메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Visualizing active membrane protein complexes by electron cryotomography

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN PRECURSOR; QUANTUM DOT; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84903121701     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5129     Document Type: Article
Times cited : (57)

References (39)
  • 1
    • 79551691125 scopus 로고    scopus 로고
    • A ferritin-based label for cellular electron cryotomography
    • Wang, Q., Mercogliano, C. P. & Löwe, J. A ferritin-based label for cellular electron cryotomography. Structure 19, 147-154 (2011).
    • (2011) Structure , vol.19 , pp. 147-154
    • Wang, Q.1    Mercogliano, C.P.2    Löwe, J.3
  • 2
    • 34548627873 scopus 로고    scopus 로고
    • Concatenated metallothionein as a clonable gold label for electron microscopy
    • DOI 10.1016/j.jsb.2007.06.010, PII S1047847707001499
    • Mercogliano, C. P. & DeRosier, D. J. Concatenated metallothionein as a clonable gold label for electron microscopy. J. Struct. Biol. 160, 70-82 (2007). (Pubitemid 47405236)
    • (2007) Journal of Structural Biology , vol.160 , Issue.1 , pp. 70-82
    • Mercogliano, C.P.1    DeRosier, D.J.2
  • 3
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • DOI 10.1016/0005-2728(96)00022-9
    • Harrison, P. M. & Arosio, P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275, 161-203 (1996). (Pubitemid 26248989)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 4
    • 28844456522 scopus 로고    scopus 로고
    • Gold nanocluster formation using metallothionein: Mass spectrometry and electron microscopy
    • DOI 10.1016/j.jmb.2005.10.026, PII S0022283605012611
    • Mercogliano, C. P. & DeRosier, D. J. Gold nanocluster formation using metallothionein: mass spectrometry and electron microscopy. J. Mol. Biol. 355, 211-223 (2006). (Pubitemid 41774126)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.2 , pp. 211-223
    • Mercogliano, C.P.1    DeRosier, D.J.2
  • 5
    • 84861017091 scopus 로고    scopus 로고
    • Specific, sensitive, high-resolution detection of protein molecules in eukaryotic cells using metal-tagging transmission electron microscopy
    • Risco, C. et al. Specific, sensitive, high-resolution detection of protein molecules in eukaryotic cells using metal-tagging transmission electron microscopy. Structure 20, 759-766 (2012).
    • (2012) Structure , vol.20 , pp. 759-766
    • Risco, C.1
  • 6
    • 59149094180 scopus 로고    scopus 로고
    • Visualization of proteins in intact cells with a clonable tag for electron microscopy
    • Diestra, E., Fontana, J., Guichard, P., Marco, S. & Risco, C. Visualization of proteins in intact cells with a clonable tag for electron microscopy. J. Struct. Biol. 165, 157-168 (2009).
    • (2009) J. Struct. Biol. , vol.165 , pp. 157-168
    • Diestra, E.1    Fontana, J.2    Guichard, P.3    Marco, S.4    Risco, C.5
  • 8
    • 77957573768 scopus 로고    scopus 로고
    • Fluorescent labeling of tetracysteine-tagged proteins in intact cells
    • Hoffmann, C. et al. Fluorescent labeling of tetracysteine-tagged proteins in intact cells. Nat. Protoc. 5, 1666-1677 (2010).
    • (2010) Nat. Protoc. , vol.5 , pp. 1666-1677
    • Hoffmann, C.1
  • 10
    • 41949108948 scopus 로고    scopus 로고
    • The application of fluorescent quantum dots to confocal, multiphoton, and electron microscopic imaging
    • Deerinck, J. The application of fluorescent quantum dots to confocal, multiphoton, and electron microscopic imaging. Toxicol. Pathol. 36, 112-116 (2008).
    • (2008) Toxicol. Pathol. , vol.36 , pp. 112-116
    • Deerinck, J.1
  • 11
    • 0347418285 scopus 로고    scopus 로고
    • Application of Quantum Dots as Probes for Correlative Fluorescence, Conventional, and Energy-filtered Transmission Electron Microscopy
    • Nisman, R., Dellaire, G., Ren, Y., Li, R. & Bazett-Jones, D. P. Application of quantum dots as probes for correlative fluorescence, conventional, and energyfiltered transmission electron microscopy. J. Histochem. Cytochem. 52, 13-18 (2004). (Pubitemid 38032129)
    • (2004) Journal of Histochemistry and Cytochemistry , vol.52 , Issue.1 , pp. 13-18
    • Nisman, R.1    Dellaire, G.2    Ren, Y.3    Li, R.4    Bazett-Jones, D.P.5
  • 12
    • 27144475807 scopus 로고    scopus 로고
    • Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots
    • DOI 10.1038/nmeth791, PII N791
    • Giepmans, B. N., Deerinck, T. J., Smarr, B. L., Jones, Y. Z. & Ellisman, M. H. Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. Nat. Methods 2, 743-749 (2005). (Pubitemid 41486205)
    • (2005) Nature Methods , vol.2 , Issue.10 , pp. 743-749
    • Giepmans, B.N.G.1    Deerinck, T.J.2    Smarr, B.L.3    Jones, Y.Z.4    Ellisman, M.H.5
  • 13
    • 77953807458 scopus 로고    scopus 로고
    • The many faces of the mitochondrial TIM23 complex
    • Mokranjac, D. & Neupert, W. The many faces of the mitochondrial TIM23 complex. Biochim. Biophys. Acta 1797, 1045-1054 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1045-1054
    • Mokranjac, D.1    Neupert, W.2
  • 14
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: From proteomics to functional mechanisms
    • Schmidt, O., Pfanner, N. & Meisinger, C. Mitochondrial protein import: from proteomics to functional mechanisms. Nat. Rev. Mol. Cell Biol. 11, 655-667 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 15
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo, T. & Yamano, K. Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390, 723-730 (2009).
    • (2009) Biol. Chem. , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 16
    • 0024454311 scopus 로고
    • Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites
    • I
    • Rassow, J. et al. Translocation arrest by reversible folding of a precursor protein imported into mitochondria-a means to quantitate translocation contact sites. J. Cell Biol. 109, 1421-1428 (1989). (Pubitemid 19251200)
    • (1989) Journal of Cell Biology , vol.109 , Issue.4 , pp. 1421-1428
    • Rassow, J.1    Guiard, B.2    Wienhues, U.3    Herzog, V.4    Hartl, F.-U.5    Neupert, W.6
  • 17
    • 0037009088 scopus 로고    scopus 로고
    • Contact sites between the outer and inner membrane of mitochondria - Role in protein transport
    • DOI 10.1016/S0167-4889(02)00263-X, PII S016748890200263X
    • Reichert, A. S. & Neupert, W. Contact sites between the outer and inner membrane of mitochondria-role in protein transport. Biochim. Biophys. Acta 1592, 41-49 (2002). (Pubitemid 35015164)
    • (2002) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1592 , Issue.1 , pp. 41-49
    • Reichert, A.S.1    Neupert, W.2
  • 18
    • 0030845840 scopus 로고    scopus 로고
    • The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44
    • DOI 10.1093/emboj/16.17.5408
    • Dekker, P. J. et al. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16, 5408-5419 (1997). (Pubitemid 27380148)
    • (1997) EMBO Journal , vol.16 , Issue.17 , pp. 5408-5419
    • Dekker, P.J.T.1    Martin, F.2    Maarse, A.C.3    Bomer, U.4    Muller, H.5    Guiard, B.6    Meijer, M.7    Rassow, J.8    Pfanner, N.9
  • 19
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • DOI 10.1016/j.bbamcr.2006.04.006, PII S0167488906000851
    • Mannella, C. A. Structure and dynamics of the mitochondrial inner membrane cristae. Biochim. Biophys. Acta 1763, 542-548 (2006). (Pubitemid 44015951)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.5-6 , pp. 542-548
    • Mannella, C.A.1
  • 20
    • 56349166020 scopus 로고    scopus 로고
    • Cristae formation-linking ultrastructure and function of mitochondria
    • Zick, M., Rabl, R. & Reichert, A. S. Cristae formation-linking ultrastructure and function of mitochondria. Biochim. Biophys. Acta 1793, 5-19 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 5-19
    • Zick, M.1    Rabl, R.2    Reichert, A.S.3
  • 22
    • 4544378532 scopus 로고    scopus 로고
    • Mitochondrial fusion intermediates revealed in vitro
    • DOI 10.1126/science.1100612
    • Meeusen, S., McCaffery, J. M. & Nunnari, J. Mitochondrial fusion intermediates revealed in vitro. Science 305, 1747-1752 (2004). (Pubitemid 39249636)
    • (2004) Science , vol.305 , Issue.5691 , pp. 1747-1752
    • Meeusen, S.1    McCaffery, J.M.2    Nunnari, J.3
  • 23
    • 80052010249 scopus 로고    scopus 로고
    • Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient
    • Wurm, C. A. et al. Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient. Proc. Natl Acad. Sci. 108, 13546-13551 (2011).
    • (2011) Proc. Natl Acad. Sci. , vol.108 , pp. 13546-13551
    • Wurm, C.A.1
  • 24
    • 84859265052 scopus 로고    scopus 로고
    • Role of MINOS in mitochondrial membrane architecture and biogenesis
    • van der Laan, M., Bohnert, M., Wiedemann, N. & Pfanner, N. Role of MINOS in mitochondrial membrane architecture and biogenesis. Trends Cell Biol. 22, 185-192 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 185-192
    • Van Der Laan, M.1    Bohnert, M.2    Wiedemann, N.3    Pfanner, N.4
  • 25
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • DOI 10.1083/jcb.200605138
    • Vogel, F., Bornhövd, C., Neupert, W. & Reichert, A. S. Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 175, 237-247 (2006). (Pubitemid 44631418)
    • (2006) Journal of Cell Biology , vol.175 , Issue.2 , pp. 237-247
    • Vogel, F.1    Bornhovd, C.2    Neupert, W.3    Reichert, A.S.4
  • 27
    • 59849090705 scopus 로고    scopus 로고
    • Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import
    • Tamura, Y. et al. Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import. J. Cell Biol. 184, 129-141 (2009).
    • (2009) J. Cell Biol. , vol.184 , pp. 129-141
    • Tamura, Y.1
  • 28
    • 33745841363 scopus 로고    scopus 로고
    • Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p
    • DOI 10.1038/nsmb1106, PII NSMB1106
    • Wu, Y. & Sha, B. Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p. Nat. Struct. Mol. Biol. 13, 589-593 (2006). (Pubitemid 44036468)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.7 , pp. 589-593
    • Wu, Y.1    Sha, B.2
  • 29
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., Kovaleva, E. & Schatz, P. J. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Prot. Sci. 8, 921-929 (1999). (Pubitemid 29165423)
    • (1999) Protein Science , vol.8 , Issue.4 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 30
    • 84870500426 scopus 로고    scopus 로고
    • DOLORS: Versatile strategy for internal labeling and domain localization in electron microscopy
    • Lau, P. W., Potter, C. S., Carragher, B. & MacRae, I. J. DOLORS: versatile strategy for internal labeling and domain localization in electron microscopy. Structure. 20, 1995-2002 (2012).
    • (2012) Structure , vol.20 , pp. 1995-2002
    • Lau, P.W.1    Potter, C.S.2    Carragher, B.3    MacRae, I.J.4
  • 31
    • 84859128639 scopus 로고    scopus 로고
    • Penetration of amphiphilic quantum dots through model and cellular plasma membranes
    • Dubavik, A. et al. Penetration of amphiphilic quantum dots through model and cellular plasma membranes. ACS Nano 6, 2150-2156 (2012).
    • (2012) ACS Nano , vol.6 , pp. 2150-2156
    • Dubavik, A.1
  • 32
    • 0026520064 scopus 로고
    • Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
    • Koll, H. et al. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68, 1163-1175 (1992).
    • (1992) Cell , vol.68 , pp. 1163-1175
    • Koll, H.1
  • 33
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R., S. & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27 (1989).
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 35
    • 84862626955 scopus 로고    scopus 로고
    • Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes
    • Gebert, M. et al. Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes. J. Cell Biol. 197, 595-604 (2012).
    • (2012) J. Cell Biol. , vol.197 , pp. 595-604
    • Gebert, M.1
  • 36
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • DOI 10.1006/jsbi.1996.0013
    • Kremer, J. R., Mastronade, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71-76 (1996). (Pubitemid 26093126)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 37
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis, A. S. & Hegerl, R. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 135, 239-250 (2001).
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.