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Volumn 11, Issue , 2017, Pages

Gp78 E3 ubiquitin ligase: Essential functions and contributions in proteostasis

Author keywords

Cancer; E3 ubiquitin ligases; Gp78; Neurodegenerative diseases; Neurons

Indexed keywords

CD82 ANTIGEN; COPPER ZINC SUPEROXIDE DISMUTASE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; DIACYLGLYCEROL ACYLTRANSFERASE 2; GLYCOPROTEIN; GLYCOPROTEIN 78; HEAT SHOCK PROTEIN 70; HISTONE DEACETYLASE 6; INTERFERON; PEPTIDES AND PROTEINS; PHOSPHATIDYLINOSITOL 3 KINASE; RAM 1 HOMOLOG; STEROL REGULATORY ELEMENT BINDING PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VERY LOW DENSITY LIPOPROTEIN;

EID: 85032009771     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2017.00259     Document Type: Review
Times cited : (45)

References (173)
  • 1
    • 84874700285 scopus 로고    scopus 로고
    • Cholesterol homeostasis: A key to prevent or slow down neurodegeneration
    • Anchisi, L., Dessi, S., Pani, A., and Mandas, A. (2013). Cholesterol homeostasis: a key to prevent or slow down neurodegeneration. Front. Physiol. 3:486. doi: 10.3389/fphys.2012.00486
    • (2013) Front. Physiol , vol.3 , pp. 486
    • Anchisi, L.1    Dessi, S.2    Pani, A.3    Mandas, A.4
  • 2
    • 70549109093 scopus 로고    scopus 로고
    • Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1
    • Ballar, P., Ors, A. U., Yang, H., and Fang, S. (2010). Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1. Int. J. Biochem. Cell Biol. 42, 167–173. doi: 10.1016/j.biocel.2009.10.005
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , pp. 167-173
    • Ballar, P.1    Ors, A.U.2    Yang, H.3    Fang, S.4
  • 3
    • 33845917801 scopus 로고    scopus 로고
    • The role of a novel p97/valosincontaining protein-interacting motif of gp78 in endoplasmic reticulumassociated degradation
    • Ballar, P., Shen, Y., Yang, H., and Fang, S. (2006). The role of a novel p97/valosincontaining protein-interacting motif of gp78 in endoplasmic reticulumassociated degradation. J. Biol. Chem. 281, 35359–35368. doi: 10.1074/jbc.M603355200
    • (2006) J. Biol. Chem , vol.281 , pp. 35359-35368
    • Ballar, P.1    Shen, Y.2    Yang, H.3    Fang, S.4
  • 4
    • 36348954034 scopus 로고    scopus 로고
    • Identification of SVIP as an endogenous inhibitor of endoplasmic reticulumassociated degradation
    • Ballar, P., Zhong, Y., Nagahama, M., Tagaya, M., Shen, Y., and Fang, S. (2007). Identification of SVIP as an endogenous inhibitor of endoplasmic reticulumassociated degradation. J. Biol. Chem. 282, 33908–33914. doi: 10.1074/jbc.M704446200
    • (2007) J. Biol. Chem , vol.282 , pp. 33908-33914
    • Ballar, P.1    Zhong, Y.2    Nagahama, M.3    Tagaya, M.4    Shen, Y.5    Fang, S.6
  • 5
    • 0031847686 scopus 로고    scopus 로고
    • Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum
    • Benlimame, N., Le, P. U., and Nabi, I. R. (1998). Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol. Biol. Cell 9, 1773–1786. doi: 10.1091/mbc.9.7.1773
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1773-1786
    • Benlimame, N.1    Le, P.U.2    Nabi, I.R.3
  • 6
    • 0028968280 scopus 로고
    • Autocrine motility factor receptor is a marker for a distinct membranous tubular organelle
    • Benlimame, N., Simard, D., and Nabi, I. R. (1995). Autocrine motility factor receptor is a marker for a distinct membranous tubular organelle. J. Cell Biol. 129, 459–471. doi: 10.1083/jcb.129.2.459
    • (1995) J. Cell Biol , vol.129 , pp. 459-471
    • Benlimame, N.1    Simard, D.2    Nabi, I.R.3
  • 7
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I., and Bulleid, N. J. (2011). Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 80, 71–99. doi: 10.1146/annurev-biochem-062209-093836
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 8
    • 84954207877 scopus 로고    scopus 로고
    • Ribosome-associated protein quality control
    • Brandman, O., and Hegde, R. S. (2016). Ribosome-associated protein quality control. Nat. Struct. Mol. Biol. 23, 7–15. doi: 10.1038/nsmb.3147
    • (2016) Nat. Struct. Mol. Biol , vol.23 , pp. 7-15
    • Brandman, O.1    Hegde, R.S.2
  • 9
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • Buchberger, A., Bukau, B., and Sommer, T. (2010). Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell 40, 238–252. doi: 10.1016/j.molcel.2010.10.001
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 10
    • 34547464338 scopus 로고    scopus 로고
    • Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase
    • Cao, J., Wang, J., Qi, W., Miao, H. H., Wang, J., Ge, L., et al. (2007). Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase. Cell Metab. 6, 115–128. doi: 10.1016/j.cmet.2007.07.002
    • (2007) Cell Metab , vol.6 , pp. 115-128
    • Cao, J.1    Wang, J.2    Qi, W.3    Miao, H.H.4    Wang, J.5    Ge, L.6
  • 11
    • 84905374434 scopus 로고    scopus 로고
    • Varicella-zoster virus glycoprotein expression differentially induces the unfolded protein response in infected cells
    • Carpenter, J. E., and Grose, C. (2014). Varicella-zoster virus glycoprotein expression differentially induces the unfolded protein response in infected cells. Front. Microbiol. 5:322. doi: 10.3389/fmicb.2014.00322
    • (2014) Front. Microbiol , vol.5 , pp. 322
    • Carpenter, J.E.1    Grose, C.2
  • 12
    • 84933557467 scopus 로고    scopus 로고
    • Deacetylation of HSPA5 by HDAC6 leads to GP78-mediated HSPA5 ubiquitination at K447 and suppresses metastasis of breast cancer
    • Chang, Y. W., Tseng, C. F., Wang, M. Y., Chang, W. C., Lee, C. C., Chen, L. T., et al. (2015). Deacetylation of HSPA5 by HDAC6 leads to GP78-mediated HSPA5 ubiquitination at K447 and suppresses metastasis of breast cancer. Oncogene 35, 1517–1528. doi: 10.1038/onc.2015.214
    • (2015) Oncogene , vol.35 , pp. 1517-1528
    • Chang, Y.W.1    Tseng, C.F.2    Wang, M.Y.3    Chang, W.C.4    Lee, C.C.5    Chen, L.T.6
  • 13
    • 84904719533 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase gp78 protects against ER stress in zebrafish liver
    • Chen, Z., Ballar, P., Fu, Y., Luo, J., Du, S., and Fang, S. (2014). The E3 ubiquitin ligase gp78 protects against ER stress in zebrafish liver. J. Genet. Genomics 41, 357–368. doi: 10.1016/j.jgg.2014.05.005
    • (2014) J. Genet. Genomics , vol.41 , pp. 357-368
    • Chen, Z.1    Ballar, P.2    Fu, Y.3    Luo, J.4    Du, S.5    Fang, S.6
  • 14
    • 84866558646 scopus 로고    scopus 로고
    • Gp78: A multifaceted ubiquitin ligase that integrates a unique protein degradation pathway from the endoplasmic reticulum
    • Chen, Z., Du, S., and Fang, S. (2012). Gp78: a multifaceted ubiquitin ligase that integrates a unique protein degradation pathway from the endoplasmic reticulum. Curr. Protein Pept. Sci. 13, 414–424. doi: 10.2174/138920312802430590
    • (2012) Curr. Protein Pept. Sci , vol.13 , pp. 414-424
    • Chen, Z.1    Du, S.2    Fang, S.3
  • 15
    • 31044437051 scopus 로고    scopus 로고
    • The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger and an E2-binding site
    • Chen, B., Mariano, J., Tsai, Y. C., Chan, A. H., Cohen, M., and Weissman, A. M. (2006). The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger and an E2-binding site. Proc. Natl. Acad. Sci. U S A 103, 341–346. doi: 10.1073/pnas.0506618103
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 341-346
    • Chen, B.1    Mariano, J.2    Tsai, Y.C.3    Chan, A.H.4    Cohen, M.5    Weissman, A.M.6
  • 17
    • 84902551040 scopus 로고    scopus 로고
    • Autophagy coupling interplay: Can improve cellular repair and aging?
    • Chhangani, D., Chinchwadkar, S., and Mishra, A. (2014). Autophagy coupling interplay: can improve cellular repair and aging? Mol. Neurobiol. 49, 1270–1281. doi: 10.1007/s12035-013-8599-z
    • (2014) Mol. Neurobiol , vol.49 , pp. 1270-1281
    • Chhangani, D.1    Chinchwadkar, S.2    Mishra, A.3
  • 18
    • 84867440649 scopus 로고    scopus 로고
    • E3 ubiquitin ligases in protein quality control mechanism
    • Chhangani, D., Joshi, A. P., and Mishra, A. (2012). E3 ubiquitin ligases in protein quality control mechanism. Mol. Neurobiol. 45, 571–585. doi: 10.1007/s12035-012-8273-x
    • (2012) Mol. Neurobiol , vol.45 , pp. 571-585
    • Chhangani, D.1    Joshi, A.P.2    Mishra, A.3
  • 19
    • 84880923587 scopus 로고    scopus 로고
    • Protein quality control system in neurodegeneration: A healing company hard to beat but failure is fatal
    • Chhangani, D., and Mishra, A. (2013). Protein quality control system in neurodegeneration: a healing company hard to beat but failure is fatal. Mol. Neurobiol. 48, 141–156. doi: 10.1007/s12035-013-8411-0
    • (2013) Mol. Neurobiol , vol.48 , pp. 141-156
    • Chhangani, D.1    Mishra, A.2
  • 20
    • 40749110529 scopus 로고    scopus 로고
    • Autocrine motility factor receptor: A clinical review
    • Chiu, C. G., St-Pierre, P., Nabi, I. R., and Wiseman, S. M. (2008). Autocrine motility factor receptor: a clinical review. Expert Rev. Anticancer Ther. 8, 207–217. doi: 10.1586/14737140.8.2.207
    • (2008) Expert Rev. Anticancer Ther , vol.8 , pp. 207-217
    • Chiu, C.G.1    St-Pierre, P.2    Nabi, I.R.3    Wiseman, S.M.4
  • 21
    • 84903818479 scopus 로고    scopus 로고
    • Regulation of diacylglycerol acyltransferase 2 protein stability by gp78-associated endoplasmic-reticulum-associated degradation
    • Choi, K., Kim, H., Kang, H., Lee, S. Y., Lee, S. J., Back, S. H., et al. (2014). Regulation of diacylglycerol acyltransferase 2 protein stability by gp78-associated endoplasmic-reticulum-associated degradation. FEBS J. 281, 3048–3060. doi: 10.1111/febs.12841
    • (2014) FEBS J , vol.281 , pp. 3048-3060
    • Choi, K.1    Kim, H.2    Kang, H.3    Lee, S.Y.4    Lee, S.J.5    Back, S.H.6
  • 22
    • 84868629163 scopus 로고    scopus 로고
    • Attenuated adenosine-to-inosine editing of microRNA-376a_ promotes invasiveness of glioblastoma cells
    • Choudhury, Y., Tay, F. C., Lam, D. H., Sandanaraj, E., Tang, C., Ang, B.-T., et al. (2012). Attenuated adenosine-to-inosine editing of microRNA-376a_ promotes invasiveness of glioblastoma cells. J. Clin. Invest. 122, 4059–4076. doi: 10.1172/JCI62925
    • (2012) J. Clin. Invest , vol.122 , pp. 4059-4076
    • Choudhury, Y.1    Tay, F.C.2    Lam, D.H.3    Sandanaraj, E.4    Tang, C.5    Ang, B.-T.6
  • 23
    • 84898729879 scopus 로고    scopus 로고
    • Cleaning up in the endoplasmic reticulum: Ubiquitin in charge
    • Christianson, J. C., and Ye, Y. (2014). Cleaning up in the endoplasmic reticulum: ubiquitin in charge. Nat. Struct. Mol. Biol. 21, 325–335. doi: 10.1038/nsmb.2793
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 325-335
    • Christianson, J.C.1    Ye, Y.2
  • 24
    • 67449110736 scopus 로고    scopus 로고
    • Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78
    • Das, R., Mariano, J., Tsai, Y. C., Kalathur, R. C., Kostova, Z., Li, J., et al. (2009). Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78. Mol. Cell 34, 674–685. doi: 10.1016/j.molcel.2009.05.010
    • (2009) Mol. Cell , vol.34 , pp. 674-685
    • Das, R.1    Mariano, J.2    Tsai, Y.C.3    Kalathur, R.C.4    Kostova, Z.5    Li, J.6
  • 25
    • 44849131929 scopus 로고    scopus 로고
    • Feedback regulation of cholesterol synthesis: Sterolaccelerated ubiquitination and degradation of HMG CoA reductase
    • Debose-Boyd, R. A. (2008). Feedback regulation of cholesterol synthesis: sterolaccelerated ubiquitination and degradation of HMG CoA reductase. Cell Res. 18, 609–621. doi: 10.1038/cr.2008.61
    • (2008) Cell Res , vol.18 , pp. 609-621
    • Debose-Boyd, R.A.1
  • 26
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis, R. J. (2001). Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26, 597–604. doi: 10.1016/s0968-0004(01)01938-7
    • (2001) Trends Biochem. Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 27
    • 33746090453 scopus 로고    scopus 로고
    • Prognostic value of cell motility activation factors in patients with tongue squamous cell carcinoma
    • Endo, K., Shirai, A., Furukawa, M., and Yoshizaki, T. (2006). Prognostic value of cell motility activation factors in patients with tongue squamous cell carcinoma. Hum. Pathol. 37, 1111–1116. doi: 10.1016/j.humpath.2006.03.020
    • (2006) Hum. Pathol , vol.37 , pp. 1111-1116
    • Endo, K.1    Shirai, A.2    Furukawa, M.3    Yoshizaki, T.4
  • 28
    • 70349328536 scopus 로고    scopus 로고
    • The complex biology of autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and its receptor, the gp78/AMFR E3 ubiquitin ligase
    • Fairbank, M., St-Pierre, P., and Nabi, I. R. (2009). The complex biology of autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and its receptor, the gp78/AMFR E3 ubiquitin ligase. Mol. Biosyst. 5, 793–801. doi: 10.1039/b820820b
    • (2009) Mol. Biosyst , vol.5 , pp. 793-801
    • Fairbank, M.1    St-Pierre, P.2    Nabi, I.R.3
  • 29
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang, S., Ferrone, M., Yang, C., Jensen, J. P., Tiwari, S., and Weissman, A. M. (2001). The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U S A 98, 14422–14427. doi: 10.1073/pnas.251401598
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 30
    • 0037331103 scopus 로고    scopus 로고
    • RING finger ubiquitin protein ligases: Implications for tumorigenesis, metastasis and for molecular targets in cancer
    • Fang, S., Lorick, K. L., Jensen, J. P., and Weissman, A. M. (2003). RING finger ubiquitin protein ligases: implications for tumorigenesis, metastasis and for molecular targets in cancer. Semin Cancer Biol. 13, 5–14. doi: 10.1016/s1044-579x(02)00095-0
    • (2003) Semin Cancer Biol , vol.13 , pp. 5-14
    • Fang, S.1    Lorick, K.L.2    Jensen, J.P.3    Weissman, A.M.4
  • 31
    • 67649822858 scopus 로고    scopus 로고
    • The AAA-ATPase p97 facilitates degradation of apolipoprotein B by the ubiquitinproteasome pathway
    • Fisher, E. A., Lapierre, L. R., Junkins, R. D., and McLeod, R. S. (2008). The AAA-ATPase p97 facilitates degradation of apolipoprotein B by the ubiquitinproteasome pathway. J. Lipid Res. 49, 2149–2160. doi: 10.1194/jlr.M800108-JLR200
    • (2008) J. Lipid Res , vol.49 , pp. 2149-2160
    • Fisher, E.A.1    Lapierre, L.R.2    Junkins, R.D.3    McLeod, R.S.4
  • 32
    • 79955839745 scopus 로고    scopus 로고
    • Autocrine motility factor/phosphoglucose isomerase regulates ER stress and cell death through control of ER calcium release
    • Fu, M., Li, L., Albrecht, T., Johnson, J. D., Kojic, L. D., and Nabi, I. R. (2011). Autocrine motility factor/phosphoglucose isomerase regulates ER stress and cell death through control of ER calcium release. Cell Death Differ. 18, 1057–1070. doi: 10.1038/cdd.2010.181
    • (2011) Cell Death Differ , vol.18 , pp. 1057-1070
    • Fu, M.1    Li, L.2    Albrecht, T.3    Johnson, J.D.4    Kojic, L.D.5    Nabi, I.R.6
  • 33
    • 84876524198 scopus 로고    scopus 로고
    • Regulation of mitophagy by the Gp78 E3 ubiquitin ligase
    • Fu, M., St-Pierre, P., Shankar, J., Wang, P. T., Joshi, B., and Nabi, I. R. (2013). Regulation of mitophagy by the Gp78 E3 ubiquitin ligase. Mol. Biol. Cell 24, 1153–1162. doi: 10.1091/mbc.E12-08-0607
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1153-1162
    • Fu, M.1    St-Pierre, P.2    Shankar, J.3    Wang, P.T.4    Joshi, B.5    Nabi, I.R.6
  • 34
    • 0034816920 scopus 로고    scopus 로고
    • Tumor autocrine motility factor is an angiogenic factor hat stimulates endothelial cell motility
    • Funasaka, T., Haga, A., Raz, A., and Nagase, H. (2001). Tumor autocrine motility factor is an angiogenic factor hat stimulates endothelial cell motility. Biochem. Biophys. Res. Commun. 284, 1116–1125. doi: 10.1006/bbrc.2001.4912
    • (2001) Biochem. Biophys. Res. Commun , vol.284 , pp. 1116-1125
    • Funasaka, T.1    Haga, A.2    Raz, A.3    Nagase, H.4
  • 35
    • 0037144363 scopus 로고    scopus 로고
    • Autocrine motility factor secreted by tumor cells upregulates vascular endothelial growth factor receptor (Flt-1) expression in endothelial cells
    • Funasaka, T., Haga, A., Raz, A., and Nagase, H. (2002). Autocrine motility factor secreted by tumor cells upregulates vascular endothelial growth factor receptor (Flt-1) expression in endothelial cells. Int. J. Cancer 101, 217–223. doi: 10.1002/ijc.10617
    • (2002) Int. J. Cancer , vol.101 , pp. 217-223
    • Funasaka, T.1    Haga, A.2    Raz, A.3    Nagase, H.4
  • 36
    • 34249315460 scopus 로고    scopus 로고
    • Downregulation of phosphoglucose isomerase/autocrine motility factor results in mesenchymal-to-epithelial transition of human lung fibrosarcoma cells
    • Funasaka, T., Hu, H., Yanagawa, T., Hogan, V., and Raz, A. (2007). Downregulation of phosphoglucose isomerase/autocrine motility factor results in mesenchymal-to-epithelial transition of human lung fibrosarcoma cells. Cancer Res. 67, 4236–4243. doi: 10.1158/0008-5472.can-06-3935
    • (2007) Cancer Res , vol.67 , pp. 4236-4243
    • Funasaka, T.1    Hu, H.2    Yanagawa, T.3    Hogan, V.4    Raz, A.5
  • 37
    • 84859612545 scopus 로고    scopus 로고
    • Protein quality control in neurodegenerative disease
    • Gestwicki, J. E., and Garza, D. (2012). Protein quality control in neurodegenerative disease. Prog. Mol. Biol. Transl. Sci. 107, 327–353. doi: 10.1016/B978-0-12-385883-2.00003-5
    • (2012) Prog. Mol. Biol. Transl. Sci , vol.107 , pp. 327-353
    • Gestwicki, J.E.1    Garza, D.2
  • 38
    • 36248938166 scopus 로고    scopus 로고
    • Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2C levels
    • Goetz, J. G., Genty, H., St-Pierre, P., Dang, T., Joshi, B., Sauvé, R., et al. (2007). Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2C levels. J. Cell Sci. 120, 3553–3564. doi: 10.1242/jcs.03486
    • (2007) J. Cell Sci , vol.120 , pp. 3553-3564
    • Goetz, J.G.1    Genty, H.2    St-Pierre, P.3    Dang, T.4    Joshi, B.5    Sauvé, R.6
  • 39
    • 27144447999 scopus 로고    scopus 로고
    • Giant cell tumors of the bone: Molecular profiling and expression analysis of Ephrin A1 receptor, Claudin 7, CD52, FGFR3 and AMFR
    • Guenther, R., Krenn, V., Morawietz, L., Dankof, A., Melcher, I., Schaser, K. D., et al. (2005). Giant cell tumors of the bone: molecular profiling and expression analysis of Ephrin A1 receptor, Claudin 7, CD52, FGFR3 and AMFR. Pathol. Res. Pract. 201, 649–663. doi: 10.1016/j.prp.2005.07.005
    • (2005) Pathol. Res. Pract , vol.201 , pp. 649-663
    • Guenther, R.1    Krenn, V.2    Morawietz, L.3    Dankof, A.4    Melcher, I.5    Schaser, K.D.6
  • 40
    • 33646487483 scopus 로고    scopus 로고
    • The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF
    • Haga, A., Tanaka, N., Funasaka, T., Hashimoto, K., Nakamura, K. T., Watanabe, H., et al. (2006). The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF. J. Mol. Biol. 358, 741–753. doi: 10.1016/j.jmb.2006.02.046
    • (2006) J. Mol. Biol , vol.358 , pp. 741-753
    • Haga, A.1    Tanaka, N.2    Funasaka, T.3    Hashimoto, K.4    Nakamura, K.T.5    Watanabe, H.6
  • 41
    • 84944463374 scopus 로고    scopus 로고
    • Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease
    • Hara, T., Hashimoto, Y., Akuzawa, T., Hirai, R., Kobayashi, H., and Sato, K. (2014). Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease. Sci. Rep. 4:6992. doi: 10.1038/srep06992
    • (2014) Sci. Rep , vol.4 , pp. 6992
    • Hara, T.1    Hashimoto, Y.2    Akuzawa, T.3    Hirai, R.4    Kobayashi, H.5    Sato, K.6
  • 42
    • 85021678559 scopus 로고    scopus 로고
    • Protein misfolding diseases
    • Hartl, F. U. (2017). Protein misfolding diseases. Annu. Rev. Biochem. 86, 21–26. doi: 10.1146/annurev-biochem-061516-044518
    • (2017) Annu. Rev. Biochem , vol.86 , pp. 21-26
    • Hartl, F.U.1
  • 43
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324–332. doi: 10.1038/nature10317
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 44
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert, D. N., and Molinari, M. (2007). In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 87, 1377–1408. doi: 10.1152/physrev.00050.2006
    • (2007) Physiol. Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 45
    • 0025285731 scopus 로고
    • Retinoic acid inhibition of human melanoma cell invasion through a reconstituted basement membrane and its relation to decreases in the expression of proteolytic enzymes and motility factor receptor
    • Hendrix, M. J., Wood, W. R., Seftor, E. A., Lotan, D., Nakajima, M., Misiorowski, R. L., et al. (1990). Retinoic acid inhibition of human melanoma cell invasion through a reconstituted basement membrane and its relation to decreases in the expression of proteolytic enzymes and motility factor receptor. Cancer Res. 50, 4121–4130.
    • (1990) Cancer Res , vol.50 , pp. 4121-4130
    • Hendrix, M.J.1    Wood, W.R.2    Seftor, E.A.3    Lotan, D.4    Nakajima, M.5    Misiorowski, R.L.6
  • 46
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A., and Ciechanover, A. (1992). The ubiquitin system for protein degradation. Ann. Rev. Biochem. 61, 761–807. doi: 10.1146/annurev.bi.61.070192.003553
    • (1992) Ann. Rev. Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 47
    • 84906794886 scopus 로고    scopus 로고
    • Proteostasis impairment in protein-misfolding and-aggregation diseases
    • Hipp, M. S., Park, S.-H., and Hartl, F. U. (2014). Proteostasis impairment in protein-misfolding and-aggregation diseases. Trends Cell Biol. 24, 506–514. doi: 10.1016/j.tcb.2014.05.003
    • (2014) Trends Cell Biol , vol.24 , pp. 506-514
    • Hipp, M.S.1    Park, S.-H.2    Hartl, F.U.3
  • 48
    • 0030469819 scopus 로고    scopus 로고
    • Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer
    • Hirono, Y., Fushida, S., Yonemura, Y., Yamamoto, H., Watanabe, H., and Raz, A. (1996). Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer. Br. J. Cancer 74, 2003–2007. doi: 10.1038/bjc.1996.667
    • (1996) Br. J. Cancer , vol.74 , pp. 2003-2007
    • Hirono, Y.1    Fushida, S.2    Yonemura, Y.3    Yamamoto, H.4    Watanabe, H.5    Raz, A.6
  • 49
    • 33744454931 scopus 로고    scopus 로고
    • Antibody responses associated with the graft-versus-leukemia effect in adult T-cell leukemia
    • Hishizawa, M., Imada, K., Sakai, T., Nishikori, M., Arima, N., Tsudo, M., et al. (2006). Antibody responses associated with the graft-versus-leukemia effect in adult T-cell leukemia. Int. J. Hematol. 83, 351–355. doi: 10.1532/ijh97.05173
    • (2006) Int. J. Hematol , vol.83 , pp. 351-355
    • Hishizawa, M.1    Imada, K.2    Sakai, T.3    Nishikori, M.4    Arima, N.5    Tsudo, M.6
  • 50
    • 56049111865 scopus 로고    scopus 로고
    • Drug development against metastasis-related genes and their pathways: A rationale for cancer therapy
    • Iiizumi, M., Liu, W., Pai, S. K., Furuta, E., and Watabe, K. (2008). Drug development against metastasis-related genes and their pathways: a rationale for cancer therapy. Biochim. Biophys. Acta 1786, 87–104. doi: 10.1016/j.bbcan.2008.07.002
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 87-104
    • Iiizumi, M.1    Liu, W.2    Pai, S.K.3    Furuta, E.4    Watabe, K.5
  • 51
    • 70349943834 scopus 로고    scopus 로고
    • STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
    • Ishikawa, H., Ma, Z., and Barber, G. N. (2009). STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature 461, 788–792. doi: 10.1038/nature08476
    • (2009) Nature , vol.461 , pp. 788-792
    • Ishikawa, H.1    Ma, Z.2    Barber, G.N.3
  • 52
    • 84892660511 scopus 로고    scopus 로고
    • Regulation of mitochondrial antiviral signaling (MAVS) expression and signaling by the mitochondria-associated endoplasmic reticulum membrane (MAM) protein Gp78
    • Jacobs, J. L., Zhu, J., Sarkar, S. N., and Coyne, C. B. (2014). Regulation of mitochondrial antiviral signaling (MAVS) expression and signaling by the mitochondria-associated endoplasmic reticulum membrane (MAM) protein Gp78. J. Biol. Chem. 289, 1604–1616. doi: 10.1074/jbc.M113.520254
    • (2014) J. Biol. Chem , vol.289 , pp. 1604-1616
    • Jacobs, J.L.1    Zhu, J.2    Sarkar, S.N.3    Coyne, C.B.4
  • 53
    • 32044444363 scopus 로고    scopus 로고
    • Expression of autocrine motility factor (AMF) and its receptor, AMFR, in human breast cancer
    • Jiang, W. G., Raz, A., Douglas-Jones, A., and Mansel, R. E. (2006). Expression of autocrine motility factor (AMF) and its receptor, AMFR, in human breast cancer. J. Histochem. Cytochem. 54, 231–241. doi: 10.1369/jhc.5a6785.2005
    • (2006) J. Histochem. Cytochem , vol.54 , pp. 231-241
    • Jiang, W.G.1    Raz, A.2    Douglas-Jones, A.3    Mansel, R.E.4
  • 54
    • 84991735277 scopus 로고    scopus 로고
    • A decade of boon or burden: What has the CHIP ever done for cellular protein quality control mechanism implicated in neurodegeneration and aging?
    • Joshi, V., Amanullah, A., Upadhyay, A., Mishra, R., Kumar, A., and Mishra, A. (2016). A decade of boon or burden: what has the CHIP ever done for cellular protein quality control mechanism implicated in neurodegeneration and aging? Front. Mol. Neurosci. 9:93. doi: 10.3389/fnmol.2016.00093
    • (2016) Front. Mol. Neurosci , vol.9 , pp. 93
    • Joshi, V.1    Amanullah, A.2    Upadhyay, A.3    Mishra, R.4    Kumar, A.5    Mishra, A.6
  • 55
    • 77950556316 scopus 로고    scopus 로고
    • A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase
    • Joshi, B., Li, L., and Nabi, I. R. (2010). A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase. J. Biol. Chem. 285, 8830–8839. doi: 10.1074/jbc.M109.074344
    • (2010) J. Biol. Chem , vol.285 , pp. 8830-8839
    • Joshi, B.1    Li, L.2    Nabi, I.R.3
  • 56
    • 0035106231 scopus 로고    scopus 로고
    • Autocrine motility factor receptor expression in patients with stage I non-small cell lung cancer
    • Kara, M., Ohta, Y., Tanaka, Y., Oda, M., and Watanabe, Y. (2001). Autocrine motility factor receptor expression in patients with stage I non-small cell lung cancer. Ann. Thorac Surg. 71, 944–948. doi: 10.1016/s0003-4975(00)02135-4
    • (2001) Ann. Thorac Surg , vol.71 , pp. 944-948
    • Kara, M.1    Ohta, Y.2    Tanaka, Y.3    Oda, M.4    Watanabe, Y.5
  • 57
    • 0033999415 scopus 로고    scopus 로고
    • Correlation between loss of E-cadherin expression and overexpression of autocrine motility factor receptor in association with progression of human gastric cancers
    • Kawanishi, K., Doki, Y., Shiozaki, H., Yano, M., Inoue, M., Fukuchi, N., et al. (2000). Correlation between loss of E-cadherin expression and overexpression of autocrine motility factor receptor in association with progression of human gastric cancers. Am. J. Clin. Pathol. 113, 266–274. doi: 10.1309/jh4q-25q5-0trv-w99u
    • (2000) Am. J. Clin. Pathol , vol.113 , pp. 266-274
    • Kawanishi, K.1    Doki, Y.2    Shiozaki, H.3    Yano, M.4    Inoue, M.5    Fukuchi, N.6
  • 58
    • 24644448848 scopus 로고    scopus 로고
    • Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas
    • Kaynak, K., Kara, M., Oz, B., Akgoz, B., Sar, M., and Raz, A. (2005). Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas. Acta Chir. Belg. 105, 378–382. doi: 10.1080/00015458.2005.11679740
    • (2005) Acta Chir. Belg , vol.105 , pp. 378-382
    • Kaynak, K.1    Kara, M.2    Oz, B.3    Akgoz, B.4    Sar, M.5    Raz, A.6
  • 59
    • 78149241047 scopus 로고    scopus 로고
    • Liver cytochrome P450 3A ubiquitination in vivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: Physiological and pharmacological relevance
    • Kim, S. M., Acharya, P., Engel, J. C., and Correia, M. A. (2010). Liver cytochrome P450 3A ubiquitination in vivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: physiological and pharmacological relevance. J. Biol. Chem. 285, 35866–35877. doi: 10.1074/jbc.M110.167189
    • (2010) J. Biol. Chem , vol.285 , pp. 35866-35877
    • Kim, S.M.1    Acharya, P.2    Engel, J.C.3    Correia, M.A.4
  • 60
    • 56349089024 scopus 로고    scopus 로고
    • Raft-dependent endocytosis of autocrine motility factor/phosphoglucose isomerase: A potential drug delivery route for tumor cells
    • Kojic, L. D., Wiseman, S. M., Ghaidi, F., Joshi, B., Nedev, H., Saragovi, H. U., et al. (2008). Raft-dependent endocytosis of autocrine motility factor/phosphoglucose isomerase: a potential drug delivery route for tumor cells. PLoS One 3:e3597. doi: 10.1371/journal.pone.0003597
    • (2008) Plos One , vol.3
    • Kojic, L.D.1    Wiseman, S.M.2    Ghaidi, F.3    Joshi, B.4    Nedev, H.5    Saragovi, H.U.6
  • 61
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito, R. R. (1997). ER quality control: the cytoplasmic connection. Cell 88, 427–430. doi: 10.1016/s0092-8674(00)81881-4
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 62
    • 0029655913 scopus 로고    scopus 로고
    • Autocrine motility factor receptor as a possible urine marker for transitional cell carcinoma of the bladder
    • Korman, H. J., Peabody, J. O., Cerny, J. C., Farah, R. N., Yao, J., and Raz, A. (1996). Autocrine motility factor receptor as a possible urine marker for transitional cell carcinoma of the bladder. J. Urol. 155, 347–349. doi: 10.1097/00005392-199601000-00137
    • (1996) J. Urol , vol.155 , pp. 347-349
    • Korman, H.J.1    Peabody, J.O.2    Cerny, J.C.3    Farah, R.N.4    Yao, J.5    Raz, A.6
  • 63
    • 84883187967 scopus 로고    scopus 로고
    • Emerging roles of E3 ubiquitin ligases in autophagy
    • Kuang, E., Qi, J., and Ronai, Z. E. (2013). Emerging roles of E3 ubiquitin ligases in autophagy. Trends Biochem. Sci. 38, 453–460. doi: 10.1016/j.tibs.2013.06.008
    • (2013) Trends Biochem. Sci , vol.38 , pp. 453-460
    • Kuang, E.1    Qi, J.2    Ronai, Z.E.3
  • 64
    • 0033794698 scopus 로고    scopus 로고
    • Clathrinmediated endocytosis and recycling of autocrine motility factor receptor to fibronectin fibrils is a limiting factor for NIH-3T3 cell motility
    • Le, P. U., Benlimame, N., Lagana, A., Raz, A., and Nabi, I. R. (2000). Clathrinmediated endocytosis and recycling of autocrine motility factor receptor to fibronectin fibrils is a limiting factor for NIH-3T3 cell motility. J. Cell Sci. 113, 3227–3240. doi: 10.1007/978-3-0348-7494-6_11
    • (2000) J. Cell Sci , vol.113 , pp. 3227-3240
    • Le, P.U.1    Benlimame, N.2    Lagana, A.3    Raz, A.4    Nabi, I.R.5
  • 65
    • 0034212768 scopus 로고    scopus 로고
    • Expression of the AMF/neuroleukin receptor in developing and adult brain cerebellum
    • Leclerc, N., Vallée, A., and Nabi, I. R. (2000). Expression of the AMF/neuroleukin receptor in developing and adult brain cerebellum. J. Neurosci. Res. 60, 602–612. doi: 10.1002/(sici)1097-4547(20000601)60:5<602::aid-jnr5>3.3.co;2-6
    • (2000) J. Neurosci. Res , vol.60 , pp. 602-612
    • Leclerc, N.1    Vallée, A.2    Nabi, I.R.3
  • 66
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters, J. J. (2005). Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res. 8, 3–5. doi: 10.1089/rej.2005.8.3
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 67
    • 84945926634 scopus 로고    scopus 로고
    • P38 MAP kinase-dependent phosphorylation of the Gp78 E3 ubiquitin ligase controls ER-mitochondria association and mitochondria motility
    • Li, L., Gao, G., Shankar, J., Joshi, B., Foster, L. J., and Nabi, I. R. (2015). p38 MAP kinase-dependent phosphorylation of the Gp78 E3 ubiquitin ligase controls ER-mitochondria association and mitochondria motility. Mol. Biol. Cell 26, 3828–3840. doi: 10.1091/mbc.E15-02-0120
    • (2015) Mol. Biol. Cell , vol.26 , pp. 3828-3840
    • Li, L.1    Gao, G.2    Shankar, J.3    Joshi, B.4    Foster, L.J.5    Nabi, I.R.6
  • 68
    • 62649096662 scopus 로고    scopus 로고
    • Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2
    • Li, W., Tu, D., Li, L., Wollert, T., Ghirlando, R., Brunger, A. T., et al. (2009). Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proc. Natl. Acad. Sci. U S A 106, 3722–3727. doi: 10.1073/pnas.0808564106
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 3722-3727
    • Li, W.1    Tu, D.2    Li, L.3    Wollert, T.4    Ghirlando, R.5    Brunger, A.T.6
  • 69
    • 0037929972 scopus 로고    scopus 로고
    • Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells
    • Liang, J. S., Kim, T., Fang, S., Yamaguchi, J., Weissman, A. M., Fisher, E. A., et al. (2003). Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells. J. Biol. Chem. 278, 23984–23988. doi: 10.1074/jbc.M302683200
    • (2003) J. Biol. Chem , vol.278 , pp. 23984-23988
    • Liang, J.S.1    Kim, T.2    Fang, S.3    Yamaguchi, J.4    Weissman, A.M.5    Fisher, E.A.6
  • 71
    • 84864684825 scopus 로고    scopus 로고
    • Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis
    • Liu, T. F., Tang, J. J., Li, P. S., Shen, Y., Li, J. G., Miao, H. H., et al. (2012). Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis. Cell Metab. 16, 213–225. doi: 10.1016/j.cmet.2012.06.014
    • (2012) Cell Metab , vol.16 , pp. 213-225
    • Liu, T.F.1    Tang, J.J.2    Li, P.S.3    Shen, Y.4    Li, J.G.5    Miao, H.H.6
  • 72
    • 0026801067 scopus 로고
    • Suppression of melanoma cell motility factor receptor expression by retinoic acid
    • Lotan, R., Amos, B., Watanabe, H., and Raz, A. (1992). Suppression of melanoma cell motility factor receptor expression by retinoic acid. Cancer Res. 52, 4878–4884.
    • (1992) Cancer Res , vol.52 , pp. 4878-4884
    • Lotan, R.1    Amos, B.2    Watanabe, H.3    Raz, A.4
  • 73
    • 0036325026 scopus 로고    scopus 로고
    • A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78
    • Luo, Y., Long, J. M., Lu, C., Chan, S. L., Spangler, E. L., Mascarucci, P., et al. (2002). A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78. J. Neurochem. 80, 354–361. doi: 10.1046/j.0022-3042.2001.00707.x
    • (2002) J. Neurochem , vol.80 , pp. 354-361
    • Luo, Y.1    Long, J.M.2    Lu, C.3    Chan, S.L.4    Spangler, E.L.5    Mascarucci, P.6
  • 74
    • 0017336461 scopus 로고
    • Rabies virus protein synthesis in infected BHK-21 cells
    • Madore, H. P., and England, J. M. (1977). Rabies virus protein synthesis in infected BHK-21 cells. J. Virol. 22, 102–112.
    • (1977) J. Virol , vol.22 , pp. 102-112
    • Madore, H.P.1    England, J.M.2
  • 75
    • 0028785728 scopus 로고
    • Expression of autocrine motility factor receptor in human esophageal squamous cell carcinoma
    • Maruyama, K., Watanabe, H., Shiozaki, H., Takayama, T., Gofuku, J., Yano, H., et al. (1995). Expression of autocrine motility factor receptor in human esophageal squamous cell carcinoma. Int. J. Cancer 64, 316–321. doi: 10.1002/ijc.2910640506
    • (1995) Int. J. Cancer , vol.64 , pp. 316-321
    • Maruyama, K.1    Watanabe, H.2    Shiozaki, H.3    Takayama, T.4    Gofuku, J.5    Yano, H.6
  • 76
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • McClellan, A. J., Tam, S., Kaganovich, D., and Frydman, J. (2005). Protein quality control: chaperones culling corrupt conformations. Nat. Cell Biol. 7, 736–741. doi: 10.1038/ncb0805-736
    • (2005) Nat. Cell Biol , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 77
    • 77957189436 scopus 로고    scopus 로고
    • ERAD ubiquitin ligases: Multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum
    • Mehnert, M., Sommer, T., and Jarosch, E. (2010). ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays 32, 905–913. doi: 10.1002/bies.201000046
    • (2010) Bioessays , vol.32 , pp. 905-913
    • Mehnert, M.1    Sommer, T.2    Jarosch, E.3
  • 78
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger, M. B., Hristova, V. A., and Weissman, A. M. (2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci. 125, 531–537. doi: 10.1242/jcs.091777
    • (2012) J. Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 79
    • 84890176335 scopus 로고    scopus 로고
    • RINGtype E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
    • Metzger, M. B., Pruneda, J. N., Klevit, R. E., and Weissman, A. M. (2014). RINGtype E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim. Biophys. Acta 1843, 47–60. doi: 10.1016/j.bbamcr.2013.05.026
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 47-60
    • Metzger, M.B.1    Pruneda, J.N.2    Klevit, R.E.3    Weissman, A.M.4
  • 80
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton, A. P. (2000). Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10, 34–39. doi: 10.1016/s0959-440x(99)00045-7
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 81
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • Miranda, E., Römisch, K., and Lomas, D. A. (2004). Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J. Biol. Chem. 279, 28283–28291. doi: 10.1074/jbc.M313166200
    • (2004) J. Biol. Chem , vol.279 , pp. 28283-28291
    • Miranda, E.1    Römisch, K.2    Lomas, D.A.3
  • 82
    • 45849086552 scopus 로고    scopus 로고
    • Molecular crowding effects on structure and stability of DNA
    • Miyoshi, D., and Sugimoto, N. (2008). Molecular crowding effects on structure and stability of DNA. Biochimie 90, 1040–1051. doi: 10.1016/j.biochi.2008.02.009
    • (2008) Biochimie , vol.90 , pp. 1040-1051
    • Miyoshi, D.1    Sugimoto, N.2
  • 83
    • 44949249968 scopus 로고    scopus 로고
    • Gp78 cooperates with RMA1 in endoplasmic reticulumassociated degradation of CFTRDeltaF508
    • Morito, D., Hirao, K., Oda, Y., Hosokawa, N., Tokunaga, F., Cyr, D. M., et al. (2008). Gp78 cooperates with RMA1 in endoplasmic reticulumassociated degradation of CFTRDeltaF508. Mol. Biol. Cell 19, 1328–1336. doi: 10.1091/mbc.E07-06-0601
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1328-1336
    • Morito, D.1    Hirao, K.2    Oda, Y.3    Hosokawa, N.4    Tokunaga, F.5    Cyr, D.M.6
  • 84
    • 84961218919 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of the E3 ligase GP78 by MGRN1 in trans affects mitochondrial homeostasis
    • Mukherjee, R., and Chakrabarti, O. (2016). Ubiquitin-mediated regulation of the E3 ligase GP78 by MGRN1 in trans affects mitochondrial homeostasis. J. Cell Sci. 129, 757–773. doi: 10.1242/jcs.176537
    • (2016) J. Cell Sci , vol.129 , pp. 757-773
    • Mukherjee, R.1    Chakrabarti, O.2
  • 85
    • 0030824257 scopus 로고    scopus 로고
    • AMF-R tubules concentrate in a pericentriolar microtubule domain after MSV transformation of epithelial MDCK cells
    • Nabi, I. R., Guay, G., and Simard, D. (1997). AMF-R tubules concentrate in a pericentriolar microtubule domain after MSV transformation of epithelial MDCK cells. J. Histochem. Cytochem. 45, 1351–1363. doi: 10.1177/002215549704501004
    • (1997) J. Histochem. Cytochem , vol.45 , pp. 1351-1363
    • Nabi, I.R.1    Guay, G.2    Simard, D.3
  • 86
    • 0023635117 scopus 로고
    • Cell shape modulation alters glycosylation of a metastatic melanoma cell-surface antigen
    • Nabi, I. R., and Raz, A. (1987). Cell shape modulation alters glycosylation of a metastatic melanoma cell-surface antigen. Int. J. Cancer 40, 396–402. doi: 10.1002/ijc.2910400319
    • (1987) Int. J. Cancer , vol.40 , pp. 396-402
    • Nabi, I.R.1    Raz, A.2
  • 87
    • 0025134024 scopus 로고
    • Identification of B16–F1 melanoma autocrine motility-like factor receptor
    • Nabi, I. R., Watanabe, H., and Raz, A. (1990). Identification of B16–F1 melanoma autocrine motility-like factor receptor. Cancer Res. 50, 409–414.
    • (1990) Cancer Res , vol.50 , pp. 409-414
    • Nabi, I.R.1    Watanabe, H.2    Raz, A.3
  • 88
    • 0026572472 scopus 로고
    • Autocrine motility factor and its receptor: Role in cell locomotion and metastasis
    • Nabi, I. R., Watanabe, H., and Raz, A. (1992). Autocrine motility factor and its receptor: role in cell locomotion and metastasis. Cancer Metastasis Rev. 11, 5–20. doi: 10.1007/bf00047599
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 5-20
    • Nabi, I.R.1    Watanabe, H.2    Raz, A.3
  • 89
    • 0026042990 scopus 로고
    • Tumor cell autocrine motility factor receptor
    • Nabi, I. R., Watanabe, H., Silletti, S., and Raz, A. (1991). Tumor cell autocrine motility factor receptor. EXS 59, 163–177. doi: 10.1007/978-3-0348-7494-6_11
    • (1991) EXS , vol.59 , pp. 163-177
    • Nabi, I.R.1    Watanabe, H.2    Silletti, S.3    Raz, A.4
  • 90
    • 0030063910 scopus 로고    scopus 로고
    • Expression of autocrine motility factor receptor in cutaneous malignant melanoma
    • Nagai, Y., Ishikawa, O., Miyachi, Y., and Watanabe, H. (1996). Expression of autocrine motility factor receptor in cutaneous malignant melanoma. Dermatology 192, 8–11. doi: 10.1159/000246304
    • (1996) Dermatology , vol.192 , pp. 8-11
    • Nagai, Y.1    Ishikawa, O.2    Miyachi, Y.3    Watanabe, H.4
  • 91
    • 0027978023 scopus 로고
    • Expression of autocrine motility factor receptor in colorectal cancer as a predictor for disease recurrence
    • Nakamori, S., Watanabe, H., Kameyama, M., Imaoka, S., Furukawa, H., Ishikawa, O., et al. (1994). Expression of autocrine motility factor receptor in colorectal cancer as a predictor for disease recurrence. Cancer 74, 1855–1862. doi: 10.1002/1097-0142(19941001)74:7<1855::AIDCNCR2820740705>3.0.CO;2-1
    • (1994) Cancer , vol.74 , pp. 1855-1862
    • Nakamori, S.1    Watanabe, H.2    Kameyama, M.3    Imaoka, S.4    Furukawa, H.5    Ishikawa, O.6
  • 92
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cell-cycle control and cancer
    • Nakayama, K. I., and Nakayama, K. (2006). Ubiquitin ligases: cell-cycle control and cancer. Nat. Rev. Cancer 6, 369–381. doi: 10.1038/nrc1881
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 93
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D. F., and Youle, R. J. (2008). Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183, 795–803. doi: 10.1083/jcb.200809125
    • (2008) J. Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 94
    • 0036147033 scopus 로고    scopus 로고
    • Regulation of cell motility via high and low affinity autocrine motility factor (AMF) receptor in human oral squamous carcinoma cells
    • Niinaka, Y., Haga, A., Negishi, A., Yoshimasu, H., Raz, A., and Amagasa, T. (2002). Regulation of cell motility via high and low affinity autocrine motility factor (AMF) receptor in human oral squamous carcinoma cells. Oral Oncol. 38, 49–55. doi: 10.1016/s1368-8375(01)00022-7
    • (2002) Oral Oncol , vol.38 , pp. 49-55
    • Niinaka, Y.1    Haga, A.2    Negishi, A.3    Yoshimasu, H.4    Raz, A.5    Amagasa, T.6
  • 95
    • 0029809804 scopus 로고    scopus 로고
    • Autocrine motility factor and its receptor expressions in human oral squamous cell carcinoma (SCC) cells
    • Niinaka, Y., Oida, S., Ishisaki, A., Takeda, K., Iimura, T., Maruoka, Y., et al. (1996). Autocrine motility factor and its receptor expressions in human oral squamous cell carcinoma (SCC) cells. Int. J. Oncol. 9, 433–438. doi: 10.3892/ijo.9.3.433
    • (1996) Int. J. Oncol , vol.9 , pp. 433-438
    • Niinaka, Y.1    Oida, S.2    Ishisaki, A.3    Takeda, K.4    Iimura, T.5    Maruoka, Y.6
  • 96
    • 0034241345 scopus 로고    scopus 로고
    • Autocrine motility factor receptor expression associates with tumor progression in thymoma
    • Ohta, Y., Minato, H., Tanaka, Y., Go, T., Oda, M., and Watanabe, Y. (2000a). Autocrine motility factor receptor expression associates with tumor progression in thymoma. Int. J. Oncol. 17, 259–264. doi: 10.3892/ijo.17.2.259
    • (2000) Int. J. Oncol , vol.17 , pp. 259-264
    • Ohta, Y.1    Minato, H.2    Tanaka, Y.3    Go, T.4    Oda, M.5    Watanabe, Y.6
  • 97
    • 0034013025 scopus 로고    scopus 로고
    • Clinicopathological and biological assessment of lung cancers with pleural dissemination
    • Ohta, Y., Tanaka, Y., Hara, T., Oda, M., Watanabe, S., Shimizu, J., et al. (2000b). Clinicopathological and biological assessment of lung cancers with pleural dissemination. Ann. Thorac Surg. 69, 1025–1029. doi: 10.1016/s0003-4975(99)01579-9
    • (2000) Ann. Thorac Surg , vol.69 , pp. 1025-1029
    • Ohta, Y.1    Tanaka, Y.2    Hara, T.3    Oda, M.4    Watanabe, S.5    Shimizu, J.6
  • 98
    • 0037217949 scopus 로고    scopus 로고
    • Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3 fibroblasts induces cell transformation
    • Onishi, Y., Tsukada, K., Yokota, J., and Raz, A. (2003). Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3 fibroblasts induces cell transformation. Clin. Exp. Metastasis 20, 51–58. doi: 10.1023/A:1022594503657
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 51-58
    • Onishi, Y.1    Tsukada, K.2    Yokota, J.3    Raz, A.4
  • 99
    • 0030909233 scopus 로고    scopus 로고
    • Improved prognosis assessment for patients with bladder carcinoma
    • Otto, T., Bex, A., Schmidt, U., Raz, A., and Rübben, H. (1997). Improved prognosis assessment for patients with bladder carcinoma. Am. J. Pathol. 150, 1919–1923.
    • (1997) Am. J. Pathol , vol.150 , pp. 1919-1923
    • Otto, T.1    Bex, A.2    Schmidt, U.3    Raz, A.4    Rübben, H.5
  • 100
    • 0028179098 scopus 로고
    • Inverse relation of E-cadherin and autocrine motility factor receptor expression as a prognostic factor in patients with bladder carcinomas
    • Otto, T., Birchmeier, W., Schmidt, U., Hinke, A., Schipper, J., Rübben, H., et al. (1994). Inverse relation of E-cadherin and autocrine motility factor receptor expression as a prognostic factor in patients with bladder carcinomas. Cancer Res. 54, 3120–3123.
    • (1994) Cancer Res , vol.54 , pp. 3120-3123
    • Otto, T.1    Birchmeier, W.2    Schmidt, U.3    Hinke, A.4    Schipper, J.5    Rübben, H.6
  • 101
    • 59849092071 scopus 로고    scopus 로고
    • CYP3A4 ubiquitination by gp78 (The tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases
    • Pabarcus, M. K., Hoe, N., Sadeghi, S., Patterson, C., Wiertz, E., and Correia, M. A. (2009). CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch. Biochem. Biophys. 483, 66–74. doi: 10.1016/j.abb.2008.12.001
    • (2009) Arch. Biochem. Biophys , vol.483 , pp. 66-74
    • Pabarcus, M.K.1    Hoe, N.2    Sadeghi, S.3    Patterson, C.4    Wiertz, E.5    Correia, M.A.6
  • 102
    • 79952774815 scopus 로고    scopus 로고
    • CHIP and gp78-mediated ubiquitination of CYP3A4: Implications for the pharmacology of anticancer agents
    • Peer, C. J., Sissung, T. M., and Figg, W. D. (2011). CHIP and gp78-mediated ubiquitination of CYP3A4: implications for the pharmacology of anticancer agents. Cancer Biol. Ther. 11, 549–551. doi: 10.4161/cbt.11.6.14834
    • (2011) Cancer Biol. Ther , vol.11 , pp. 549-551
    • Peer, C.J.1    Sissung, T.M.2    Figg, W.D.3
  • 103
    • 0034667598 scopus 로고    scopus 로고
    • Proteins of the endoplasmic-reticulum-associated degradation pathway: Domain detection and function prediction
    • Ponting, C. P. (2000). Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. Biochem. J. 351, 527–535. doi: 10.1042/0264-6021:3510527
    • (2000) Biochem. J , vol.351 , pp. 527-535
    • Ponting, C.P.1
  • 104
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. (1991). Molecular biology of prion diseases. Science 252, 1515–1523. doi: 10.1126/science.1675487
    • (1991) Science , vol.252 , pp. 1515-1523
    • Prusiner, S.B.1
  • 105
    • 0027314668 scopus 로고
    • Charcot-marie-tooth disease type 1A—association with a spontaneous point mutation in the PMP22 gene
    • Roa, B. B., Garcia, C. A., Suter, U., Kulpa, D. A., Wise, C. A., Mueller, J., et al. (1993). Charcot-marie-tooth disease type 1A—association with a spontaneous point mutation in the PMP22 gene. N. Engl. J. Med. 329, 96–101. doi: 10.1136/jmg.30.10.885-b
    • (1993) N. Engl. J. Med , vol.329 , pp. 96-101
    • Roa, B.B.1    Garcia, C.A.2    Suter, U.3    Kulpa, D.A.4    Wise, C.A.5    Mueller, J.6
  • 107
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • Saibil, H. (2013). Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Mol. Cell Biol. 14, 630–642. doi: 10.1038/nrm3658
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 630-642
    • Saibil, H.1
  • 108
    • 84930625029 scopus 로고    scopus 로고
    • Parkin structure and function
    • Seirafi, M., Kozlov, G., and Gehring, K. (2015). Parkin structure and function. FEBS J. 282, 2076–2088. doi: 10.1111/febs.13249
    • (2015) FEBS J , vol.282 , pp. 2076-2088
    • Seirafi, M.1    Kozlov, G.2    Gehring, K.3
  • 109
    • 84890565296 scopus 로고    scopus 로고
    • Gp78 is specifically expressed in human prostate cancer rather than normal prostate tissue
    • Shang, Y., and Zhu, Z. (2013). gp78 is specifically expressed in human prostate cancer rather than normal prostate tissue. J. Mol. Histol. 44, 653–659. doi: 10.1007/s10735-013-9512-9
    • (2013) J. Mol. Histol , vol.44 , pp. 653-659
    • Shang, Y.1    Zhu, Z.2
  • 110
    • 84883444103 scopus 로고    scopus 로고
    • Raft endocytosis of AMF regulates mitochondrial dynamics through Rac1 signaling and the Gp78 ubiquitin ligase
    • Shankar, J., Kojic, L. D., St-Pierre, P., Wang, P. T., Fu, M., Joshi, B., et al. (2013). Raft endocytosis of AMF regulates mitochondrial dynamics through Rac1 signaling and the Gp78 ubiquitin ligase. J. Cell Sci. 126, 3295–3304. doi: 10.1242/jcs.120162
    • (2013) J. Cell Sci , vol.126 , pp. 3295-3304
    • Shankar, J.1    Kojic, L.D.2    St-Pierre, P.3    Wang, P.T.4    Fu, M.5    Joshi, B.6
  • 111
    • 84899506914 scopus 로고    scopus 로고
    • Ubiquitin ligase gp78 targets unglycosylated prion protein PrP for ubiquitylation and degradation
    • Shao, J., Choe, V., Cheng, H., Tsai, Y. C., Weissman, A. M., Luo, S., et al. (2014). Ubiquitin ligase gp78 targets unglycosylated prion protein PrP for ubiquitylation and degradation. PLoS One 9:e92290. doi: 10.1371/journal.pone.0092290
    • (2014) Plos One , vol.9
    • Shao, J.1    Choe, V.2    Cheng, H.3    Tsai, Y.C.4    Weissman, A.M.5    Luo, S.6
  • 112
    • 78649309029 scopus 로고    scopus 로고
    • The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
    • Sharma, S. K., De los Rios, P., Christen, P., Lustig, A., and Goloubinoff, P. (2010). The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat. Chem. Biol. 6, 914–920. doi: 10.1038/nchembio.455
    • (2010) Nat. Chem. Biol , vol.6 , pp. 914-920
    • Sharma, S.K.1    De Los Rios, P.2    Christen, P.3    Lustig, A.4    Goloubinoff, P.5
  • 113
    • 0000931662 scopus 로고
    • Glycoproteins
    • Sharon, N. (1984). Glycoproteins. Trends Biochem. Sci. 9, 198–202. doi: 10.1016/0968-0004(84)90139-7
    • (1984) Trends Biochem. Sci , vol.9 , pp. 198-202
    • Sharon, N.1
  • 114
    • 33845451008 scopus 로고    scopus 로고
    • ER stress differentially regulates the stabilities of ERAD ubiquitin ligases and their substrates
    • Shen, Y., Ballar, P., Apostolou, A., Doong, H., and Fang, S. (2007). ER stress differentially regulates the stabilities of ERAD ubiquitin ligases and their substrates. Biochem. Biophys. Res. Commun. 352, 919–924. doi: 10.1016/j.bbrc.2006.11.121
    • (2007) Biochem. Biophys. Res. Commun , vol.352 , pp. 919-924
    • Shen, Y.1    Ballar, P.2    Apostolou, A.3    Doong, H.4    Fang, S.5
  • 115
    • 33748792529 scopus 로고    scopus 로고
    • Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of a-1-antitrypsin
    • Shen, Y., Ballar, P., and Fang, S. (2006). Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of a-1-antitrypsin. Biochem. Biophys. Res. Commun. 349, 1285–1293. doi: 10.1016/j.bbrc.2006.08.173
    • (2006) Biochem. Biophys. Res. Commun , vol.349 , pp. 1285-1293
    • Shen, Y.1    Ballar, P.2    Fang, S.3
  • 116
    • 0032800602 scopus 로고    scopus 로고
    • The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein1
    • Shimizu, K., Tani, M., Watanabe, H., Nagamachi, Y., Niinaka, Y., Shiroishi, T., et al. (1999). The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein1. FEBS Lett. 456, 295–300. doi: 10.1016/s0014-5793(99)00966-7
    • (1999) FEBS Lett , vol.456 , pp. 295-300
    • Shimizu, K.1    Tani, M.2    Watanabe, H.3    Nagamachi, Y.4    Niinaka, Y.5    Shiroishi, T.6
  • 117
    • 70449729362 scopus 로고    scopus 로고
    • Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: Cross-talk between E3s in the endoplasmic reticulum
    • Shmueli, A., Tsai, Y. C., Yang, M., Braun, M. A., and Weissman, A. M. (2009). Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: cross-talk between E3s in the endoplasmic reticulum. Biochem. Biophys. Res. Commun. 390, 758–762. doi: 10.1016/j.bbrc.2009.10.045
    • (2009) Biochem. Biophys. Res. Commun , vol.390 , pp. 758-762
    • Shmueli, A.1    Tsai, Y.C.2    Yang, M.3    Braun, M.A.4    Weissman, A.M.5
  • 118
    • 84918576284 scopus 로고    scopus 로고
    • Adding to the STING
    • Shu, H. B., and Wang, Y. Y. (2014). Adding to the STING. Immunity 41, 871–873. doi: 10.1016/j.immuni.2014.12.002
    • (2014) Immunity , vol.41 , pp. 871-873
    • Shu, H.B.1    Wang, Y.Y.2
  • 119
    • 4143087789 scopus 로고
    • Glycoproteins: An overview
    • Shylaja, M., and Seshadri, H. S. (1989). Glycoproteins: an overview. Biochem. Edu. 17, 170–178. doi: 10.1016/0307-4412(89)90136-2
    • (1989) Biochem. Edu , vol.17 , pp. 170-178
    • Shylaja, M.1    Seshadri, H.S.2
  • 120
    • 0029893232 scopus 로고    scopus 로고
    • Regulation of autocrine motility factor receptor expression in tumor cell locomotion and metastasis
    • Silletti, S., and Raz, A. (1996). Regulation of autocrine motility factor receptor expression in tumor cell locomotion and metastasis. Curr. Top. Microbiol. Immunol. 213, 137–169. doi: 10.1007/978-3-642-61109-4_7
    • (1996) Curr. Top. Microbiol. Immunol , vol.213 , pp. 137-169
    • Silletti, S.1    Raz, A.2
  • 121
    • 0025996666 scopus 로고
    • Purification of B16–F1 melanoma autocrine motility factor and its receptor
    • Silletti, S., Watanabe, H., Hogan, V., Nabi, I. R., and Raz, A. (1991). Purification of B16–F1 melanoma autocrine motility factor and its receptor. Cancer Res. 51, 3507–3511.
    • (1991) Cancer Res , vol.51 , pp. 3507-3511
    • Silletti, S.1    Watanabe, H.2    Hogan, V.3    Nabi, I.R.4    Raz, A.5
  • 122
    • 0028806661 scopus 로고
    • Loss of cell-contact regulation and altered responses to autocrine motility factor correlate with increased malignancy in prostate cancer cells
    • Silletti, S., Yao, J. P., Pienta, K. J., and Raz, A. (1995). Loss of cell-contact regulation and altered responses to autocrine motility factor correlate with increased malignancy in prostate cancer cells. Int. J. Cancer 63, 100–105. doi: 10.1002/ijc.2910630118
    • (1995) Int. J. Cancer , vol.63 , pp. 100-105
    • Silletti, S.1    Yao, J.P.2    Pienta, K.J.3    Raz, A.4
  • 123
    • 0027423926 scopus 로고
    • Autocrine motility factor-receptor in human bladder-carcinoma - Geneexpression, loss of cell-contact regulation and chromosomal mapping
    • Silletti, S., Yao, J., Sanford, J., Mohammed, A., Otto, T., Wolman, S., et al. (1993). Autocrine motility factor-receptor in human bladder-carcinoma - geneexpression, loss of cell-contact regulation and chromosomal mapping. Int. J. Oncol. 3, 801–807. doi: 10.3892/ijo.3.5.801
    • (1993) Int. J. Oncol , vol.3 , pp. 801-807
    • Silletti, S.1    Yao, J.2    Sanford, J.3    Mohammed, A.4    Otto, T.5    Wolman, S.6
  • 124
    • 0030053624 scopus 로고    scopus 로고
    • Inverse relation of autocrine motility factor receptor and E-cadherin expression following MDCK epithelial cell transformation
    • Simard, D., and Nabi, I. R. (1996). Inverse relation of autocrine motility factor receptor and E-cadherin expression following MDCK epithelial cell transformation. Biochem. Biophys. Res. Commun. 219, 122–127. doi: 10.1006/bbrc.1996.0192
    • (1996) Biochem. Biophys. Res. Commun , vol.219 , pp. 122-127
    • Simard, D.1    Nabi, I.R.2
  • 125
    • 24944591120 scopus 로고    scopus 로고
    • Gp78, a membraneanchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase
    • Song, B. L., Sever, N., and Debose-Boyd, R. A. (2005). Gp78, a membraneanchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol. Cell 19, 829–840. doi: 10.1016/j.molcel.2005.08.009
    • (2005) Mol. Cell , vol.19 , pp. 829-840
    • Song, B.L.1    Sever, N.2    Debose-Boyd, R.A.3
  • 126
    • 84919639026 scopus 로고    scopus 로고
    • MiR–139–5p inhibits migration and invasion of colorectal cancer by downregulating AMFR and NOTCH1
    • Song, M., Yin, Y., Zhang, J., Zhang, B., Bian, Z., Quan, C., et al. (2014). MiR–139–5p inhibits migration and invasion of colorectal cancer by downregulating AMFR and NOTCH1. Protein Cell 5, 851–861. doi: 10.1007/s13238-014-0093-5
    • (2014) Protein Cell , vol.5 , pp. 851-861
    • Song, M.1    Yin, Y.2    Zhang, J.3    Zhang, B.4    Bian, Z.5    Quan, C.6
  • 127
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003). Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4, 49–60. doi: 10.1038/nrn1007
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 128
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • Soto, C., and Estrada, L. D. (2008). Protein misfolding and neurodegeneration. Arch. Neurol. 65, 184–189. doi: 10.1001/archneurol.2007.56
    • (2008) Arch. Neurol , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 129
    • 0014895932 scopus 로고
    • Glycoproteins
    • Spiro, R. G. (1970). Glycoproteins. Annu. Rev. Biochem. 39, 599–638. doi: 10.1146/annurev.bi.39.070170.003123
    • (1970) Annu. Rev. Biochem , vol.39 , pp. 599-638
    • Spiro, R.G.1
  • 130
    • 84863104967 scopus 로고    scopus 로고
    • Peripheral endoplasmic reticulum localization of the Gp78 ubiquitin ligase activity
    • St-Pierre, P., Dang, T., Joshi, B., and Nabi, I. R. (2012). Peripheral endoplasmic reticulum localization of the Gp78 ubiquitin ligase activity. J. Cell Sci. 125, 1727–1737. doi: 10.1242/jcs.096396
    • (2012) J. Cell Sci , vol.125 , pp. 1727-1737
    • St-Pierre, P.1    Dang, T.2    Joshi, B.3    Nabi, I.R.4
  • 131
    • 0141431050 scopus 로고    scopus 로고
    • Autocrine motility factor-receptor gene expression in lung cancer
    • Takanami, I., and Takeuchi, K. (2003). Autocrine motility factor-receptor gene expression in lung cancer. Jpn. J. Thorac. Cardiovasc. Surg. 51, 368–373. doi: 10.1007/BF02719469
    • (2003) Jpn. J. Thorac. Cardiovasc. Surg , vol.51 , pp. 368-373
    • Takanami, I.1    Takeuchi, K.2
  • 132
    • 0036134035 scopus 로고    scopus 로고
    • Autocrine motility factor receptor gene expression and cell motility in lung cancer cell lines
    • Takanami, I., Takeuchi, K., Watanabe, H., Yanagawa, T., and Takagishi, K. (2002). Autocrine motility factor receptor gene expression and cell motility in lung cancer cell lines. Oncol. Rep. 9, 125–128. doi: 10.3892/or.9.1.125
    • (2002) Oncol. Rep , vol.9 , pp. 125-128
    • Takanami, I.1    Takeuchi, K.2    Watanabe, H.3    Yanagawa, T.4    Takagishi, K.5
  • 133
    • 0035923277 scopus 로고    scopus 로고
    • Significance of autocrine motility factor receptor gene expression as a prognostic factor in non-small-cell lung cancer
    • Takanami, I., Takeuchi, K., Watanabe, H., Yanagawa, T., Takagishi, K., and Raz, A. (2001). Significance of autocrine motility factor receptor gene expression as a prognostic factor in non-small-cell lung cancer. Int. J. Cancer 95, 384–387. doi: 10.1002/1097-0215(20011120)95:6<384::aid-ijc1068>3.0.co;2-d
    • (2001) Int. J. Cancer , vol.95 , pp. 384-387
    • Takanami, I.1    Takeuchi, K.2    Watanabe, H.3    Yanagawa, T.4    Takagishi, K.5    Raz, A.6
  • 134
    • 0032104306 scopus 로고    scopus 로고
    • The relation between the growth patterns of gastric carcinoma and the expression of hepatocyte growth factor receptor (C-met), autocrine motility factor receptor and urokinase-type plasminogen activator receptor
    • Taniguchi, K., Yonemura, Y., Nojima, N., Hirono, Y., Fushida, S., Fujimura, T., et al. (1998). The relation between the growth patterns of gastric carcinoma and the expression of hepatocyte growth factor receptor (c-met), autocrine motility factor receptor and urokinase-type plasminogen activator receptor. Cancer 82, 2112–2122. doi: 10.1002/(sici)1097-0142(19980601)82:11<2112::aidcncr5>3.0.co;2-x
    • (1998) Cancer , vol.82 , pp. 2112-2122
    • Taniguchi, K.1    Yonemura, Y.2    Nojima, N.3    Hirono, Y.4    Fushida, S.5    Fujimura, T.6
  • 135
    • 0025087141 scopus 로고
    • Acquisition of protease resistance by prion proteins in scrapieinfected cells does not require asparagine-linked glycosylation
    • Taraboulos, A., Rogers, M., Borchelt, D. R., Mckinley, M. P., Scott, M., Serban, D., et al. (1990). Acquisition of protease resistance by prion proteins in scrapieinfected cells does not require asparagine-linked glycosylation. Proc. Natl. Acad. Sci. U S A 87, 8262–8266. doi: 10.1073/pnas.87.21.8262
    • (1990) Proc. Natl. Acad. Sci. U S A , vol.87 , pp. 8262-8266
    • Taraboulos, A.1    Rogers, M.2    Borchelt, D.R.3    McKinley, M.P.4    Scott, M.5    Serban, D.6
  • 136
    • 84944242430 scopus 로고    scopus 로고
    • Neuroleukin/autocrine motility factor receptor pathway promotes proliferation of articular chondrocytes through activation of AKT and Smad2/3
    • Tian, K., Zhong, W., Zheng, X., Zhang, J., Liu, P., Zhang, W., et al. (2015). Neuroleukin/autocrine motility factor receptor pathway promotes proliferation of articular chondrocytes through activation of AKT and Smad2/3. Sci. Rep. 5:15101. doi: 10.1038/srep15101
    • (2015) Sci. Rep , vol.5 , pp. 15101
    • Tian, K.1    Zhong, W.2    Zheng, X.3    Zhang, J.4    Liu, P.5    Zhang, W.6
  • 137
    • 0036100276 scopus 로고    scopus 로고
    • Expression and function of the AMF receptor by human melanoma in experimental and clinical systems
    • Tímár, J., Rásó, E., Döme, B., Ladányi, A., Bánfalvi, T., Gilde, K., et al. (2002). Expression and function of the AMF receptor by human melanoma in experimental and clinical systems. Clin. Exp. Metastasis 19, 225–232. doi: 10.1023/A:1015595708241
    • (2002) Clin. Exp. Metastasis , vol.19 , pp. 225-232
    • Tímár, J.1    Rásó, E.2    Döme, B.3    Ladányi, A.4    Bánfalvi, T.5    Gilde, K.6
  • 138
    • 0027136065 scopus 로고
    • Regulation of melanoma-cell motility by the lipoxygenase metabolite 12-(S)-HETE
    • Timar, J., Silletti, S., Bazaz, R., Raz, A., and Honn, K. V. (1993). Regulation of melanoma-cell motility by the lipoxygenase metabolite 12-(S)-HETE. Int. J. Cancer 55, 1003–1010. doi: 10.1002/ijc.2910550621
    • (1993) Int. J. Cancer , vol.55 , pp. 1003-1010
    • Timar, J.1    Silletti, S.2    Bazaz, R.3    Raz, A.4    Honn, K.V.5
  • 139
    • 84870495262 scopus 로고    scopus 로고
    • Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system
    • Tsai, Y. C., Leichner, G. S., Pearce, M. M., Wilson, G. L., Wojcikiewicz, R. J., Roitelman, J., et al. (2012). Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system. Mol. Biol. Cell 23, 4484–4494. doi: 10.1091/mbc.e12-08-0631
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4484-4494
    • Tsai, Y.C.1    Leichner, G.S.2    Pearce, M.M.3    Wilson, G.L.4    Wojcikiewicz, R.J.5    Roitelman, J.6
  • 140
    • 36849051990 scopus 로고    scopus 로고
    • The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation
    • Tsai, Y. C., Mendoza, A., Mariano, J. M., Zhou, M., Kostova, Z., Chen, B., et al. (2007). The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation. Nat. Med. 13, 1504–1509. doi: 10.1038/nm1686
    • (2007) Nat. Med , vol.13 , pp. 1504-1509
    • Tsai, Y.C.1    Mendoza, A.2    Mariano, J.M.3    Zhou, M.4    Kostova, Z.5    Chen, B.6
  • 141
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y., and Rapoport, T. A. (2002). Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3, 246–255. doi: 10.1038/nrm780
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 142
    • 0036682378 scopus 로고    scopus 로고
    • Activation of small GTPase Rho is required for autocrine motility factor signaling
    • Tsutsumi, S., Gupta, S. K., Hogan, V., Collard, J. G., and Raz, A. (2002). Activation of small GTPase Rho is required for autocrine motility factor signaling. Cancer Res. 62, 4484–4490.
    • (2002) Cancer Res , vol.62 , pp. 4484-4490
    • Tsutsumi, S.1    Gupta, S.K.2    Hogan, V.3    Collard, J.G.4    Raz, A.5
  • 143
    • 84961061050 scopus 로고    scopus 로고
    • Selective multifaceted E3 ubiquitin ligases barricade extreme defense: Potential therapeutic targets for neurodegeneration and ageing
    • Upadhyay, A., Amanullah, A., Chhangani, D., Mishra, R., and Mishra, A. (2015). Selective multifaceted E3 ubiquitin ligases barricade extreme defense: potential therapeutic targets for neurodegeneration and ageing. Ageing res.rev. 24, 138–159. doi: 10.1016/j.arr.2015.07.009
    • (2015) Ageing Res.Rev. , vol.24 , pp. 138-159
    • Upadhyay, A.1    Amanullah, A.2    Chhangani, D.3    Mishra, R.4    Mishra, A.5
  • 144
    • 85021367637 scopus 로고    scopus 로고
    • E3 ubiquitin ligases neurobiological mechanisms: Development to degeneration
    • Upadhyay, A., Joshi, V., Amanullah, A., Mishra, R., Arora, N., Prasad, A., et al. (2017). E3 ubiquitin ligases neurobiological mechanisms: development to degeneration. Front. Mol. Neurosci. 10:151. doi: 10.3389/fnmol.2017.00151
    • (2017) Front. Mol. Neurosci , vol.10 , pp. 151
    • Upadhyay, A.1    Joshi, V.2    Amanullah, A.3    Mishra, R.4    Arora, N.5    Prasad, A.6
  • 145
    • 33745190973 scopus 로고    scopus 로고
    • Selective inhibition of endoplasmic reticulum-associated degradation rescues DeltaF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: Therapeutic implications
    • Vij, N., Fang, S., and Zeitlin, P. L. (2006). Selective inhibition of endoplasmic reticulum-associated degradation rescues DeltaF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: therapeutic implications. J. Biol. Chem. 281, 17369–17378. doi: 10.1074/jbc.m600509200
    • (2006) J. Biol. Chem , vol.281 , pp. 17369-17378
    • Vij, N.1    Fang, S.2    Zeitlin, P.L.3
  • 146
    • 0031443467 scopus 로고    scopus 로고
    • The AMF-R tubule is a smooth ilimaquinone-sensitive subdomain of the endoplasmic reticulum
    • Wang, H. J., Benlimame, N., and Nabi, I. (1997). The AMF-R tubule is a smooth ilimaquinone-sensitive subdomain of the endoplasmic reticulum. J. Cell Sci. 110, 3043–3053.
    • (1997) J. Cell Sci , vol.110 , pp. 3043-3053
    • Wang, H.J.1    Benlimame, N.2    Nabi, I.3
  • 147
    • 84974577288 scopus 로고    scopus 로고
    • Distinct mechanisms controlling rough and smooth endoplasmic reticulum contacts with mitochondria
    • Wang, P. T., Garcin, P. O., Fu, M., Masoudi, M., St-Pierre, P., Pante, N., et al. (2015). Distinct mechanisms controlling rough and smooth endoplasmic reticulum contacts with mitochondria. J. Cell Sci. 128, 2759–2765. doi: 10.1242/jcs.171132
    • (2015) J. Cell Sci , vol.128 , pp. 2759-2765
    • Wang, P.T.1    Garcin, P.O.2    Fu, M.3    Masoudi, M.4    St-Pierre, P.5    Pante, N.6
  • 148
    • 84863052176 scopus 로고    scopus 로고
    • Multisite phosphorylation of human liver cytochrome P450 3A4 enhances Its gp78- and CHIP-mediated ubiquitination: A pivotal role of its Ser-478 residue in the gp78-catalyzed reaction
    • Wang, Y., Guan, S., Acharya, P., Liu, Y., Thirumaran, R. K., Brandman, R., et al. (2012). Multisite phosphorylation of human liver cytochrome P450 3A4 enhances Its gp78- and CHIP-mediated ubiquitination: a pivotal role of its Ser-478 residue in the gp78-catalyzed reaction. Mol. Cell. Proteomics 11:M111.010132. doi: 10.1074/mcp.m111.010132
    • (2012) Mol. Cell. Proteomics , vol.11
    • Wang, Y.1    Guan, S.2    Acharya, P.3    Liu, Y.4    Thirumaran, R.K.5    Brandman, R.6
  • 149
    • 0034683749 scopus 로고    scopus 로고
    • Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum
    • Wang, H. J., Guay, G., Pogan, L., Sauvé, R., and Nabi, I. R. (2000). Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. J. Cell Biol. 150, 1489–1498. doi: 10.1083/jcb.150.6.1489
    • (2000) J. Cell Biol , vol.150 , pp. 1489-1498
    • Wang, H.J.1    Guay, G.2    Pogan, L.3    Sauvé, R.4    Nabi, I.R.5
  • 150
    • 84899534051 scopus 로고    scopus 로고
    • Polyubiquitylation of AMF requires cooperation between the gp78 and TRIM25 ubiquitin ligases
    • Wang, Y., Ha, S. W., Zhang, T., Kho, D. H., Raz, A., and Xie, Y. (2014). Polyubiquitylation of AMF requires cooperation between the gp78 and TRIM25 ubiquitin ligases. Oncotarget 5, 2044–2051. doi: 10.18632/oncotarget.1478
    • (2014) Oncotarget , vol.5 , pp. 2044-2051
    • Wang, Y.1    Ha, S.W.2    Zhang, T.3    Kho, D.H.4    Raz, A.5    Xie, Y.6
  • 151
    • 78649284470 scopus 로고    scopus 로고
    • Autocrine motility factor receptor signaling pathway promotes cell invasion via activation of ROCK-2 in esophageal squamous cell cancer cells
    • Wang, L., Hou, G., Xue, L., Li, J., Wei, P., and Xu, P. (2010). Autocrine motility factor receptor signaling pathway promotes cell invasion via activation of ROCK-2 in esophageal squamous cell cancer cells. Cancer Invest. 28, 993–1003. doi: 10.3109/07357907.2010.483503
    • (2010) Cancer Invest , vol.28 , pp. 993-1003
    • Wang, L.1    Hou, G.2    Xue, L.3    Li, J.4    Wei, P.5    Xu, P.6
  • 152
    • 85019757919 scopus 로고    scopus 로고
    • CDK5-mediated phosphorylation-dependent ubiquitination and degradation of E3 ubiquitin ligases GP78 accelerates neuronal death in Parkinson’s disease
    • [Epub ahead of print]
    • Wang, Q., Jiao, F., Zhang, P., Yan, J., Zhang, Z., He, F., et al. (2017). CDK5-mediated phosphorylation-dependent ubiquitination and degradation of E3 ubiquitin ligases GP78 accelerates neuronal death in Parkinson’s disease. Mol. Neurobiol. doi: 10.1007/s12035-017-0579-2 [Epub ahead of print].
    • (2017) Mol. Neurobiol
    • Wang, Q.1    Jiao, F.2    Zhang, P.3    Yan, J.4    Zhang, Z.5    He, F.6
  • 153
    • 84922352637 scopus 로고    scopus 로고
    • Human liver cytochrome P450 3A4 ubiquitination: Molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a- CHIP-Hsc70-Hsp40 E2–E3 ubiquitin ligase complexes
    • Wang, Y., Kim, S. M., Trnka, M. J., Liu, Y., Burlingame, A. L., and Correia, M. A. (2015a). Human liver cytochrome P450 3A4 ubiquitination: molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a- CHIP-Hsc70-Hsp40 E2–E3 ubiquitin ligase complexes. J. Biol. Chem. 290, 3308–3332. doi: 10.1074/jbc.M114.611525
    • (2015) J. Biol. Chem , vol.290 , pp. 3308-3332
    • Wang, Y.1    Kim, S.M.2    Trnka, M.J.3    Liu, Y.4    Burlingame, A.L.5    Correia, M.A.6
  • 154
    • 84938079564 scopus 로고    scopus 로고
    • Autocrine motility factor receptor promotes the proliferation of human acute monocytic leukemia THP-1 cells
    • Wang, Y., Ma, L., Wang, C., Sheng, G., Feng, L., and Yin, C. (2015b). Autocrine motility factor receptor promotes the proliferation of human acute monocytic leukemia THP-1 cells. Int. J. Mol. Med. 36, 627–632. doi: 10.3892/ijmm.2015.2267
    • (2015) Int. J. Mol. Med , vol.36 , pp. 627-632
    • Wang, Y.1    Ma, L.2    Wang, C.3    Sheng, G.4    Feng, L.5    Yin, C.6
  • 155
    • 84918565372 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AMFR and INSIG1 bridge the activation of TBK1 kinase by modifying the adaptor STING
    • Wang, Q., Liu, X., Cui, Y., Tang, Y., Chen, W., Li, S., et al. (2014). The E3 ubiquitin ligase AMFR and INSIG1 bridge the activation of TBK1 kinase by modifying the adaptor STING. Immunity 41, 919–933. doi: 10.1016/j.immuni.2014.11.011
    • (2014) Immunity , vol.41 , pp. 919-933
    • Wang, Q.1    Liu, X.2    Cui, Y.3    Tang, Y.4    Chen, W.5    Li, S.6
  • 156
    • 33847176632 scopus 로고    scopus 로고
    • Elevated expression of autocrine motility factor receptor correlates with overexpression of RhoC and indicates poor prognosis in hepatocellular carcinoma
    • Wang, W., Yang, L. Y., Yang, Z. L., Peng, J. X., and Yang, J. Q. (2007). Elevated expression of autocrine motility factor receptor correlates with overexpression of RhoC and indicates poor prognosis in hepatocellular carcinoma. Dig. Dis. Sci. 52, 770–775. doi: 10.1007/s10620-006-9479-4
    • (2007) Dig. Dis. Sci , vol.52 , pp. 770-775
    • Wang, W.1    Yang, L.Y.2    Yang, Z.L.3    Peng, J.X.4    Yang, J.Q.5
  • 157
    • 0025740495 scopus 로고
    • Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor
    • Watanabe, H., Carmi, P., Hogan, V., Raz, T., Silletti, S., Nabi, I. R., et al. (1991a). Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor. J. Biol. Chem. 266, 13442–13448.
    • (1991) J. Biol. Chem , vol.266 , pp. 13442-13448
    • Watanabe, H.1    Carmi, P.2    Hogan, V.3    Raz, T.4    Silletti, S.5    Nabi, I.R.6
  • 158
    • 0025769292 scopus 로고
    • The relationship between motility factor receptor internalization and the lung colonization capacity of murine melanoma cells
    • Watanabe, H., Nabi, I. R., and Raz, A. (1991b). The relationship between motility factor receptor internalization and the lung colonization capacity of murine melanoma cells. Cancer Res. 51, 2699–2705.
    • (1991) Cancer Res , vol.51 , pp. 2699-2705
    • Watanabe, H.1    Nabi, I.R.2    Raz, A.3
  • 159
    • 0028296208 scopus 로고
    • Differential purification of autocrine motility factor derived from a murine protein-free fibrosarcoma
    • Watanabe, H., Kanbe, K., and Chigira, M. (1994). Differential purification of autocrine motility factor derived from a murine protein-free fibrosarcoma. Clin. Exp. Metastasis 12, 155–163. doi: 10.1007/bf01753982
    • (1994) Clin. Exp. Metastasis , vol.12 , pp. 155-163
    • Watanabe, H.1    Kanbe, K.2    Chigira, M.3
  • 160
    • 0027403585 scopus 로고
    • Expression of autocrine motility factor receptor in serum- and protein-independent fibrosarcoma cells: Implications for autonomy in tumor-cell motility and metastasis
    • Watanabe, H., Shinozaki, T., Raz, A., and Chigira, M. (1993). Expression of autocrine motility factor receptor in serum- and protein-independent fibrosarcoma cells: implications for autonomy in tumor-cell motility and metastasis. Int. J. Cancer 53, 689–695. doi: 10.1002/ijc.2910530427
    • (1993) Int. J. Cancer , vol.53 , pp. 689-695
    • Watanabe, H.1    Shinozaki, T.2    Raz, A.3    Chigira, M.4
  • 161
    • 0030012538 scopus 로고    scopus 로고
    • Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide
    • Watanabe, H., Takehana, K., Date, M., Shinozaki, T., and Raz, A. (1996). Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide. Cancer Res. 56, 2960–2963.
    • (1996) Cancer Res , vol.56 , pp. 2960-2963
    • Watanabe, H.1    Takehana, K.2    Date, M.3    Shinozaki, T.4    Raz, A.5
  • 163
    • 84897469420 scopus 로고    scopus 로고
    • Ube2g2-gp78- mediated HERP polyubiquitylation is involved in ER stress recovery
    • Yan, L., Liu, W., Zhang, H., Liu, C., Shang, Y., Ye, Y., et al. (2014). Ube2g2-gp78- mediated HERP polyubiquitylation is involved in ER stress recovery. J. Cell Sci. 127, 1417–1427. doi: 10.1242/jcs.135293
    • (2014) J. Cell Sci , vol.127 , pp. 1417-1427
    • Yan, L.1    Liu, W.2    Zhang, H.3    Liu, C.4    Shang, Y.5    Ye, Y.6
  • 164
    • 11244324729 scopus 로고    scopus 로고
    • Novel roles of the autocrine motility factor/phosphoglucose isomerase in tumor malignancy
    • Yanagawa, T., Funasaka, T., Tsutsumi, S., Watanabe, H., and Raz, A. (2004). Novel roles of the autocrine motility factor/phosphoglucose isomerase in tumor malignancy. Endocr. Relat. Cancer 11, 749–759. doi: 10.1677/erc.1.00811
    • (2004) Endocr. Relat. Cancer , vol.11 , pp. 749-759
    • Yanagawa, T.1    Funasaka, T.2    Tsutsumi, S.3    Watanabe, H.4    Raz, A.5
  • 165
    • 84862816265 scopus 로고    scopus 로고
    • Autocrine motility factor receptor is involved in the process of learning and memory in the central nervous system
    • Yang, Y., Cheng, X. R., Zhang, G. R., Zhou, W. X., and Zhang, Y. X. (2012). Autocrine motility factor receptor is involved in the process of learning and memory in the central nervous system. Behav. Brain Res. 229, 412–418. doi: 10.1016/j.bbr.2012.01.043
    • (2012) Behav. Brain Res , vol.229 , pp. 412-418
    • Yang, Y.1    Cheng, X.R.2    Zhang, G.R.3    Zhou, W.X.4    Zhang, Y.X.5
  • 166
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang, H., Liu, C., Zhong, Y., Luo, S., Monteiro, M. J., and Fang, S. (2010). Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One 5:e8905. doi: 10.1371/journal.pone.0008905
    • (2010) Plos One , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 167
    • 0030221071 scopus 로고    scopus 로고
    • Expression and function of autocrine motility factor receptor in human choriocarcinoma
    • Yelian, F. D., Liu, A., Todt, J. C., Lei, J., Qureshi, F., Jacques, S. M., et al. (1996). Expression and function of autocrine motility factor receptor in human choriocarcinoma. Gynecol. Oncol. 62, 159–165. doi: 10.1006/gyno.1996.0209
    • (1996) Gynecol. Oncol , vol.62 , pp. 159-165
    • Yelian, F.D.1    Liu, A.2    Todt, J.C.3    Lei, J.4    Qureshi, F.5    Jacques, S.M.6
  • 168
    • 79957991349 scopus 로고    scopus 로고
    • The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin
    • Ying, Z., Wang, H., Fan, H., and Wang, G. (2011). The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin. J. Biol. Chem. 286, 20835–20844. doi: 10.1074/jbc.m110.200808
    • (2011) J. Biol. Chem , vol.286 , pp. 20835-20844
    • Ying, Z.1    Wang, H.2    Fan, H.3    Wang, G.4
  • 169
    • 70350701842 scopus 로고    scopus 로고
    • Gp78, an ER associated E3, promotes SOD1 and ataxin-3 degradation
    • Ying, Z., Wang, H., Fan, H., Zhu, X., Zhou, J., Fei, E., et al. (2009). Gp78, an ER associated E3, promotes SOD1 and ataxin-3 degradation. Hum. Mol. Genet. 18, 4268–4281. doi: 10.1093/hmg/ddp380
    • (2009) Hum. Mol. Genet , vol.18 , pp. 4268-4281
    • Ying, Z.1    Wang, H.2    Fan, H.3    Zhu, X.4    Zhou, J.5    Fei, E.6
  • 171
    • 84939954649 scopus 로고    scopus 로고
    • Cholesterol metabolism and homeostasis in the brain
    • Zhang, J., and Liu, Q. (2015). Cholesterol metabolism and homeostasis in the brain. Protein Cell 6, 254–264. doi: 10.1007/s13238-014-0131-3
    • (2015) Protein Cell , vol.6 , pp. 254-264
    • Zhang, J.1    Liu, Q.2
  • 172
    • 84925425893 scopus 로고    scopus 로고
    • Gp78, an E3 ubiquitin ligase acts as a gatekeeper suppressing nonalcoholic steatohepatitis (NASH) and liver cancer
    • Zhang, T., Kho, D. H., Wang, Y., Harazono, Y., Nakajima, K., Xie, Y., et al. (2015a). Gp78, an E3 ubiquitin ligase acts as a gatekeeper suppressing nonalcoholic steatohepatitis (NASH) and liver cancer. PLoS One 10:e0118448. doi: 10.1371/journal.pone.0118448
    • (2015) Plos One , vol.10
    • Zhang, T.1    Kho, D.H.2    Wang, Y.3    Harazono, Y.4    Nakajima, K.5    Xie, Y.6
  • 173
    • 84948978497 scopus 로고    scopus 로고
    • Gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum
    • Zhang, T., Xu, Y., Liu, Y., and Ye, Y. (2015b). Gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum. Mol. Biol. Cell 26, 4438–4450. doi: 10.1091/mbc.e15-06-0354
    • (2015) Mol. Biol. Cell , vol.26 , pp. 4438-4450
    • Zhang, T.1    Xu, Y.2    Liu, Y.3    Ye, Y.4


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