receptor: evidence that the mutations affecting binding and internalization are allelic. Cell. 12: 629-641. (Pubitemid 8224404)
    • (1977) Cell , vol.12 , Issue.3 , pp. 629-641
    • Goldstein, J.L.1    Brown, M.S.2    Stone, N.J.3
  • 31
    • 0037113960 scopus 로고    scopus 로고
    • ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2
    • DOI 10.1074/jbc.M208539200
    • He, G., S. Gupta, M. Yi, P. Michaely, H. H. Hobbs, and J. C. Cohen. 2002. ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2. J. Biol. Chem. 277: 44044-44049. (Pubitemid 36157831)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44044-44049
    • He, G.1    Gupta, S.2    Yi, M.3    Michaely, P.4    Hobbs, H.H.5    Cohen, J.C.6
  • 33
    • 33749487743 scopus 로고    scopus 로고
    • The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH
    • DOI 10.1242/jcs.03217
    • Maurer, M. E., and J. A. Cooper. 2006. The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH. J. Cell Sci. 119: 4235-4246. (Pubitemid 44774030)
    • (2006) Journal of Cell Science , vol.119 , Issue.20 , pp. 4235-4246
    • Maurer, M.E.1    Cooper, J.A.2
  • 36
    • 48549088895 scopus 로고    scopus 로고
    • Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • Sigismund, S., E. Argenzio, D. Tosoni, E. Cavallaro, S. Polo, and P. P. Di Fiore. 2008. Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev. Cell. 15: 209-219.
    • (2008) Dev. Cell , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5    Di Fiore, P.P.6
  • 37
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • DOI 10.1038/nrm2216, PII NRM2216
    • Mayor, S., and R. E. Pagano. 2007. Pathways of clathrin-independent endocytosis. Nat. Rev. Mol. Cell Biol. 8: 603-612. (Pubitemid 47106613)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 38
    • 67650092919 scopus 로고    scopus 로고
    • LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor
    • Zelcer, N., C. Hong, R. Boyadjian, and P. Tontonoz. 2009. LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor. Science. 325: 100-104.
    • (2009) Science , vol.325 , pp. 100-104
    • Zelcer, N.1    Hong, C.2    Boyadjian, R.3    Tontonoz, P.4
  • 39
    • 84855510314 scopus 로고    scopus 로고
    • Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8
    • Jo, Y., P. C. Lee, P. V. Sguigna, and R. A. DeBose-Boyd. 2011. Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8. Proc. Natl. Acad. Sci. USA. 108: 20503-20508.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20503-20508
    • Jo, Y.1    Lee, P.C.2    Sguigna, P.V.3    DeBose-Boyd, R.A.4
  • 42
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C., and D. J. Klionsky. 2009. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43: 67-93.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 43
    • 77952766891 scopus 로고    scopus 로고
    • Autophagy: Assays and artifacts
    • Barth, S., D. Glick, and K. F. Macleod. 2010. Autophagy: assays and artifacts. J. Pathol. 221: 117-124.
    • (2010) J. Pathol. , vol.221 , pp. 117-124
    • Barth, S.1    Glick, D.2    Macleod, K.F.3
  • 44
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C., and H. Stenmark. 2009. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature. 458: 445-452.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 45
    • 78049404751 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8. STAM complex
    • Berlin, I., H. Schwartz, and P. D. Nash. 2010. Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8. STAM complex. J. Biol. Chem. 285: 34909-34921.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34909-34921
    • Berlin, I.1    Schwartz, H.2    Nash, P.D.3
  • 46
    • 38849164882 scopus 로고    scopus 로고
    • Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking
    • DOI 10.1016/j.yexcr.2007.10.014, PII S0014482707004909
    • Raiborg, C., L. Malerod, N. M. Pedersen, and H. Stenmark. 2008. Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking. Exp. Cell Res. 314: 801-813. (Pubitemid 351191901)
    • (2008) Experimental Cell Research , vol.314 , Issue.4 , pp. 801-813
    • Raiborg, C.1    Malerod, L.2    Pedersen, N.M.3    Stenmark, H.4
  • 47
    • 33745929286 scopus 로고    scopus 로고
    • Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation
    • DOI 10.1091/mbc.E05-11-1054
    • Razi, M., and C. E. Futter. 2006. Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation. Mol. Biol. Cell. 17: 3469-3483. (Pubitemid 44156441)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.8 , pp. 3469-3483
    • Razi, M.1    Futter, C.E.2
  • 48
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • DOI 10.1074/jbc.M210843200
    • Bache, K. G., C. Raiborg, A. Mehlum, and H. Stenmark. 2003. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278: 12513-12521. (Pubitemid 36800240)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 49
    • 0033151614 scopus 로고    scopus 로고
    • Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis
    • Komada, M., and P. Soriano. 1999. Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis. Genes Dev. 13: 1475-1485. (Pubitemid 29270251)
    • (1999) Genes and Development , vol.13 , Issue.11 , pp. 1475-1485
    • Komada, M.1    Soriano, P.2
  • 50
    • 33644861535 scopus 로고    scopus 로고
    • An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: Evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins
    • DOI 10.1091/mbc.E05-09-0899
    • Gullapalli, A., B. L. Wolfe, C. T. Griffin, T. Magnuson, and J. Trejo. 2006. An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins. Mol. Biol. Cell. 17: 1228-1238. (Pubitemid 43376544)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.3 , pp. 1228-1238
    • Gullapalli, A.1    Wolfe, B.L.2    Griffin, C.T.3    Magnuson, T.4    Trejo, J.5
  • 51
    • 84862591663 scopus 로고    scopus 로고
    • ALIX binds a YPX3L motif of the GPCR PAR1 and mediates ubiquitin-independent ESCRT-III/MVB sorting
    • Dores, M. R., B. Chen, H. Lin, U. J. Soh, M. M. Paing, W. A. Montagne, T. Meerloo, and J. Trejo. 2012. ALIX binds a YPX3L motif of the GPCR PAR1 and mediates ubiquitin-independent ESCRT-III/MVB sorting. J. Cell Biol. 197: 407-419.
    • (2012) J. Cell Biol. , vol.197 , pp. 407-419
    • Dores, M.R.1    Chen, B.2    Lin, H.3    Soh, U.J.4    Paing, M.M.5    Montagne, W.A.6    Meerloo, T.7    Trejo, J.8
  • 54
    • 0032728972 scopus 로고    scopus 로고
    • Characterization of a novel cellular defect in patients with phenotypic homozygous familial hypercholesterolemia
    • Norman, D., X. M. Sun, M. Bourbon, B. L. Knight, R. P. Naoumova, and A. K. Soutar. 1999. Characterization of a novel cellular defect in patients with phenotypic homozygous familial hypercholesterolemia. J. Clin. Invest. 104: 619-628.
    • (1999) J. Clin. Invest. , vol.104 , pp. 619-628
    • Norman, D.1    Sun, X.M.2    Bourbon, M.3    Knight, B.L.4    Naoumova, R.P.5    Soutar, A.K.6
  • 55
    • 79956098305 scopus 로고    scopus 로고
    • PEST motif serine and tyrosine phosphorylation controls vascular endothelial growth factor receptor 2 stability and downregulation
    • Meyer, R. D., S. Srinivasan, A. J. Singh, J. E. Mahoney, K. R. Gharahassanlou, and N. Rahimi. 2011. PEST motif serine and tyrosine phosphorylation controls vascular endothelial growth factor receptor 2 stability and downregulation. Mol. Cell. Biol. 31: 2010-2025.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2010-2025
    • Meyer, R.D.1    Srinivasan, S.2    Singh, A.J.3    Mahoney, J.E.4    Gharahassanlou, K.R.5    Rahimi, N.6
  • 56
    • 0037093467 scopus 로고    scopus 로고
    • Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    • DOI 10.1093/emboj/21.10.2418
    • Hewitt, E. W., L. Duncan, D. Mufti, J. Baker, P. G. Stevenson, and P. J. Lehner. 2002. Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation. EMBO J. 21: 2418-2429. (Pubitemid 34546714)
    • (2002) EMBO Journal , vol.21 , Issue.10 , pp. 2418-2429
    • Hewitt, E.W.1    Duncan, L.2    Mufti, D.3    Baker, J.4    Stevenson, P.G.5    Lehner, P.J.6
  • 57
    • 79960727241 scopus 로고    scopus 로고
    • Ubiquitination is associated with lysosomal degradation of cell surface-resident ATP-binding cassette transporter A1 (ABCA1) through the endosomal sorting complex required for transport (ESCRT) pathway
    • Mizuno, T., H. Hayashi, S. Naoi, and Y. Sugiyama. 2011. Ubiquitination is associated with lysosomal degradation of cell surface-resident ATP-binding cassette transporter A1 (ABCA1) through the endosomal sorting complex required for transport (ESCRT) pathway. Hepatology. 54: 631-643.
    • (2011) Hepatology , vol.54 , pp. 631-643
    • Mizuno, T.1    Hayashi, H.2    Naoi, S.3    Sugiyama, Y.4
  • 58
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • DOI 10.1038/nrm2162, PII NRM2162
    • Williams, R. L., and S. Urbe. 2007. The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell Biol. 8: 355-368. (Pubitemid 46643239)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 59
    • 78049404751 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8.STAM complex
    • Berlin, I., H. Schwartz, and P. D. Nash. 2010. Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8.STAM complex. J. Biol. Chem. 285: 34909-34921.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34909-34921
    • Berlin, I.1    Schwartz, H.2    Nash, P.D.3
  • 60
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., G. Marino, and B. Levine. 2010. Autophagy and the integrated stress response. Mol. Cell. 40: 280-293.
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.