메뉴 건너뛰기




Volumn 254, Issue 1, 1998, Pages 1-5

Protein translocation into the endoplasmic reticulum (ER) two similar routes with different modes

Author keywords

Endoplasmic reticulum; Mammal; Protein translocation; Yeast

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; SIGNAL PEPTIDASE; SIGNAL RECOGNITION PARTICLE;

EID: 0032523828     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2540001.x     Document Type: Review
Times cited : (28)

References (50)
  • 1
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G. & Dobberstein, B. (1975) Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma, J. Cell Biol. 67, 835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 2
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T. A., Jungnickel, B. & Kutay, U. (1996) Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochein. 65, 271-303.
    • (1996) Annu. Rev. Biochein. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 3
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence-specific sorting and translocation
    • Wiedmann, B., Sakai, H., Davis, T. A. & Wiedmann, M. (1994) A protein complex required for signal-sequence-specific sorting and translocation, Nature 370, 434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4
  • 4
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulun membrane
    • Görlich, D. & Rapoport, T. A. (1993) Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulun membrane. Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 5
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B. & Rapoport, T. A. (1995) A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
    • (1995) Cell , vol.82 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 6
    • 0026466143 scopus 로고
    • A mammalian homolog of SEC61p and SHCYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich, D., Prehn, S., Hartmann, E., Kalies, K. U. & Rapoport, T. A. (1992) A mammalian homolog of SEC61p and SHCYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71, 489-503.
    • (1992) Cell , vol.71 , pp. 489-503
    • Görlich, D.1    Prehn, S.2    Hartmann, E.3    Kalies, K.U.4    Rapoport, T.A.5
  • 7
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes, W., Prehn, S. & Rapoport, T. A. (1994) Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane, EMBO J. 13, 3973-3982.
    • (1994) EMBO J. , vol.13 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 8
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex
    • Kalies, K.-U., Görlich, D. &. Rapoport, T. A. (1994) Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex, J. Cell Biol. 126, 925-934.
    • (1994) J. Cell Biol. , vol.126 , pp. 925-934
    • Kalies, K.-U.1    Görlich, D.2    Rapoport, T.A.3
  • 9
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies, R. J. & Schekman, R. (1987) A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105, 633-645.
    • (1987) J. Cell Biol. , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 10
    • 0038415649 scopus 로고    scopus 로고
    • Protein translocation in the three domains of life: Variations on a theme
    • Pohlschröder, M., Prinz., W. A., Hartmann, E. & Beckwith, J. (1997) Protein translocation in the three domains of life: Variations on a theme. Cell 91, 563-566.
    • (1997) Cell , vol.91 , pp. 563-566
    • Pohlschröder, M.1    Prinz, W.A.2    Hartmann, E.3    Beckwith, J.4
  • 11
    • 0028365045 scopus 로고
    • The SecA inhibitor, azide, reversibly blocks the translocation of subset of proteins across the chloroplast thylakoid membrane
    • Knott, T. G. & Robinson, C. (1994) The SecA inhibitor, azide, reversibly blocks the translocation of subset of proteins across the chloroplast thylakoid membrane, J. Biol. Chem. 269, 7843-7846.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7843-7846
    • Knott, T.G.1    Robinson, C.2
  • 12
    • 0026509379 scopus 로고
    • The S. cerevisiae SEC65 gene encodes a component of the yeast signal recognition particle with homology to human SRP19
    • Stirling, C. J. & Hewitt, E. W. (1992) The S. cerevisiae SEC65 gene encodes a component of the yeast signal recognition particle with homology to human SRP19, Nature 356, 534-537.
    • (1992) Nature , vol.356 , pp. 534-537
    • Stirling, C.J.1    Hewitt, E.W.2
  • 13
    • 0027520458 scopus 로고
    • The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum
    • Esnault, Y., Blondel, M. O., Deshaies. R. J., Schekman, R. & Kepes, F. (1993) The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J. 12, 4083-4093.
    • (1993) EMBO J. , vol.12 , pp. 4083-4093
    • Esnault, Y.1    Blondel, M.O.2    Deshaies, R.J.3    Schekman, R.4    Kepes, F.5
  • 14
    • 0029881380 scopus 로고    scopus 로고
    • A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae
    • Finke, K., Plath, K., Panzner, S., Prehn, S., Rapoport, T. A., Hartmann, E. & Summer, T. (1996) A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae, EMBO J. 15, 1482-1494.
    • (1996) EMBO J. , vol.15 , pp. 1482-1494
    • Finke, K.1    Plath, K.2    Panzner, S.3    Prehn, S.4    Rapoport, T.A.5    Hartmann, E.6    Summer, T.7
  • 15
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • Görlich, D., Hartmann, E., Prehn, S. & Rapoport, T. A. (1992) A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature 357, 47-52.
    • (1992) Nature , vol.357 , pp. 47-52
    • Görlich, D.1    Hartmann, E.2    Prehn, S.3    Rapoport, T.A.4
  • 16
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane
    • Voigt, S., Jungnickel, B., Hartmann, E. & Rapoport, T. A. (1996) Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane. J. Cell Biol. 134, 25-35.
    • (1996) J. Cell Biol. , vol.134 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 17
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do, H., Falcone, D., Lin, J., Andrews, D. W. & Johnson, A. E. (1996) The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85, 369-378.
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 18
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
    • Panzner, S., Dreier, L., Hartmann, E., Kostka, S. & Rapoport, T. A. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p, Cell 81, 561-570.
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 19
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng, D. T. Brown, J. D. & Walter, P. (1996) Signal sequences specify the targeting route to the endoplasmic reticulum membrane, J. Cell Biol. 134, 269-278.
    • (1996) J. Cell Biol. , vol.134 , pp. 269-278
    • Ng, D.T.1    Brown, J.D.2    Walter, P.3
  • 20
    • 0030764015 scopus 로고    scopus 로고
    • Protein transport by purified yeast sec complex and kar2p without membranes
    • Matlack, K. E. S., Plath, K., Misselwitz, B. & Rapoport, T. A. (1997) Protein transport by purified yeast sec complex and kar2p without membranes, Science 277, 938-941.
    • (1997) Science , vol.277 , pp. 938-941
    • Matlack, K.E.S.1    Plath, K.2    Misselwitz, B.3    Rapoport, T.A.4
  • 21
    • 0024828302 scopus 로고
    • Sec62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum
    • Deshaies, R. J. & Schekman, R. (1989) Sec62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum, J. Cell Biol. 109, 2653-2664.
    • (1989) J. Cell Biol. , vol.109 , pp. 2653-2664
    • Deshaies, R.J.1    Schekman, R.2
  • 22
    • 0024835142 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • Rothblatt, J. A., Deshaies, R. J., Sanders, S. L., Daum, G. & Schekman, R. (1989) Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109, 2641-2652.
    • (1989) J. Cell Biol. , vol.109 , pp. 2641-2652
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 23
    • 0024787847 scopus 로고
    • A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an escherichia-coli heat shock protein
    • Sadler, I., Chiang, A., Kurihara, T. Rothblatt, J., Way, J. & Silver, P. (1989) A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an escherichia-coli heat shock protein, J. Cell Biol. 109, 2665-2675.
    • (1989) J. Cell Biol. , vol.109 , pp. 2665-2675
    • Sadler, I.1    Chiang, A.2    Kurihara, T.3    Rothblatt, J.4    Way, J.5    Silver, P.6
  • 24
    • 0028088419 scopus 로고
    • Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae
    • Fang, H. & Green, N. (1994) Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae, Mol. Biol. Cell 5, 933-942.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 933-942
    • Fang, H.1    Green, N.2
  • 25
    • 0028022701 scopus 로고
    • Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex
    • Feldheim, D. & Schekman, R. (1994) Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J. Cell Biol. 126, 935-943.
    • (1994) J. Cell Biol. , vol.126 , pp. 935-943
    • Feldheim, D.1    Schekman, R.2
  • 26
    • 0027136175 scopus 로고
    • Genetic interactions between KAR2 and SEC63. encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum
    • Scidmore, M. A., Okamura, H. H. & Rose, M. D. (1993) Genetic interactions between KAR2 and SEC63. encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum, Mol. Biol. Cell 4, 1145-1159.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1145-1159
    • Scidmore, M.A.1    Okamura, H.H.2    Rose, M.D.3
  • 27
    • 0029021905 scopus 로고
    • A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s
    • Schlenstedt, G., Harris, S., Risse, B., Lill, R. & Silver, P. A. (1995) A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s, J. Cell Biol. 129, 979-988.
    • (1995) J. Cell Biol. , vol.129 , pp. 979-988
    • Schlenstedt, G.1    Harris, S.2    Risse, B.3    Lill, R.4    Silver, P.A.5
  • 28
    • 0025339295 scopus 로고
    • Loss of Bip/Grp78 function blocks translocation of secretory proteins in yeast
    • Vogel, J. P., Misra, L. M. & Rose, M. D. (1990) Loss of Bip/Grp78 function blocks translocation of secretory proteins in yeast, J. Cell Biol. 110, 1885-1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 29
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • Evans, E. A., Gilmore, R. & Blobel, G. (1986) Purification of microsomal signal peptidase as a complex. Proc. Natl Acad. Sci. USA 83, 581-585.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 30
    • 0030063873 scopus 로고    scopus 로고
    • Membrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complex
    • Kalies, K.-U. & Hartmann, E. (1996) Membrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complex. J. Biol. Chem. 271, 3925-3929.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3925-3929
    • Kalies, K.-U.1    Hartmann, E.2
  • 31
    • 0030962027 scopus 로고    scopus 로고
    • A specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitro
    • Reiss, G., te Heesen, S., Gilmore, R., Zufferey, R. & Aebi, M. (1997) A specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitro, EMBO J. 16, 1164-1172.
    • (1997) EMBO J. , vol.16 , pp. 1164-1172
    • Reiss, G.1    Te Heesen, S.2    Gilmore, R.3    Zufferey, R.4    Aebi, M.5
  • 32
    • 0023192259 scopus 로고
    • A signal sequence receptor in the endoplasmic reticulum membrane
    • Wiedmann, M., Kurzchalia, T. V., Hartmann, E. & Rapoport, T. A. (1987) A signal sequence receptor in the endoplasmic reticulum membrane. Nature 328, 830-833.
    • (1987) Nature , vol.328 , pp. 830-833
    • Wiedmann, M.1    Kurzchalia, T.V.2    Hartmann, E.3    Rapoport, T.A.4
  • 33
    • 0025310666 scopus 로고
    • Identification of a ribosome receptor in the rough endoplasmic reticulum
    • Savitz, A. J. & Meyer, D. I. (1990) Identification of a ribosome receptor in the rough endoplasmic reticulum. Nature 346, 540-544.
    • (1990) Nature , vol.346 , pp. 540-544
    • Savitz, A.J.1    Meyer, D.I.2
  • 34
    • 0026098723 scopus 로고
    • Identification of a membrane protein responsible for ribosome binding in rough microsomal membranes
    • Tazawa, S., Unuma, M., Tondokoro, N., Asano, Y., Ohsumi, T., Ichimura, T. & Sugano, H. (1991) Identification of a membrane protein responsible for ribosome binding in rough microsomal membranes, Biochem. (Tokyo) 109, 89-98.
    • (1991) Biochem. (Tokyo) , vol.109 , pp. 89-98
    • Tazawa, S.1    Unuma, M.2    Tondokoro, N.3    Asano, Y.4    Ohsumi, T.5    Ichimura, T.6    Sugano, H.7
  • 35
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore, R. & Blobel, G. (1985) Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell 42, 497-505.
    • (1985) Cell , vol.42 , pp. 497-505
    • Gilmore, R.1    Blobel, G.2
  • 36
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S. M. & Blobel, G. (1991) A protein-conducting channel in the endoplasmic reticulum, Cell 65, 371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 37
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K. S., Reinhart, G. D. & Johnson, A. E. (1993) The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115.
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 38
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane
    • Hamman, B. D., Chen, J.-C., Johnson, E. E. & Johnson, A. E. (1997) The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell 89, 535-544.
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.-C.2    Johnson, E.E.3    Johnson, A.E.4
  • 40
    • 0031473345 scopus 로고    scopus 로고
    • Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61p complex
    • Beckmann, R., Bubeck, D., Grassucci, R., Penczek, P., Verschoor, A., Blobel, G. & Frank, J. (1997) Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61p complex, Science 278, 2123-2126.
    • (1997) Science , vol.278 , pp. 2123-2126
    • Beckmann, R.1    Bubeck, D.2    Grassucci, R.3    Penczek, P.4    Verschoor, A.5    Blobel, G.6    Frank, J.7
  • 41
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K. S., Liao, S. R., Worrell, V. E., Reinhart, G. D. & Johnson, A. E. (1994) Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore, Cell 78, 461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.R.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 42
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H. & Johnson, A. E. (1997) Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90, 31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 43
    • 0029002962 scopus 로고
    • The protein conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M. W., Brunner, J. & Dobberstein, B. (1995) The protein conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer, Cell 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 45
    • 0029894267 scopus 로고    scopus 로고
    • Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration
    • Borel, A. C. & Simon, S. M. (1996) Biogenesis of polytopic membrane proteins: membrane segments assemble within translocation channels prior to membrane integration, Cell 85, 379-389.
    • (1996) Cell , vol.85 , pp. 379-389
    • Borel, A.C.1    Simon, S.M.2
  • 46
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A. & Ploegh, H. L (1996) Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.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
  • 47
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R. K., Böhmler, S., Bordallo, J., Sommer, T. & Wolf, D. H. (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Böhmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 48
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T. & Jentsch, S. (1993) A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365, 176-179.
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 49
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cuelp in uhiquitination and degradation at the ER surface
    • Biederer, T., Volkwein, C. & Sommer, T. (1997) Role of Cuelp in uhiquitination and degradation at the ER surface. Science 278, 1806-1809.
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.