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Volumn 20, Issue 8, 2013, Pages 965-972

Structural changes in the mitochondrial Tim23 channel are coupled to the proton-motive force

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; FUNGAL PROTEIN; PROTEIN TIM23; PROTON; UNCLASSIFIED DRUG;

EID: 84881427620     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2613     Document Type: Article
Times cited : (63)

References (65)
  • 1
    • 0027146417 scopus 로고
    • Imaging in five dimensions: Time-dependent membrane potentials in individual mitochondria
    • Loew, L.M., Tuft, R.A., Carrington, W. & Fay, F.S. Imaging in fve dimensions: time-dependent membrane potentials in individual mitochondria. Biophys. J. 65, 2396-2407 (1993). (Pubitemid 24005971)
    • (1993) Biophysical Journal , vol.65 , Issue.6 , pp. 2396-2407
    • Loew, L.M.1    Tuft, R.A.2    Carrington, W.3    Fay, F.S.4
  • 2
    • 84861895328 scopus 로고    scopus 로고
    • Measurements and implications of the membrane dipole potential
    • Wang, L. Measurements and implications of the membrane dipole potential. Annu. Rev. Biochem. 81, 615-635 (2012).
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 615-635
    • Wang, L.1
  • 3
    • 67649810749 scopus 로고    scopus 로고
    • Nanoscopic description of biomembrane electrostatics: Results of molecular dynamics simulations and fuorescence probing
    • Demchenko, A.P. & Yesylevskyy, S.O. Nanoscopic description of biomembrane electrostatics: results of molecular dynamics simulations and fuorescence probing. Chem. Phys. Lipids 160, 63-84 (2009).
    • (2009) Chem. Phys. Lipids , vol.160 , pp. 63-84
    • Demchenko, A.P.1    Yesylevskyy, S.O.2
  • 5
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska, A., Koehler, CM., Milenkovic, D., Lithgow, T. & Pfanner, N. Importing mitochondrial proteins: machineries and mechanisms. Cell 138, 628-644 (2009).
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 6
    • 79851512985 scopus 로고    scopus 로고
    • Structural insight into the mitochondrial protein import system
    • Endo, T., Yamano, K. & Kawano, S. Structural insight into the mitochondrial protein import system. Biochim. Biophys. Acta 1808, 955-970 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 955-970
    • Endo, T.1    Yamano, K.2    Kawano, S.3
  • 8
    • 79851514913 scopus 로고    scopus 로고
    • Understanding the molecular mechanism of protein translocation across the mitochondrial inner membrane: Still a long way to go
    • Marom, M., Azem, A. & Mokranjac, D. Understanding the molecular mechanism of protein translocation across the mitochondrial inner membrane: still a long way to go. Biochim. Biophys. Acta 1808, 990-1001 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 990-1001
    • Marom, M.1    Azem, A.2    Mokranjac, D.3
  • 9
    • 84866724626 scopus 로고    scopus 로고
    • Biogenesis of lipids and proteins within biological membranes
    • ed. Yeagle, P.L.) CRC
    • Alder, N.N. Biogenesis of lipids and proteins within biological membranes. in The Structure of Biological Membranes (ed. Yeagle, P.L.) 315-377 (CRC, 2011).
    • (2011) The Structure of Biological Membranes , pp. 315-377
    • Alder, N.N.1
  • 10
    • 0024999562 scopus 로고
    • Polypeptides traverse the mitochondrial envelope in an extended state
    • DOI 10.1016/0014-5793(90)81469-5
    • Rassow, J., Hartl, F.U., Guiard, B., Pfanner, N. & Neupert, W. Polypeptides traverse the mitochondrial envelope in an extended state. FEBS Lett. 275, 190-194 (1990). (Pubitemid 20386206)
    • (1990) FEBS Letters , vol.275 , Issue.1-2 , pp. 190-194
    • Rassow, J.1    Hartl, F.-U.2    Guiard, B.3    Pfanner, N.4    Neupert, W.5
  • 14
    • 0037111988 scopus 로고    scopus 로고
    • Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes
    • DOI 10.1016/S0092-8674(02)01053-X
    • Yamamoto, H. et al. Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. Cell 111, 519-528 (2002). (Pubitemid 35356557)
    • (2002) Cell , vol.111 , Issue.4 , pp. 519-528
    • Yamamoto, H.1    Esaki, M.2    Kanamori, T.3    Tamura, Y.4    Nishikawa, S.-I.5    Endo, T.6
  • 15
    • 83755168897 scopus 로고    scopus 로고
    • Direct interaction of mitochondrial targeting presequences with purifed components of the TIM23 protein complex
    • Marom, M. et al. Direct interaction of mitochondrial targeting presequences with purifed components of the TIM23 protein complex. J. Biol. Chem. 286, 43809-43815 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 43809-43815
    • Marom, M.1
  • 16
    • 81355147404 scopus 로고    scopus 로고
    • Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex
    • Schulz, C. et al. Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex. J. Cell Biol. 195, 643-656 (2011).
    • (2011) J. Cell Biol. , vol.195 , pp. 643-656
    • Schulz, C.1
  • 17
    • 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
  • 19
    • 73549085843 scopus 로고    scopus 로고
    • Distinct forms of mitochondrial TOM-TIM supercomplexes defne signal-dependent states of preprotein sorting
    • Chacinska, A. et al. Distinct forms of mitochondrial TOM-TIM supercomplexes defne signal-dependent states of preprotein sorting. Mol. Cell Biol. 30, 307-318 (2010).
    • (2010) Mol. Cell Biol. , vol.30 , pp. 307-318
    • Chacinska, A.1
  • 20
  • 21
    • 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
  • 22
    • 33750949389 scopus 로고    scopus 로고
    • A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria
    • van der Laan, M. et al. A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria. Curr. Biol. 16, 2271-2276 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 2271-2276
    • Van Der Laan, M.1
  • 23
    • 37249039150 scopus 로고    scopus 로고
    • Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain
    • DOI 10.1083/jcb.200709087
    • Wiedemann, N., van der Laan, M., Hutu, D.P., Rehling, P. & Pfanner, N. Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain. J. Cell Biol. 179, 1115-1122 (2007). (Pubitemid 350277731)
    • (2007) Journal of Cell Biology , vol.179 , Issue.6 , pp. 1115-1122
    • Wiedemann, N.1    Van Der Laan, M.2    Hutu, D.P.3    Rehling, P.4    Pfanner, N.5
  • 24
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • Glick, B.S. et al. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell 69, 809-822 (1992).
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1
  • 25
    • 79952744648 scopus 로고    scopus 로고
    • TIM23-mediated insertion of transmembrane a-helices into the mitochondrial inner membrane
    • Botelho, S.C. et al. TIM23-mediated insertion of transmembrane a-helices into the mitochondrial inner membrane. EMBO J. 30, 1003-1011 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1003-1011
    • Botelho, S.C.1
  • 26
    • 34848838019 scopus 로고    scopus 로고
    • Motor-free mitochondrial presequence translocase drives membrane integration of preproteins
    • van der Laan, M. et al. Motor-free mitochondrial presequence translocase drives membrane integration of preproteins. Nat. Cell Biol. 9, 1152-1159 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1152-1159
    • Van Der Laan, M.1
  • 27
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import: ΔΨ Drives the movement of presequences
    • Martin, J., Mahlke, K. & Pfanner, N. Role of an energized inner membrane in mitochondrial protein import: A\|/drives the movement of presequences. J. Biol. Chem. 266, 18051-18057 (1991). (Pubitemid 21908046)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.27 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 28
    • 48449091228 scopus 로고    scopus 로고
    • Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface
    • Alder, N.N., Jensen, R.E. & Johnson, A.E. Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface. Cell 134, 439-450 (2008).
    • (2008) Cell , vol.134 , pp. 439-450
    • Alder, N.N.1    Jensen, R.E.2    Johnson, A.E.3
  • 29
    • 0030968336 scopus 로고    scopus 로고
    • Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC
    • DOI 10.1083/jcb.137.2.377
    • Lohret, T.A., Jensen, R.E. & Kinnally, K.W. Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC. J. Cell Biol. 137, 377-386 (1997). (Pubitemid 27181291)
    • (1997) Journal of Cell Biology , vol.137 , Issue.2 , pp. 377-386
    • Lohret, T.A.1    Jensen, R.E.2    Kinnally, K.W.3
  • 30
    • 33947509012 scopus 로고    scopus 로고
    • Tim17p regulates the twin pore structure and voltage gating of the mitochondrial protein import complex TIM23
    • DOI 10.1074/jbc.M607551200
    • Martinez-Caballero, S., Grigoriev, S.M., Herrmann, J.M., Campo, M.L. & Kinnally, K.W. Tim17p regulates the twin pore structure and voltage gating of the mitochondrial protein import complex TIM23. J. Biol. Chem. 282, 3584-3593 (2007). (Pubitemid 47084460)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3584-3593
    • Martinez-Caballero, S.1    Grigoriev, S.M.2    Herrmann, J.M.3    Campo, M.L.4    Kinnally, K.W.5
  • 31
    • 0030272378 scopus 로고    scopus 로고
    • Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
    • DOI 10.1016/S0092-8674(00)81320-3
    • Bauer, M.F., Sirrenberg, C, Neupert, W. & Brunner, M. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87, 33-41 (1996). (Pubitemid 26337388)
    • (1996) Cell , vol.87 , Issue.1 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 32
    • 14844334925 scopus 로고    scopus 로고
    • Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria
    • DOI 10.1074/jbc.M412158200
    • Meier, S., Neupert, W. & Herrmann, J.M. Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria. J. Biol. Chem. 280, 7777-7785 (2005). (Pubitemid 40349671)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7777-7785
    • Meier, S.1    Neupert, W.2    Herrmann, J.M.3
  • 34
    • 0036221085 scopus 로고    scopus 로고
    • Protein unfolding by the mitochondrial membrane potential
    • DOI 10.1038/nsb772
    • Huang, S., Ratliff, K.S. & Matouschek, A. Protein unfolding by the mitochondrial membrane potential. Nat. Struct. Biol. 9, 301-307 (2002). (Pubitemid 34289904)
    • (2002) Nature Structural Biology , vol.9 , Issue.4 , pp. 301-307
    • Huang, S.1    Ratliff, K.S.2    Matouschek, A.3
  • 35
    • 38749103444 scopus 로고    scopus 로고
    • Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits
    • DOI 10.1091/mbc.E07-07-0669
    • Alder, N.N., Sutherland, J., Buhring, A.I., Jensen, R.E. & Johnson, A.E. Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits. Mol. Biol. Cell 19, 159-170 (2008). (Pubitemid 351186142)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 159-170
    • Alder, N.N.1    Sutherland, J.2    Buhring, A.I.3    Jensen, R.E.4    Johnson, A.E.5
  • 36
    • 0033739682 scopus 로고    scopus 로고
    • 2 modulates the A\|/-dependence of translocation of the matrix-targeting sequence
    • 2 modulates the A\|/-dependence of translocation of the matrix-targeting sequence. Mol. Biol. Cell 11, 3977-3991 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3977-3991
    • Geissler, A.1
  • 37
    • 0017659528 scopus 로고
    • Spectroscopic and immunochemical studies with nitrobenzoxadiazolealanine, a fluorescent dinitrophenyl analogue
    • Lancet, D. & Pecht, I. Spectroscopic and immunochemical studies with nitrobenzoxadiazolealanine, a fuorescent dinitrophenyl analogue. Biochemistry 16, 5150-5157 (1977). (Pubitemid 8222211)
    • (1977) Biochemistry , vol.16 , Issue.23 , pp. 5150-5157
    • Lancet, D.1    Pecht, I.2
  • 38
    • 0026212510 scopus 로고
    • Time-resolved fuorescence of nitrobenzoxadiazole-aminohexanoic acid: Effect of intermolecular hydrogen-bonding on non-radiative decay
    • Lin, S. & Struve, W.S. Time-resolved fuorescence of nitrobenzoxadiazole-aminohexanoic acid: effect of intermolecular hydrogen-bonding on non-radiative decay. Photochem. Photobiol. 54, 361-365 (1991).
    • (1991) Photochem. Photobiol. , vol.54 , pp. 361-365
    • Lin, S.1    Struve, W.S.2
  • 39
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L. et al. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195, 659-685 (1987).
    • (1987) J. Mol. Biol. , vol.195 , pp. 659-685
    • Cornette, J.L.1
  • 40
    • 17044400916 scopus 로고    scopus 로고
    • Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels
    • Silberberg, S.D., Chang, T.H. & Swartz, K.J. Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels. J. Gen. Physiol. 125, 347-359 (2005).
    • (2005) J. Gen. Physiol. , vol.125 , pp. 347-359
    • Silberberg, S.D.1    Chang, T.H.2    Swartz, K.J.3
  • 41
    • 70449597292 scopus 로고    scopus 로고
    • Studies of a-helicity and intersegmental interactions in voltage-gated Na+ channels: S2D4
    • Ma, Z., Kong, J. & Kallen, R.G. Studies of a-helicity and intersegmental interactions in voltage-gated Na+ channels: S2D4. PLoS ONE 4, e7674 (2009).
    • (2009) PLoS ONE , vol.4
    • Ma, Z.1    Kong, J.2    Kallen, R.G.3
  • 42
    • 2442551481 scopus 로고    scopus 로고
    • During apoptosis Bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria
    • DOI 10.1016/S1097-2765(04)00263-1, PII S1097276504002631
    • Kim, P.K., Annis, M.G., Dlugosz, P.J., Leber, B. & Andrews, D.W. During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria. Mol. Cell 14, 523-529 (2004). (Pubitemid 38648805)
    • (2004) Molecular Cell , vol.14 , Issue.4 , pp. 523-529
    • Kim, P.K.1    Annis, M.G.2    Dlugosz, P.J.3    Leber, B.4    Andrews, D.W.5
  • 43
    • 0142042958 scopus 로고    scopus 로고
    • 0 during ATP synthesis
    • DOI 10.1016/S0005-2728(03)00110-5
    • Baracca, A., Sgarbi, G., Solaini, G. & Lenaz, G. Rhodamine 123 as a probe of mitochondrial membrane potential: evaluation of proton fux through F0 during ATP synthesis. Biochim. Biophys. Acta 1606, 137-146 (2003). (Pubitemid 37267877)
    • (2003) Biochimica et Biophysica Acta - Bioenergetics , vol.1606 , Issue.1-3 , pp. 137-146
    • Baracca, A.1    Sgarbi, G.2    Solaini, G.3    Lenaz, G.4
  • 44
    • 67349266230 scopus 로고    scopus 로고
    • Position of helical kinks in membrane protein crystal structures and the accuracy of computational prediction
    • Hall, S.E., Roberts, K. & Vaidehi, N. Position of helical kinks in membrane protein crystal structures and the accuracy of computational prediction. J. Mol. Graph. Model. 27, 944-950 (2009).
    • (2009) J. Mol. Graph. Model. , vol.27 , pp. 944-950
    • Hall, S.E.1    Roberts, K.2    Vaidehi, N.3
  • 45
    • 78650702465 scopus 로고    scopus 로고
    • Improved helix and kink characterization in membrane proteins allows evaluation of kink sequence predictors
    • Langelaan, D.N., Wieczorek, M., Blouin, C. & Rainey, J.K. Improved helix and kink characterization in membrane proteins allows evaluation of kink sequence predictors. J. Chem. Inf. Model. 50, 2213-2220 (2010).
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 2213-2220
    • Langelaan, D.N.1    Wieczorek, M.2    Blouin, C.3    Rainey, J.K.4
  • 46
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • DOI 10.1016/j.jsb.2007.01.011, PII S1047847707000317
    • Screpanti, E. & Hunte, C. Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 159, 261-267 (2007). (Pubitemid 47095395)
    • (2007) Journal of Structural Biology , vol.159 , Issue.2 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 50
    • 84861434240 scopus 로고    scopus 로고
    • Shifting hydrogen bonds may produce fexible transmembrane helices
    • Cao, Z. & Bowie, J.U. Shifting hydrogen bonds may produce fexible transmembrane helices. Proc. Natl. Acad. Sci. USA 109, 8121-8126 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8121-8126
    • Cao, Z.1    Bowie, J.U.2
  • 51
    • 54049142467 scopus 로고    scopus 로고
    • A role for the two-helix fnger of the SecA ATPase in protein translocation
    • Erlandson, K.J. et al. A role for the two-helix fnger of the SecA ATPase in protein translocation. Nature 455, 984-987 (2008).
    • (2008) Nature , vol.455 , pp. 984-987
    • Erlandson, K.J.1
  • 52
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K.J. Sensing voltage across lipid membranes. Nature 456, 891-897 (2008).
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 53
    • 67650245365 scopus 로고    scopus 로고
    • Regulation and pharmacology of the mitochondrial permeability transition pore
    • Zorov, D.B. et al. Regulation and pharmacology of the mitochondrial permeability transition pore. Cardiovasc. Res. 83, 213-225 (2009).
    • (2009) Cardiovasc. Res. , vol.83 , pp. 213-225
    • Zorov, D.B.1
  • 54
    • 0038421272 scopus 로고    scopus 로고
    • Imaging the permeability pore transition in single mitochondria
    • Hüser, J., Rechenmacher, C.E. & Blatter, L.A. Imaging the permeability pore transition in single mitochondria. Biophys. J. 74, 2129-2137 (1998). (Pubitemid 28157948)
    • (1998) Biophysical Journal , vol.74 , Issue.4 , pp. 2129-2137
    • Huser, J.1    Rechenmacher, C.E.2    Blatter, L.A.3
  • 55
    • 0037879052 scopus 로고    scopus 로고
    • m) in apoptosis; an update
    • DOI 10.1023/A:1022945107762
    • Ly, J.D., Grubb, D.R. & Lawen, A. The mitochondrial membrane potential Δψ(m) in apoptosis; an update. Apoptosis 8, 115-128 (2003). (Pubitemid 36553052)
    • (2003) Apoptosis , vol.8 , Issue.2 , pp. 115-128
    • Ly, J.D.1    Grubb, D.R.2    Lawen, A.3
  • 56
    • 0037745119 scopus 로고    scopus 로고
    • Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore
    • DOI 10.1042/0264-6021:3430311
    • Hüser, J. & Blatter, L.A. Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore. Biochem. J. 343, 311-317 (1999). (Pubitemid 29511762)
    • (1999) Biochemical Journal , vol.343 , Issue.2 , pp. 311-317
    • Huser, J.1    Blatter, L.A.2
  • 57
    • 0035879072 scopus 로고    scopus 로고
    • Spontaneous changes in mitochondrial membrane potential in cultured neurons
    • Buckman, J.F. & Reynolds, I.J. Spontaneous changes in mitochondrial membrane potential in cultured neurons. J. Neurosci. 21, 5054-5065 (2001). (Pubitemid 32622931)
    • (2001) Journal of Neuroscience , vol.21 , Issue.14 , pp. 5054-5065
    • Buckman, J.F.1    Reynolds, I.J.2
  • 59
    • 84860125979 scopus 로고    scopus 로고
    • Pulsing of membrane potential in individual mitochondria: A stress-induced mechanism to regulate respiratory bioenergetics in Arabidopsis
    • Schwarzländer, M. et al. Pulsing of membrane potential in individual mitochondria: a stress-induced mechanism to regulate respiratory bioenergetics in Arabidopsis. Plant Cell 24, 1188-1201 (2012).
    • (2012) Plant Cell , vol.24 , pp. 1188-1201
    • Schwarzländer, M.1
  • 60
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria: Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., Bohni, P.C. & Schatz, G. Import of proteins into mitochondria: cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257, 13028-13033 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 61
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson, A.H. & Blobel, G. Cell-free translation of messenger RNA in a wheat germ system. Methods Enzymol. 96, 38-50 (1983).
    • (1983) Methods Enzymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 62
    • 33846137294 scopus 로고    scopus 로고
    • A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import
    • DOI 10.1128/MCB.01391-06
    • Krayl, M., Lim, J.H., Martin, F., Guiard, B. & Voos, W. A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import. Mol. Cell. Biol. 27, 411-425 (2007). (Pubitemid 46080113)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.2 , pp. 411-425
    • Krayl, M.1    Lim, J.H.2    Martin, F.3    Guiard, B.4    Voos, W.5
  • 63
    • 0025008104 scopus 로고
    • Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria
    • Pfanner, N. et al. Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria. J. Biol. Chem. 265, 16324-16329 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 16324-16329
    • Pfanner, N.1
  • 64
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • DOI 10.1016/0092-8674(94)90424-3
    • Crowley, K.S., Liao, S., Worrell, V.E., Reinhart, G.D. & Johnson, A.E. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78, 461-471 (1994). (Pubitemid 24250810)
    • (1994) Cell , vol.78 , Issue.3 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 65
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • DOI 10.1016/0092-8674(93)90640-C
    • Crowley, K.S., Reinhart, G.D. & Johnson, A.E. The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115 (1993). (Pubitemid 23180485)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.