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Volumn 4, Issue DECEMBER2015, 2015, Pages

Nanobodies: Site-specific labeling for super-resolution imaging, rapid epitope- mapping and native protein complex isolation

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GREEN FLUORESCENT PROTEIN; MALTOSE BINDING PROTEIN; NANOBODY; MACROMOLECULE; NUCLEOPORIN;

EID: 84956906213     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.11349     Document Type: Article
Times cited : (164)

References (90)
  • 2
    • 79960766105 scopus 로고    scopus 로고
    • Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile
    • Amlacher S, Sarges P, Flemming D, van Noort V, Kunze R, Devos DP, Arumugam M, Bork P, Hurt E. 2011. Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile. Cell 146:277–289. doi: 10.1016/j.cell.2011.06.039.
    • (2011) Cell , vol.146 , pp. 277-289
    • Amlacher, S.1    Sarges, P.2    Flemming, D.3    Van Noort, V.4    Kunze, R.5    Devos, D.P.6    Arumugam, M.7    Bork, P.8    Hurt, E.9
  • 4
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Arbabi Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S. 1997. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Letters 414:521–526. doi: 10.1016/S0014-5793(97)01062-4.
    • (1997) FEBS Letters , vol.414 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 5
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in escherichia coli
    • Baneyx F, Mujacic M. 2004. Recombinant protein folding and misfolding in escherichia coli. Nature Biotechnology 22:1399–1408. doi: 10.1038/nbt1029.
    • (2004) Nature Biotechnology , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 6
    • 34648826792 scopus 로고    scopus 로고
    • Multicolor super-resolution imaging with photo-switchable fluorescent probes
    • Bates M, Huang B, Dempsey GT, Zhuang X. 2007. Multicolor super-resolution imaging with photo-switchable fluorescent probes. Science 317:1749–1753. doi: 10.1126/science.1146598.
    • (2007) Science , vol.317 , pp. 1749-1753
    • Bates, M.1    Huang, B.2    Dempsey, G.T.3    Zhuang, X.4
  • 7
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D, Kovaleva E, Schatz PJ. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Science 8:921–929. doi: 10.1110/ps.8.4.921.
    • (1999) Protein Science , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 8
    • 0022981734 scopus 로고
    • Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of xenopus eggs
    • Blow JJ, Laskey RA. 1986. Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of xenopus eggs. Cell 47:577–587. doi: 10.1016/0092-8674(86)90622-7.
    • (1986) Cell , vol.47 , pp. 577-587
    • Blow, J.J.1    Laskey, R.A.2
  • 11
    • 34248663955 scopus 로고    scopus 로고
    • The single-step method of RNA isolation by acid guanidinium thiocyanate– phenol–chloroform extraction: Twenty-something years on
    • Chomczynski P, Sacchi N. 2006. The single-step method of RNA isolation by acid guanidinium thiocyanate– phenol–chloroform extraction: Twenty-something years on. Nature Protocols 1:581–585. doi: 10.1038/nprot.2006.83.
    • (2006) Nature Protocols , vol.1 , pp. 581-585
    • Chomczynski, P.1    Sacchi, N.2
  • 13
    • 84946235454 scopus 로고    scopus 로고
    • Nup62.Nup58.Nup54 nucleoporin complex
    • Nup62.Nup58.Nup54 nucleoporin complex. Science 350:106–110. doi: 10.1126/science.aac7420.
    • Science , vol.350 , pp. 106-110
  • 14
    • 79959851876 scopus 로고    scopus 로고
    • A roadmap to generate renewable protein binders to the human proteome
    • Colwill, K., Gräslund, S. 2011. A roadmap to generate renewable protein binders to the human proteome. Nature Methods 8:551–558. doi: 10.1038/nmeth.1607.
    • (2011) Nature Methods , vol.8 , pp. 551-558
    • Colwill, K.1    Gräslund, S.2
  • 16
    • 66949126546 scopus 로고    scopus 로고
    • Strategies for successful recombinant expression of disulfide bond-dependent proteins in escherichia coli
    • De Marco A. 2009. Strategies for successful recombinant expression of disulfide bond-dependent proteins in escherichia coli. Microbial Cell Factories 8:26. doi: 10.1186/1475-2859-8-26.
    • (2009) Microbial Cell Factories , vol.8 , pp. 26
    • De Marco, A.1
  • 17
    • 82355191588 scopus 로고    scopus 로고
    • Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging
    • Dempsey GT, Vaughan JC, Chen KH, Bates M, Zhuang X. 2011. Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging. Nature Methods 8:1027–1036. doi: 10.1038/nmeth.1768.
    • (2011) Nature Methods , vol.8 , pp. 1027-1036
    • Dempsey, G.T.1    Vaughan, J.C.2    Chen, K.H.3    Bates, M.4    Zhuang, X.5
  • 19
    • 84908130853 scopus 로고    scopus 로고
    • Bacterial cytoplasm as an effective cell compartment for producing functional VHH-based affinity reagents and camelidae IgG-like recombinant antibodies
    • Djender S, Schneider A, Beugnet A, Crepin R, Desrumeaux KE, Romani C, Moutel S, Perez F, de Marco A. 2014. Bacterial cytoplasm as an effective cell compartment for producing functional VHH-based affinity reagents and camelidae IgG-like recombinant antibodies. Microbial Cell Factories 13. doi: 10.1186/s12934-014-0140-1.
    • (2014) Microbial Cell Factories , pp. 13
    • Djender, S.1    Schneider, A.2    Beugnet, A.3    Crepin, R.4    Desrumeaux, K.E.5    Romani, C.6    Moutel, S.7    Perez, F.8    De Marco, A.9
  • 20
    • 0027418576 scopus 로고
    • The portal protein of bacteriophage SPP1: A DNA pump with 13- fold symmetry
    • Dube P, Tavares P, Lurz R, van Heel M. 1993. The portal protein of bacteriophage SPP1: A DNA pump with 13- fold symmetry. The EMBO Journal 12:1303–1309.
    • (1993) The EMBO Journal , vol.12 , pp. 1303-1309
    • Dube, P.1    Tavares, P.2    Lurz, R.3    Van Heel, M.4
  • 22
    • 84894037012 scopus 로고    scopus 로고
    • Interaction of Nup53 with Ndc1 and Nup155 is required for nuclear pore complex assembly
    • Eisenhardt N, Redolfi J, Antonin W. 2014. Interaction of Nup53 with Ndc1 and Nup155 is required for nuclear pore complex assembly. Journal of Cell Science 127:908–921. doi: 10.1242/jcs.141739.
    • (2014) Journal of Cell Science , vol.127 , pp. 908-921
    • Eisenhardt, N.1    Redolfi, J.2    Antonin, W.3
  • 23
    • 0022311470 scopus 로고
    • Developmental changes in keratin patterns during epidermal maturation
    • Ellison TR, Mathisen PM, Miller L. 1985. Developmental changes in keratin patterns during epidermal maturation. Developmental Biology 112:329–337. doi: 10.1016/0012-1606(85)90403-8.
    • (1985) Developmental Biology , vol.112 , pp. 329-337
    • Ellison, T.R.1    Mathisen, P.M.2    Miller, L.3
  • 24
    • 84921810953 scopus 로고    scopus 로고
    • Site-specific biotinylation of purified proteins using BirA
    • Fairhead M, Howarth M. 2015. Site-specific biotinylation of purified proteins using BirA. Methods in Molecular Biology 1266:171–184. doi: 10.1007/978-1-4939-2272-7_12.
    • (2015) Methods in Molecular Biology , vol.1266 , pp. 171-184
    • Fairhead, M.1    Howarth, M.2
  • 25
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in escherichia coli
    • Feilmeier BJ, Iseminger G, Schroeder D, Webber H, Phillips GJ. 2000. Green fluorescent protein functions as a reporter for protein localization in escherichia coli. Journal of Bacteriology 182:4068–4076. doi: 10.1128/JB.182.14.4068-4076.2000.
    • (2000) Journal of Bacteriology , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 26
    • 0025939317 scopus 로고
    • A complex of nuclear pore proteins required for pore function
    • Finlay DR. 1991. A complex of nuclear pore proteins required for pore function. The Journal of Cell Biology 114: 169–183. doi: 10.1083/jcb.114.1.169.
    • (1991) The Journal of Cell Biology , vol.114 , pp. 169-183
    • Finlay, D.R.1
  • 27
    • 84900598505 scopus 로고    scopus 로고
    • A new set of highly efficient, tag-cleaving proteases for purifying recombinant proteins
    • Frey S, Görlich D. 2014. A new set of highly efficient, tag-cleaving proteases for purifying recombinant proteins. Journal of Chromatography A 1337:95–105. doi: 10.1016/j.chroma.2014.02.029.
    • Journal of Chromatography A , pp. 95-105
    • Frey, S.1    2014, G.2
  • 29
    • 84926140423 scopus 로고    scopus 로고
    • Engineered high-affinity nanobodies recognizing staphylococcal protein a and suitable for native isolation of protein complexes
    • Fridy PC, Thompson MK, Ketaren NE, Rout MP. 2015. Engineered high-affinity nanobodies recognizing staphylococcal protein a and suitable for native isolation of protein complexes. Analytical Biochemistry 477:92–94. doi: 10.1016/j.ab.2015.02.013.
    • (2015) Analytical Biochemistry , vol.477 , pp. 92-94
    • Fridy, P.C.1    Thompson, M.K.2    Ketaren, N.E.3    Rout, M.P.4
  • 31
    • 0037323478 scopus 로고    scopus 로고
    • Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes
    • Griffis ER. 2003. Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes. Molecular Biology of the Cell 14:600–610. doi: 10.1091/mbc.E02-09-0582.
    • (2003) Molecular Biology of the Cell , vol.14 , pp. 600-610
    • Griffis, E.R.1
  • 35
    • 0032488888 scopus 로고    scopus 로고
    • Crystallographic structure of an intact IgG1 monoclonal antibody
    • Harris LJ, Skaletsky E, McPherson A. 1998. Crystallographic structure of an intact IgG1 monoclonal antibody. Journal of Molecular Biology 275:861–872. doi: 10.1006/jmbi.1997.1508.
    • (1998) Journal of Molecular Biology , vol.275 , pp. 861-872
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 36
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex
    • Hawryluk-Gara LA. 2005. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Molecular Biology of the Cell 16:2382–2394. doi: 10.1091/mbc.E04-10-0857.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 2382-2394
    • Hawryluk-Gara, L.A.1
  • 38
    • 58149236663 scopus 로고    scopus 로고
    • Microscopy and its focal switch
    • Hell SW. 2009. Microscopy and its focal switch. Nature Methods 6:24–32. doi: 10.1038/nmeth.1291.
    • (2009) Nature Methods , vol.6 , pp. 24-32
    • Hell, S.W.1
  • 40
    • 0036672039 scopus 로고    scopus 로고
    • The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98
    • Hodel AE, Hodel MR, Griffis ER, Hennig KA, Ratner GA, Xu S, Powers MA. 2002. The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98. Molecular Cell 10:347–358. doi: 10.1016/S1097-2765(02)00589-0.
    • (2002) Molecular Cell , vol.10 , pp. 347-358
    • Hodel, A.E.1    Hodel, M.R.2    Griffis, E.R.3    Hennig, K.A.4    Ratner, G.A.5    Xu, S.6    Powers, M.A.7
  • 41
    • 0029767680 scopus 로고    scopus 로고
    • Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins
    • Hu T. 1996. Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. The Journal of Cell Biology 134:589–601. doi: 10.1083/jcb.134.3.589.
    • (1996) The Journal of Cell Biology , vol.134 , pp. 589-601
    • Hu, T.1
  • 42
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • Huang B, Bates M, Zhuang X. 2009. Super-resolution fluorescence microscopy. Annual Review of Biochemistry 78:993–1016. doi: 10.1146/annurev.biochem.77.061906.092014.
    • (2009) Annual Review of Biochemistry , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 43
    • 84928783218 scopus 로고    scopus 로고
    • Towards understanding nuclear pore complex architecture and dynamics in the age of integrative structural analysis
    • Hurt E, Beck M. 2015. Towards understanding nuclear pore complex architecture and dynamics in the age of integrative structural analysis. Current Opinion in Cell Biology 34:31–38. doi: 10.1016/j.ceb.2015.04.009.
    • (2015) Current Opinion in Cell Biology , vol.34 , pp. 31-38
    • Hurt, E.1    Beck, M.2
  • 44
    • 84865260520 scopus 로고    scopus 로고
    • The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model
    • Hu¨ lsmann BB, Labokha AA, Go¨ rlich D. 2012. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150:738–751. doi: 10.1016/j.cell.2012.07.019.
    • (2012) Cell , vol.150 , pp. 738-751
    • Lsmann, H.1    Bb, L.A.2    Rlich, G.3
  • 45
    • 36849079742 scopus 로고    scopus 로고
    • Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture
    • Jeudy S, Schwartz TU. 2007. Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture. Journal of Biological Chemistry 282:34904–34912. doi: 10.1074/jbc.M705479200.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 34904-34912
    • Jeudy, S.1    Schwartz, T.U.2
  • 49
    • 53149112694 scopus 로고    scopus 로고
    • Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions
    • Liu L, Spurrier J, Butt TR, Strickler JE. 2008. Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions. Protein Expression and Purification 62:21–28. doi: 10.1016/j.pep.2008.07.010.
    • (2008) Protein Expression and Purification , vol.62 , pp. 21-28
    • Liu, L.1    Spurrier, J.2    Butt, T.R.3    Strickler, J.E.4
  • 50
    • 84860601037 scopus 로고    scopus 로고
    • SHuffle, a novel escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm
    • Lobstein J, Emrich CA, Jeans C, Faulkner M, Riggs P, Berkmen M. 2012. SHuffle, a novel escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm. Microbial Cell Factories 11:56. doi: 10.1186/1475-2859-11-56.
    • (2012) Microbial Cell Factories , vol.11 , pp. 56
    • Lobstein, J.1    Emrich, C.A.2    Jeans, C.3    Faulkner, M.4    Riggs, P.5    Berkmen, M.6
  • 51
    • 84858110907 scopus 로고    scopus 로고
    • Super- resolution imaging visualizes the eightfold symmetry of gp210 proteins around the nuclear pore complex and resolves the central channel with nanometer resolution
    • Löschberger A, van de Linde S, Dabauvalle MC, Rieger B, Heilemann M, Krohne G, Sauer M. 2012. Super- resolution imaging visualizes the eightfold symmetry of gp210 proteins around the nuclear pore complex and resolves the central channel with nanometer resolution. Journal of Cell Science 125:570–575. doi: 10.1242/jcs.098822.
    • (2012) Journal of Cell Science , vol.125 , pp. 570-575
    • Löschberger, A.1    Van De Linde, S.2    Dabauvalle, M.C.3    Rieger, B.4    Heilemann, M.5    Krohne, G.6    Sauer, M.7
  • 52
    • 34347248421 scopus 로고    scopus 로고
    • Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (vHHs)
    • Maass DR, Sepulveda J, Pernthaner A, Shoemaker CB. 2007. Alpaca (lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (vHHs). Journal of Immunological Methods 324:13–25. doi: 10.1016/j.jim.2007.04.008.
    • (2007) Journal of Immunological Methods , vol.324 , pp. 13-25
    • Maass, D.R.1    Sepulveda, J.2    Pernthaner, A.3    Shoemaker, C.B.4
  • 54
    • 84900991913 scopus 로고    scopus 로고
    • Site-specific labeling of cysteine-tagged camelid single-domain antibody-fragments for use in molecular imaging
    • Massa S, Xavier C, De Vos J, Caveliers V, Lahoutte T, Muyldermans S, Devoogdt N. 2014. Site-specific labeling of cysteine-tagged camelid single-domain antibody-fragments for use in molecular imaging. Bioconjugate Chemistry 25:979–988. doi: 10.1021/bc500111t.
    • (2014) Bioconjugate Chemistry , vol.25 , pp. 979-988
    • Massa, S.1    Xavier, C.2    De Vos, J.3    Caveliers, V.4    Lahoutte, T.5    Muyldermans, S.6    Devoogdt, N.7
  • 56
    • 0017745455 scopus 로고
    • Comparison of in vivo and in vitro ribosomal RNA synthesis in nucleolar mutants ofXenopus laevis
    • Miller L, Daniel JC. 1977. Comparison of in vivo and in vitro ribosomal RNA synthesis in nucleolar mutants ofXenopus laevis. In Vitro 13:557–563. doi: 10.1007/BF02627851.
    • (1977) Vitro , vol.13 , pp. 557-563
    • Miller, L.1    Daniel, J.C.2
  • 57
    • 78049508819 scopus 로고    scopus 로고
    • Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane
    • Mitchell JM, Mansfeld J, Capitanio J, Kutay U, Wozniak RW. 2010. Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane. The Journal of Cell Biology 191:505–521. doi: 10.1083/jcb.201007098.
    • (2010) The Journal of Cell Biology , vol.191 , pp. 505-521
    • Mitchell, J.M.1    Mansfeld, J.2    Capitanio, J.3    Kutay, U.4    Wozniak, R.W.5
  • 58
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: Natural single-domain antibodies
    • Muyldermans S. 2013. Nanobodies: Natural single-domain antibodies. Annual Review of Biochemistry 82:775–797. doi: 10.1146/annurev-biochem-063011-092449.
    • (2013) Annual Review of Biochemistry , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 59
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. 2007. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nature Protocols 2:2212–2221. doi: 10.1038/nprot.2007.321.
    • (2007) Nature Protocols , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 60
    • 37549005602 scopus 로고    scopus 로고
    • Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in escherichia coli
    • Olichon A, Surrey T. 2007. Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in escherichia coli. Journal of Biological Chemistry 282:36314–36320. doi: 10.1074/jbc.M704908200.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 36314-36320
    • Olichon, A.1    Surrey, T.2
  • 62
    • 84959488694 scopus 로고    scopus 로고
    • Single-molecule microscopy of molecules tagged with GFP or RFP derivatives in mammalian cells using nanobody binders
    • Platonova E, Winterflood CM, Junemann A, Albrecht D, Faix J, Ewers H. 2015. Single-molecule microscopy of molecules tagged with GFP or RFP derivatives in mammalian cells using nanobody binders. Methods 88. doi: 10.1016/j.ymeth.2015.06.018.
    • (2015) Methods , pp. 88
    • Platonova, E.1    Winterflood, C.M.2    Junemann, A.3    Albrecht, D.4    Faix, J.5    Ewers, H.6
  • 63
    • 84861979783 scopus 로고    scopus 로고
    • A simple, versatile method for GFP-based super-resolution microscopy via nanobodies
    • Ries J, Kaplan C, Platonova E, Eghlidi H, Ewers H. 2012. A simple, versatile method for GFP-based super-resolution microscopy via nanobodies. Nature Methods 9:582–584. doi: 10.1038/nmeth.1991.
    • (2012) Nature Methods , vol.9 , pp. 582-584
    • Ries, J.1    Kaplan, C.2    Platonova, E.3    Eghlidi, H.4    Ewers, H.5
  • 66
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust MJ, Bates M, Zhuang X. 2006. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (sTORM). Nature Methods 3:793–796. doi: 10.1038/nmeth929.
    • (2006) Nature Methods , vol.3 , pp. 793-796
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 67
    • 84857217101 scopus 로고    scopus 로고
    • The c-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes
    • Sachdev R, Sieverding C, Flotenmeyer M, Antonin W. 2012. The c-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes. Molecular Biology of the Cell 23:740–749. doi: 10.1091/mbc.E11-09-0761.
    • (2012) Molecular Biology of the Cell , vol.23 , pp. 740-749
    • Sachdev, R.1    Sieverding, C.2    Flotenmeyer, M.3    Antonin, W.4
  • 68
    • 0038016841 scopus 로고    scopus 로고
    • Automatic CTF correction for single particles based upon multivariate statistical analysis of individual power spectra
    • Sander B, Golas MM, Stark H. 2003. Automatic CTF correction for single particles based upon multivariate statistical analysis of individual power spectra. Journal of Structural Biology 142:392–401. doi: 10.1016/S1047-8477(03)00072-8.
    • (2003) Journal of Structural Biology , vol.142 , pp. 392-401
    • Sander, B.1    Golas, M.M.2    Stark, H.3
  • 69
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in escherichia coli
    • Schatz PJ. 1993. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in escherichia coli. Bio/Technology 11:1138–1143. doi: 10.1038/nbt1093-1138.
    • (1993) Bio/Technology , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 71
    • 70349759984 scopus 로고    scopus 로고
    • ITRAQ-labeling of in-gel digested proteins for relative quantification
    • Schmidt C, Urlaub H. 2009. ITRAQ-labeling of in-gel digested proteins for relative quantification. Methods in Molecular Biology 564:207–226. doi: 10.1007/978-1-60761-157-8_12.
    • (2009) Methods in Molecular Biology , vol.564 , pp. 207-226
    • Schmidt, C.1    Urlaub, H.2
  • 72
    • 84879823647 scopus 로고    scopus 로고
    • Structural evaluation of EGFR inhibition mechanisms for Nanobodies/VHH domains
    • Schmitz KR, Bagchi A, Roovers RC, van Bergen en Henegouwen PMP, Ferguson KM. 2013. Structural evaluation of EGFR inhibition mechanisms for Nanobodies/VHH domains. Structure 21:1214–1224. doi: 10.1016/j.str.2013.05.008.
    • (2013) Structure , vol.21 , pp. 1214-1224
    • Schmitz, K.R.1    Bagchi, A.2    Roovers, R.C.3
  • 73
    • 38149118681 scopus 로고    scopus 로고
    • Structural basis of the Nic96 subcomplex organization in the nuclear pore channel
    • Schrader N, Stelter P, Flemming D, Kunze R, Hurt E, Vetter IR. 2008. Structural basis of the Nic96 subcomplex organization in the nuclear pore channel. Molecular Cell 29:46–55. doi: 10.1016/j.molcel.2007.10.022.
    • (2008) Molecular Cell , vol.29 , pp. 46-55
    • Schrader, N.1    Stelter, P.2    Flemming, D.3    Kunze, R.4    Hurt, E.5    Vetter, I.R.6
  • 74
    • 0034599816 scopus 로고    scopus 로고
    • Structure and assembly of the Nup84p complex
    • Siniossoglou S. 2000. Structure and assembly of the Nup84p complex. The Journal of Cell Biology 149:41–54. doi: 10.1083/jcb.149.1.41.
    • (2000) The Journal of Cell Biology , vol.149 , pp. 41-54
    • Siniossoglou, S.1
  • 75
    • 84861529586 scopus 로고    scopus 로고
    • Molecular basis for the anchoring of proto- oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex
    • Stuwe T, Schada von Borzyskowski L, Davenport AM, Hoelz A. 2012. Molecular basis for the anchoring of proto- oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex. Journal of Molecular Biology 419: 330–346. doi: 10.1016/j.jmb.2012.03.024.
    • (2012) Journal of Molecular Biology , vol.419 , pp. 330-346
    • Stuwe, T.1    Von Schada Borzyskowski, L.2    Davenport, A.M.3    Hoelz, A.4
  • 78
    • 84881241505 scopus 로고    scopus 로고
    • Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging
    • Szymborska A, de Marco A, Daigle N, Cordes VC, Briggs JAG, Ellenberg J. 2013. Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging. Science 341:655–658. doi: 10.1126/science.1240672.
    • (2013) Science , vol.341 , pp. 655-658
    • Szymborska, A.1    De Marco, A.2    Daigle, N.3    Cordes, V.C.4    Briggs, J.5    Ellenberg, J.6
  • 79
    • 77954388089 scopus 로고    scopus 로고
    • The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex
    • Theerthagiri G, Eisenhardt N, Schwarz H, Antonin W. 2010. The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex. The Journal of Cell Biology 189:1129–1142. doi: 10.1083/jcb.200912045.
    • (2010) The Journal of Cell Biology , vol.189 , pp. 1129-1142
    • Theerthagiri, G.1    Eisenhardt, N.2    Schwarz, H.3    Antonin, W.4
  • 81
    • 0035851914 scopus 로고    scopus 로고
    • Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export
    • Vasu S. 2001. Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. The Journal of Cell Biology 155:339–354. doi: 10.1083/jcb.200108007.
    • (2001) The Journal of Cell Biology , vol.155 , pp. 339-354
    • Vasu, S.1
  • 83
    • 84900845312 scopus 로고    scopus 로고
    • The diverse roles of the Nup93/Nic96 complex proteins – structural scaffolds of the nuclear pore complex with additional cellular functions
    • Vollmer B, Antonin W. 2014. The diverse roles of the Nup93/Nic96 complex proteins – structural scaffolds of the nuclear pore complex with additional cellular functions. Biological Chemistry 395:515–528. doi: 10.1515/hsz-2013-0285.
    • (2014) Biological Chemistry , vol.395 , pp. 515-528
    • Vollmer, B.1    Antonin, W.2
  • 89
    • 84886153348 scopus 로고    scopus 로고
    • High-yield production of functional soluble single-domain antibodies in the cytoplasm of escherichia coli
    • Zarschler K, Witecy S, Kapplusch F, Foerster C, Stephan H. 2013. High-yield production of functional soluble single-domain antibodies in the cytoplasm of escherichia coli. Microbial Cell Factories 12:97. doi: 10.1186/1475-2859-12-97.
    • (2013) Microbial Cell Factories , vol.12 , pp. 97
    • Zarschler, K.1    Witecy, S.2    Kapplusch, F.3    Foerster, C.4    Stephan, H.5
  • 90
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. 2008. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. doi: 10.1186/1471-2105-9-40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1


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