메뉴 건너뛰기




Volumn 16, Issue 19, 1997, Pages 5847-5854

Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein

Author keywords

Endocytosis; Lys63 chains; Transporter; Ubiquitin; Yeast

Indexed keywords

ARGININE; LYSINE; MEMBRANE PROTEIN; PERMEASE; PROTEASOME; UBIQUITIN;

EID: 0030881952     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.19.5847     Document Type: Article
Times cited : (327)

References (56)
  • 1
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Amason,T. and Ellison,M.J. (1994) Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell Biol., 14, 7876-7883.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7876-7883
    • Amason, T.1    Ellison, M.J.2
  • 2
    • 0030028574 scopus 로고    scopus 로고
    • Novel multiubiquitin chain linkages catalyzed by the conjugating enzyme E2epf and RAD6 are recognized by 26S proteasome subunit 5
    • Baboshina,O.V. and Haas,A.L. (1996) Novel multiubiquitin chain linkages catalyzed by the conjugating enzyme E2epf and RAD6 are recognized by 26S proteasome subunit 5. J. Biol. Chem., 271, 2823-2831.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2823-2831
    • Baboshina, O.V.1    Haas, A.L.2
  • 3
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair,A., Finley,D. and Varshavsky,A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 4
    • 0006033514 scopus 로고
    • Role of ubiquitin specific proteases in protein degradation
    • Baker,R.T., Gilchrist,C., Wyndham,A., Wang,X.W. and Johnson,E. (1995) Role of ubiquitin specific proteases in protein degradation. Yeast, 11, 349.
    • (1995) Yeast , vol.11 , pp. 349
    • Baker, R.T.1    Gilchrist, C.2    Wyndham, A.3    Wang, X.W.4    Johnson, E.5
  • 5
    • 0028999726 scopus 로고
    • Biogenesis, structure and function of the yeast 20S proteasome
    • Chen,P. and Hochstrasser,M. (1995) Biogenesis, structure and function of the yeast 20S proteasome. EMBO J., 14, 2620-2630.
    • (1995) EMBO J. , vol.14 , pp. 2620-2630
    • Chen, P.1    Hochstrasser, M.2
  • 6
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor
    • Chen,P., Johnson,P., Sommer,T., Jentsch,S. and Hochstrasser,M. (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor. Cell, 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 7
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover,A. (1994) The ubiquitin-proteasome proteolytic pathway. Cell 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 8
    • 0028235965 scopus 로고
    • A 26S protease subunit that binds ubiquitin conjugates
    • Deveraux,Q., Ustrell,V., Pickart,C. and Rechsteiner,M. (1994) A 26S protease subunit that binds ubiquitin conjugates. J. Biol Chem., 269, 7059-7061.
    • (1994) J. Biol Chem. , vol.269 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 9
    • 0025913944 scopus 로고
    • The N-end rule is mediated by the UBC2 (RAD6) ubiquitin-conjugating enzyme
    • Dohmen,J.D., Madura,K., Bartel,B. and Varshavsky,A. (1991) The N-end rule is mediated by the UBC2 (RAD6) ubiquitin-conjugating enzyme. Proc. Natl Acad. Sci. USA, 88, 7351-7355.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7351-7355
    • Dohmen, J.D.1    Madura, K.2    Bartel, B.3    Varshavsky, A.4
  • 10
    • 0023654338 scopus 로고
    • Chemical synthesis expression of a cassette adapted ubiquitin gene
    • Ecker,D.J., Ishaq Khan,M., Marsh,J., Butt,T.R. and Crooke,S.T. (1987) Chemical synthesis and expression of a cassette adapted ubiquitin gene. J. Biol. Chem., 262, 3524-3527.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3524-3527
    • Ecker, D.J.1    Ishaq Khan, M.2    Marsh, J.3    Butt, T.R.4    Crooke, S.T.5
  • 11
    • 0030041980 scopus 로고    scopus 로고
    • The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole
    • Egner,R. and Kuchler,K. (1996) The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole. FEBS Lett., 378, 177-181.
    • (1996) FEBS Lett. , vol.378 , pp. 177-181
    • Egner, R.1    Kuchler, K.2
  • 12
    • 0025838227 scopus 로고
    • Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function
    • Ellison,M. and Hochstrasser,M. (1991) Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function. J. Biol. Chem., 266, 21150-21157.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21150-21157
    • Ellison, M.1    Hochstrasser, M.2
  • 13
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley,D., Sadis,S., Monia,B.P., Boucher,P., Ecker,D.J., Crooke,S.T. and Chau,V. (1994) Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol., 14, 5501-5509.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 14
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan,J.M., Moreau,V., André,B., Volland,C. and Haguenauer-Tsapis,R. (1996) Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem., 271, 10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    André, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 15
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest division in G2/metaphase
    • Ghislain,M., Udarvy,A. and Mann,C. (1993) S. cerevisiae 26S protease mutants arrest division in G2/metaphase. Nature, 366, 358-362.
    • (1993) Nature , vol.366 , pp. 358-362
    • Ghislain, M.1    Udarvy, A.2    Mann, C.3
  • 16
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz,D., St Jean,A., Woods,R.A. and Schiestl,R.H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res., 20, 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 17
    • 0041371758 scopus 로고
    • Amino acid transporters in yeast: Structure, function and regulation
    • De Pont,J. (ed.). Elsevier Science Publishers BV
    • Grenson,M. (1992) Amino acid transporters in yeast: structure, function and regulation. In De Pont,J. (ed.), Molecular Aspects of Transport Proteins. Elsevier Science Publishers BV. pp. 219-245.
    • (1992) Molecular Aspects of Transport Proteins , pp. 219-245
    • Grenson, M.1
  • 18
    • 0028971506 scopus 로고
    • NPI1. an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein,C., Springael,J.Y., Volland,C., Haguenauer-Tsapis,R. and Andre,B. (1995) NPI1. an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol., 18, 77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 19
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko,A. and Ciechanover,A. (1992) The ubiquitin system for protein degradation. Annit. Rev. Biochem., 61, 761-807.
    • (1992) Annit. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 20
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its Ugand-stimulated endocytosis
    • Hicke,L. and Riezman,H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its Ugand-stimulated endocytosis. Cell, 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 21
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser,M. (1996a) Protein degradation or regulation: Ub the judge. Cell, 84, 813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 22
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser,M. (1996b) Ubiquitin-dependent protein degradation. Annu. Rev. Genet., 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 24
    • 0029821534 scopus 로고    scopus 로고
    • The tail of a ubiquitin-conjugating enzyme redirects multiubiquitin chain synthesis from the lysine 48-linked configuration to a novel nonlysine-linked form
    • Hodgins,R., Gwozd,C., Arnason,T., Cummings,M. and Ellison,M.J. (1996) The tail of a ubiquitin-conjugating enzyme redirects multiubiquitin chain synthesis from the lysine 48-linked configuration to a novel nonlysine-linked form. J. Biol. Chem., 271, 28766-28771.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28766-28771
    • Hodgins, R.1    Gwozd, C.2    Arnason, T.3    Cummings, M.4    Ellison, M.J.5
  • 25
    • 0029036701 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse,J.M., Scheffner,M., Beaudenon,S. and Howley,PM. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA, 92, 2563-2567.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 26
    • 0030888109 scopus 로고    scopus 로고
    • The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase
    • Huibregste,J.M., Yang,J.C. and Beadenon,S.L. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA, 94, 3656-3661.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3656-3661
    • Huibregste, J.M.1    Yang, J.C.2    Beadenon, S.L.3
  • 27
    • 0031045984 scopus 로고    scopus 로고
    • Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway
    • Jeffers,M., Taylor,G.A., Weidner,K.M., Omura,S. and Van de Woude,G.F. (1997) Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway. Mol. Cell. Biol., 17, 799-808.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 799-808
    • Jeffers, M.1    Taylor, G.A.2    Weidner, K.M.3    Omura, S.4    Van de Woude, G.F.5
  • 28
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch,S. (1992) The ubiquitin-conjugation system. Annu. Rev. Genet., 26, 179-207.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 30
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson,E.S., Ma,P.C.M., Ota,I.M. and Varshavsky,A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem., 270, 17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.M.2    Ota, I.M.3    Varshavsky, A.4
  • 31
    • 0023871832 scopus 로고
    • Primary structure of the uracil transport protein of Saccharomvces cerevisiae
    • Jund,R., Weber,E. and Chevallier,M.R. (1988) Primary structure of the uracil transport protein of Saccharomvces cerevisiae. Eur. J. Biochem., 171, 417-424.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 417-424
    • Jund, R.1    Weber, E.2    Chevallier, M.R.3
  • 32
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B
    • King,R.W., Peters,J.-M., Tugendreich,S., Rolfe,M., Hieter,P. and Kirschner,M. (1995) A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B. Cell, 81, 279-288.
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W.1    Peters, J.-M.2    Tugendreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.6
  • 33
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kolling,R. and Hollenberg,C.P. (1994) The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J., 13, 3261-3271.
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 34
    • 0040123316 scopus 로고    scopus 로고
    • The linker region of the ABC-transporter Ste6 mediates ubiquitination and fast turnover of the protein
    • Kölling,R. and Losko,S. (1997) The linker region of the ABC-transporter Ste6 mediates ubiquitination and fast turnover of the protein. EMBO J., 16, 2251-2261.
    • (1997) EMBO J. , vol.16 , pp. 2251-2261
    • Kölling, R.1    Losko, S.2
  • 35
    • 0031055949 scopus 로고    scopus 로고
    • Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npil/rsp5 and ubiquitin-hydrolase npi2/doa4
    • Lucero,P. and Lagunas,R. (1997) Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npil/rsp5 and ubiquitin-hydrolase npi2/doa4. FEMS Microbiol. Lett., 147, 273-277.
    • (1997) FEMS Microbiol. Lett. , vol.147 , pp. 273-277
    • Lucero, P.1    Lagunas, R.2
  • 36
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated platelet-derived growth factor beta-receptor involves ubiquitin-proteasome proteolytic pathway
    • Mori,S., Tanaka,K., Omura,S. and Saito,Y. (1995) Degradation process of ligand-stimulated platelet-derived growth factor beta-receptor involves ubiquitin-proteasome proteolytic pathway. J. Biol. Chem., 270, 29447-29452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 37
    • 0027427249 scopus 로고
    • The yeast doa4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa,F.R. and Hochstrasser,M. (1993) The yeast doa4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature, 366, 313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 39
    • 0026521192 scopus 로고
    • The proteasome/ multicatalytic-multifunctional proteinase. in vivo function in the ubiquitin-dependent N-end rule pathway of protein degradation in eukaryotes
    • Richter-Ruoff,B., Heinemeyer,W. and Wolf,D.H. (1992) The proteasome/ multicatalytic-multifunctional proteinase. In vivo function in the ubiquitin-dependent N-end rule pathway of protein degradation in eukaryotes. FEBS Lett., 302, 192-196.
    • (1992) FEBS Lett. , vol.302 , pp. 192-196
    • Richter-Ruoff, B.1    Heinemeyer, W.2    Wolf, D.H.3
  • 40
    • 0029781462 scopus 로고    scopus 로고
    • Ubiquitination of the yeast a-factor receptor
    • Roth,A.F. and Davis,N.G. (1996) Ubiquitination of the yeast a-factor receptor. J. Cell Biol., 134, 661-674.
    • (1996) J. Cell Biol. , vol.134 , pp. 661-674
    • Roth, A.F.1    Davis, N.G.2
  • 41
    • 0029948974 scopus 로고    scopus 로고
    • Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome
    • Shild,L., Lu,Y., Gautschi,I., Schneeberger,E., Lifton,R.P. and Rossier,B.C. (1996) Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome. EMBO J., 15, 2381-2387.
    • (1996) EMBO J. , vol.15 , pp. 2381-2387
    • Shild, L.1    Lu, Y.2    Gautschi, I.3    Schneeberger, E.4    Lifton, R.P.5    Rossier, B.C.6
  • 42
    • 0028815630 scopus 로고
    • Catabolite inactivation of fructose- 1,6-biphosphatase of Saccharomxces cerevisiae
    • Schork,S.M., Thumm,M. and Wolf,D.H. (1995) Catabolite inactivation of fructose- 1,6-biphosphatase of Saccharomxces cerevisiae. J. Biol. Chem., 270, 26446-26450.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26446-26450
    • Schork, S.M.1    Thumm, M.2    Wolf, D.H.3
  • 43
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert,W. and Jentsch,S. (1990). Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J., 9, 543-550.
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 45
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis,S., Haas,A.L. and Finley,D. (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol., 15, 1265-1273.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 47
    • 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 Schwarz,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    Schwarz, A.L.5
  • 48
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis
    • Sudakin,V., Ganoth,D., Dahan,A., Heller,H., Hershko,J., Luca,F.C., Ruderman,J.V. and Hershko,A. (1995) The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol. Biol. Cell, 6, 185-198.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 185-198
    • Sudakin, V.1    Ganoth, D.2    Dahan, A.3    Heller, H.4    Hershko, J.5    Luca, F.C.6    Ruderman, J.V.7    Hershko, A.8
  • 49
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding Mcb1 is a component of 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker,S., Sadis,S., Rubin,D.M., Glickman,M., Fu,H., Coux,O., Wefes,I., Finley,D. and Vierstra,R.D. (1996) The multiubiquitin-chain-binding Mcb1 is a component of 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol., 16, 6020-6028.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 50
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky,A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Sci. USA, 93, 12142-12149.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 51
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8A resolution
    • Vijay-Kumar,S., Bugg,C.E. and Cook,W.J. (1987) Structure of ubiquitin refined at 1.8A resolution. J. Mol. Biol., 194, 531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 52
    • 0027057980 scopus 로고
    • In vivo phosphorylation of the yeast uracil pennease
    • Volland,C., Garnier,C. and Haguenauer-Tsapis,R. (1992) In vivo phosphorylation of the yeast uracil pennease. J. Biol. Chem., 267, 23767-23771.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23767-23771
    • Volland, C.1    Garnier, C.2    Haguenauer-Tsapis, R.3
  • 53
    • 0028307059 scopus 로고
    • Endocytosis and degradation of the yeast uracil pennease under adverse conditions
    • Volland,C., Urban-Grimal,D., Géraud,G. and Haguenauer-Tsapis,R. (1994) Endocytosis and degradation of the yeast uracil pennease under adverse conditions. J. Biol. Chem., 269, 9833-9841.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9833-9841
    • Volland, C.1    Urban-Grimal, D.2    Géraud, G.3    Haguenauer-Tsapis, R.4
  • 54
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward,C.L., Omura,S. and Kopito,R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell, 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 56
    • 1842374437 scopus 로고    scopus 로고
    • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5
    • Zoladek,T. Tobiasz,A., Vaduva,G., Boguta,M., Martin,N.C. and Hopper,A.K. (1997) MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Genetics, 145, 595-603.
    • (1997) Genetics , vol.145 , pp. 595-603
    • Zoladek, T.1    Tobiasz, A.2    Vaduva, G.3    Boguta, M.4    Martin, N.C.5    Hopper, A.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.