메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

Nanobody Mediated Crystallization of an Archeal Mechanosensitive Channel

Author keywords

[No Author keywords available]

Indexed keywords

MECHANOSENSITIVE CHANNEL; MEMBRANE PROTEIN; NANOBODY; UNCLASSIFIED DRUG;

EID: 84886913778     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077984     Document Type: Article
Times cited : (20)

References (66)
  • 1
    • 79953900818 scopus 로고    scopus 로고
    • Overcoming barriers to membrane protein structure determination
    • doi:10.1038/nbt.1833
    • Bill RM, Henderson PJ, Iwata S, Kunji ER, Michel H, et al. (2011) Overcoming barriers to membrane protein structure determination. Nat Biotechnol 29: 335-340. doi:10.1038/nbt.1833. PubMed: 21478852.
    • (2011) Nat Biotechnol , vol.29 , pp. 335-340
    • Bill, R.M.1    Henderson, P.J.2    Iwata, S.3    Kunji, E.R.4    Michel, H.5
  • 2
    • 84864221004 scopus 로고    scopus 로고
    • A new era of GPCR structural and chemical biology
    • doi:10.1038/nchembio.1025
    • Granier S, Kobilka B, (2012) A new era of GPCR structural and chemical biology. Nat Chem Biol 8: 670-673. doi:10.1038/nchembio.1025. PubMed: 22810761.
    • (2012) Nat Chem Biol , vol.8 , pp. 670-673
    • Granier, S.1    Kobilka, B.2
  • 3
    • 84874258738 scopus 로고    scopus 로고
    • Structural advances for the major facilitator superfamily (MFS) transporters
    • doi:10.1016/j.tibs.2013.01.003
    • Yan N, (2013) Structural advances for the major facilitator superfamily (MFS) transporters. Trends Biochem Sci 38: 151-159. doi:10.1016/j.tibs.2013.01.003. PubMed: 23403214.
    • (2013) Trends Biochem Sci , vol.38 , pp. 151-159
    • Yan, N.1
  • 4
    • 69249088472 scopus 로고    scopus 로고
    • A prokaryotic perspective on pentameric ligand-gated ion channel structure
    • doi:10.1016/j.sbi.2009.07.006
    • Hilf RJ, Dutzler R, (2009) A prokaryotic perspective on pentameric ligand-gated ion channel structure. Curr Opin Struct Biol 19: 418-424. doi:10.1016/j.sbi.2009.07.006. PubMed: 19646860.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 418-424
    • Hilf, R.J.1    Dutzler, R.2
  • 5
    • 77951585158 scopus 로고    scopus 로고
    • Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1
    • doi:10.1126/science.1186303
    • Shimamura T, Weyand S, Beckstein O, Rutherford NG, Hadden JM, et al. (2010) Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1. Science 328: 470-473. doi:10.1126/science.1186303. PubMed: 20413494.
    • (2010) Science , vol.328 , pp. 470-473
    • Shimamura, T.1    Weyand, S.2    Beckstein, O.3    Rutherford, N.G.4    Hadden, J.M.5
  • 6
    • 84878896166 scopus 로고    scopus 로고
    • Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
    • Quistgaard EM, Löw C, Moberg P, Trésaugues L, Nordlund P, (2013) Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters. Nat Struct Mol Biol, 20: 766-8. PubMed: 23624861.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 766-768
    • Quistgaard, E.M.1    Löw, C.2    Moberg, P.3    Trésaugues, L.4    Nordlund, P.5
  • 7
    • 84883489166 scopus 로고    scopus 로고
    • Structural insights into substrate recognition in proton-dependent oligopeptide transporters
    • Guettou F, Quistgaard EM, Trésaugues L, Moberg P, Jegerschöld C, et al. (2013) Structural insights into substrate recognition in proton-dependent oligopeptide transporters. EMBO Rep, 14: 804-10. PubMed: 23867627.
    • (2013) EMBO Rep , vol.14 , pp. 804-810
    • Guettou, F.1    Quistgaard, E.M.2    Trésaugues, L.3    Moberg, P.4    Jegerschöld, C.5
  • 8
    • 80052083563 scopus 로고    scopus 로고
    • Nanobody stabilization of G protein-coupled receptor conformational states
    • doi:10.1016/j.sbi.2011.06.011
    • Steyaert J, Kobilka BK, (2011) Nanobody stabilization of G protein-coupled receptor conformational states. Curr Opin Struct Biol 21: 567-572. doi:10.1016/j.sbi.2011.06.011. PubMed: 21782416.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 567-572
    • Steyaert, J.1    Kobilka, B.K.2
  • 9
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • doi:10.1126/science.1082708
    • Dutzler R, Campbell EB, MacKinnon R, (2003) Gating the selectivity filter in ClC chloride channels. Science 300: 108-112. doi:10.1126/science.1082708. PubMed: 12649487.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 10
    • 69249107262 scopus 로고    scopus 로고
    • Engineering of recombinant crystallization chaperones
    • doi:10.1016/j.sbi.2009.04.008
    • Koide S, (2009) Engineering of recombinant crystallization chaperones. Curr Opin Struct Biol 19: 449-457. doi:10.1016/j.sbi.2009.04.008. PubMed: 19477632.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 449-457
    • Koide, S.1
  • 11
    • 84856001167 scopus 로고    scopus 로고
    • Crystallization chaperone strategies for membrane proteins
    • doi:10.1016/j.ymeth.2011.08.004
    • Lieberman RL, Culver JA, Entzminger KC, Pai JC, Maynard JA, (2011) Crystallization chaperone strategies for membrane proteins. Methods 55: 293-302. doi:10.1016/j.ymeth.2011.08.004. PubMed: 21854852.
    • (2011) Methods , vol.55 , pp. 293-302
    • Lieberman, R.L.1    Culver, J.A.2    Entzminger, K.C.3    Pai, J.C.4    Maynard, J.A.5
  • 12
    • 80054856259 scopus 로고    scopus 로고
    • DARPins and other repeat protein scaffolds: advances in engineering and applications
    • doi:10.1016/j.copbio.2011.06.004
    • Boersma YL, Plückthun A, (2011) DARPins and other repeat protein scaffolds: advances in engineering and applications. Curr Opin Biotechnol 22: 849-857. doi:10.1016/j.copbio.2011.06.004. PubMed: 21715155.
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 849-857
    • Boersma, Y.L.1    Plückthun, A.2
  • 13
    • 77953130101 scopus 로고    scopus 로고
    • Affibody molecules: engineered proteins for therapeutic, diagnostic and biotechnological applications
    • doi:10.1016/j.febslet.2010.04.014
    • Löfblom J, Feldwisch J, Tolmachev V, Carlsson J, Ståhl S, et al. (2010) Affibody molecules: engineered proteins for therapeutic, diagnostic and biotechnological applications. FEBS Lett 584: 2670-2680. doi:10.1016/j.febslet.2010.04.014. PubMed: 20388508.
    • (2010) FEBS Lett , vol.584 , pp. 2670-2680
    • Löfblom, J.1    Feldwisch, J.2    Tolmachev, V.3    Carlsson, J.4    Ståhl, S.5
  • 14
    • 80053438315 scopus 로고    scopus 로고
    • Non-immunoglobulin based protein scaffolds
    • doi:10.1016/j.copbio.2011.06.002
    • Löfblom J, Frejd FY, Ståhl S, (2011) Non-immunoglobulin based protein scaffolds. Curr Opin Biotechnol 22: 843-848. doi:10.1016/j.copbio.2011.06.002. PubMed: 21726995.
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 843-848
    • Löfblom, J.1    Frejd, F.Y.2    Ståhl, S.3
  • 15
    • 34249852867 scopus 로고    scopus 로고
    • High-affinity single-domain binding proteins with a binary-code interface
    • doi:10.1073/pnas.0700149104
    • Koide A, Gilbreth RN, Esaki K, Tereshko V, Koide S, (2007) High-affinity single-domain binding proteins with a binary-code interface. Proc Natl Acad Sci U S A 104: 6632-6637. doi:10.1073/pnas.0700149104. PubMed: 17420456.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6632-6637
    • Koide, A.1    Gilbreth, R.N.2    Esaki, K.3    Tereshko, V.4    Koide, S.5
  • 16
    • 18544397601 scopus 로고    scopus 로고
    • Directed evolution of high-affinity antibody mimics using mRNA display
    • Xu L, Aha P, Gu K, Kuimelis RG, Kurz M, et al. (2002) Directed evolution of high-affinity antibody mimics using mRNA display. Chem Biol 9: 933-942.
    • (2002) Chem Biol , vol.9 , pp. 933-942
    • Xu, L.1    Aha, P.2    Gu, K.3    Kuimelis, R.G.4    Kurz, M.5
  • 17
    • 34247098240 scopus 로고    scopus 로고
    • Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies
    • doi:10.1016/j.jmb.2007.02.029
    • Lipovsek D, Lippow SM, Hackel BJ, Gregson MW, Cheng P, et al. (2007) Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies. J Mol Biol 368: 1024-1041. doi:10.1016/j.jmb.2007.02.029. PubMed: 17382960.
    • (2007) J Mol Biol , vol.368 , pp. 1024-1041
    • Lipovsek, D.1    Lippow, S.M.2    Hackel, B.J.3    Gregson, M.W.4    Cheng, P.5
  • 18
    • 43549110330 scopus 로고    scopus 로고
    • Alternative binding proteins: anticalins - harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities
    • doi:10.1111/j.1742-4658.2008.06439.x
    • Skerra A, (2008) Alternative binding proteins: anticalins- harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities. FEBS J 275: 2677-2683. doi:10.1111/j.1742-4658.2008.06439.x. PubMed: 18435758.
    • (2008) FEBS J , vol.275 , pp. 2677-2683
    • Skerra, A.1
  • 19
    • 0027310612 scopus 로고
    • Naturally occurring antibodies devoid of light chains
    • doi:10.1038/363446a0
    • Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, et al. (1993) Naturally occurring antibodies devoid of light chains. Nature 363: 446-448. doi:10.1038/363446a0. PubMed: 8502296.
    • (1993) Nature , vol.363 , pp. 446-448
    • Hamers-Casterman, C.1    Atarhouch, T.2    Muyldermans, S.3    Robinson, G.4    Hamers, C.5
  • 20
    • 0344447084 scopus 로고    scopus 로고
    • Potent enzyme inhibitors derived from dromedary heavy-chain antibodies
    • doi:10.1093/emboj/17.13.3512
    • Lauwereys M, Arbabi Ghahroudi M, Desmyter A, Kinne J, Hölzer W, et al. (1998) Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. EMBO J 17: 3512-3520. doi:10.1093/emboj/17.13.3512. PubMed: 9649422.
    • (1998) EMBO J , vol.17 , pp. 3512-3520
    • Lauwereys, M.1    Arbabi Ghahroudi, M.2    Desmyter, A.3    Kinne, J.4    Hölzer, W.5
  • 21
    • 33645241975 scopus 로고    scopus 로고
    • Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
    • doi:10.1073/pnas.0505379103
    • De Genst E, Silence K, Decanniere K, Conrath K, Loris R, et al. (2006) Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. Proc Natl Acad Sci U S A 103: 4586-4591. doi:10.1073/pnas.0505379103. PubMed: 16537393.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4586-4591
    • De Genst, E.1    Silence, K.2    Decanniere, K.3    Conrath, K.4    Loris, R.5
  • 22
    • 79952152956 scopus 로고    scopus 로고
    • Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant
    • doi:10.1073/pnas.1008560108
    • Domanska K, Vanderhaegen S, Srinivasan V, Pardon E, Dupeux F, et al. (2011) Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant. Proc Natl Acad Sci U S A 108: 1314-1319. doi:10.1073/pnas.1008560108. PubMed: 21220305.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1314-1319
    • Domanska, K.1    Vanderhaegen, S.2    Srinivasan, V.3    Pardon, E.4    Dupeux, F.5
  • 23
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • doi:10.1016/j.str.2008.11.011
    • Korotkov KV, Pardon E, Steyaert J, Hol WG, (2009) Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17: 255-265. doi:10.1016/j.str.2008.11.011. PubMed: 19217396.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 24
    • 77956885443 scopus 로고    scopus 로고
    • Structure and properties of a complex of alpha-synuclein and a single-domain camelid antibody
    • doi:10.1016/j.jmb.2010.07.001
    • De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, et al. (2010) Structure and properties of a complex of alpha-synuclein and a single-domain camelid antibody. J Mol Biol 402: 326-343. doi:10.1016/j.jmb.2010.07.001. PubMed: 20620148.
    • (2010) J Mol Biol , vol.402 , pp. 326-343
    • De Genst, E.J.1    Guilliams, T.2    Wellens, J.3    O'Day, E.M.4    Waudby, C.A.5
  • 25
    • 84863497306 scopus 로고    scopus 로고
    • SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly
    • Baranova E, Fronzes R, Garcia-Pino A, Van Gerven N, Papapostolou D, et al. (2012) SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly. Nature 487: 119-122. PubMed: 22722836.
    • (2012) Nature , vol.487 , pp. 119-122
    • Baranova, E.1    Fronzes, R.2    Garcia-Pino, A.3    Van Gerven, N.4    Papapostolou, D.5
  • 26
    • 84863282398 scopus 로고    scopus 로고
    • Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody
    • doi:10.1093/nar/gkr867
    • Park YJ, Pardon E, Wu M, Steyaert J, Hol WG, (2012) Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody. Nucleic Acids Res 40: 1828-1840. doi:10.1093/nar/gkr867. PubMed: 22039098.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1828-1840
    • Park, Y.J.1    Pardon, E.2    Wu, M.3    Steyaert, J.4    Hol, W.G.5
  • 27
    • 61449174868 scopus 로고    scopus 로고
    • Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase
    • Conrath K, Pereira AS, Martins CE, Timóteo CG, Tavares P, et al. (2009) Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase. Protein Sci 18: 619-628. PubMed: 19241371.
    • (2009) Protein Sci , vol.18 , pp. 619-628
    • Conrath, K.1    Pereira, A.S.2    Martins, C.E.3    Timóteo, C.G.4    Tavares, P.5
  • 28
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the beta2 adrenergic receptor-Gs protein complex
    • doi:10.1038/nature10361
    • Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, et al. (2011) Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 477: 549-555. doi:10.1038/nature10361. PubMed: 21772288.
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1    DeVree, B.T.2    Zou, Y.3    Kruse, A.C.4    Chung, K.Y.5
  • 29
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor
    • doi:10.1038/nature09648
    • Rasmussen SG, Choi HJ, Fung JJ, Pardon E, Casarosa P, et al. (2011) Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor. Nature 469: 175-180. doi:10.1038/nature09648. PubMed: 21228869.
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.1    Choi, H.J.2    Fung, J.J.3    Pardon, E.4    Casarosa, P.5
  • 30
    • 55949108402 scopus 로고    scopus 로고
    • Ion channels in microbes
    • doi:10.1152/physrev.00005.2008
    • Martinac B, Saimi Y, Kung C, (2008) Ion channels in microbes. Physiol Rev 88: 1449-1490. doi:10.1152/physrev.00005.2008. PubMed: 18923187.
    • (2008) Physiol Rev , vol.88 , pp. 1449-1490
    • Martinac, B.1    Saimi, Y.2    Kung, C.3
  • 31
    • 77957942877 scopus 로고    scopus 로고
    • Mechanosensitive channels in microbes
    • doi:10.1146/annurev.micro.112408.134106
    • Kung C, Martinac B, Sukharev S, (2010) Mechanosensitive channels in microbes. Annu Rev Microbiol 64: 313-329. doi:10.1146/annurev.micro.112408.134106. PubMed: 20825352.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 313-329
    • Kung, C.1    Martinac, B.2    Sukharev, S.3
  • 32
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • doi:10.1038/nature03896
    • Kung C, (2005) A possible unifying principle for mechanosensation. Nature 436: 647-654. doi:10.1038/nature03896. PubMed: 16079835.
    • (2005) Nature , vol.436 , pp. 647-654
    • Kung, C.1
  • 33
    • 0033118214 scopus 로고    scopus 로고
    • Managing hypoosmotic stress: aquaporins and mechanosensitive channels in Escherichia coli
    • doi:10.1016/S1369-5274(99)80029-0
    • Booth IR, Louis P, (1999) Managing hypoosmotic stress: aquaporins and mechanosensitive channels in Escherichia coli. Curr Opin Microbiol 2: 166-169. doi:10.1016/S1369-5274(99)80029-0. PubMed: 10322175.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 166-169
    • Booth, I.R.1    Louis, P.2
  • 34
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity
    • doi:10.1093/emboj/18.7.1730
    • Levina N, Tötemeyer S, Stokes NR, Louis P, Jones MA, et al. (1999) Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity. EMBO J 18: 1730-1737. doi:10.1093/emboj/18.7.1730. PubMed: 10202137.
    • (1999) EMBO J , vol.18 , pp. 1730-1737
    • Levina, N.1    Tötemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5
  • 35
    • 0028224356 scopus 로고
    • A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
    • doi:10.1038/368265a0
    • Sukharev SI, Blount P, Martinac B, Blattner FR, Kung C, (1994) A large-conductance mechanosensitive channel in E. coli encoded by mscL alone. Nature 368: 265-268. doi:10.1038/368265a0. PubMed: 7511799.
    • (1994) Nature , vol.368 , pp. 265-268
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Blattner, F.R.4    Kung, C.5
  • 36
    • 0037335595 scopus 로고    scopus 로고
    • Two families of mechanosensitive channel proteins
    • doi:10.1128/MMBR.67.1.66-85.2003, table of contents
    • Pivetti CD, Yen MR, Miller S, Busch W, Tseng YH, et al. (2003) Two families of mechanosensitive channel proteins. Microbiol Mol Biol Rev 67: 66-85, table of contents doi:10.1128/MMBR.67.1.66-85.2003. PubMed: 12626684.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 66-85
    • Pivetti, C.D.1    Yen, M.R.2    Miller, S.3    Busch, W.4    Tseng, Y.H.5
  • 37
    • 69049103033 scopus 로고    scopus 로고
    • Conserved motifs in mechanosensitive channels MscL and MscS
    • doi:10.1007/s00249-009-0460-y
    • Balleza D, Gómez-Lagunas F, (2009) Conserved motifs in mechanosensitive channels MscL and MscS. Eur Biophys J 38: 1013-1027. doi:10.1007/s00249-009-0460-y. PubMed: 19424690.
    • (2009) Eur Biophys J , vol.38 , pp. 1013-1027
    • Balleza, D.1    Gómez-Lagunas, F.2
  • 38
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • doi:10.1126/science.1077945
    • Bass RB, Strop P, Barclay M, Rees DC, (2002) Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 298: 1582-1587. doi:10.1126/science.1077945. PubMed: 12446901.
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 39
    • 50649125767 scopus 로고    scopus 로고
    • The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution
    • doi:10.1126/science.1159262
    • Wang W, Black SS, Edwards MD, Miller S, Morrison EL, et al. (2008) The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution. Science 321: 1179-1183. doi:10.1126/science.1159262. PubMed: 18755969.
    • (2008) Science , vol.321 , pp. 1179-1183
    • Wang, W.1    Black, S.S.2    Edwards, M.D.3    Miller, S.4    Morrison, E.L.5
  • 40
    • 84875880032 scopus 로고    scopus 로고
    • Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 A and 4.1 A resolutions
    • Lai JY, Poon YS, Kaiser JT, Rees DC, (2013) Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 A and 4.1 A resolutions. Protein Sci.
    • (2013) Protein Sci
    • Lai, J.Y.1    Poon, Y.S.2    Kaiser, J.T.3    Rees, D.C.4
  • 41
    • 84868120537 scopus 로고    scopus 로고
    • Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance
    • doi:10.1073/pnas.1207977109
    • Zhang X, Wang J, Feng Y, Ge J, Li W, et al. (2012) Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance. Proc Natl Acad Sci U S A 109: 18180-18185. doi:10.1073/pnas.1207977109. PubMed: 23074248.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 18180-18185
    • Zhang, X.1    Wang, J.2    Feng, Y.3    Ge, J.4    Li, W.5
  • 42
    • 0026498230 scopus 로고
    • Black lipid membranes of tetraether lipids from Thermoplasma acidophilum
    • doi:10.1016/0005-2760(92)90312-J
    • Stern J, Freisleben HJ, Janku S, Ring K, (1992) Black lipid membranes of tetraether lipids from Thermoplasma acidophilum. Biochim Biophys Acta 1128: 227-236. doi:10.1016/0005-2760(92)90312-J. PubMed: 1420295.
    • (1992) Biochim Biophys Acta , vol.1128 , pp. 227-236
    • Stern, J.1    Freisleben, H.J.2    Janku, S.3    Ring, K.4
  • 43
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • doi:10.1093/nar/18.20.6069
    • Aslanidis C, de Jong PJ, (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18: 6069-6074. doi:10.1093/nar/18.20.6069. PubMed: 2235490.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 44
    • 3543050105 scopus 로고    scopus 로고
    • His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors
    • doi:10.1023/B:jsfg.0000031965.37625.0e
    • Woestenenk EA, Hammarström M, van den Berg S, Härd T, Berglund H, (2004) His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. J Struct Funct Genomics 5: 217-229. doi:10.1023/B:jsfg.0000031965.37625.0e. PubMed: 15503425.
    • (2004) J Struct Funct Genomics , vol.5 , pp. 217-229
    • Woestenenk, E.A.1    Hammarström, M.2    van den Berg, S.3    Härd, T.4    Berglund, H.5
  • 45
    • 84872758293 scopus 로고    scopus 로고
    • Optimisation of over-expression in E. coli and biophysical characterisation of human membrane protein synaptogyrin 1
    • doi:10.1371/journal.pone.0038244
    • Löw C, Jegerschöld C, Kovermann M, Moberg P, Nordlund P, (2012) Optimisation of over-expression in E. coli and biophysical characterisation of human membrane protein synaptogyrin 1. PLOS ONE 7: e38244. doi:10.1371/journal.pone.0038244. PubMed: 22675529.
    • (2012) PLOS ONE , vol.7
    • Löw, C.1    Jegerschöld, C.2    Kovermann, M.3    Moberg, P.4    Nordlund, P.5
  • 46
    • 0034812589 scopus 로고    scopus 로고
    • Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae
    • doi:10.1128/AAC.45.10.2807-2812.2001
    • Conrath KE, Lauwereys M, Galleni M, Matagne A, Frère JM, et al. (2001) Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae. Antimicrob Agents Chemother 45: 2807-2812. doi:10.1128/AAC.45.10.2807-2812.2001. PubMed: 11557473.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 2807-2812
    • Conrath, K.E.1    Lauwereys, M.2    Galleni, M.3    Matagne, A.4    Frère, J.M.5
  • 47
    • 84875982058 scopus 로고    scopus 로고
    • High-throughput analytical gel filtration screening of integral membrane proteins for structural studies
    • Löw C, Moberg P, Quistgaard EM, Hedrén M, Guettou F, et al. (2013) High-throughput analytical gel filtration screening of integral membrane proteins for structural studies. Biochim Biophys Acta, 1830: 3497-508. PubMed: 23403133.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 3497-3508
    • Löw, C.1    Moberg, P.2    Quistgaard, E.M.3    Hedrén, M.4    Guettou, F.5
  • 48
    • 0041929590 scopus 로고    scopus 로고
    • Structure and mechanism in prokaryotic mechanosensitive channels
    • doi:10.1016/S0959-440X(03)00106-4
    • Perozo E, Rees DC, (2003) Structure and mechanism in prokaryotic mechanosensitive channels. Curr Opin Struct Biol 13: 432-442. doi:10.1016/S0959-440X(03)00106-4. PubMed: 12948773.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 432-442
    • Perozo, E.1    Rees, D.C.2
  • 49
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • doi:10.1016/S0014-5793(01)02980-5
    • Drew DE, von Heijne G, Nordlund P, de Gier JW, (2001) Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli. FEBS Lett 507: 220-224. doi:10.1016/S0014-5793(01)02980-5. PubMed: 11684102.
    • (2001) FEBS Lett , vol.507 , pp. 220-224
    • Drew, D.E.1    von Heijne, G.2    Nordlund, P.3    de Gier, J.W.4
  • 50
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • doi:10.1038/nmeth0406-303
    • Drew D, Lerch M, Kunji E, Slotboom DJ, de Gier JW, (2006) Optimization of membrane protein overexpression and purification using GFP fusions. Nat Methods 3: 303-313. doi:10.1038/nmeth0406-303. PubMed: 16554836.
    • (2006) Nat Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    de Gier, J.W.5
  • 51
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • doi:10.1038/nprot.2008.44
    • Drew D, Newstead S, Sonoda Y, Kim H, von Heijne G, et al. (2008) GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat Protoc 3: 784-798. doi:10.1038/nprot.2008.44. PubMed: 18451787.
    • (2008) Nat Protoc , vol.3 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    von Heijne, G.5
  • 52
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • doi:10.1016/j.str.2006.01.013
    • Kawate T, Gouaux E, (2006) Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14: 673-681. doi:10.1016/j.str.2006.01.013. PubMed: 16615909.
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 53
    • 84864853832 scopus 로고    scopus 로고
    • A fluorescence-detection size-exclusion chromatography-based thermostability assay for membrane protein precrystallization screening
    • doi:10.1016/j.str.2012.06.009
    • Hattori M, Hibbs RE, Gouaux E, (2012) A fluorescence-detection size-exclusion chromatography-based thermostability assay for membrane protein precrystallization screening. Structure 20: 1293-1299. doi:10.1016/j.str.2012.06.009. PubMed: 22884106.
    • (2012) Structure , vol.20 , pp. 1293-1299
    • Hattori, M.1    Hibbs, R.E.2    Gouaux, E.3
  • 54
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • doi:10.1128/JB.182.14.4068-4076.2000
    • Feilmeier BJ, Iseminger G, Schroeder D, Webber H, Phillips GJ, (2000) Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J Bacteriol 182: 4068-4076. doi:10.1128/JB.182.14.4068-4076.2000. PubMed: 10869087.
    • (2000) J Bacteriol , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 55
    • 58149478359 scopus 로고    scopus 로고
    • A green fluorescent protein screen for identification of well-expressed membrane proteins from a cohort of extremophilic organisms
    • Hammon J, Palanivelu DV, Chen J, Patel C, Minor DL Jr., (2009) A green fluorescent protein screen for identification of well-expressed membrane proteins from a cohort of extremophilic organisms. Protein Sci 18: 121-133. PubMed: 19177357.
    • (2009) Protein Sci , vol.18 , pp. 121-133
    • Hammon, J.1    Palanivelu, D.V.2    Chen, J.3    Patel, C.4    Minor Jr., D.L.5
  • 56
    • 54249167046 scopus 로고    scopus 로고
    • Production and characterization of a high-affinity nanobody against human endoglin
    • doi:10.1089/hyb.2008.0014
    • Ahmadvand D, Rasaee MJ, Rahbarizadeh F, Mohammadi M, (2008) Production and characterization of a high-affinity nanobody against human endoglin. Hybridoma (Larchmt) 27: 353-360. doi:10.1089/hyb.2008.0014. PubMed: 18847348.
    • (2008) Hybridoma (Larchmt) , vol.27 , pp. 353-360
    • Ahmadvand, D.1    Rasaee, M.J.2    Rahbarizadeh, F.3    Mohammadi, M.4
  • 57
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • doi:10.1038/nature10737
    • Krishnamurthy H, Gouaux E, (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481: 469-474. doi:10.1038/nature10737. PubMed: 22230955.
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 58
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • doi:10.1016/S0005-2736(02)00717-4
    • Kiefer H, (2003) In vitro folding of alpha-helical membrane proteins. Biochim Biophys Acta 1610: 57-62. doi:10.1016/S0005-2736(02)00717-4. PubMed: 12586380.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 59
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: not just a soap opera
    • doi:10.1016/j.bbamem.2004.04.011
    • Seddon AM, Curnow P, Booth PJ, (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochim Biophys Acta 1666: 105-117. doi:10.1016/j.bbamem.2004.04.011. PubMed: 15519311.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 60
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • doi:10.1073/pnas.94.20.10547
    • Ostermeier C, Harrenga A, Ermler U, Michel H, (1997) Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc Natl Acad Sci U S A 94: 10547-10553. doi:10.1073/pnas.94.20.10547. PubMed: 9380672.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 61
    • 0037022594 scopus 로고    scopus 로고
    • Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c
    • doi:10.1073/pnas.052704699
    • Lange C, Hunte C, (2002) Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Proc Natl Acad Sci U S A 99: 2800-2805. doi:10.1073/pnas.052704699. PubMed: 11880631.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 62
    • 27344442574 scopus 로고    scopus 로고
    • Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane
    • doi:10.1073/pnas.0507651102
    • Lee SY, Lee A, Chen J, MacKinnon R, (2005) Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc Natl Acad Sci U S A 102: 15441-15446. doi:10.1073/pnas.0507651102. PubMed: 16223877.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15441-15446
    • Lee, S.Y.1    Lee, A.2    Chen, J.3    MacKinnon, R.4
  • 63
    • 79954422505 scopus 로고    scopus 로고
    • Designed ankyrin repeat protein binders for the crystallization of AcrB: plasticity of the dominant interface
    • doi:10.1016/j.jsb.2011.01.014
    • Monroe N, Sennhauser G, Seeger MA, Briand C, Grütter MG, (2011) Designed ankyrin repeat protein binders for the crystallization of AcrB: plasticity of the dominant interface. J Struct Biol 174: 269-281. doi:10.1016/j.jsb.2011.01.014. PubMed: 21296164.
    • (2011) J Struct Biol , vol.174 , pp. 269-281
    • Monroe, N.1    Sennhauser, G.2    Seeger, M.A.3    Briand, C.4    Grütter, M.G.5
  • 64
    • 84873431135 scopus 로고    scopus 로고
    • Structures of a Na+-coupled, substrate-bound MATE multidrug transporter
    • doi:10.1073/pnas.1219901110
    • Lu M, Symersky J, Radchenko M, Koide A, Guo Y, et al. (2013) Structures of a Na+-coupled, substrate-bound MATE multidrug transporter. Proc Natl Acad Sci U S A 110: 2099-2104. doi:10.1073/pnas.1219901110. PubMed: 23341609.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 2099-2104
    • Lu, M.1    Symersky, J.2    Radchenko, M.3    Koide, A.4    Guo, Y.5
  • 65
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • doi:10.1093/nar/gkn238
    • Cole C, Barber JD, Barton GJ, (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36: W197-W201. doi:10.1093/nar/gkn238. PubMed: 18463136.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 66
    • 84886918513 scopus 로고    scopus 로고
    • SIAS, Available
    • SIAS. Available: http://imed.med.ucm.es/Tools/sias.html. Accessed 2013 September 17.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.