메뉴 건너뛰기




Volumn 15, Issue 2, 2005, Pages 213-220

Targeting proteins to membranes: Structure of the signal recognition particle

Author keywords

[No Author keywords available]

Indexed keywords

DOCKING PROTEIN; GUANOSINE TRIPHOSPHATE; RIBONUCLEOPROTEIN; SIGNAL RECOGNITION PARTICLE; TRANSLOCON;

EID: 17044419154     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.03.007     Document Type: Review
Times cited : (183)

References (59)
  • 2
    • 0035283319 scopus 로고    scopus 로고
    • The signal recognition particle of archaea
    • J. Eichler, and R. Moll The signal recognition particle of archaea Trends Microbiol 9 2001 130 136
    • (2001) Trends Microbiol , vol.9 , pp. 130-136
    • Eichler, J.1    Moll, R.2
  • 4
    • 0032784010 scopus 로고    scopus 로고
    • Signal sequence recognition and protein targeting
    • R.M. Stroud, and P. Walter Signal sequence recognition and protein targeting Curr Opin Struct Biol 9 1999 754 759
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 754-759
    • Stroud, R.M.1    Walter, P.2
  • 5
    • 3943099373 scopus 로고    scopus 로고
    • Structural insights into the signal recognition particle
    • J.A. Doudna, and R.T. Batey Structural insights into the signal recognition particle Annu Rev Biochem 73 2004 539 557
    • (2004) Annu Rev Biochem , vol.73 , pp. 539-557
    • Doudna, J.A.1    Batey, R.T.2
  • 6
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • S.O. Shan, and P. Walter Co-translational protein targeting by the signal recognition particle FEBS Lett 579 2005 921 926
    • (2005) FEBS Lett , vol.579 , pp. 921-926
    • Shan, S.O.1    Walter, P.2
  • 9
    • 0037310079 scopus 로고    scopus 로고
    • S-domain assembly of the signal recognition particle
    • A.E. Sauer-Ericksson, and T. Hainzl S-domain assembly of the signal recognition particle Curr Opin Struct Biol 13 2003 64 70
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 64-70
    • Sauer-Ericksson, A.E.1    Hainzl, T.2
  • 10
    • 0035913989 scopus 로고    scopus 로고
    • Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
    • K. Wild, I. Sinning, and S. Cusack Crystal structure of an early protein-RNA assembly complex of the signal recognition particle Science 294 2001 598 601
    • (2001) Science , vol.294 , pp. 598-601
    • Wild, K.1    Sinning, I.2    Cusack, S.3
  • 11
    • 0036289536 scopus 로고    scopus 로고
    • Structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle
    • C. Oubridge, A. Kuglstatter, L. Jovine, and K. Nagai Structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle Mol Cell 9 2002 1251 1261 The authors describe the crystal structure of a non-cognate binary complex between archaeal Methanococcus jannaschii SRP19 and the human S domain of 7S RNA.
    • (2002) Mol Cell , vol.9 , pp. 1251-1261
    • Oubridge, C.1    Kuglstatter, A.2    Jovine, L.3    Nagai, K.4
  • 12
    • 0037071839 scopus 로고    scopus 로고
    • Structure of the SRP19 RNA complex and implications for signal recognition particle assembly
    • T. Hainzl, S. Huang, and A.E. Sauer-Eriksson Structure of the SRP19 RNA complex and implications for signal recognition particle assembly Nature 417 2002 767 771 The crystal structure of the archaeal binary complex formed between SRP19 and the S domain of the 7S RNA from M. jannaschii is reported. It illustrates the molecular basis of SRP19 binding to the S domain and the overall architecture of the RNA, showing the stabilizing interactions established between RNA helices 6 and 8, which stack against each other to form the S domain.
    • (2002) Nature , vol.417 , pp. 767-771
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 13
    • 0036785939 scopus 로고    scopus 로고
    • Induced structural changes of 7SL RNA during the assembly of human signal recognition particle
    • A. Kuglstatter, C. Oubridge, and K. Nagai Induced structural changes of 7SL RNA during the assembly of human signal recognition particle Nat Struct Biol 9 2002 740 744 This article presents the X-ray structure of the ternary complex between human SRP19, SRP54 (M domain) and the S domain of 7S RNA. Binding of the M domain induces conformational changes in the RNA. A mechanism of S domain assembly in humans is proposed.
    • (2002) Nat Struct Biol , vol.9 , pp. 740-744
    • Kuglstatter, A.1    Oubridge, C.2    Nagai, K.3
  • 14
    • 0030926002 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle Alu RNA binding heterodimer SRP9/14
    • D.E. Birse, U. Kapp, K. Strub, S. Cusack, and A. Åberg The crystal structure of the signal recognition particle Alu RNA binding heterodimer SRP9/14 EMBO J 16 1997 3757 3766
    • (1997) EMBO J , vol.16 , pp. 3757-3766
    • Birse, D.E.1    Kapp, U.2    Strub, K.3    Cusack, S.4    Åberg, A.5
  • 15
    • 0034626729 scopus 로고    scopus 로고
    • Structure and assembly of the Alu domain of the signal recognition particle
    • O. Weichenrieder, K. Wild, K. Strub, and S. Cusack Structure and assembly of the Alu domain of the signal recognition particle Nature 408 2000 167 173
    • (2000) Nature , vol.408 , pp. 167-173
    • Weichenrieder, O.1    Wild, K.2    Strub, K.3    Cusack, S.4
  • 16
    • 0030832397 scopus 로고    scopus 로고
    • Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
    • T. Powers, and P. Walter Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor EMBO J 16 1997 4880 4886
    • (1997) EMBO J , vol.16 , pp. 4880-4886
    • Powers, T.1    Walter, P.2
  • 17
    • 0035007334 scopus 로고    scopus 로고
    • Visualizing induced fit in early assembly of the human signal recognition particle
    • M.A. Rose, and K.M. Weeks Visualizing induced fit in early assembly of the human signal recognition particle Nat Struct Biol 8 2001 515 520
    • (2001) Nat Struct Biol , vol.8 , pp. 515-520
    • Rose, M.A.1    Weeks, K.M.2
  • 18
    • 0035798197 scopus 로고    scopus 로고
    • An archaeal protein homolog to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA
    • H. Maeshima, E. Okuno, T. Aimi, T. Morinaga, and T. Itoh An archaeal protein homolog to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA FEBS Lett 507 2001 336 340
    • (2001) FEBS Lett , vol.507 , pp. 336-340
    • Maeshima, H.1    Okuno, E.2    Aimi, T.3    Morinaga, T.4    Itoh, T.5
  • 19
    • 0036799450 scopus 로고    scopus 로고
    • Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii
    • I. Tozik, Q. Huang, C. Zwieb, and J. Eichler Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii Nucleic Acids Res 30 2002 4166 4175
    • (2002) Nucleic Acids Res , vol.30 , pp. 4166-4175
    • Tozik, I.1    Huang, Q.2    Zwieb, C.3    Eichler, J.4
  • 20
    • 0035896023 scopus 로고    scopus 로고
    • Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
    • R.T. Batey, M.B. Sagar, and J. Doudna Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle J Mol Biol 307 2001 229 246
    • (2001) J Mol Biol , vol.307 , pp. 229-246
    • Batey, R.T.1    Sagar, M.B.2    Doudna, J.3
  • 21
    • 0036786231 scopus 로고    scopus 로고
    • Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly
    • R.T. Batey, and J. Doudna Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly Biochemistry 41 2002 11703 11710
    • (2002) Biochemistry , vol.41 , pp. 11703-11710
    • Batey, R.T.1    Doudna, J.2
  • 22
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • R.J. Keenan, D.J. Freymann, P. Walter, and R.M. Stroud Crystal structure of the signal sequence binding subunit of the signal recognition particle Cell 94 1998 181 191
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.J.2    Walter, P.3    Stroud, R.M.4
  • 23
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • D.M. Freymann, R.J. Keenan, R.M. Stroud, and P. Walter Structure of the conserved GTPase domain of the signal recognition particle Nature 385 1997 361 364
    • (1997) Nature , vol.385 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 25
    • 0034658294 scopus 로고    scopus 로고
    • The crystal structure of the conserved GTPase core from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for SRP-SRP receptor complex
    • G. Montoya, K. Te Kaat, R. Moll, G. Schafer, and I. Sinning The crystal structure of the conserved GTPase core from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for SRP-SRP receptor complex Structure 8 2000 515 525
    • (2000) Structure , vol.8 , pp. 515-525
    • Montoya, G.1    Te Kaat, K.2    Moll, R.3    Schafer, G.4    Sinning, I.5
  • 26
    • 0034808131 scopus 로고    scopus 로고
    • The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase
    • S. Padmanabhan, and D.M. Freymann The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase Structure 9 2001 859 867
    • (2001) Structure , vol.9 , pp. 859-867
    • Padmanabhan, S.1    Freymann, D.M.2
  • 27
    • 0036308832 scopus 로고    scopus 로고
    • Structural basis for mobility in the 1.1Å crystal structure of the NG domain of Thermus aquaticus Ffh
    • U. Ramirez, G. Minasov, P.J. Focia, R.M. Stroud, P. Walter, P. Juhn, and D.M. Freymann Structural basis for mobility in the 1.1Å crystal structure of the NG domain of Thermus aquaticus Ffh J Mol Biol 320 2002 783 799
    • (2002) J Mol Biol , vol.320 , pp. 783-799
    • Ramirez, U.1    Minasov, G.2    Focia, P.J.3    Stroud, R.M.4    Walter, P.5    Juhn, P.6    Freymann, D.M.7
  • 29
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal recognition particle receptor FtsY
    • G. Montoya, C. Svensson, J. Luirink, and I. Sinning Crystal structure of the NG domain from the signal recognition particle receptor FtsY Nature 385 1997 365 368
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 30
    • 0004489150 scopus 로고
    • Structure of the signal recognition particle by electron microscopy
    • D.W. Andrews, P. Walter, and F.P. Ottensmeyer Structure of the signal recognition particle by electron microscopy Proc Natl Acad Sci USA 82 1985 785 789
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 785-789
    • Andrews, D.W.1    Walter, P.2    Ottensmeyer, F.P.3
  • 31
    • 0023443260 scopus 로고
    • Evidence for an extended 7SL RNA structure in the signal recognition particle
    • D.W. Andrews, P. Walter, and F.P. Ottensmeyer Evidence for an extended 7SL RNA structure in the signal recognition particle EMBO J 6 1987 3471 3477
    • (1987) EMBO J , vol.6 , pp. 3471-3477
    • Andrews, D.W.1    Walter, P.2    Ottensmeyer, F.P.3
  • 32
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation arrested ribosome
    • M. Halic, T. Becker, M.R. Pool, C.M.T. Spahn, R.A. Grassucci, J. Frank, and R. Beckmann Structure of the signal recognition particle interacting with the elongation arrested ribosome Nature 427 2004 808 814 The authors present cryo-EM reconstructions of SRP-RNC complexes. By fitting the known X-ray structures of SRP and SRP RNA subdomains in the cryo-EM density maps, the authors propose a model of both the interaction between SRP, the ribosome and a nascent chain, and SRP-mediated translation elongation arrest.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.T.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 33
    • 0037406142 scopus 로고    scopus 로고
    • The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome
    • S. Gu, F. Peske, H. Wieden, M.V. Rodnina, and W. Wintermeyer The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome RNA 9 2003 566 573
    • (2003) RNA , vol.9 , pp. 566-573
    • Gu, S.1    Peske, F.2    Wieden, H.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 34
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • M.R. Pool, J. Stumm, T.A. Fulga, I. Sinning, and B. Dobberstein Distinct modes of signal recognition particle interaction with the ribosome Science 297 2002 1345 1348
    • (2002) Science , vol.297 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 36
    • 0346096862 scopus 로고    scopus 로고
    • Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition
    • L. Terzi, M.R. Pool, B. Dobberstein, and K. Strub Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition Biochemistry 43 2004 107 117
    • (2004) Biochemistry , vol.43 , pp. 107-117
    • Terzi, L.1    Pool, M.R.2    Dobberstein, B.3    Strub, K.4
  • 37
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • R.T. Batey, R.P. Rambo, L. Lucast, B. Rha, and J. Doudna Crystal structure of the ribonucleoprotein core of the signal recognition particle Science 287 2000 1232 1239
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.5
  • 38
    • 0033600728 scopus 로고    scopus 로고
    • Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 Å resolution: Evidence for the mechanism of signal peptide binding
    • W.M. Clemons Jr., K. Gowda, S.D. Black, C. Zwieb, and V. Ramakrishnan Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 Å resolution: evidence for the mechanism of signal peptide binding J Mol Biol 292 1999 697 705
    • (1999) J Mol Biol , vol.292 , pp. 697-705
    • Clemons Jr., W.M.1    Gowda, K.2    Black, S.D.3    Zwieb, C.4    Ramakrishnan, V.5
  • 39
    • 0344304454 scopus 로고    scopus 로고
    • Crystal structure of the complete core of archaeal signal recognition particle and implications for inter-domain communication
    • K.R. Rosendal, K. Wild, G. Montoya, and I. Sinning Crystal structure of the complete core of archaeal signal recognition particle and implications for inter-domain communication Proc Natl Acad Sci USA 100 2003 14701 14706 This article reports the low-resolution crystallographic structure of the SRP from the archaeon Ssol in the absence or presence of a fragment of the SRP RNA. This is the first structure of a full-length SRP54 in which the linker between the NG and M domains is observed.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14701-14706
    • Rosendal, K.R.1    Wild, K.2    Montoya, G.3    Sinning, I.4
  • 40
    • 0037195855 scopus 로고    scopus 로고
    • Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain
    • R.M. Cleverley, and L.M. Gierasch Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain J Biol Chem 277 2002 46763 46768
    • (2002) J Biol Chem , vol.277 , pp. 46763-46768
    • Cleverley, R.M.1    Gierasch, L.M.2
  • 41
  • 43
    • 0029963973 scopus 로고    scopus 로고
    • Regulation by the ribosome of the GTPase of the signal recognition particle during protein targeting
    • G. Bacher, H. Lutcke, B. Jungnickel, T.A. Rapoport, and B. Dobberstein Regulation by the ribosome of the GTPase of the signal recognition particle during protein targeting Nature 381 1996 248 251
    • (1996) Nature , vol.381 , pp. 248-251
    • Bacher, G.1    Lutcke, H.2    Jungnickel, B.3    Rapoport, T.A.4    Dobberstein, B.5
  • 45
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • T. Powers, and P. Walter Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases Science 269 1995 1422 1424
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 46
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • ••]) is the first to report the high-resolution structure of the universally conserved heterodimeric core of a targeting complex comprising the twinned GTPase domains of an SRP (Ffh) and its cognate SR (FtsY) from Thermus aquaticus. This structure reveals the crucial role of GTP in SRP-SR association and reciprocal activation, thus explaining the unidirectionality of the targeting reaction.
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1    Shan, S.-O.2    Napetschnig, J.3    Savage, D.F.4    Walter, P.5    Stroud, R.M.6
  • 48
    • 0034723143 scopus 로고    scopus 로고
    • Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
    • J.R. Jagath, M.V. Rodnina, and W. Wintermeyer Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP J Mol Biol 295 2000 745 753
    • (2000) J Mol Biol , vol.295 , pp. 745-753
    • Jagath, J.R.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 49
    • 0037140924 scopus 로고    scopus 로고
    • Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY
    • I.V. Shepotinovskaya, and D.M. Freymann Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY Biochim Biophys Acta 1597 2002 107 114
    • (2002) Biochim Biophys Acta , vol.1597 , pp. 107-114
    • Shepotinovskaya, I.V.1    Freymann, D.M.2
  • 50
    • 8844253060 scopus 로고    scopus 로고
    • Mechanism of association and reciprocal activation of two GTPases
    • S.-O. Shan, R.M. Stroud, and P. Walter Mechanism of association and reciprocal activation of two GTPases PLoS Biol 2 2004 e320 This article presents an extensive biochemical analysis of the FtsY-Ffh interaction, combining site-directed mutagenesis and kinetics. It dissects the various stages of bacterial SRP-SR complex formation and activation.
    • (2004) PLoS Biol , vol.2 , pp. 320
    • Shan, S.-O.1    Stroud, R.M.2    Walter, P.3
  • 51
    • 0037459447 scopus 로고    scopus 로고
    • Structural basis for the function of the β subunit if the eukaryotic signal recognition particle
    • T. Schwartz, and G. Blobel Structural basis for the function of the β subunit if the eukaryotic signal recognition particle Cell 112 2003 793 803 This article presents the first X-ray structure of a complex between the regulatory domain (SRx) of eukaryotic SRα and its membrane-docking subunit, SRβ.
    • (2003) Cell , vol.112 , pp. 793-803
    • Schwartz, T.1    Blobel, G.2
  • 52
    • 0035341399 scopus 로고    scopus 로고
    • SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon
    • T.A. Fulga, I. Sinning, B. Dobberstein, and M.R. Pool SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon EMBO J 20 2001 2338 2347
    • (2001) EMBO J , vol.20 , pp. 2338-2347
    • Fulga, T.A.1    Sinning, I.2    Dobberstein, B.3    Pool, M.R.4
  • 53
    • 0041977048 scopus 로고    scopus 로고
    • Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum
    • E.C. Mandon, Y. Jiang, and R. Gilmore Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum J Cell Biol 162 2003 575 585
    • (2003) J Cell Biol , vol.162 , pp. 575-585
    • Mandon, E.C.1    Jiang, Y.2    Gilmore, R.3
  • 54
    • 0034596007 scopus 로고    scopus 로고
    • Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor
    • P. Peluso, D. Hershlag, S. Nock, D. Freymann, A.E. Johnson, and P. Walter Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor Science 288 2000 1640 1643
    • (2000) Science , vol.288 , pp. 1640-1643
    • Peluso, P.1    Hershlag, D.2    Nock, S.3    Freymann, D.4    Johnson, A.E.5    Walter, P.6
  • 55
    • 0034602866 scopus 로고    scopus 로고
    • Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel
    • W. Song, D. Maden, and R. Gilmore Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel Cell 100 2000 333 343
    • (2000) Cell , vol.100 , pp. 333-343
    • Song, W.1    Maden, D.2    Gilmore, R.3
  • 56
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein conducting channel associated with the translating 80S ribosome
    • R. Beckmann, C.M. Spahn, N. Eswar, J. Helmers, P.A. Penczek, A. Sali, J. Frank, and G. Blobel Architecture of the protein conducting channel associated with the translating 80S ribosome Cell 107 2001 361 372
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 57
  • 58
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • C. Breyton, W. Haase, T.A. Rapoport, W. Kühlbrandt, and I. Collinson Three-dimensional structure of the bacterial protein-translocation complex SecYEG Nature 418 2002 662 665
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kühlbrandt, W.4    Collinson, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.