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Volumn 24, Issue 5, 2013, Pages 543-554

Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MEMBRANE PROTEIN; MIA40 ENZYME; MITOCHONDRIAL PROTEIN; OXIDOREDUCTASE; TIM22 PROTEIN; UNCLASSIFIED DRUG;

EID: 84874584406     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-09-0649     Document Type: Article
Times cited : (68)

References (60)
  • 1
    • 64049101797 scopus 로고    scopus 로고
    • Structural and functional requirements for activity of the tim9-tim10 complex in mitochondrial protein import
    • Baker MJ, Webb CT, Stroud DA, Palmer CS, Frazier AE, Guiard B, Chacinska A, Gulbis JM, Ryan MT
    • Baker MJ, Webb CT, Stroud DA, Palmer CS, Frazier AE, Guiard B, Chacinska A, Gulbis JM, Ryan MT (2009). Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import. Mol Biol Cell 20, 769-779.
    • (2009) Mol Biol Cell , vol.20 , pp. 769-779
  • 3
    • 78650555680 scopus 로고    scopus 로고
    • Molecular chaperone function of mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import
    • Banci L et al. (2010). Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import. Proc Natl Acad Sci USA 107, 20190-20195.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20190-20195
    • Banci, L.1
  • 5
    • 84858004499 scopus 로고    scopus 로고
    • Mitochondrial protein import: From transport pathways to an integrated network
    • Becker T, Böttinger L, Pfanner N (2012). Mitochondrial protein import: from transport pathways to an integrated network. Trends Biochem Sci 37, 85-91.
    • (2012) Trends Biochem Sci , vol.37 , pp. 85-91
    • Becker, T.1    Böttinger, L.2    Pfanner, N.3
  • 6
    • 77149120128 scopus 로고    scopus 로고
    • Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in erv1 and proofread by glutathione
    • Bien M, Longen S, Wagener N, Chwalla I, Herrmann JM, Riemer J (2010). Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Mol Cell 37, 516-528.
    • (2010) Mol Cell , vol.37 , pp. 516-528
    • Bien, M.1    Longen, S.2    Wagener, N.3    Chwalla, I.4    Herrmann, J.M.5    Riemer, J.6
  • 8
    • 84866091394 scopus 로고    scopus 로고
    • Role of twin cys-xaa9-cys motif cysteines in mitochondrial import of the cytochrome c oxidase biogenesis factor cmc1
    • Bourens M, Dabir DV, Tienson HL, Sorokina I, Koehler CM, Barrientos A (2012). Role of twin Cys-Xaa9-Cys motif cysteines in mitochondrial import of the cytochrome c oxidase biogenesis factor Cmc1. J Biol Chem 287, 31258-31269.
    • (2012) J Biol Chem , vol.287 , pp. 31258-31269
    • Bourens, M.1    Dabir, D.V.2    Tienson, H.L.3    Sorokina, I.4    Koehler, C.M.5    Barrientos, A.6
  • 12
    • 73549085843 scopus 로고    scopus 로고
    • Distinct forms of mitochondrial tom-tim supercomplexes define signal-dependent states of preprotein sorting
    • Chacinska A et al. (2010). Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting. Mol Cell Biol 30, 307-318.
    • (2010) Mol Cell Biol , vol.30 , pp. 307-318
    • Chacinska, A.1
  • 13
    • 0036499987 scopus 로고    scopus 로고
    • The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
    • DOI 10.1093/emboj/21.5.942
    • Curran SP, Leuenberger D, Oppliger W, Koehler CM (2002). The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. EMBO J 21, 942-953. (Pubitemid 34206167)
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 14
    • 33846817047 scopus 로고    scopus 로고
    • The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import
    • DOI 10.1091/mbc.E06-06-0546
    • Davis AJ, Alder NN, Jensen RE, Johnson AE (2007). The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import. Mol Biol Cell 18, 475-486. (Pubitemid 46213217)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.2 , pp. 475-486
    • Davis, A.J.1    Alder, N.N.2    Jensen, R.E.3    Johnson, A.E.4
  • 15
    • 84857643393 scopus 로고    scopus 로고
    • Unresolved mysteries in the biogenesis of mitochondrial membrane proteins
    • Dimmer KS, Rapaport D (2012). Unresolved mysteries in the biogenesis of mitochondrial membrane proteins. Biochim Biophys Acta 1818, 1085-1090.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1085-1090
    • Dimmer, K.S.1    Rapaport, D.2
  • 16
    • 84871792997 scopus 로고    scopus 로고
    • Mitochondrial protein import: Common principles and physiological networks
    • Dudek J, Rehling P, van der Laan M (2013). Mitochondrial protein import: common principles and physiological networks. Biochim Biophys Acta 1833, 274-285.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 274-285
    • Dudek, J.1    Rehling, P.2    Van Der Laan, M.3
  • 17
    • 77957024844 scopus 로고    scopus 로고
    • Structural basis for the disulfide relay system in the mitochondrial intermembrane space
    • Endo T, Yamano K, Kawano S (2010). Structural basis for the disulfide relay system in the mitochondrial intermembrane space. Antioxid Redox Signal 13, 1359-1373.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1359-1373
    • Endo, T.1    Yamano, K.2    Kawano, S.3
  • 18
    • 0033564856 scopus 로고    scopus 로고
    • Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex
    • DOI 10.1093/emboj/18.12.3214
    • Endres M, Neupert W, Brunner M (1999). Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex. EMBO J 18, 3214-3221. (Pubitemid 29276568)
    • (1999) EMBO Journal , vol.18 , Issue.12 , pp. 3214-3221
    • Endres, M.1    Neupert, W.2    Brunner, M.3
  • 20
    • 44649125317 scopus 로고    scopus 로고
    • Assembly of the three small Tim proteins precedes docking to the mitochondrial carrier translocase
    • DOI 10.1038/embor.2008.49, PII EMBOR200849
    • Gebert N, Chacinska A, Wagner K, Guiard B, Koehler CM, Rehling P, Pfanner N, Wiedemann N (2008). Assembly of the three small Tim proteins precedes docking to the mitochondrial carrier translocase. EMBO Rep 9, 548-554. (Pubitemid 351772918)
    • (2008) EMBO Reports , vol.9 , Issue.6 , pp. 548-554
    • Gebert, N.1    Chacinska, A.2    Wagner, K.3    Guiard, B.4    Koehler, C.M.5    Rehling, P.6    Pfanner, N.7    Wiedemann, N.8
  • 21
    • 83455219457 scopus 로고    scopus 로고
    • Dual function of sdh3 in the respiratory chain and tim22 protein translocase of the mitochondrial inner membrane
    • Gebert N et al. (2011). Dual function of Sdh3 in the respiratory chain and TIM22 protein translocase of the mitochondrial inner membrane. Mol Cell 44, 811-818.
    • (2011) Mol Cell , vol.44 , pp. 811-818
    • Gebert, N.1
  • 22
    • 80054711990 scopus 로고    scopus 로고
    • Mitochondrial ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system
    • Gross DP, Burgard CA, Reddehase S, Leitch JM, Culotta VC, Hell K (2011). Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system. Mol Biol Cell 22, 3758-3767.
    • (2011) Mol Biol Cell , vol.22 , pp. 3758-3767
    • Gross, D.P.1    Burgard, C.A.2    Reddehase, S.3    Leitch, J.M.4    Culotta, V.C.5    Hell, K.6
  • 23
    • 38049132624 scopus 로고    scopus 로고
    • Functional characterization of mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space
    • Grumbt B, Stroobant V, Terziyska N, Israel L, Hell K (2007). Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space. J Biol Chem 282, 37461-37470.
    • (2007) J Biol Chem , vol.282 , pp. 37461-37470
    • Grumbt, B.1    Stroobant, V.2    Terziyska, N.3    Israel, L.4    Hell, K.5
  • 24
    • 84856853161 scopus 로고    scopus 로고
    • Mitochondrial disulfide relay: Redox-regulated protein import into the intermembrane space
    • Herrmann JM, Riemer J (2012). Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space. J Biol Chem 287, 4426-4433.
    • (2012) J Biol Chem , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 25
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 Complex of Neurospora crassa Functions in the Assembly of Proteins into Both Mitochondrial Membranes
    • DOI 10.1074/jbc.M313037200
    • Hoppins SC, Nargang FE (2004). The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes. J Biol Chem 279, 12396-12405. (Pubitemid 38445807)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 26
    • 84860154289 scopus 로고    scopus 로고
    • Targeting and maturation of erv1/alr in the mitochondrial intermembrane space
    • Kallergi E et al. (2012). Targeting and maturation of Erv1/ALR in the mitochondrial intermembrane space. ACS Chem Biol 7, 707-714.
    • (2012) ACS Chem Biol , vol.7 , pp. 707-714
    • Kallergi, E.1
  • 28
    • 80054690509 scopus 로고    scopus 로고
    • Mia40-dependent oxidation of cysteines in domain i of ccs1 controls its distribution between mitochondria and the cytosol
    • Klöppel C, Suzuki Y, Kojer K, Petrungaro C, Longen S, Fiedler S, Keller S, Riemer J (2011). Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol. Mol Biol Cell 22, 3749-3757.
    • (2011) Mol Biol Cell , vol.22 , pp. 3749-3757
    • Klöppel, C.1    Suzuki, Y.2    Kojer, K.3    Petrungaro, C.4    Longen, S.5    Fiedler, S.6    Keller, S.7    Riemer, J.8
  • 29
    • 0346687594 scopus 로고    scopus 로고
    • 3C motif
    • DOI 10.1016/j.tibs.2003.11.003
    • Koehler CM (2004). The small Tim proteins and the twin Cx3C motif. Trends Biochem Sci 29, 1-4. (Pubitemid 38068471)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.1 , pp. 1-4
    • Koehler, C.M.1
  • 30
    • 84864119697 scopus 로고    scopus 로고
    • Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the mia40 redox state
    • Kojer K, Bien M, Gangel H, Morgan B, Dick TP, Riemer J (2012). Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state. EMBO J 31, 3169-3182.
    • (2012) EMBO J , vol.31 , pp. 3169-3182
    • Kojer, K.1    Bien, M.2    Gangel, H.3    Morgan, B.4    Dick, T.P.5    Riemer, J.6
  • 31
    • 0032854652 scopus 로고    scopus 로고
    • Biogenesis of Tim proteins of the mitochondrial carrier import pathway: Differential targeting mechanisms and crossing over with the main import pathway
    • Kurz M, Martin H, Rassow J, Pfanner N, Ryan MT (1999). Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathway. Mol Biol Cell 10, 2461-2474. (Pubitemid 29343146)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.7 , pp. 2461-2474
    • Kurz, M.1    Martin, H.2    Rassow, J.3    Pfanner, N.4    Ryan, M.T.5
  • 32
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • DOI 10.1093/embo-reports/kve161
    • Lange H, Lisowsky T, Gerber J, Mühlenhoff U, Kispal G, Lill R (2001). An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep 2, 715-720. (Pubitemid 32798715)
    • (2001) EMBO Reports , vol.2 , Issue.8 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 33
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert LI, Jakob U (2004). Protein thiol modifications visualized in vivo. PLoS Biol 2, e333.
    • (2004) PLoS Biol , vol.2
    • Leichert, L.I.1    Jakob, U.2
  • 36
    • 0035099421 scopus 로고    scopus 로고
    • Protein import channel of the outer mitochondrial membrane: A highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small Tom proteins, and import receptors
    • DOI 10.1128/MCB.21.7.2337-2348.2001
    • Meisinger C, Ryan MT, Hill K, Model K, Lim JH, Sickmann A, Müller H, Meyer HE, Wagner R, Pfanner N (2001). Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors. Mol Cell Biol 21, 2337-2348. (Pubitemid 32222087)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2337-2348
    • Meisinger, C.1    Ryan, M.T.2    Hill, K.3    Model, K.4    Lim, J.H.5    Sickmann, A.6    Muller, H.7    Meyer, H.E.8    Wagner, R.9    Pfanner, N.10
  • 37
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • DOI 10.1016/j.cell.2005.04.011, PII S0092867405003570
    • Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, Herrmann JM (2005). A disulfide relay system in the intermembrane space of mito-chondria that mediates protein import. Cell 121, 1059-1069. (Pubitemid 40884396)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 38
    • 34547929482 scopus 로고    scopus 로고
    • Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: Site-specific recognition of cysteine residues by the intermembrane space receptor Mia40
    • DOI 10.1074/jbc.M703294200
    • Milenkovic D, Gabriel K, Guiard B, Schulze-Specking A, Pfanner N, Chacinska A (2007). Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40. J Biol Chem 282, 22472-22480. (Pubitemid 47267346)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22472-22480
    • Milenkovic, D.1    Gabriel, K.2    Guiard, B.3    Schulze-Specking, A.4    Pfanner, N.5    Chacinska, A.6
  • 40
    • 56349144637 scopus 로고    scopus 로고
    • Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling
    • Mokranjac D, Neupert W (2009). Thirty years of protein translocation into mitochondria: unexpectedly complex and still puzzling. Biochim Biophys Acta 1793, 33-41.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 33-41
    • Mokranjac, D.1    Neupert, W.2
  • 41
    • 38749148392 scopus 로고    scopus 로고
    • Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space
    • DOI 10.1091/mbc.E07-08-0814
    • Müller JM, Milenkovic D, Guiard B, Pfanner N, Chacinska A (2008). Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space. Mol Biol Cell 19, 226-236. (Pubitemid 351186148)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 226-236
    • Muller, J.M.1    Milenkovic, D.2    Guiard, B.3    Pfanner, N.4    Chacinska, A.5
  • 42
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W, Herrmann JM (2007). Translocation of proteins into mitochondria. Annu Rev Biochem 76, 723-749.
    • (2007) Annu Rev Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 44
    • 0037459118 scopus 로고    scopus 로고
    • Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane - A guided tour
    • DOI 10.1016/S0022-2836(02)01440-7
    • Rehling P, Pfanner N, Meisinger C (2003b). Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane -a guided tour. J Mol Biol 326, 639-657. (Pubitemid 36279308)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.3 , pp. 639-657
    • Rehling, P.1    Pfanner, N.2    Meisinger, C.3
  • 46
    • 77956309299 scopus 로고    scopus 로고
    • Oxidative protein folding in the mitochondrial intermembrane space
    • Sideris DP, Tokatlidis K (2010). Oxidative protein folding in the mitochondrial intermembrane space. Antioxid Redox Signal 13, 1189-1204.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1189-1204
    • Sideris, D.P.1    Tokatlidis, K.2
  • 47
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of dna in saccharomyces cerevisiae
    • Sikorski RS, Hieter P (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 48
    • 84861329438 scopus 로고    scopus 로고
    • The mia pathway: A tight bond between protein transport and oxidative folding in mitochondria
    • Stojanovski D, Bragoszewski P, Chacinska A (2012). The MIA pathway: a tight bond between protein transport and oxidative folding in mitochondria. Biochim Biophys Acta 1823, 1142-1150.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 1142-1150
    • Stojanovski, D.1    Bragoszewski, P.2    Chacinska, A.3
  • 50
    • 84873470266 scopus 로고    scopus 로고
    • Disulfide bond formation: Sulfhydryl oxidase alr controls mitochondrial biogenesis of human mia40
    • doi:10.1111/tra.12030
    • Sztolsztener ME, Brewinska A, Guiard B, Chacinska A (2012). Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40. Traffic, doi:10.1111/tra.12030.
    • (2012) Traffic
    • Sztolsztener, M.E.1    Brewinska, A.2    Guiard, B.3    Chacinska, A.4
  • 51
    • 33847726691 scopus 로고    scopus 로고
    • The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway
    • DOI 10.1016/j.febslet.2007.02.014, PII S0014579307001597
    • Terziyska N, Grumbt B, Bien M, Neupert W, Herrmann JM, Hell K (2007). The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway. FEBS Lett 581, 1098-1102. (Pubitemid 46385931)
    • (2007) FEBS Letters , vol.581 , Issue.6 , pp. 1098-1102
    • Terziyska, N.1    Grumbt, B.2    Bien, M.3    Neupert, W.4    Herrmann, J.M.5    Hell, K.6
  • 53
    • 0036840342 scopus 로고    scopus 로고
    • Mitochondrial import of the ADP/ATP carrier: The essential TIM complex of the intermembrane space is required for precursor release from the TOM complex
    • DOI 10.1128/MCB.22.22.7780-7789.2002
    • Truscott KN, Wiedemann N, Rehling P, Müller H, Meisinger C, Pfanner N, Guiard B (2002). Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex. Mol Cell Biol 22, 7780-7789. (Pubitemid 35217289)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.22 , pp. 7780-7789
    • Truscott, K.N.1    Wiedemann, N.2    Rehling, P.3    Muller, H.4    Meisinger, C.5    Pfanner, N.6    Guiard, B.7
  • 55
    • 80054718239 scopus 로고    scopus 로고
    • Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis
    • von der Malsburg K et al. (2011). Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis. Dev Cell 21, 694-707.
    • (2011) Dev Cell , vol.21 , pp. 694-707
    • Von Der Malsburg, K.1
  • 57
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9"10 reveals a six-bladed α-propeller
    • DOI 10.1016/j.molcel.2005.11.010, PII S1097276505017703
    • Webb CT, Gorman MA, Lazarou M, Ryan MT, Gulbis JM (2006). Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller. Mol Cell 21, 123-133. (Pubitemid 43017854)
    • (2006) Molecular Cell , vol.21 , Issue.1 , pp. 123-133
    • Webb, C.T.1    Gorman, M.A.2    Lazarou, M.3    Ryan, M.T.4    Gulbis, J.M.5
  • 58
    • 84869226106 scopus 로고    scopus 로고
    • Atp23 biogenesis reveals a chaperone-like folding activity of mia40 in the ims of mito-chondria
    • Weckbecker D, Longen S, Riemer J, Herrmann JM (2012). Atp23 biogenesis reveals a chaperone-like folding activity of Mia40 in the IMS of mito-chondria. EMBO J 31, 4348-4358.
    • (2012) EMBO J , vol.31 , pp. 4348-4358
    • Weckbecker, D.1    Longen, S.2    Riemer, J.3    Herrmann, J.M.4
  • 59
    • 0035283084 scopus 로고    scopus 로고
    • The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria
    • DOI 10.1093/emboj/20.5.951
    • Wiedemann N, Pfanner N, Ryan MT (2001). The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria. EMBO J 20, 951-960. (Pubitemid 32186786)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 951-960
    • Wiedemann, N.1    Pfanner, N.2    Ryan, M.T.3
  • 60
    • 2442421175 scopus 로고    scopus 로고
    • Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: Intermembrane space components are involved in an early stage of the assembly pathway
    • DOI 10.1074/jbc.M400050200
    • Wiedemann N, Truscott KN, Pfannschmidt S, Guiard B, Meisinger C, Pfanner N (2004). Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway. J Biol Chem 279, 18188-18194. (Pubitemid 38623231)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18188-18194
    • Wiedemann, N.1    Truscott, K.N.2    Pfannschmidt, S.3    Guiard, B.4    Meisinger, C.5    Pfanner, N.6


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