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Proteasomes: Destruction as a programme
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Hilt W, Wolf DH. Proteasomes: destruction as a programme. Trends Biochem Sci. 21:1996;96-102.
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Hilt, W.1
Wolf, D.H.2
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2
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0030016595
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Structure and functions of the 20S and 26S proteasomes
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Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem. 65:1996;801-847.
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Annu Rev Biochem
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Coux, O.1
Tanaka, K.2
Goldberg, A.L.3
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3
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0030897031
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Structure of 20S proteasome from yeast at 2.4 Å resolution
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Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature. 386:1997;463-471.
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Nature
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Groll, M.1
Ditzel, L.2
Lowe, J.3
Stock, D.4
Bochtler, M.5
Bartunik, H.D.6
Huber, R.7
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4
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0029118989
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Differences in catalytic activities and subunit pattern of multicatalytic proteinase complexes (proteasomes) isolated from bovine pituitary, lung, and liver: Changes in LMP7 and the component necessary for expression of the chymotrypsin-like activity
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Cardozo C, Eleuteri AM, Orlowski M. Differences in catalytic activities and subunit pattern of multicatalytic proteinase complexes (proteasomes) isolated from bovine pituitary, lung, and liver: changes in LMP7 and the component necessary for expression of the chymotrypsin-like activity. J Biol Chem. 270:1995;22645-22651.
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J Biol Chem
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Cardozo, C.1
Eleuteri, A.M.2
Orlowski, M.3
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5
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0029917002
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Processing and delivery of peptides presented by MHC class I molecules
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Lehner PJ, Cresswell P. Processing and delivery of peptides presented by MHC class I molecules. Curr Opin Immunol. 8:1996;59-67.
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Curr Opin Immunol
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Lehner, P.J.1
Cresswell, P.2
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6
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0026651895
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Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells
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Rivett AJ, Palmer A, Knecht E. Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells. J Histoch Cytochem. 40:1992;1165-1172.
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Rivett, A.J.1
Palmer, A.2
Knecht, E.3
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7
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0029815028
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Immunohistochemical distribution and electron microscopic subcellular localization of the proteasome in the rat CNS
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of special interest. A study of the distribution of proteasomes in the rat central nervous system by immunoelectron microscopy showing a ubiquitous but not homogenous distribution
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Mengual E, Arizti P, Rodrigo J, Gimenez Amaya JM, Castano JG. Immunohistochemical distribution and electron microscopic subcellular localization of the proteasome in the rat CNS. of special interest J Neurosci. 16:1996;6331-6341 A study of the distribution of proteasomes in the rat central nervous system by immunoelectron microscopy showing a ubiquitous but not homogenous distribution.
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(1996)
J Neurosci
, vol.16
, pp. 6331-6341
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Mengual, E.1
Arizti, P.2
Rodrigo, J.3
Gimenez Amaya, J.M.4
Castano, J.G.5
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8
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0028238846
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Changes in proteasome localization during the cell cycle
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???
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Palmer A, Mason GGF, Paramio JM, Knecht E, Rivett AJ. Changes in proteasome localization during the cell cycle. Eur J Cell Biol. 64:1994;???
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(1994)
Eur J Cell Biol
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Palmer, A.1
Mason, G.G.F.2
Paramio, J.M.3
Knecht, E.4
Rivett, A.J.5
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9
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0028944691
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??? immunocytochemical detectability of proteasome ??? depending on cell growth and fixation condition of lung cancer cell lines
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???, ???
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Machiels ???, ??? MER, Broers JLV, Hendil KB, Ramaekers FCS. ??? immunocytochemical detectability of proteasome ??? depending on cell growth and fixation condition of lung cancer cell lines. Eur J Cell Biol. 66:1995;282-292.
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(1995)
Eur J Cell Biol
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, pp. 282-292
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MacHiels1
M, E.R.2
Broers, J.L.V.3
Hendil, K.B.4
Ramaekers, F.C.S.5
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10
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0028886003
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Localization of proteasomal antigens during different phases of the cell cycle in HeLa cells
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Wojcik C, Paweletz N, Schroeter D. Localization of proteasomal antigens during different phases of the cell cycle in HeLa cells. Eur J Cell Biol. 68:1995;191-198.
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(1995)
Eur J Cell Biol
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, pp. 191-198
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Wojcik, C.1
Paweletz, N.2
Schroeter, D.3
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11
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0028234770
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Distinct 19 S and 20 S subsomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm
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Peters JM, Franke WW, Kleinschmidt JA. Distinct 19 S and 20 S subsomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem. 269:1994;7709-7718.
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(1994)
J Biol Chem
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Peters, J.M.1
Franke, W.W.2
Kleinschmidt, J.A.3
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12
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0028267689
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Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin vimentin and desmin type
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Olink-Coux M, Arcangelitti C, Pinardi F, Minisini R, Huesca M, Chezzi C, Scherrer K. Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin vimentin and desmin type. J Cell Sci. 107:1994;353-366.
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J Cell Sci
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Olink-Coux, M.1
Arcangelitti, C.2
Pinardi, F.3
Minisini, R.4
Huesca, M.5
Chezzi, C.6
Scherrer, K.7
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13
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0031586013
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Prosome cytodistribution relative to desmin and actin filaments in dividing C2.7 myoblasts and during myotube formation in vitro
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De Conto F, Missorini S, Arcangeletti C, Pinardi F, Montarras D, Pinset C, Vassy J, Geraud G, Chezzi C, Scherrer K. Prosome cytodistribution relative to desmin and actin filaments in dividing C2.7 myoblasts and during myotube formation in vitro. Exp Cell Res. 233:1997;99-117.
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Exp Cell Res
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, pp. 99-117
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De Conto, F.1
Missorini, S.2
Arcangeletti, C.3
Pinardi, F.4
Montarras, D.5
Pinset, C.6
Vassy, J.7
Geraud, G.8
Chezzi, C.9
Scherrer, K.10
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14
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0030010769
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Subpopulations of proteasomes in rat liver nuclei microsomes and cytosol
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of special interest. Further analysis of proteasome distribution in isolated subcellular fractions from rat liver shows proteasomes in the smooth endoplasmic reticulum and Golgi. Investigation of the composition of proteasomes in nuclei, microsomes and cytosol using monospecific antibodies for some subunits showed that subunit Z was enriched in nuclear proteasomes, whereas LMP2 which was relatively low in nuclei showed a small enrichment in the microsomes
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Palmer A, Rivett AJ, Thomson S, Hendil KB, Butcher GW, Fuertes G, Knecht E. Subpopulations of proteasomes in rat liver nuclei microsomes and cytosol. of special interest Biochem J. 316:1996;401-407 Further analysis of proteasome distribution in isolated subcellular fractions from rat liver shows proteasomes in the smooth endoplasmic reticulum and Golgi. Investigation of the composition of proteasomes in nuclei, microsomes and cytosol using monospecific antibodies for some subunits showed that subunit Z was enriched in nuclear proteasomes, whereas LMP2 which was relatively low in nuclei showed a small enrichment in the microsomes.
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(1996)
Biochem J
, vol.316
, pp. 401-407
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Palmer, A.1
Rivett, A.J.2
Thomson, S.3
Hendil, K.B.4
Butcher, G.W.5
Fuertes, G.6
Knecht, E.7
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16
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0027518334
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Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control
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Amsterdam A, Pitzer F, Baumeister W. Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control. Proc Natl Acad Sci USA. 90:1993;10-99.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 10-99
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Amsterdam, A.1
Pitzer, F.2
Baumeister, W.3
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17
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0030599208
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Removal of proteasomes from the nucleus and their accumulation in apoptotic blebs during programmed cell death
-
of special interest. Immunocytochemical studies using confocal microscopy show that proteasomes in apoptotic immortalized cAMP-stimulated rat ovarian granulosa cells are removed from the nucleus and accumulate within the apoptotic blebs at the periphery of the cell
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Pitzer F, Dantes A, Fuchs T, Baumeister W, Amsterdam A. Removal of proteasomes from the nucleus and their accumulation in apoptotic blebs during programmed cell death. of special interest FEBS Lett. 394:1996;47-50 Immunocytochemical studies using confocal microscopy show that proteasomes in apoptotic immortalized cAMP-stimulated rat ovarian granulosa cells are removed from the nucleus and accumulate within the apoptotic blebs at the periphery of the cell.
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(1996)
FEBS Lett
, vol.394
, pp. 47-50
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Pitzer, F.1
Dantes, A.2
Fuchs, T.3
Baumeister, W.4
Amsterdam, A.5
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18
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0029997779
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Subcellular localization of proteasomes in apoptotic lung tumor cell and persistence as compared to intermediate filaments
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of special interest. Study of proteasome localization and levels during apoptosis in a lung cancer cell line showing that upon increased chromatin condensation nuclear proteasomes were found predominantly surrounding the chromatin and that proteasomes were also detected in the apoptotic bodies and cytoplasmic vesicles
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Machiels BM, Henfling MER, Schutte B, Van Engeland M, Broers JLV, Ramaekers FCS. Subcellular localization of proteasomes in apoptotic lung tumor cell and persistence as compared to intermediate filaments. of special interest Eur J Cell Biol. 70:1996;250-259 Study of proteasome localization and levels during apoptosis in a lung cancer cell line showing that upon increased chromatin condensation nuclear proteasomes were found predominantly surrounding the chromatin and that proteasomes were also detected in the apoptotic bodies and cytoplasmic vesicles.
-
(1996)
Eur J Cell Biol
, vol.70
, pp. 250-259
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-
MacHiels, B.M.1
Henfling, M.E.R.2
Schutte, B.3
Van Engeland, M.4
Broers, J.L.V.5
Ramaekers, F.C.S.6
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19
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0029857608
-
Immunocytochemical localization of multicatalytic protease complex (proteasome) during generation of murine IL-2-activated natural killer (A-NK) cells
-
of special interest. Immunofluorescence and immunogold electron microscopic studies showing that murine A-NK cells treated with interleukin-2 accumulate proteasome in large intracytoplasmic pools
-
Nannmark U, Kitson RP, Johansson BR, Rivett AJ, Goldfarb RH. Immunocytochemical localization of multicatalytic protease complex (proteasome) during generation of murine IL-2-activated natural killer (A-NK) cells. of special interest Eur J Cell Biol. 71:1996;402-408 Immunofluorescence and immunogold electron microscopic studies showing that murine A-NK cells treated with interleukin-2 accumulate proteasome in large intracytoplasmic pools.
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(1996)
Eur J Cell Biol
, vol.71
, pp. 402-408
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-
Nannmark, U.1
Kitson, R.P.2
Johansson, B.R.3
Rivett, A.J.4
Goldfarb, R.H.5
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20
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0029934284
-
Functional analysis of eukaryotic 20S proteasome nuclear localization signal
-
of special interest. In vitro import studies with permeabilized cells show that a putative nuclear localization signal is able to induce complete trans??? of the reporter protein into the nucleus. However in transiently-transfected cells deletion of the putative nuclear localization signal alone did not abolish nuclear translocation of the subunit
-
Knuehl C, Seelig A, Brecht B, Henklein P, Kloetzel PM. Functional analysis of eukaryotic 20S proteasome nuclear localization signal. of special interest Exp Cell Res. 225:1996;67-74 In vitro import studies with permeabilized cells show that a putative nuclear localization signal is able to induce complete trans??? of the reporter protein into the nucleus. However in transiently-transfected cells deletion of the putative nuclear localization signal alone did not abolish nuclear translocation of the subunit.
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(1996)
Exp Cell Res
, vol.225
, pp. 67-74
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Knuehl, C.1
Seelig, A.2
Brecht, B.3
Henklein, P.4
Kloetzel, P.M.5
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21
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0029558611
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Nuclear localization signals of human and Thermoplasma proteasome: Alpha subunits are functional in vitro
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Nederlof PM, Wang HR, Baumeister W. Nuclear localization signals of human and Thermoplasma proteasome: alpha subunits are functional in vitro. Proc Natl Acad Sci USA. 92:1995;12060-12064.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 12060-12064
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Nederlof, P.M.1
Wang, H.R.2
Baumeister, W.3
-
22
-
-
0030919574
-
Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences
-
of special interest. Demonstration that fluorescently labelled 20S proteasomes accumulate in the nucleus in permeabilized cells and studies with recombinant protein and isolated nuclei to investigate the role of a putative nuclear localization signal
-
Wang HR, Kania M, Baumeister W, Nederlof PM. Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences. of special interest Eur J Cell Biol. 73:1997;105-113 Demonstration that fluorescently labelled 20S proteasomes accumulate in the nucleus in permeabilized cells and studies with recombinant protein and isolated nuclei to investigate the role of a putative nuclear localization signal.
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(1997)
Eur J Cell Biol
, vol.73
, pp. 105-113
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-
Wang, H.R.1
Kania, M.2
Baumeister, W.3
Nederlof, P.M.4
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23
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0029786564
-
Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes
-
of outstanding interest. Transfection of cells with a C3 proteasome subunit demonstrates that nuclear C3 is important in the control of cell growth and that both the putative nuclear localization signal and Tyr121 are important for nuclear localization
-
Benedict CM, Clawson GA. Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes. of outstanding interest Biochemistry. 35:1996;11612-11621 Transfection of cells with a C3 proteasome subunit demonstrates that nuclear C3 is important in the control of cell growth and that both the putative nuclear localization signal and Tyr121 are important for nuclear localization.
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(1996)
Biochemistry
, vol.35
, pp. 11612-11621
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Benedict, C.M.1
Clawson, G.A.2
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24
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0029828991
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Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
-
of outstanding interest. Demonstration by immunoprecipitation experiments that the human cytomegalovirus US2 gene product is able to dislocate newly synthesised MHC class I molecules from the endoplasmic reticulum to the cytosol delivering them to the proteasome via the Sec61 complex
-
Wiertz EJHJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. of outstanding interest Nature. 384:1996;432-438 Demonstration by immunoprecipitation experiments that the human cytomegalovirus US2 gene product is able to dislocate newly synthesised MHC class I molecules from the endoplasmic reticulum to the cytosol delivering them to the proteasome via the Sec61 complex.
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(1996)
Nature
, vol.384
, pp. 432-438
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-
Wiertz, E.J.H.J.1
Tortorella, D.2
Bogyo, M.3
Yu, J.4
Mothes, W.5
Jones, T.R.6
Rapoport, T.A.7
Ploegh, H.L.8
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25
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0028840915
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Degradation of CFTR by the ubiquitin-proteasome pathway
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Ward L, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 83:1995;121-127.
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(1995)
Cell
, vol.83
, pp. 121-127
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Ward, L.1
Omura, S.2
Kopito, R.R.3
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26
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0028858161
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Multiple proteolytic systems including the proteasome contribute to CFTR processing
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Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR. Multiple proteolytic systems including the proteasome contribute to CFTR processing. Cell. 83:1995;129-135.
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(1995)
Cell
, vol.83
, pp. 129-135
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-
Jensen, T.J.1
Loo, M.A.2
Pind, S.3
Williams, D.B.4
Goldberg, A.L.5
Riordan, J.R.6
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27
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0030447659
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Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
-
of outstanding interest. Demonstration that degradation of the mutant α1-antitrypsin Z that accumulates in the endoplasmic reticulum (ER) lumen in yeast is mediated by proteasomes after export from the ER to the cytoplasm
-
Werner ED, Brodsky JL, McCracken AA. Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate. of outstanding interest Proc Natl Acad Sci USA. 93:1996;13797-13801 Demonstration that degradation of the mutant α1-antitrypsin Z that accumulates in the endoplasmic reticulum (ER) lumen in yeast is mediated by proteasomes after export from the ER to the cytoplasm.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 13797-13801
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Werner, E.D.1
Brodsky, J.L.2
McCracken, A.A.3
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28
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0029788023
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Degradation of a mutant secretory protein alpha1-antitrypsin Z in the endoplasmic reticulum requires proteasome activity
-
of special interest. Demonstration that degradation in the endoplasmic reticulum of a transfected mutant secretory protein, α1-antitrypsin Z, which is associated with infantile liver disease and adult-onset emphysema of α1-antitrypsin deficiency, is inhibited by the proteasome inhibitor lactacystin
-
Qu D, Teckman JH, Omura S, Perlmutter DH. Degradation of a mutant secretory protein alpha1-antitrypsin Z in the endoplasmic reticulum requires proteasome activity. of special interest J Biol Chem. 271:1996;22791-22795 Demonstration that degradation in the endoplasmic reticulum of a transfected mutant secretory protein, α1-antitrypsin Z, which is associated with infantile liver disease and adult-onset emphysema of α1-antitrypsin deficiency, is inhibited by the proteasome inhibitor lactacystin.
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(1996)
J Biol Chem
, vol.271
, pp. 22791-22795
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-
Qu, D.1
Teckman, J.H.2
Omura, S.3
Perlmutter, D.H.4
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29
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0029838640
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ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
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of outstanding interest. Studies of the endoplasmic reticulum degradation system for proteolysis of misfolded or unassembled proteins using yeast mutants defective in the breakdown of a mutated soluble vacuolar protein (carboxypeptidase yscY) showing the involvement of ubiquitin-conjugating enzyme Ubc7p and the 26S proteasome
-
Hiller MM, Finger A, Schweiger M, Wolf DH. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. of outstanding interest Science. 273:1996;1725-1728 Studies of the endoplasmic reticulum degradation system for proteolysis of misfolded or unassembled proteins using yeast mutants defective in the breakdown of a mutated soluble vacuolar protein (carboxypeptidase yscY) showing the involvement of ubiquitin-conjugating enzyme Ubc7p and the 26S proteasome.
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(1996)
Science
, vol.273
, pp. 1725-1728
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Hiller, M.M.1
Finger, A.2
Schweiger, M.3
Wolf, D.H.4
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30
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10244270656
-
Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B
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of special interest. Studies with proteasome inhibitors show that newly synthesized apolipoprotein B may be degraded by proteasomes in a ubiquitin-dependent process while normally secreted apolipoprotein B is not ubiquitinated
-
Yeung SJ, San Hwan Chen, Chan L. Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B. of special interest Biochemistry. 35:1996;13843-13848 Studies with proteasome inhibitors show that newly synthesized apolipoprotein B may be degraded by proteasomes in a ubiquitin-dependent process while normally secreted apolipoprotein B is not ubiquitinated.
-
(1996)
Biochemistry
, vol.35
, pp. 13843-13848
-
-
Yeung, S.J.1
San Hwan, C.2
Chan, L.3
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31
-
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0029811218
-
Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase an integral endoplasmic reticulum membrane protein
-
of outstanding interest. Results of a genetic screen which identified three genes involved in the degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase. One of the genes encodes the p97/TRAP component of 26S proteasomes but the function of the other two was no elucidated
-
Hampton RY, Gardner RG, Rine J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase an integral endoplasmic reticulum membrane protein. of outstanding interest Mol Biol Cell. 7:1996;2029-2044 Results of a genetic screen which identified three genes involved in the degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase. One of the genes encodes the p97/TRAP component of 26S proteasomes but the function of the other two was no elucidated.
-
(1996)
Mol Biol Cell
, vol.7
, pp. 2029-2044
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-
Hampton, R.Y.1
Gardner, R.G.2
Rine, J.3
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32
-
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0029837381
-
Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
-
of special interest. Regulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase when cells are presented with an excess of sterols or mevalonate is inhibited by the proteasome inhibitor lactacystin. The ubiquitin system in apparently not required
-
McGee TP, Cheng HH, Kumagai H, Omura S, Simoni RD. Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. of special interest J Biol Chem. 271:1996;25630-25638 Regulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase when cells are presented with an excess of sterols or mevalonate is inhibited by the proteasome inhibitor lactacystin. The ubiquitin system in apparently not required.
-
(1996)
J Biol Chem
, vol.271
, pp. 25630-25638
-
-
McGee, T.P.1
Cheng, H.H.2
Kumagai, H.3
Omura, S.4
Simoni, R.D.5
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33
-
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0029985369
-
Degradation of subunits of the Sec61p complex an integral component of the ER membrane by the ubiquitin-proteasome pathway
-
of special interest. Studies with yeast demonstrate that the proteolysis of an unassembled mutant form of the multispanning membrane protein Sec61p and the associated protein Sss1p is mediated by the ubiquitin-proteasome pathway since it requires polyubiquitination, the presence of a membrane-bound (Ubc6), a soluble (Ubc7) ubiquitin-conjugating enzyme, and a functional proteasome
-
Biederer T, Volkwein C, Sommer T. Degradation of subunits of the Sec61p complex an integral component of the ER membrane by the ubiquitin-proteasome pathway. of special interest EMBO J. 15:1996;2069-2076 Studies with yeast demonstrate that the proteolysis of an unassembled mutant form of the multispanning membrane protein Sec61p and the associated protein Sss1p is mediated by the ubiquitin-proteasome pathway since it requires polyubiquitination, the presence of a membrane-bound (Ubc6), a soluble (Ubc7) ubiquitin-conjugating enzyme, and a functional proteasome.
-
(1996)
EMBO J
, vol.15
, pp. 2069-2076
-
-
Biederer, T.1
Volkwein, C.2
Sommer, T.3
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