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Volumn 1, Issue 3, 2001, Pages 401-409

Ssh1p Determines the Translocation and Dislocation Capacities of the Yeast Endoplasmic Reticulum

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENT; CYCLOHEXIMIDE; FUNGAL PROTEIN; MEMBRANE PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SEC61 PROTEIN; SEC61 PROTEIN, S CEREVISIAE; SEC65 PROTEIN, FUNGUS; SEC65 PROTEIN, S CEREVISIAE; SIGNAL RECOGNITION PARTICLE;

EID: 0035463587     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1534-5807(01)00043-0     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 0030665270 scopus 로고    scopus 로고
    • Cloning of SEC61 homologues from Schizosaccharomyces pombe and Yarrowia lipolytica reveals the extent of functional conservation within this core component of the ER translocation machinery
    • Broughton J., Swennen D., Wilkinson B.M., Joyet P., Gaillardin C., Stirling C.J. Cloning of SEC61 homologues from Schizosaccharomyces pombe and Yarrowia lipolytica reveals the extent of functional conservation within this core component of the ER translocation machinery. J. Cell Sci. 110:1997;2715-2727.
    • (1997) J. Cell Sci. , vol.110 , pp. 2715-2727
    • Broughton, J.1    Swennen, D.2    Wilkinson, B.M.3    Joyet, P.4    Gaillardin, C.5    Stirling, C.J.6
  • 2
    • 0033637082 scopus 로고    scopus 로고
    • Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway
    • Casagrande R., Stern P., Diehn M., Shamu C., Osario M., Zuniga M., Brown P.O., Ploegh H. Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol. Cell. 5:2000;729-735.
    • (2000) Mol. Cell , vol.5 , pp. 729-735
    • Casagrande, R.1    Stern, P.2    Diehn, M.3    Shamu, C.4    Osario, M.5    Zuniga, M.6    Brown, P.O.7    Ploegh, H.8
  • 3
    • 0029969899 scopus 로고    scopus 로고
    • A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors
    • Craven R.A., Egerton M., Stirling C.J. A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. EMBO J. 15:1996;2640-2650.
    • (1996) EMBO J. , vol.15 , pp. 2640-2650
    • Craven, R.A.1    Egerton, M.2    Stirling, C.J.3
  • 4
    • 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. The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell. 73:1993;1101-1115.
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 5
    • 0024828302 scopus 로고
    • SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum
    • Deshaies R.J., Schekman R. SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. J. Cell Biol. 109:1989;2653-2664.
    • (1989) J. Cell Biol. , vol.109 , pp. 2653-2664
    • Deshaies, R.J.1    Schekman, R.2
  • 7
    • 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. The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic-reticulum. EMBO J. 12:1993;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
  • 8
    • 0028151096 scopus 로고
    • SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus
    • Esnault Y., Feldheim D., Blondel M.O., Schekman R., Kepes F. SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J. Biol. Chem. 269:1994;27478-27485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27478-27485
    • Esnault, Y.1    Feldheim, D.2    Blondel, M.O.3    Schekman, R.4    Kepes, F.5
  • 9
    • 0024411733 scopus 로고
    • The most abundant small cytoplasmic RNA of Saccharomyces cerevisiae has an important function required for normal cell growth
    • Felici F., Cesareni G., Hughes J.M. The most abundant small cytoplasmic RNA of Saccharomyces cerevisiae has an important function required for normal cell growth. Mol. Cell. Biol. 9:1989;3260-3268.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3260-3268
    • Felici, F.1    Cesareni, G.2    Hughes, J.M.3
  • 10
    • 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., Sommer T. A second trimeric complex containing homologs of the Sec61p complex functions in protein-transport across the ER membrane of S. cerevisiae. EMBO J. 15:1996;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    Sommer, T.7
  • 11
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat. Cell Biol. 2:2000;379-384.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 12
    • 0034712930 scopus 로고    scopus 로고
    • The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane
    • Gillece P., Pilon M., Romisch K. The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. USA. 97:2000;4609-4614.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4609-4614
    • Gillece, P.1    Pilon, M.2    Romisch, K.3
  • 13
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • Hamman B.D., Chen J.C., Johnson E.E., Johnson A.E. The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane. Cell. 89:1997;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
  • 14
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman B.D., Hendershot L.M., Johnson A.E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 92:1998;747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 16
    • 0025949923 scopus 로고
    • The signal recognition particle in S. cerevisiae
    • Hann B.C., Walter P. The signal recognition particle in S. cerevisiae. Cell. 67:1991;131-144.
    • (1991) Cell , vol.67 , pp. 131-144
    • Hann, B.C.1    Walter, P.2
  • 17
    • 0027958547 scopus 로고
    • Evolutionary conservation of components of the protein translocation complex
    • Hartmann E., Sommer T., Prehn S., Görlich D., Jentsch S., Rapoport T.A. Evolutionary conservation of components of the protein translocation complex. Nature. 367:1994;654-657.
    • (1994) Nature , vol.367 , pp. 654-657
    • Hartmann, E.1    Sommer, T.2    Prehn, S.3    Görlich, D.4    Jentsch, S.5    Rapoport, T.A.6
  • 18
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller M.M., Finger A., Schweiger M., Wolf D.H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 273:1996;1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 19
    • 0028173668 scopus 로고
    • The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae
    • Holmstrøm K., Brandt T., Kallesøe T. The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae. Yeast. 10:1994;S47-S62.
    • (1994) Yeast , vol.10
    • Holmstrøm, K.1    Brandt, T.2    Kallesøe, T.3
  • 20
    • 0034664243 scopus 로고    scopus 로고
    • The ER translocon and retrotranslocation: Is the shift into reverse manual or automatic?
    • Johnson A.E., Haigh N.G. The ER translocon and retrotranslocation. is the shift into reverse manual or automatic? Cell. 102:2000;709-712.
    • (2000) Cell , vol.102 , pp. 709-712
    • Johnson, A.E.1    Haigh, N.G.2
  • 21
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson A.E., van Waes M.A. The translocon. a dynamic gateway at the ER membrane Annu. Rev. Cell Dev. Biol. 15:1999;799-842.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 799-842
    • Johnson, A.E.1    Van Waes, M.A.2
  • 22
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop M., Finger A., Braun T., Hellmuth K., Wolf D.H. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15:1996;753-763.
    • (1996) EMBO J. , vol.15 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 23
    • 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. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell. 90:1997;31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 24
    • 0035173051 scopus 로고    scopus 로고
    • Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway
    • Mutka S.C., Walter P. Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. Mol. Biol. Cell. 12:2001;577-588.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 577-588
    • Mutka, S.C.1    Walter, P.2
  • 25
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng D.T.W., Brown J.D., Walter P. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134:1996;269-278.
    • (1996) J. Cell Biol. , vol.134 , pp. 269-278
    • Ng, D.T.W.1    Brown, J.D.2    Walter, P.3
  • 26
    • 0034632033 scopus 로고    scopus 로고
    • The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
    • Ng D.T., Spear E.D., Walter P. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J. Cell Biol. 150:2000;77-88.
    • (2000) J. Cell Biol. , vol.150 , pp. 77-88
    • Ng, D.T.1    Spear, E.D.2    Walter, P.3
  • 27
    • 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. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell. 81:1995;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
  • 28
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath K., Mothes W., Wilkinson B.M., Stirling C.J., Rapoport T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell. 94:1998;795-807.
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 29
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • Plemper R.K., Wolf D.H. Retrograde protein translocation. ERADication of secretory proteins in health and disease Trends Biochem. Sci. 24:1999;266-270.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 30
    • 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. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388:1997;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
  • 31
    • 0034678632 scopus 로고    scopus 로고
    • Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
    • a
    • Prinz A., Behrens C., Rapoport T.A., Hartmann E., Kalies K.U. Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA. EMBO J. 19:2000;1900-1906. a.
    • (2000) EMBO J. , vol.19 , pp. 1900-1906
    • Prinz, A.1    Behrens, C.2    Rapoport, T.A.3    Hartmann, E.4    Kalies, K.U.5
  • 32
    • 0033787091 scopus 로고    scopus 로고
    • Sec61p is the main ribosome receptor in the endoplasmic reticulum of Saccharomyces cerevisiae
    • b
    • Prinz A., Hartmann E., Kalies K.U. Sec61p is the main ribosome receptor in the endoplasmic reticulum of Saccharomyces cerevisiae. Biol. Chem. 381:2000;1025-1029. b.
    • (2000) Biol. Chem. , vol.381 , pp. 1025-1029
    • Prinz, A.1    Hartmann, E.2    Kalies, K.U.3
  • 34
    • 0033490112 scopus 로고    scopus 로고
    • Surfing the Sec61 channel: Bidirectional protein translocation across the ER membrane
    • Romisch K. Surfing the Sec61 channel. bidirectional protein translocation across the ER membrane J. Cell Sci. 112:1999;4185-4191.
    • (1999) J. Cell Sci. , vol.112 , pp. 4185-4191
    • Romisch, K.1
  • 35
    • 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. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109:1989;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
  • 36
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon S.M., Blobel G. A protein-conducting channel in the endoplasmic reticulum. Cell. 65:1991;371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 37
    • 0026509379 scopus 로고
    • The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19
    • Stirling C.J., Hewitt E.W. The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19. Nature. 356:1992;534-537.
    • (1992) Nature , vol.356 , pp. 534-537
    • Stirling, C.J.1    Hewitt, E.W.2
  • 38
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling C.J., Rothblatt J., Hosobuchi M., Deshaies R., Schekman R. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell. 3:1992;129-142.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 39
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas B.J., Rothstein R. Elevated recombination rates in transcriptionally active DNA. Cell. 56:1989;619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 40
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell. 101:2000;249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 41
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson J.R., Stirling C.J. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J. 19:2000;6440-6452.
    • (2000) EMBO J. , vol.19 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 42
    • 0033229970 scopus 로고    scopus 로고
    • The economics of ribosome biosynthesis in yeast
    • Warner J.R. The economics of ribosome biosynthesis in yeast. Trends Biochem. Sci. 24:1999;437-440.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 437-440
    • Warner, J.R.1
  • 43
    • 0029817931 scopus 로고    scopus 로고
    • Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
    • Wilkinson B.M., Critchley A.J., Stirling C.J. Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J. Biol. Chem. 271:1996;25590-25597.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25590-25597
    • Wilkinson, B.M.1    Critchley, A.J.2    Stirling, C.J.3
  • 44
    • 0030812436 scopus 로고    scopus 로고
    • Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p
    • a
    • Wilkinson B.M., Esnault Y., Craven R.A., Skiba F., Fieschi J., Kepes F., Stirling C.J. Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p. EMBO J. 16:1997;4549-4559. a.
    • (1997) EMBO J. , vol.16 , pp. 4549-4559
    • Wilkinson, B.M.1    Esnault, Y.2    Craven, R.A.3    Skiba, F.4    Fieschi, J.5    Kepes, F.6    Stirling, C.J.7
  • 45
    • 0030933426 scopus 로고    scopus 로고
    • Protein translocation across the membrane of the endoplasmic reticulum
    • b
    • Wilkinson B.M., Regnacq M., Stirling C.J. Protein translocation across the membrane of the endoplasmic reticulum. J. Membr. Biol. 155:1997;189-197. b.
    • (1997) J. Membr. Biol. , vol.155 , pp. 189-197
    • Wilkinson, B.M.1    Regnacq, M.2    Stirling, C.J.3
  • 46
    • 0034614525 scopus 로고    scopus 로고
    • Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation
    • Wilkinson B.M., Tyson J.R., Reid P.J., Stirling C.J. Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation. J. Biol. Chem. 275:2000;521-529.
    • (2000) J. Biol. Chem. , vol.275 , pp. 521-529
    • Wilkinson, B.M.1    Tyson, J.R.2    Reid, P.J.3    Stirling, C.J.4
  • 47
    • 0032803068 scopus 로고    scopus 로고
    • Probing the molecular environment of membrane proteins in vivo
    • Wittke S., Lewke N., Muller S., Johnsson N. Probing the molecular environment of membrane proteins in vivo. Mol. Biol. Cell. 10:1999;2519-2530.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2519-2530
    • Wittke, S.1    Lewke, N.2    Muller, S.3    Johnsson, N.4
  • 48
    • 0035862963 scopus 로고    scopus 로고
    • Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo
    • Young B.P., Craven R.A., Reid P.J., Willer M., Stirling C.J. Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J. 20:2001;262-271.
    • (2001) EMBO J. , vol.20 , pp. 262-271
    • Young, B.P.1    Craven, R.A.2    Reid, P.J.3    Willer, M.4    Stirling, C.J.5
  • 49
    • 0033382189 scopus 로고    scopus 로고
    • The engagement of Sec61p in the ER dislocation process
    • Zhou M., Schekman R. The engagement of Sec61p in the ER dislocation process. Mol. Cell. 4:1999;925-934.
    • (1999) Mol. Cell , vol.4 , pp. 925-934
    • Zhou, M.1    Schekman, R.2


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