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Volumn 185, Issue 3, 2014, Pages 405-417

Chemically functionalized carbon films for single molecule imaging

Author keywords

Biological ligands; C3PO RNA complex; Carbon films; ChemiC; Chemical functionalization; Single particle cryoEM

Indexed keywords

BIOLOGICAL LIGANDS; C3PO/RNA COMPLEX; CARBON FILMS; CHEMIC; CHEMICAL FUNCTIONALIZATION; SINGLE PARTICLE CRYOEM;

EID: 84894427376     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2014.01.006     Document Type: Article
Times cited : (32)

References (42)
  • 2
    • 33847755972 scopus 로고    scopus 로고
    • Purification, cutting, and sidewall functionalization of multiwalled carbon nanotubes using potassium permanganate solutions
    • Aitchison T.J., Ginic-Markovic M., Matisons J.G., Simon G.P., Fredericks P.M. Purification, cutting, and sidewall functionalization of multiwalled carbon nanotubes using potassium permanganate solutions. J. Phys. Chem. C 2007, 111:2440-2446.
    • (2007) J. Phys. Chem. C , vol.111 , pp. 2440-2446
    • Aitchison, T.J.1    Ginic-Markovic, M.2    Matisons, J.G.3    Simon, G.P.4    Fredericks, P.M.5
  • 5
    • 0031257718 scopus 로고    scopus 로고
    • A method for establishing the handedness of biological macromolecules
    • Belnap D.M., Olson N.H., Baker T.S. A method for establishing the handedness of biological macromolecules. J. Struct. Biol. 1997, 120:44-51.
    • (1997) J. Struct. Biol. , vol.120 , pp. 44-51
    • Belnap, D.M.1    Olson, N.H.2    Baker, T.S.3
  • 8
    • 80054033858 scopus 로고    scopus 로고
    • Transfer-printing of single dna molecule arrays on graphene for high-resolution electron imaging and analysis
    • Cerf A., Alava T., Barton R.A., Craighead H.G. Transfer-printing of single dna molecule arrays on graphene for high-resolution electron imaging and analysis. Nano Lett. 2011, 11:4232-4238.
    • (2011) Nano Lett. , vol.11 , pp. 4232-4238
    • Cerf, A.1    Alava, T.2    Barton, R.A.3    Craighead, H.G.4
  • 9
    • 46549085153 scopus 로고    scopus 로고
    • A "tagless" strategy for identification of stable protein complexes genome-wide by multidimensional orthogonal chromatographic separation and iTRAQ reagent tracking
    • Dong M., Yang L.L., Williams K., Fisher S.J., Hall S.C., Biggin M.D., Jin J., Witkowska H.E. A "tagless" strategy for identification of stable protein complexes genome-wide by multidimensional orthogonal chromatographic separation and iTRAQ reagent tracking. J. Proteome Res. 2008, 7:1836-1849.
    • (2008) J. Proteome Res. , vol.7 , pp. 1836-1849
    • Dong, M.1    Yang, L.L.2    Williams, K.3    Fisher, S.J.4    Hall, S.C.5    Biggin, M.D.6    Jin, J.7    Witkowska, H.E.8
  • 13
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 14
    • 0036009139 scopus 로고    scopus 로고
    • Micropattern formation in supported lipid membranes
    • Groves J.T., Boxer S.G. Micropattern formation in supported lipid membranes. Acc. Chem. Res. 2002, 35:149-157.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 149-157
    • Groves, J.T.1    Boxer, S.G.2
  • 15
    • 0035221240 scopus 로고    scopus 로고
    • Protein microarrays for highly parallel detection and quantitation of specific proteins and antibodies in complex solutions
    • Haab B.B., Dunham M.J., Brown P.O. Protein microarrays for highly parallel detection and quantitation of specific proteins and antibodies in complex solutions. Genome Biol. 2001, 2.
    • (2001) Genome Biol. , vol.2
    • Haab, B.B.1    Dunham, M.J.2    Brown, P.O.3
  • 18
    • 70349140553 scopus 로고    scopus 로고
    • Tris-nitrilotriacetic acids of subnanomolar affinity toward hexahistidine tagged molecules
    • Huang Z., Hwang P., Watson D.S., Cao L., Szoka F.C. Tris-nitrilotriacetic acids of subnanomolar affinity toward hexahistidine tagged molecules. Bioconjug. Chem. 2009, 20:1667-1672.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1667-1672
    • Huang, Z.1    Hwang, P.2    Watson, D.S.3    Cao, L.4    Szoka, F.C.5
  • 20
    • 4043151338 scopus 로고    scopus 로고
    • Electron microscopic analysis of KvAP voltage-dependent K+ channels in an open conformation
    • Jiang Q.X., Wang D.N., MacKinnon R. Electron microscopic analysis of KvAP voltage-dependent K+ channels in an open conformation. Nature 2004, 430(7001):806-810.
    • (2004) Nature , vol.430 , Issue.7001 , pp. 806-810
    • Jiang, Q.X.1    Wang, D.N.2    MacKinnon, R.3
  • 21
    • 42449146663 scopus 로고    scopus 로고
    • Monolayer purification: a rapid method for isolating protein complexes for single-particle electron microscopy
    • Kelly D.F., Dukovski D., Walz T. Monolayer purification: a rapid method for isolating protein complexes for single-particle electron microscopy. Proc. Natl. Acad. Sci. USA 2008, 105:4703-4708.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4703-4708
    • Kelly, D.F.1    Dukovski, D.2    Walz, T.3
  • 22
    • 77954384708 scopus 로고    scopus 로고
    • Strategy for the use of affinity grids to prepare non-his-tagged macromolecular complexes for single-particle electron microscopy
    • Kelly D.F., Dukovski D., Walz T. Strategy for the use of affinity grids to prepare non-his-tagged macromolecular complexes for single-particle electron microscopy. J. Mol. Biol. 2010, 400:675-681.
    • (2010) J. Mol. Biol. , vol.400 , pp. 675-681
    • Kelly, D.F.1    Dukovski, D.2    Walz, T.3
  • 23
    • 77953635299 scopus 로고    scopus 로고
    • Biochemical principles of small RNA pathways
    • Liu Q., Paroo Z. Biochemical principles of small RNA pathways. Annu. Rev. Biochem. 2010, 79:295-319.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 295-319
    • Liu, Q.1    Paroo, Z.2
  • 24
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 25
    • 28444437427 scopus 로고    scopus 로고
    • Slicer function of Drosophila Argonautes and its involvement in RISC formation
    • Miyoshi K., Tsukumo H., Nagami T., Siomi H., Siomi M.C. Slicer function of Drosophila Argonautes and its involvement in RISC formation. Genes Dev. 2005, 19:2837-2848.
    • (2005) Genes Dev. , vol.19 , pp. 2837-2848
    • Miyoshi, K.1    Tsukumo, H.2    Nagami, T.3    Siomi, H.4    Siomi, M.C.5
  • 26
    • 67049136583 scopus 로고    scopus 로고
    • Chemical vapour deposition: making graphene on a large scale
    • Obraztsov A.N. Chemical vapour deposition: making graphene on a large scale. Nat. Nanotechnol. 2009, 4:212-213.
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 212-213
    • Obraztsov, A.N.1
  • 27
    • 80054030401 scopus 로고    scopus 로고
    • Oxidative doping renders graphene hydrophilic, facilitating its use as a support in biological TEM
    • Pantelic R.S., Suk J.W., Hao Y.F., Ruoff R.S., Stahlberg H. Oxidative doping renders graphene hydrophilic, facilitating its use as a support in biological TEM. Nano Lett. 2011, 11:4319-4323.
    • (2011) Nano Lett. , vol.11 , pp. 4319-4323
    • Pantelic, R.S.1    Suk, J.W.2    Hao, Y.F.3    Ruoff, R.S.4    Stahlberg, H.5
  • 29
    • 84875217890 scopus 로고    scopus 로고
    • Structural basis for duplex RNA recognition and cleavage by Archaeoglobus fulgidus C3PO
    • Parizotto E.A., Lowe E.D., Parker J.S. Structural basis for duplex RNA recognition and cleavage by Archaeoglobus fulgidus C3PO. Nat. Struct. Mol. Biol. 2013, 20:380-386.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 380-386
    • Parizotto, E.A.1    Lowe, E.D.2    Parker, J.S.3
  • 30
    • 67049114637 scopus 로고    scopus 로고
    • Chemical methods for the production of graphenes
    • Park S., Ruoff R.S. Chemical methods for the production of graphenes. Nat. Nanotechnol. 2009, 4:217-224.
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 217-224
    • Park, S.1    Ruoff, R.S.2
  • 31
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P., Radermacher M., Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 1992, 40:33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 34
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush D.R., Maurice T., Roth D., Novick P. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 1996, 15:6483-6494.
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 37
    • 0021460767 scopus 로고
    • Protein diffusion coefficient measurements by laminar flow analysis: method and applications
    • Walters R.R., Graham J.F., Moore R.M., Anderson D.J. Protein diffusion coefficient measurements by laminar flow analysis: method and applications. Anal. Biochem. 1984, 140:190-195.
    • (1984) Anal. Biochem. , vol.140 , pp. 190-195
    • Walters, R.R.1    Graham, J.F.2    Moore, R.M.3    Anderson, D.J.4
  • 38
    • 53949089843 scopus 로고    scopus 로고
    • Streptavidin crystals as nanostructured supports and image-calibration references for cryo-EM data collection
    • Wang L., Ounjai P., Sigworth F.J. Streptavidin crystals as nanostructured supports and image-calibration references for cryo-EM data collection. J. Struct. Biol. 2008, 164:190-198.
    • (2008) J. Struct. Biol. , vol.164 , pp. 190-198
    • Wang, L.1    Ounjai, P.2    Sigworth, F.J.3
  • 41
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 Angstrom structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu X.K., Jin L., Zhou Z.H. 3.88 Angstrom structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 2008, 453:415-419.
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.K.1    Jin, L.2    Zhou, Z.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.