메뉴 건너뛰기




Volumn 111, Issue 2, 2014, Pages 670-674

Self-assembled lipid and membrane protein polyhedral nanoparticles

Author keywords

Electron microscopy; Membrane protein structure; Microfluidic devices; Proteoliposomes

Indexed keywords

CONNEXIN 26; MEMBRANE PROTEIN POLYHEDRAL NANOPARTICLE; NANOPARTICLE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 84892569345     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1321936111     Document Type: Article
Times cited : (19)

References (31)
  • 2
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • White SH (2004) The progress of membrane protein structure determination. Protein Sci 13(7):1948-1949.
    • (2004) Protein Sci , vol.13 , Issue.7 , pp. 1948-1949
    • White, S.H.1
  • 3
    • 0242574743 scopus 로고    scopus 로고
    • Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
    • Zhang W, et al. (2003) Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat Struct Biol 10(11):907-912.
    • (2003) Nat Struct Biol , vol.10 , Issue.11 , pp. 907-912
    • Zhang, W.1
  • 4
    • 8544236968 scopus 로고    scopus 로고
    • Membrane structure and interactions with protein and DNA in bacteriophage PRD1
    • Cockburn JJB, et al. (2004) Membrane structure and interactions with protein and DNA in bacteriophage PRD1. Nature 432(7013):122-125.
    • (2004) Nature , vol.432 , Issue.7013 , pp. 122-125
    • Cockburn, J.J.B.1
  • 5
    • 0035822093 scopus 로고    scopus 로고
    • Self-assembly of regular hollow icosahedra in salt-free catanionic solutions
    • Dubois M, et al. (2001) Self-assembly of regular hollow icosahedra in salt-free catanionic solutions. Nature 411(6838):672-675.
    • (2001) Nature , vol.411 , Issue.6838 , pp. 672-675
    • Dubois, M.1
  • 6
    • 6344225965 scopus 로고    scopus 로고
    • Shape control through molecular segregation in giant surfactant aggregates
    • Dubois M, et al. (2004) Shape control through molecular segregation in giant surfactant aggregates. Proc Natl Acad Sci USA 101(42):15082-15087.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.42 , pp. 15082-15087
    • Dubois, M.1
  • 7
    • 0032561127 scopus 로고    scopus 로고
    • A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
    • Takeda K, et al. (1998) A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J Mol Biol 283(2):463-474.
    • (1998) J Mol Biol , vol.283 , Issue.2 , pp. 463-474
    • Takeda, K.1
  • 8
    • 0031932860 scopus 로고    scopus 로고
    • Electron cryomicroscopy of bacteriorhodopsin vesicles: Mechanism of vesicle formation
    • Denkov ND, Yoshimura H, Kouyama T, Walz J, Nagayama K (1998) Electron cryomicroscopy of bacteriorhodopsin vesicles: Mechanism of vesicle formation. Biophys J 74(3):1409-1420.
    • (1998) Biophys J , vol.74 , Issue.3 , pp. 1409-1420
    • Denkov, N.D.1    Yoshimura, H.2    Kouyama, T.3    Walz, J.4    Nagayama, K.5
  • 9
    • 11944267977 scopus 로고    scopus 로고
    • An icosahedral assembly of the lightharvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes
    • Hino T, Kanamori E, Shen JR, Kouyama T (2004) An icosahedral assembly of the lightharvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes. Acta Crystallogr D Biol Crystallogr 60(Pt 5):803-809.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 5 , pp. 803-809
    • Hino, T.1    Kanamori, E.2    Shen, J.R.3    Kouyama, T.4
  • 10
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • Liu Z, et al. (2004) Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature 428(6980):287-292.
    • (2004) Nature , vol.428 , Issue.6980 , pp. 287-292
    • Liu, Z.1
  • 11
    • 0031790857 scopus 로고    scopus 로고
    • Macromolecular structure determination by electron microscopy: New advances and recent results
    • Stowell MH, Miyazawa A, Unwin N (1998) Macromolecular structure determination by electron microscopy: New advances and recent results. Curr Opin Struct Biol 8(5):595-600.
    • (1998) Curr Opin Struct Biol , vol.8 , Issue.5 , pp. 595-600
    • Stowell, M.H.1    Miyazawa, A.2    Unwin, N.3
  • 13
    • 67650282016 scopus 로고    scopus 로고
    • Electron crystallography as a technique to study the structures of membrane proteins in a lipid environment
    • Raunser S, Walz T (2009) Electron crystallography as a technique to study the structures of membrane proteins in a lipid environment. Ann. Rev. Biophys. 38:89-105.
    • (2009) Ann. Rev. Biophys. , vol.38 , pp. 89-105
    • Raunser, S.1    Walz, T.2
  • 14
    • 79954454533 scopus 로고    scopus 로고
    • Structural physiology based on electron crystallography
    • Fujiyoshi Y (2011) Structural physiology based on electron crystallography. Protein Sci 20(5):806-817.
    • (2011) Protein Sci , vol.20 , Issue.5 , pp. 806-817
    • Fujiyoshi, Y.1
  • 15
    • 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
    • Levina N, 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(7):1730-1737.
    • (1999) EMBO J , vol.18 , Issue.7 , pp. 1730-1737
    • Levina, N.1
  • 16
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass RB, Strop P, Barclay M, Rees DC (2002) Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 298(5598):1582-1587.
    • (2002) Science , vol.298 , Issue.5598 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 17
    • 33947151603 scopus 로고    scopus 로고
    • Electron crystallography of membrane proteins: Two-dimensional crystallization and screening by electron microscopy
    • Schmidt-Krey I (2007) Electron crystallography of membrane proteins: Two-dimensional crystallization and screening by electron microscopy. Methods 41(4):417-426.
    • (2007) Methods , vol.41 , Issue.4 , pp. 417-426
    • Schmidt-Krey, I.1
  • 18
    • 34047126893 scopus 로고    scopus 로고
    • Structures of the prokaryotic mechanosensitive channels MscL and MscS
    • Steinbacher S, Bass RB, Strop P, Rees DC (2007) Structures of the prokaryotic mechanosensitive channels MscL and MscS. Curr Topics Membranes 58:1-24.
    • (2007) Curr Topics Membranes , vol.58 , pp. 1-24
    • Steinbacher, S.1    Bass, R.B.2    Strop, P.3    Rees, D.C.4
  • 19
    • 50649125767 scopus 로고    scopus 로고
    • The structure of an open form of an E. Coli mechanosensitive channel at 3.45 A resolution
    • Wang WJ, et al. (2008) The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution. Science 321(5893):1179-1183.
    • (2008) Science , vol.321 , Issue.5893 , pp. 1179-1183
    • Wang, W.J.1
  • 20
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka K, et al. (1999) The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: Implication of the charge distribution. J Mol Biol 286(3): 861-882.
    • (1999) J Mol Biol , vol.286 , Issue.3 , pp. 861-882
    • Mitsuoka, K.1
  • 21
    • 0029903197 scopus 로고    scopus 로고
    • Electroncrystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff N, Ceska TA, Downing KH, Baldwin JM, Henderson R (1996) Electroncrystallographic refinement of the structure of bacteriorhodopsin. J Mol Biol 259(3): 393-421.
    • (1996) J Mol Biol , vol.259 , Issue.3 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 22
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • Gonen T, et al. (2005) Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 438(7068):633-638.
    • (2005) Nature , vol.438 , Issue.7068 , pp. 633-638
    • Gonen, T.1
  • 23
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of threedimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR (1996) Computer visualization of threedimensional image data using IMOD. J Struct Biol 116(1):71-76.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 24
    • 33747598723 scopus 로고    scopus 로고
    • The molecular architecture of axonemes revealed by cryoelectron tomography
    • Nicastro D, et al. (2006) The molecular architecture of axonemes revealed by cryoelectron tomography. Science 313(5789):944-948.
    • (2006) Science , vol.313 , Issue.5789 , pp. 944-948
    • Nicastro, D.1
  • 25
    • 78649340178 scopus 로고    scopus 로고
    • Minimal bending energies of bilayer polyhedra
    • Haselwandter CA, Phillips R (2010) Minimal bending energies of bilayer polyhedra. Phys Rev Lett 105(22):228101.
    • (2010) Phys Rev Lett , vol.105 , Issue.22 , pp. 228101
    • Haselwandter, C.A.1    Phillips, R.2
  • 26
    • 36949077319 scopus 로고
    • Structure of small viruses
    • Crick FHC, Watson JD (1956) Structure of small viruses. Nature 177(4506):473-475.
    • (1956) Nature , vol.177 , Issue.4506 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 27
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar DL, Klug A (1962) Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol 27:1-24.
    • (1962) Cold Spring Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Caspar, D.L.1    Klug, A.2
  • 28
    • 52949090437 scopus 로고    scopus 로고
    • Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles
    • Plevka P, Tars K, Liljas L (2008) Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles. Protein Sci 17(10):1731-1739.
    • (2008) Protein Sci , vol.17 , Issue.10 , pp. 1731-1739
    • Plevka, P.1    Tars, K.2    Liljas, L.3
  • 29
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for highresolution single-particle reconstructions. J Struct Biol 128(1):82-97.
    • (1999) J Struct Biol , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 30
    • 84887063602 scopus 로고    scopus 로고
    • Microfluidic device for super-fast evaluation of membrane protein nanoparticle formation
    • Wu H-J, et al. (2013) Microfluidic device for super-fast evaluation of membrane protein nanoparticle formation. Micro & Nano Letters 8(10):672-675.
    • (2013) Micro & Nano Letters , vol.8 , Issue.10 , pp. 672-675
    • Wu, H.-J.1
  • 31
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera?a visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera?a visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.