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Volumn 1, Issue 6, 2012, Pages 607-614

Identification of the ubiquitin ligase Triad1 as a regulator of endosomal transport

Author keywords

Degradation; EGF; Endosome; GH; Membrane receptors; Triad1

Indexed keywords


EID: 84964806089     PISSN: None     EISSN: 20466390     Source Type: Journal    
DOI: 10.1242/bio.2012778     Document Type: Article
Times cited : (20)

References (56)
  • 1
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a vps protein complex required for normal endosome function
    • Babst, M., Wendland, B., Estepa, E. J. and Emr, S. D. (1998). The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982-2993.
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 2
    • 33646184769 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins
    • Bayle, J., Lopez, S., Iwaï, K., Dubreuil, P. and De Sepulveda, P. (2006). The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins. FEBS Lett. 580, 2609-2614.
    • (2006) FEBS Lett. , vol.580 , pp. 2609-2614
    • Bayle, J.1    Lopez, S.2    Iwaï, K.3    Dubreuil, P.4    De Sepulveda, P.5
  • 3
    • 0742288015 scopus 로고    scopus 로고
    • Direct sorting of the yeast uracil permease to the endosomal system is controlled by uracil binding and Rsp5p-dependent ubiquitylation
    • Blondel, M.-O., Morvan, J., Dupré, S., Urban-Grimal, D., Haguenauer-Tsapis, R. and Volland, C. (2004). Direct sorting of the yeast uracil permease to the endosomal system is controlled by uracil binding and Rsp5p-dependent ubiquitylation. Mol. Biol. Cell 15, 883-895.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 883-895
    • Blondel, M.-O.1    Morvan, J.2    Dupré, S.3    Urban-Grimal, D.4    Haguenauer-Tsapis, R.5    Volland, C.6
  • 4
    • 3042694692 scopus 로고    scopus 로고
    • Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding
    • Blot, V., Perugi, F., Gay, B., Prévost, M. C., Briant, L., Tangy, F., Abriel, H., Staub, O., Dokhélar, M. C. and Pique, C. (2004). Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell Sci. 117, 2357-2367.
    • (2004) J. Cell Sci. , vol.117 , pp. 2357-2367
    • Blot, V.1    Perugi, F.2    Gay, B.3    Prévost, M.C.4    Briant, L.5    Tangy, F.6    Abriel, H.7    Staub, O.8    Dokhélar, M.C.9    Pique, C.10
  • 5
    • 76449094465 scopus 로고    scopus 로고
    • Parkin-mediated ubiquitin signalling in aggresome formation and autophagy
    • Chin, L. S., Olzmann, J. A. and Li, L. (2010). Parkin-mediated ubiquitin signalling in aggresome formation and autophagy. Biochem. Soc. Trans. 38, 144-149.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 144-149
    • Chin, L.S.1    Olzmann, J.A.2    Li, L.3
  • 6
    • 0020550999 scopus 로고
    • Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents
    • Ciechanover, A., Schwartz, A. L., Dautry-Varsat, A. and Lodish, H. F. (1983). Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents. J. Biol. Chem. 258, 9681-9689.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9681-9689
    • Ciechanover, A.1    Schwartz, A.L.2    Dautry-Varsat, A.3    Lodish, H.F.4
  • 7
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: Same molecule, different degradation pathways
    • Clague, M. J. and Urbé, S. (2010). Ubiquitin: same molecule, different degradation pathways. Cell 143, 682-685.
    • (2010) Cell , vol.143 , pp. 682-685
    • Clague, M.J.1    Urbé, S.2
  • 8
    • 2442509573 scopus 로고    scopus 로고
    • The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo
    • Dunn, R., Klos, D. A., Adler, A. S. and Hicke, L. (2004). The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo. J. Cell Biol. 165, 135-144.
    • (2004) J. Cell Biol. , vol.165 , pp. 135-144
    • Dunn, R.1    Klos, D.A.2    Adler, A.S.3    Hicke, L.4
  • 10
    • 32944455458 scopus 로고    scopus 로고
    • March-III is a novel component of endosomes with properties similar to those of March-II
    • Fukuda, H., Nakamura, N. and Hirose, S. (2006). March-III Is a novel component of endosomes with properties similar to those of March-II. J. Biochem. 139, 137-145.
    • (2006) J. Biochem. , vol.139 , pp. 137-145
    • Fukuda, H.1    Nakamura, N.2    Hirose, S.3
  • 11
    • 0033521670 scopus 로고    scopus 로고
    • Identification of a novel ubiquitin conjugation motif, required for ligandinduced internalization of the growth hormone receptor
    • Govers, R., ten Broeke, T., van Kerkhof, P., Schwartz, A. L. and Strous, G. J. (1999). Identification of a novel ubiquitin conjugation motif, required for ligandinduced internalization of the growth hormone receptor. EMBO J. 18, 28-36.
    • (1999) EMBO J. , vol.18 , pp. 28-36
    • Govers, R.1    Ten Broeke, T.2    Van Kerkhof, P.3    Schwartz, A.L.4    Strous, G.J.5
  • 12
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema, E. H., Valdez-Taubas, J. and Pelham, H. R. B. (2004). Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. EMBO J. 23, 1279-1288.
    • (2004) EMBO J. , vol.23 , pp. 1279-1288
    • Hettema, E.H.1    Valdez-Taubas, J.2    Pelham, H.R.B.3
  • 13
    • 33744958957 scopus 로고    scopus 로고
    • Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin
    • Huang, Y., Niwa, J.-i., Sobue, G. and Breitwieser, G. E. (2006). Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. J. Biol. Chem. 281, 11610-11617.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11610-11617
    • Huang, Y.1    Niwa, J.-I.2    Sobue, G.3    Breitwieser, G.E.4
  • 14
    • 33846297722 scopus 로고    scopus 로고
    • Dorfin-CHIP chimeric proteins potently ubiquitylate and degrade familial ALS-related mutant SOD1 proteins and reduce their cellular toxicity
    • Ishigaki, S., Niwa, J., Yamada, S., Takahashi, M., Ito, T., Sone, J., Doyu, M., Urano, F. and Sobue, G. (2007). Dorfin-CHIP chimeric proteins potently ubiquitylate and degrade familial ALS-related mutant SOD1 proteins and reduce their cellular toxicity. Neurobiol. Dis. 25, 331-341.
    • (2007) Neurobiol. Dis. , vol.25 , pp. 331-341
    • Ishigaki, S.1    Niwa, J.2    Yamada, S.3    Takahashi, M.4    Ito, T.5    Sone, J.6    Doyu, M.7    Urano, F.8    Sobue, G.9
  • 15
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting: Ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S
    • Katzmann, D. J., Sarkar, S., Chu, T., Audhya, A. and Emr, S. D. (2004). Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol. Biol. Cell 15, 468-480.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 16
    • 78650775634 scopus 로고    scopus 로고
    • UEV-1 is an ubiquitin-conjugating enzyme variant that regulates glutamate receptor trafficking in C elegans neurons
    • Kramer, L. B., Shim, J., Previtera, M. L., Isack, N. R., Lee, M. C., Firestein, B. L. and Rongo, C. (2010). UEV-1 is an ubiquitin-conjugating enzyme variant that regulates glutamate receptor trafficking in C. elegans neurons. PLoS ONE 5, e14291.
    • (2010) PLoS ONE , vol.5 , pp. e14291
    • Kramer, L.B.1    Shim, J.2    Previtera, M.L.3    Isack, N.R.4    Lee, M.C.5    Firestein, B.L.6    Rongo, C.7
  • 17
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C. and André, B. (2009). K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 185, 493-502.
    • (2009) J. Cell Biol. , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    André, B.3
  • 19
    • 34248227351 scopus 로고    scopus 로고
    • Rab cascades and tethering factors in the endomembrane system
    • Markgraf, D. F., Peplowska, K. and Ungermann, C. (2007). Rab cascades and tethering factors in the endomembrane system. FEBS Lett. 581, 2125-2130.
    • (2007) FEBS Lett , vol.581 , pp. 2125-2130
    • Markgraf, D.F.1    Peplowska, K.2    Ungermann, C.3
  • 24
    • 2442717708 scopus 로고    scopus 로고
    • The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies
    • Morvan, J., Froissard, M., Haguenauer-Tsapis, R. and Urban-Grimal, D. (2004). The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies. Traffic 5, 383-392.
    • (2004) Traffic , vol.5 , pp. 383-392
    • Morvan, J.1    Froissard, M.2    Haguenauer-Tsapis, R.3    Urban-Grimal, D.4
  • 25
    • 54549102284 scopus 로고    scopus 로고
    • Derailed endocytosis: An emerging feature of cancer
    • Mosesson, Y., Mills, G. B. and Yarden, Y. (2008). Derailed endocytosis: an emerging feature of cancer. Nat. Rev. Cancer 8, 835-850.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 835-850
    • Mosesson, Y.1    Mills, G.B.2    Yarden, Y.3
  • 26
    • 16344381891 scopus 로고    scopus 로고
    • March-II is a syntaxin- 6-binding protein involved in endosomal trafficking
    • Nakamura, N., Fukuda, H., Kato, A. and Hirose, S. (2005). March-II is a syntaxin- 6-binding protein involved in endosomal trafficking. Mol. Biol. Cell 16, 1696-1710.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1696-1710
    • Nakamura, N.1    Fukuda, H.2    Kato, A.3    Hirose, S.4
  • 27
    • 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.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 28
    • 67949091245 scopus 로고    scopus 로고
    • Vps-C complexes: Gatekeepers of endolysosomal traffic
    • Nickerson, D. P., Brett, C. L. and Merz, A. J. (2009). Vps-C complexes: gatekeepers of endolysosomal traffic. Curr. Opin. Cell Biol. 21, 543-551.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 543-551
    • Nickerson, D.P.1    Brett, C.L.2    Merz, A.J.3
  • 29
    • 67749127761 scopus 로고    scopus 로고
    • Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter: Role of lysine 63-linked ubiquitin chains
    • Paiva, S., Vieira, N., Nondier, I., Haguenauer-Tsapis, R., Casal, M. and Urban-Grimal, D. (2009). Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter: role of lysine 63-linked ubiquitin chains. J. Biol. Chem. 284, 19228-19236.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19228-19236
    • Paiva, S.1    Vieira, N.2    Nondier, I.3    Haguenauer-Tsapis, R.4    Casal, M.5    Urban-Grimal, D.6
  • 31
    • 38849164882 scopus 로고    scopus 로고
    • Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking
    • Raiborg, C., Malerød, L., Pedersen, N. M. and Stenmark, H. (2008). Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking. Exp. Cell Res. 314, 801-813.
    • (2008) Exp. Cell Res. , vol.314 , pp. 801-813
    • Raiborg, C.1    Malerød, L.2    Pedersen, N.M.3    Stenmark, H.4
  • 32
    • 1542283806 scopus 로고    scopus 로고
    • Mammalian late vacuole protein sorting orthologues participate in early endosomal fusion and interact with the cytoskeleton
    • Richardson, S. C., Winistorfer, S. C., Poupon, V., Luzio, J. P. and Piper, R. C. (2004). Mammalian late vacuole protein sorting orthologues participate in early endosomal fusion and interact with the cytoskeleton. Mol. Biol. Cell 15, 1197-1210.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1197-1210
    • Richardson, S.C.1    Winistorfer, S.C.2    Poupon, V.3    Luzio, J.P.4    Piper, R.C.5
  • 33
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink, J., Ghigo, E., Kalaidzidis, Y. and Zerial, M. (2005). Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 34
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • Row, P. E., Prior, I. A., McCullough, J., Clague, M. J. and Urbé, S. (2006). The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 281, 12618-12624.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbé, S.5
  • 35
    • 2342423251 scopus 로고    scopus 로고
    • ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
    • Sachse, M., Strous, G. J. and Klumperman, J. (2004). ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles. J. Cell Sci. 117, 1699-1708.
    • (2004) J. Cell Sci. , vol.117 , pp. 1699-1708
    • Sachse, M.1    Strous, G.J.2    Klumperman, J.3
  • 36
    • 0034662876 scopus 로고    scopus 로고
    • A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
    • Seals, D. F., Eitzen, G., Margolis, N., Wickner, W. T. and Price, A. (2000). A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc. Natl. Acad. Sci. USA 97, 9402-9407.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9402-9407
    • Seals, D.F.1    Eitzen, G.2    Margolis, N.3    Wickner, W.T.4    Price, A.5
  • 37
    • 38449099776 scopus 로고    scopus 로고
    • Cryosectioning and immunolabeling
    • Slot, J. W. and Geuze, H. J. (2007). Cryosectioning and immunolabeling. Nat. Protoc. 2, 2480-2491.
    • (2007) Nat. Protoc. , vol.2 , pp. 2480-2491
    • Slot, J.W.1    Geuze, H.J.2
  • 38
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin, A. and Goh, L. K. (2009). Endocytosis and intracellular trafficking of ErbBs. Exp. Cell Res. 315, 683-696.
    • (2009) Exp. Cell Res. , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 41
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G. J., van Kerkhof, P., Govers, R., Ciechanover, A. and Schwartz, A. L. (1996). The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 15, 3806-3812.
    • (1996) EMBO J. , vol.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 42
    • 67349135343 scopus 로고    scopus 로고
    • ESCRT proteins in physiology and disease
    • Stuffers, S., Brech, A. and Stenmark, H. (2009a). ESCRT proteins in physiology and disease. Exp. Cell Res. 315, 1619-1626.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1619-1626
    • Stuffers, S.1    Brech, A.2    Stenmark, H.3
  • 43
    • 67249110996 scopus 로고    scopus 로고
    • Multivesicular endosome biogenesis in the absence of ESCRTs
    • Stuffers, S., Sem Wegner, C., Stenmark, H. and Brech, A. (2009b). Multivesicular endosome biogenesis in the absence of ESCRTs. Traffic 10, 925-937.
    • (2009) Traffic , vol.10 , pp. 925-937
    • Stuffers, S.1    Sem Wegner, C.2    Stenmark, H.3    Brech, A.4
  • 45
    • 0037073739 scopus 로고    scopus 로고
    • Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways
    • van Dam, E. M., Ten Broeke, T., Jansen, K., Spijkers, P. and Stoorvogel, W. (2002). Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways. J. Biol. Chem. 277, 48876-48883.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48876-48883
    • Van Dam, E.M.1    Ten Broeke, T.2    Jansen, K.3    Spijkers, P.4    Stoorvogel, W.5
  • 46
    • 0034864712 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway regulates lysosomal degradation of the growth hormone receptor and its ligand
    • van Kerkhof, P. and Strous, G. J. (2001). The ubiquitin-proteasome pathway regulates lysosomal degradation of the growth hormone receptor and its ligand. Biochem. Soc. Trans. 29, 488-493.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 488-493
    • Van Kerkhof, P.1    Strous, G.J.2
  • 47
    • 0034695587 scopus 로고    scopus 로고
    • Endocytosis and degradation of the growth hormone receptor are proteasomedependent
    • van Kerkhof, P., Govers, R., Alves dos Santos, C. M. and Strous, G. J. (2000). Endocytosis and degradation of the growth hormone receptor are proteasomedependent. J. Biol. Chem. 275, 1575-1580.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1575-1580
    • Van Kerkhof, P.1    Govers, R.2    Alves Dos-Santos, C.M.3    Strous, G.J.4
  • 48
    • 0035159679 scopus 로고    scopus 로고
    • Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins
    • van Kerkhof, P., Alves dos Santos, C. M., Sachse, M., Klumperman, J., Bu, G. and Strous, G. J. (2001). Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins. Mol. Biol. Cell 12, 2556-2566.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2556-2566
    • Van Kerkhof, P.1    Alves Dos-Santos, C.M.2    Sachse, M.3    Klumperman, J.4    Bu, G.5    Strous, G.J.6
  • 49
    • 34547115036 scopus 로고    scopus 로고
    • The ubiquitin ligase SCF(beta TrCP) regulates the degradation of the growth hormone receptor
    • van Kerkhof, P., Putters, J. and Strous, G. J. (2007). The ubiquitin ligase SCF(beta TrCP) regulates the degradation of the growth hormone receptor. J. Biol. Chem. 282, 20475-20483.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20475-20483
    • Van Kerkhof, P.1    Putters, J.2    Strous, G.J.3
  • 50
  • 51
    • 56149101340 scopus 로고    scopus 로고
    • Correlative lightelectron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections
    • van Rijnsoever, C., Oorschot, V. and Klumperman, J. (2008). Correlative lightelectron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections. Nat. Methods 5, 973-980.
    • (2008) Nat. Methods , vol.5 , pp. 973-980
    • Van Rijnsoever, C.1    Oorschot, V.2    Klumperman, J.3
  • 52
    • 50249171794 scopus 로고    scopus 로고
    • Polyubiquitination of prolactin receptor stimulates its internalization, postinternalization sorting, and degradation via the lysosomal pathway
    • Varghese, B., Barriere, H., Carbone, C. J., Banerjee, A., Swaminathan, G., Plotnikov, A., Xu, P., Peng, J., Goffin, V., Lukacs, G. L. et al. (2008). Polyubiquitination of prolactin receptor stimulates its internalization, postinternalization sorting, and degradation via the lysosomal pathway. Mol. Cell. Biol. 28, 5275-5287.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5275-5287
    • Varghese, B.1    Barriere, H.2    Carbone, C.J.3    Banerjee, A.4    Swaminathan, G.5    Plotnikov, A.6    Xu, P.7    Peng, J.8    Goffin, V.9    Lukacs, G.L.10
  • 54
    • 79955772246 scopus 로고    scopus 로고
    • HoxA10 influences protein ubiquitination by activating transcription of ARIH2, the gene encoding Triad1
    • Wang, H., Bei, L., Shah, C. A., Horvath, E. and Eklund, E. A. (2011). HoxA10 influences protein ubiquitination by activating transcription of ARIH2, the gene encoding Triad1. J. Biol. Chem. 286, 16832-16845.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16832-16845
    • Wang, H.1    Bei, L.2    Shah, C.A.3    Horvath, E.4    Eklund, E.A.5
  • 55
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel, D. M., Lissounov, A., Brzovic, P. S. and Klevit, R. E. (2011). UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474, 105-108.
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 56
    • 47149092772 scopus 로고    scopus 로고
    • Multivesicular bodies: Co-ordinated progression to maturity
    • Woodman, P. G. and Futter, C. E. (2008). Multivesicular bodies: co-ordinated progression to maturity. Curr. Opin. Cell Biol. 20, 408-414.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 408-414
    • Woodman, P.G.1    Futter, C.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.