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Volumn 31, Issue 3, 2012, Pages 707-719

Tail-anchor targeting by a Get3 tetramer: The structure of an archaeal homologue

Author keywords

Arr4p; bioSAXS; GET pathway; protein transport; TRC40

Indexed keywords

ARCHAEAL PROTEIN; FUNGAL PROTEIN; MEMBRANE PROTEIN; PROTEIN GET3; TAIL ANCHORED PROTEIN; TETRAMER; UNCLASSIFIED DRUG;

EID: 84856413908     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.433     Document Type: Article
Times cited : (35)

References (66)
  • 2
    • 77953245945 scopus 로고    scopus 로고
    • Automated identification of pathways from quantitative genetic interaction data
    • Battle A, Jonikas MC, Walter P, Weissman JS, Koller D (2010) Automated identification of pathways from quantitative genetic interaction data. Mol Syst Biol 6: 379
    • (2010) Mol Syst Biol , vol.6 , pp. 379
    • Battle, A.1    Jonikas, M.C.2    Walter, P.3    Weissman, J.S.4    Koller, D.5
  • 3
    • 0037424360 scopus 로고    scopus 로고
    • Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M212725200
    • Beilharz T, Egan B, Silver PA, Hofmann K, Lithgow T (2003) Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 278: 8219-8223 (Pubitemid 36800565)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8219-8223
    • Beilharz, T.1    Egan, B.2    Silver, P.A.3    Hofmann, K.4    Lithgow, T.5
  • 4
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein HD, Poritz MA, Strub K, Hoben PJ, Brenner S, Walter P (1989) Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340: 482-486
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 5
    • 0038153194 scopus 로고    scopus 로고
    • The tale of tail-anchored proteins: Coming from the cytosol and looking for a membrane
    • DOI 10.1083/jcb.200303069
    • Borgese N, Colombo S, Pedrazzini E (2003) The tale of tail-anchored proteins: coming from the cytosol and looking for a membrane. J Cell Biol 161: 1013-1019 (Pubitemid 36870163)
    • (2003) Journal of Cell Biology , vol.161 , Issue.6 , pp. 1013-1019
    • Borgese, N.1    Colombo, S.2    Pedrazzini, E.3
  • 6
    • 77954378286 scopus 로고    scopus 로고
    • Remote origins of tail-anchored proteins
    • Borgese N, Righi M (2010) Remote origins of tail-anchored proteins. Traffic 11: 877-885
    • (2010) Traffic , vol.11 , pp. 877-885
    • Borgese, N.1    Righi, M.2
  • 7
    • 0029808945 scopus 로고    scopus 로고
    • The sequence of a 16 691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames
    • DOI 10.1002/(SICI)1097-0061(199610)12:13<1377::AID-YEA35>3.0.CO;2-R
    • Boskovic J, Soler-Mira A, García-Cantalejo JM, Ballesta JP, Jiménez A, Remacha M (1996) The sequence of a 16 691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames. Yeast 12: 1377-1384 (Pubitemid 26354302)
    • (1996) Yeast , vol.12 , Issue.13 , pp. 1377-1384
    • Boskovic, J.1    Soler-Mira, A.2    Garcia-Cantalejo, J.M.3    Ballesta, J.P.G.4    Jimenez, A.5    Remacha, M.6
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst D 50: 760-763
    • (1994) Acta Cryst D , vol.50 , pp. 760-763
  • 10
    • 80053210242 scopus 로고    scopus 로고
    • A structural model of SGT2 and its interactions with chaperones and Get4/Get5
    • Chartron JW, Gonzalez GM, Clemons Jr WM (2011) A structural model of SGT2 and its interactions with chaperones and Get4/Get5. J Biol Chem 286: 34325-34334
    • (2011) J Biol Chem , vol.286 , pp. 34325-34334
    • Chartron, J.W.1    Gonzalez, G.M.2    Clemons Jr., W.M.3
  • 12
    • 0025850512 scopus 로고
    • Substrate-induced dimerization of the ArsA protein, the catalytic component of an anion-translocating ATPase
    • Ching MH, Kaur P, Karkaria CE, Steiner RF, Rosen BP (1991) Substrate-induced dimerization of the ArsA protein, the catalytic component of an anion-translocating ATPase. J Biol Chem 266: 2327-2332 (Pubitemid 21909067)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.4 , pp. 2327-2332
    • Mei-Hsu, C.1    Kaur, P.2    Karkaria, C.E.3    Steiner, R.F.4    Rosen, B.P.5
  • 15
    • 46749104133 scopus 로고    scopus 로고
    • Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
    • DOI 10.1242/jcs.020321
    • Favaloro V, Spasic M, Schwappach B, Dobberstein B (2008) Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J Cell Sci 121: 1832-1840 (Pubitemid 351943376)
    • (2008) Journal of Cell Science , vol.121 , Issue.11 , pp. 1832-1840
    • Favaloro, V.1    Spasic, M.2    Schwappach, B.3    Dobberstein, B.4
  • 17
    • 0035901493 scopus 로고    scopus 로고
    • Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus
    • DOI 10.1093/emboj/20.8.1819
    • Hayashi I, Oyama T, Morikawa K (2001) Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus. EMBO J 20: 1819-1828 (Pubitemid 32397385)
    • (2001) EMBO Journal , vol.20 , Issue.8 , pp. 1819-1828
    • Hayashi, I.1    Oyama, T.2    Morikawa, K.3
  • 18
    • 77951246542 scopus 로고    scopus 로고
    • The crystal structures of yeast get3 suggest a mechanism for tail-anchored protein membrane insertion
    • Hu J, Li J, Qian X, Denic V, Sha B (2009) The crystal structures of yeast get3 suggest a mechanism for tail-anchored protein membrane insertion. PLoS ONE 4: e8061
    • (2009) PLoS ONE , vol.4
    • Hu, J.1    Li, J.2    Qian, X.3    Denic, V.4    Sha, B.5
  • 19
  • 20
    • 35948944937 scopus 로고    scopus 로고
    • A bioinformatics approach to identifying tail-anchored proteins in the human genome
    • DOI 10.1111/j.1600-0854.2007.00661.x
    • Kalbfleisch T, Cambon A, Wattenberg BW (2007) A bioinformatics approach to identifying tail-anchored proteins in the human genome. Traffic 8: 1687-1694 (Pubitemid 350066681)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1687-1694
    • Kalbfleisch, T.1    Cambon, A.2    Wattenberg, B.W.3
  • 21
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • DOI 10.1016/S0092-8674(00)81418-X
    • 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 (Pubitemid 28348006)
    • (1998) Cell , vol.94 , Issue.2 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 22
    • 0036525752 scopus 로고    scopus 로고
    • Sec61β - A component of the archaeal protein secretory system
    • DOI 10.1016/S0968-0004(01)02055-2, PII S0968000401020552
    • Kinch LN, Saier MH, Grishin NV (2002) Sec61beta-a component of the archaeal protein secretory system. Trends Biochem Sci 27: 170-171 (Pubitemid 34270759)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.4 , pp. 170-171
    • Kinch, L.N.1    Saier Jr., M.H.2    Grishin, N.V.3
  • 23
    • 0141484613 scopus 로고    scopus 로고
    • PRIMUS: A Windows PC-based system for small-angle scattering data analysis
    • Konarev PV, Volkov VV, Sokolova AV, Koch MHJ, Svergun DI (2003) PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J Appl Cryst 36: 1277-1282
    • (2003) J Appl Cryst , vol.36 , pp. 1277-1282
    • Konarev, P.V.1    Volkov, V.V.2    Sokolova, A.V.3    Mhj, K.4    Svergun, D.I.5
  • 24
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • DOI 10.1006/jmbi.1993.1115
    • Koonin EV (1993) A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. J Mol Biol 229: 1165-1174 (Pubitemid 23091831)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.4 , pp. 1165-1174
    • Koonin, E.V.1
  • 26
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 27
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305: 567-580 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 28
    • 0027401769 scopus 로고
    • A class of membrane proteins with a C-terminal anchor
    • Kutay U, Hartmann E, Rapoport TA (1993) A class of membrane proteins with a C-terminal anchor. Trends Cell Biol 3: 72-75 (Pubitemid 23072280)
    • (1993) Trends in Cell Biology , vol.3 , Issue.3 , pp. 72-75
    • Kutay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 29
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • Leipe DD, Wolf YI, Koonin EV, Aravind L (2002) Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317: 41-72 (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 30
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: Structure and DNA binding of the Soj dimer - A conserved biological switch
    • DOI 10.1038/sj.emboj.7600530
    • Leonard T, Butler P, Löwe J (2005) Bacterial chromosome segregation: structure and DNA binding of the Soj dimer-a conserved biological switch. EMBO J 24: 270-282 (Pubitemid 40216132)
    • (2005) EMBO Journal , vol.24 , Issue.2 , pp. 270-282
    • Leonard, T.A.1    Butler, P.J.2    Lowe, J.3
  • 32
    • 79957745796 scopus 로고    scopus 로고
    • A biochemical analysis of the constraints of tail-anchored protein biogenesis
    • Leznicki P,Warwicker J, High S (2011) A biochemical analysis of the constraints of tail-anchored protein biogenesis. Biochem J 436: 719-727
    • (2011) Biochem J , vol.436 , pp. 719-727
    • Leznicki, P.1    Warwicker, J.2    High, S.3
  • 33
    • 34250862251 scopus 로고    scopus 로고
    • SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
    • DOI 10.1379/CSC-220R.1
    • Liou S-T, Cheng M-Y, Wang C (2007) SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae. Cell Stress Chaperones 12: 59-70 (Pubitemid 47403329)
    • (2007) Cell Stress and Chaperones , vol.12 , Issue.1 , pp. 59-70
    • Liou, S.-T.1    Cheng, M.-Y.2    Wang, C.3
  • 34
    • 13544271768 scopus 로고    scopus 로고
    • Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions
    • DOI 10.1016/j.abb.2004.12.020
    • Liou S-T, Wang C (2005) Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions. Arch Biochem Biophys 435: 253-263 (Pubitemid 40222464)
    • (2005) Archives of Biochemistry and Biophysics , vol.435 , Issue.2 , pp. 253-263
    • Liou, S.-T.1    Wang, C.2
  • 36
    • 80052407064 scopus 로고    scopus 로고
    • The mechanism of membrane-associated steps in tailanchored protein insertion
    • Mariappan M, Mateja A, Dobosz M, Bove E, Hegde RS, Keenan RJ (2011) The mechanism of membrane-associated steps in tailanchored protein insertion. Nature 477: 61-66
    • (2011) Nature , vol.477 , pp. 61-66
    • Mariappan, M.1    Mateja, A.2    Dobosz, M.3    Bove, E.4    Hegde, R.S.5    Keenan, R.J.6
  • 38
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Cryst D 63: 32-41
    • (2007) Acta Cryst D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 39
    • 33644852489 scopus 로고    scopus 로고
    • The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol
    • DOI 10.1074/jbc.M507481200
    • Metz J, Wächter A, Schmidt B, Bujnicki JM, Schwappach B (2006) The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J Biol Chem 281: 410-417 (Pubitemid 43671202)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 410-417
    • Metz, J.1    Wachter, A.2    Schmidt, B.3    Bujnicki, J.M.4    Schwappach, B.5
  • 40
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA (2006a) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Cryst D 62: 439-450
    • (2006) Acta Cryst D , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 41
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J, Merritt EA (2006b) TLSMD web server for the generation of multi-group TLS models. J Appl Cryst 39: 109-111
    • (2006) J Appl Cryst , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 42
    • 70349416733 scopus 로고    scopus 로고
    • Tail-anchored proteins in plants
    • Pedrazzini E (2009) Tail-anchored proteins in plants. J Plant Biol 52: 88-101
    • (2009) J Plant Biol , vol.52 , pp. 88-101
    • Pedrazzini, E.1
  • 44
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam CD, Hammel M, Hura GL, Tainer JA (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q Rev Biophys 40: 191-285 (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 45
    • 70350359860 scopus 로고    scopus 로고
    • Biogenesis of tail-anchored proteins: The beginning for the end?
    • Rabu C, Schmid V, Schwappach B, High S (2009) Biogenesis of tail-anchored proteins: the beginning for the end? J Cell Sci 122: 3605-3612
    • (2009) J Cell Sci , vol.122 , pp. 3605-3612
    • Rabu, C.1    Schmid, V.2    Schwappach, B.3    High, S.4
  • 46
    • 33847118046 scopus 로고    scopus 로고
    • TFB1 or TFB2 Is Sufficient for Thermococcus kodakaraensis Viability and for Basal Transcription in Vitro
    • DOI 10.1016/j.jmb.2006.12.069, PII S0022283606017682
    • Santangelo TJ, Cubonová L, James CL, Reeve JN (2007) TFB1 or TFB2 is sufficient for Thermococcus kodakaraensis viability and for basal transcription in vitro. J Mol Biol 367: 344-357 (Pubitemid 46295427)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.2 , pp. 344-357
    • Santangelo, T.J.1    Cubonova, L.2    James, C.L.3    Reeve, J.N.4
  • 47
    • 0030611701 scopus 로고    scopus 로고
    • --stabilized nitrogenase complex and its implications for signal transduction
    • DOI 10.1038/387370a0
    • Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC (1997) Structure of ADPAIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 387: 370-376 (Pubitemid 27227195)
    • (1997) Nature , vol.387 , Issue.6631 , pp. 370-376
    • Schindelin, H.1    Kisker, C.2    Schlessman, J.L.3    Howard, J.B.4    Rees, D.C.5
  • 49
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • DOI 10.1016/j.febslet.2004.11.049
    • Shan S-O, Walter P (2005) Co-translational protein targeting by the signal recognition particle. FEBS Lett 579: 921-926 (Pubitemid 40361866)
    • (2005) FEBS Letters , vol.579 , pp. 921-926
    • Shan, S.-O.1    Walter, P.2
  • 50
    • 80051672009 scopus 로고    scopus 로고
    • A conserved archaeal pathway for tail-anchored membrane protein insertion
    • Sherrill J, Mariappan M, Dominik P, Hegde RS, Keenan RS (2011) A conserved archaeal pathway for tail-anchored membrane protein insertion. Traffic 12: 1119-1123
    • (2011) Traffic , vol.12 , pp. 1119-1123
    • Sherrill, J.1    Mariappan, M.2    Dominik, P.3    Hegde, R.S.4    Keenan, R.S.5
  • 51
    • 77955499241 scopus 로고    scopus 로고
    • Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting
    • Simpson PJ, Schwappach B, Dohlman HG, Isaacson RL (2010) Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting. Structure 18: 897-902
    • (2010) Structure , vol.18 , pp. 897-902
    • Simpson, P.J.1    Schwappach, B.2    Dohlman, H.G.3    Isaacson, R.L.4
  • 52
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • DOI 10.1146/annurev.biochem.66.1.639
    • Sprang SR (1997) G protein mechanisms: insights from structural analysis. Annu Rev Biochem 66: 639-678 (Pubitemid 27274670)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 53
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
    • DOI 10.1016/j.cell.2007.01.036, PII S009286740700195X
    • Stefanovic S, Hegde RS (2007) Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 128: 1147-1159 (Pubitemid 46427870)
    • (2007) Cell , vol.128 , Issue.6 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 56
    • 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
  • 57
    • 70349299919 scopus 로고    scopus 로고
    • Model for eukaryotic tail-anchored protein binding based on the structure of Get3
    • Suloway CJM, Chartron JW, Zaslaver M, Clemons WM (2009) Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc Natl Acad Sci USA 106: 14849-14854
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14849-14854
    • Cjm, S.1    Chartron, J.W.2    Zaslaver, M.3    Clemons, W.M.4
  • 58
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • DOI 10.1107/S0021889892001663
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 25: 495-503 (Pubitemid 23564996)
    • (1992) Journal of Applied Crystallography , vol.25 , Issue.PART 4 , pp. 495-503
    • Svergun, D.I.1
  • 59
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76: 2879-2886 (Pubitemid 29269438)
    • (1999) Biophysical Journal , vol.76 , Issue.6 , pp. 2879-2886
    • Svergun, D.I.1
  • 60
    • 0141866871 scopus 로고    scopus 로고
    • A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein
    • DOI 10.1074/jbc.M301558200
    • Tobaben S, Varoqueaux F, Brose N, Stahl B, Meyer G (2003) A brainspecific isoform of small glutamine-rich tetratricopeptide repeatcontaining protein binds to Hsc70 and the cysteine string protein. J Biol Chem 278: 38376-38383 (Pubitemid 37221730)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38376-38383
    • Tobaben, S.1    Varoqueaux, F.2    Brose, N.3    Stahl, B.4    Meyer, G.5
  • 62
    • 0033522918 scopus 로고    scopus 로고
    • The ATPase mechanism of ArsA, the catalytic subunit of the arsenite pump
    • Walmsley AR, Zhou T, Borges-Walmsley MI, Rosen BP (1999) The ATPase mechanism of ArsA, the catalytic subunit of the arsenite pump. J Biol Chem 274: 16153-16161
    • (1999) J Biol Chem , vol.274 , pp. 16153-16161
    • Walmsley, A.R.1    Zhou, T.2    Borges-Walmsley, M.I.3    Rosen, B.P.4
  • 63
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang F, Brown EC, Mak G, Zhuang J, Denic V (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell 40: 159-171
    • (2010) Mol Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 64
    • 38449090521 scopus 로고    scopus 로고
    • The use of fungal in vitro systems for studying translational regulation
    • Wu C, Amrani N, Jacobson A, Sachs MS (2007) The use of fungal in vitro systems for studying translational regulation. Methods Enzymol 429: 203-225
    • (2007) Methods Enzymol , vol.429 , pp. 203-225
    • Wu, C.1    Amrani, N.2    Jacobson, A.3    Sachs, M.S.4
  • 65
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • DOI 10.1038/nbt0303-262
    • Wu CC, Yates JR (2003) The application of mass spectrometry to membrane proteomics. Nat Biotech 21: 262-267 (Pubitemid 36314809)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.