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Volumn 3, Issue 10, 2008, Pages

Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; MOLECULAR SCAFFOLD; SIGNAL RECOGNITION PARTICLE; SIGNAL RECOGNITION PARTICLE 19; SIGNAL RECOGNITION PARTICLE 54; UNCLASSIFIED DRUG; RIBONUCLEOPROTEIN;

EID: 55849105200     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003528     Document Type: Article
Times cited : (23)

References (63)
  • 1
    • 13844266603 scopus 로고    scopus 로고
    • The signal recognition particle and its interactions during protein targeting
    • Halic M, Beckmann R (2005) The signal recognition particle and its interactions during protein targeting. Curr Opin Struct Biol 15: 116-125.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 116-125
    • Halic, M.1    Beckmann, R.2
  • 2
    • 17044419154 scopus 로고    scopus 로고
    • Targeting proteins to membranes: Structure of the signal recognition particle
    • Egea PF, Stroud RM, Walter P (2005) Targeting proteins to membranes: structure of the signal recognition particle. Curr Opin Struct Biol 15: 213-220.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 213-220
    • Egea, P.F.1    Stroud, R.M.2    Walter, P.3
  • 3
    • 0034596007 scopus 로고    scopus 로고
    • Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor
    • Peluso P, Herschlag D, Nock S, Freymann DM, Johnson AE, et al. (2000) Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor. Science 288: 1640-1643.
    • (2000) Science , vol.288 , pp. 1640-1643
    • Peluso, P.1    Herschlag, D.2    Nock, S.3    Freymann, D.M.4    Johnson, A.E.5
  • 5
    • 0041813302 scopus 로고    scopus 로고
    • Structure, function and evolution of the signal recognition particle
    • Nagai K, Oubridge C, Kuglstatter A, Menichelli E, Isel C, et al. (2003) Structure, function and evolution of the signal recognition particle. Embo J 22: 3479-3485.
    • (2003) Embo J , vol.22 , pp. 3479-3485
    • Nagai, K.1    Oubridge, C.2    Kuglstatter, A.3    Menichelli, E.4    Isel, C.5
  • 6
    • 0037310079 scopus 로고    scopus 로고
    • S-domain assembly of the signal recognition particle
    • Sauer-Eriksson AE, Hainzl T (2003) S-domain assembly of the signal recognition particle. Curr Opin Struct Biol 13: 64-70.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 64-70
    • Sauer-Eriksson, A.E.1    Hainzl, T.2
  • 7
    • 0034654251 scopus 로고    scopus 로고
    • Assembly of archaeal signal recognition particle from recombinant components
    • Bhuiyan SH, Gowda K, Hotokezaka H, Zwieb C (2000) Assembly of archaeal signal recognition particle from recombinant components. Nucleic Acids Res 28: 1365-1373.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1365-1373
    • Bhuiyan, S.H.1    Gowda, K.2    Hotokezaka, H.3    Zwieb, C.4
  • 8
    • 0034711041 scopus 로고    scopus 로고
    • Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle
    • Diener JL, Wilson C (2000) Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle. Biochemistry 39: 12862-12874.
    • (2000) Biochemistry , vol.39 , pp. 12862-12874
    • Diener, J.L.1    Wilson, C.2
  • 9
    • 22244451030 scopus 로고    scopus 로고
    • Structural insights into SRP RNA: An induced fit mechanism for SRP assembly
    • Hainzl T, Huang S, Sauer-Eriksson AE (2005) Structural insights into SRP RNA: an induced fit mechanism for SRP assembly. Rna 11: 1043-1050.
    • (2005) Rna , vol.11 , pp. 1043-1050
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 10
    • 0036799450 scopus 로고    scopus 로고
    • Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii
    • Tozik I, Huang Q, Zwieb C, Eichler J (2002) Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii. Nucleic Acids Res 30: 4166-4175.
    • (2002) Nucleic Acids Res , vol.30 , pp. 4166-4175
    • Tozik, I.1    Huang, Q.2    Zwieb, C.3    Eichler, J.4
  • 11
    • 0035798197 scopus 로고    scopus 로고
    • An archaeal protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA
    • Maeshima H, Okuno E, Aimi T, Morinaga T, Itoh T (2001) An archaeal protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA. FEBS Lett 507: 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
  • 12
    • 33845931895 scopus 로고    scopus 로고
    • SRP19 is a dispensable component of the signal recognition particle in Archaea
    • Yurist S, Dahan I, Eichler J (2007) SRP19 is a dispensable component of the signal recognition particle in Archaea. J Bacteriol 189: 276-279.
    • (2007) J Bacteriol , vol.189 , pp. 276-279
    • Yurist, S.1    Dahan, I.2    Eichler, J.3
  • 13
    • 0034687215 scopus 로고    scopus 로고
    • Nuclear export of yeast signal recognition particle lacking Srp54p by the Xpo1p/Crm1p NES-dependent pathway
    • Ciufo LF, Brown JD (2000) Nuclear export of yeast signal recognition particle lacking Srp54p by the Xpo1p/Crm1p NES-dependent pathway. Curr Biol 10: 1256-1264.
    • (2000) Curr Biol , vol.10 , pp. 1256-1264
    • Ciufo, L.F.1    Brown, J.D.2
  • 14
    • 0035858874 scopus 로고    scopus 로고
    • Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export
    • Grosshans H, Deinert K, Hurt E, Simos G (2001) Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol 153: 745-762.
    • (2001) J Cell Biol , vol.153 , pp. 745-762
    • Grosshans, H.1    Deinert, K.2    Hurt, E.3    Simos, G.4
  • 15
    • 0032493374 scopus 로고    scopus 로고
    • Localization of signal recognition particle RNA in the nucleolus of mammalian cells
    • Jacobson MR, Pederson T (1998) Localization of signal recognition particle RNA in the nucleolus of mammalian cells. Proc Natl Acad Sci U S A 95: 7981-7986.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7981-7986
    • Jacobson, M.R.1    Pederson, T.2
  • 18
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • Keenan RJ, Freymann DM, Walter P, Stroud RM (1998) Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94: 181-191.
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 19
    • 0344304454 scopus 로고    scopus 로고
    • Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
    • Rosendal KR, Wild K, Montoya G, Sinning I (2003) Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication. Proc Natl Acad Sci U S A 100: 14701-14706.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14701-14706
    • Rosendal, K.R.1    Wild, K.2    Montoya, G.3    Sinning, I.4
  • 20
    • 35448950462 scopus 로고    scopus 로고
    • Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle
    • Hainzl T, Huang S, Sauer-Eriksson AE (2007) Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle. Proc Natl Acad Sci U S A 104: 14911-14916.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14911-14916
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 21
    • 0024024901 scopus 로고
    • The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length
    • Siegel V, Walter P (1988) The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length. Embo J 7: 1769-1775.
    • (1988) Embo J , vol.7 , pp. 1769-1775
    • Siegel, V.1    Walter, P.2
  • 22
    • 2542614508 scopus 로고    scopus 로고
    • Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor
    • Buskiewicz I, Deuerling E, Gu SQ, Jockel J, Rodnina MV, et al. (2004) Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proc Natl Acad Sci U S A 101: 7902-7906.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7902-7906
    • Buskiewicz, I.1    Deuerling, E.2    Gu, S.Q.3    Jockel, J.4    Rodnina, M.V.5
  • 23
    • 22444441692 scopus 로고    scopus 로고
    • Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET
    • Buskiewicz I, Peske F, Wieden HJ, Gryczynski I, Rodnina MV, et al. (2005) Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET. J Mol Biol 351: 417-430.
    • (2005) J Mol Biol , vol.351 , pp. 417-430
    • Buskiewicz, I.1    Peske, F.2    Wieden, H.J.3    Gryczynski, I.4    Rodnina, M.V.5
  • 24
    • 21844456918 scopus 로고    scopus 로고
    • Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY
    • Buskiewicz I, Kubarenko A, Peske F, Rodnina MV, Wintermeyer W (2005) Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY. Rna 11: 947-957.
    • (2005) Rna , vol.11 , pp. 947-957
    • Buskiewicz, I.1    Kubarenko, A.2    Peske, F.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 25
    • 28544445590 scopus 로고    scopus 로고
    • RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle
    • Spanggord RJ, Siu F, Ke A, Doudna JA (2005) RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle. Nat Struct Mol Biol 12: 1116-1122.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1116-1122
    • Spanggord, R.J.1    Siu, F.2    Ke, A.3    Doudna, J.A.4
  • 26
    • 0033600728 scopus 로고    scopus 로고
    • Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: Evidence for the mechanism of signal peptide binding
    • Clemons WM Jr, Gowda K, Black SD, Zwieb C, Ramakrishnan V (1999) Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding. J Mol Biol 292: 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
  • 27
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA (2000) Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287: 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.A.5
  • 28
    • 0037071839 scopus 로고    scopus 로고
    • Structure of the SRP19 RNA complex and implications for signal recognition particle assembly
    • Hainzl T, Huang S, Sauer-Eriksson AE (2002) Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Nature 417: 767-771.
    • (2002) Nature , vol.417 , pp. 767-771
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 29
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, et al. (2004) Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427: 808-814.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5
  • 30
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • Halic M, Blau M, Becker T, Mielke T, Pool MR, et al. (2006) Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 444: 507-511.
    • (2006) Nature , vol.444 , pp. 507-511
    • Halic, M.1    Blau, M.2    Becker, T.3    Mielke, T.4    Pool, M.R.5
  • 31
    • 34347399347 scopus 로고    scopus 로고
    • The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting
    • Bradshaw N, Walter P (2007) The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting. Mol Biol Cell 18: 2728-2734.
    • (2007) Mol Biol Cell , vol.18 , pp. 2728-2734
    • Bradshaw, N.1    Walter, P.2
  • 32
    • 0032813781 scopus 로고    scopus 로고
    • Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP
    • Freymann DM, Keenan RJ, Stroud RM, Walter P (1999) Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol 6: 793-801.
    • (1999) Nat Struct Biol , vol.6 , pp. 793-801
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 33
    • 0347089151 scopus 로고    scopus 로고
    • Novel protein and Mg2+ configurations in the Mg2+GDP complex of the SRP GTPase ffh
    • Focia PJ, Alam H, Lu T, Ramirez UD, Freymann DM (2004) Novel protein and Mg2+ configurations in the Mg2+GDP complex of the SRP GTPase ffh. Proteins 54: 222-230.
    • (2004) Proteins , vol.54 , pp. 222-230
    • Focia, P.J.1    Alam, H.2    Lu, T.3    Ramirez, U.D.4    Freymann, D.M.5
  • 34
    • 0037447254 scopus 로고    scopus 로고
    • Induced nucleotide specificity in a GTPase
    • Shan SO, Walter P (2003) Induced nucleotide specificity in a GTPase. Proc Natl Acad Sci U S A 100: 4480-4485.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4480-4485
    • Shan, S.O.1    Walter, P.2
  • 35
    • 17644425296 scopus 로고    scopus 로고
    • Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor
    • Shan SO, Walter P (2005) Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor. Biochemistry 44: 6214-6222.
    • (2005) Biochemistry , vol.44 , pp. 6214-6222
    • Shan, S.O.1    Walter, P.2
  • 37
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, et al. (2004) Substrate twinning activates the signal recognition particle and its receptor. Nature 427: 215-221.
    • (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
  • 38
    • 33745644462 scopus 로고    scopus 로고
    • Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site
    • Focia PJ, Gawronski-Salerno J, Coon JSt, Freymann DM (2006) Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site. J Mol Biol 360: 631-643.
    • (2006) J Mol Biol , vol.360 , pp. 631-643
    • Focia, P.J.1    Gawronski-Salerno, J.2    Coon, J.S.3    Freymann, D.M.4
  • 39
    • 33947320768 scopus 로고    scopus 로고
    • Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY
    • Gawronski-Salerno J, Freymann DM (2007) Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY. J Struct Biol 158: 122-128.
    • (2007) J Struct Biol , vol.158 , pp. 122-128
    • Gawronski-Salerno, J.1    Freymann, D.M.2
  • 40
    • 33847016483 scopus 로고    scopus 로고
    • X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases
    • Gawronski-Salerno J, Coon JSt, Focia PJ, Freymann DM (2007) X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases. Proteins 66: 984-995.
    • (2007) Proteins , vol.66 , pp. 984-995
    • Gawronski-Salerno, J.1    Coon, J.S.2    Focia, P.J.3    Freymann, D.M.4
  • 41
    • 0036290864 scopus 로고    scopus 로고
    • Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle
    • Pakhomova ON, Deep S, Huang Q, Zwieb C, Hinck AP (2002) Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle. J Mol Biol 317: 145-158.
    • (2002) J Mol Biol , vol.317 , pp. 145-158
    • Pakhomova, O.N.1    Deep, S.2    Huang, Q.3    Zwieb, C.4    Hinck, A.P.5
  • 42
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C, Ito N, Evans PR, Teo CH, Nagai K (1994) Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372: 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 43
    • 0031568337 scopus 로고    scopus 로고
    • The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe
    • Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, et al. (1997) The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. Structure 5: 59-68.
    • (1997) Structure , vol.5 , pp. 59-68
    • Goldgur, Y.1    Mosyak, L.2    Reshetnikova, L.3    Ankilova, V.4    Lavrik, O.5
  • 44
    • 0035913989 scopus 로고    scopus 로고
    • Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
    • Wild K, Sinning I, Cusack S (2001) Crystal structure of an early protein-RNA assembly complex of the signal recognition particle. Science 294: 598-601.
    • (2001) Science , vol.294 , pp. 598-601
    • Wild, K.1    Sinning, I.2    Cusack, S.3
  • 45
    • 0036289536 scopus 로고    scopus 로고
    • Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle
    • Oubridge C, Kuglstatter A, Jovine L, Nagai K (2002) Crystal 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: 1251-1261.
    • (2002) Mol Cell , vol.9 , pp. 1251-1261
    • Oubridge, C.1    Kuglstatter, A.2    Jovine, L.3    Nagai, K.4
  • 46
    • 0036785939 scopus 로고    scopus 로고
    • Induced structural changes of 7SL RNA during the assembly of human signal recognition particle
    • Kuglstatter A, Oubridge C, Nagai K (2002) Induced structural changes of 7SL RNA during the assembly of human signal recognition particle. Nat Struct Biol 9: 740-744.
    • (2002) Nat Struct Biol , vol.9 , pp. 740-744
    • Kuglstatter, A.1    Oubridge, C.2    Nagai, K.3
  • 47
    • 0035007334 scopus 로고    scopus 로고
    • Visualizing induced fit in early assembly of the human signal recognition particle
    • Rose MA, Weeks KM (2001) Visualizing induced fit in early assembly of the human signal recognition particle. Nat Struct Biol 8: 515-520.
    • (2001) Nat Struct Biol , vol.8 , pp. 515-520
    • Rose, M.A.1    Weeks, K.M.2
  • 48
    • 34247599773 scopus 로고    scopus 로고
    • A threefold RNA-protein interface in the signal recognition particle gates native complex assembly
    • Maity TS, Weeks KM (2007) A threefold RNA-protein interface in the signal recognition particle gates native complex assembly. J Mol Biol 369: 512-524.
    • (2007) J Mol Biol , vol.369 , pp. 512-524
    • Maity, T.S.1    Weeks, K.M.2
  • 49
    • 33845571197 scopus 로고    scopus 로고
    • Compartmentalization directs assembly of the signal recognition particle
    • Maity TS, Leonard CW, Rose MA, Fried HM, Weeks KM (2006) Compartmentalization directs assembly of the signal recognition particle. Biochemistry 45: 14955-14964.
    • (2006) Biochemistry , vol.45 , pp. 14955-14964
    • Maity, T.S.1    Leonard, C.W.2    Rose, M.A.3    Fried, H.M.4    Weeks, K.M.5
  • 50
    • 1642528981 scopus 로고    scopus 로고
    • Two strategically placed base pairs in helix 8 of mammalian signal recognition particle RNA are crucial for the SPR19-dependent binding of protein SRP54
    • Yin J, Yang CH, Zwieb C (2004) Two strategically placed base pairs in helix 8 of mammalian signal recognition particle RNA are crucial for the SPR19-dependent binding of protein SRP54. Rna 10: 574-580.
    • (2004) Rna , vol.10 , pp. 574-580
    • Yin, J.1    Yang, C.H.2    Zwieb, C.3
  • 51
    • 0032727991 scopus 로고    scopus 로고
    • Themes in RNA-protein recognition
    • Draper DE (1999) Themes in RNA-protein recognition. J Mol Biol 293: 255-270.
    • (1999) J Mol Biol , vol.293 , pp. 255-270
    • Draper, D.E.1
  • 52
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 53
    • 33847290484 scopus 로고    scopus 로고
    • Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems
    • Doublie S (2007) Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems. Methods Mol Biol 363: 91-108.
    • (2007) Methods Mol Biol , vol.363 , pp. 91-108
    • Doublie, S.1
  • 54
    • 0242710958 scopus 로고    scopus 로고
    • Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing
    • Strub MP, Hoh F, Sanchez JF, Strub JM, Bock A, et al. (2003) Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing. Structure 11: 1359-1367.
    • (2003) Structure , vol.11 , pp. 1359-1367
    • Strub, M.P.1    Hoh, F.2    Sanchez, J.F.3    Strub, J.M.4    Bock, A.5
  • 55
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology 276: 305-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 305-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AG (2006) The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 62: 48-57.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 57
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
  • 58
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • Holton J, Alber T (2004) Automated protein crystal structure determination using ELVES. Proc Natl Acad Sci U S A 101: 1537-1542.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 61
  • 62
    • 0034142070 scopus 로고    scopus 로고
    • Novel approach to phasing proteins: Derivatization by short cryo-soaking with halides
    • Dauter Z, Dauter M, Rajashankar KR (2000) Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr D Biol Crystallogr 56: 232-237.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 232-237
    • Dauter, Z.1    Dauter, M.2    Rajashankar, K.R.3
  • 63
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5


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