메뉴 건너뛰기




Volumn 1833, Issue 2, 2013, Pages 360-370

Processing peptidases in mitochondria and chloroplasts

Author keywords

Chloroplast; Mitochondria; Mitochondrial disease; Presequence protease; Processing peptidase; Targeting peptide

Indexed keywords

ALANINE; ARGININE; ATP23 PROTEIN; CARBOXY TERMINAL PROCESSING PROTEASE; CARDIOLIPIN; CYCLOOXYGENASE 2; CYTOCHROME C PEROXIDASE; GLUTATHIONE REDUCTASE; GLYCINE; INNER MEMBRANE PEPTIDASE; LEUCINE; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; MITOCHONDRIAL MATRIX ATPASE ASSOCIATED WITH CELLULAR ACTIVITY PROTEASE; MITOCHONDRIAL PROCESSING PEPTIDASE; MITOCHONDRIAL PROTEIN; PROLINE; RHOMBOID PROTEASE; SERINE; STROMAL PROCESSING PEPTIDASE; THYLAKOID PROCESSING PEPTIDASE; UNCLASSIFIED DRUG;

EID: 84871796609     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.03.012     Document Type: Review
Times cited : (152)

References (171)
  • 1
    • 46149095496 scopus 로고    scopus 로고
    • The mitochondrial proteome: from inventory to function
    • Meisinger C., Sickmann A., Pfanner N. The mitochondrial proteome: from inventory to function. Cell 2008, 134:22-24.
    • (2008) Cell , vol.134 , pp. 22-24
    • Meisinger, C.1    Sickmann, A.2    Pfanner, N.3
  • 5
    • 2642578319 scopus 로고    scopus 로고
    • A new approach for plant proteomics: characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry
    • Zabrouskov V., Giacomelli L., van Wijk K.J., McLafferty F.W. A new approach for plant proteomics: characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry. Mol. Cell. Proteomics 2003, 2:1253-1260.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1253-1260
    • Zabrouskov, V.1    Giacomelli, L.2    van Wijk, K.J.3    McLafferty, F.W.4
  • 7
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 2007, 76:723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 8
    • 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. 2010, 11:655-667.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 9
    • 84858004499 scopus 로고    scopus 로고
    • Mitochondrial protein import: from transport pathways to an integrated network
    • Becker T., Bottinger L., Pfanner N. Mitochondrial protein import: from transport pathways to an integrated network. Trends Biochem. Sci. 2012, 37:85-91.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 85-91
    • Becker, T.1    Bottinger, L.2    Pfanner, N.3
  • 10
    • 77953020406 scopus 로고    scopus 로고
    • On the mechanism of preprotein import by the mitochondrial presequence translocase
    • van der Laan M., Hutu D.P., Rehling P. On the mechanism of preprotein import by the mitochondrial presequence translocase. Biochim. Biophys. Acta 2010, 1803:732-739.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 732-739
    • van der Laan, M.1    Hutu, D.P.2    Rehling, P.3
  • 11
    • 0024276898 scopus 로고
    • Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein
    • Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.U., Neupert W. Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell 1988, 53:795-806.
    • (1988) Cell , vol.53 , pp. 795-806
    • Hawlitschek, G.1    Schneider, H.2    Schmidt, B.3    Tropschug, M.4    Hartl, F.U.5    Neupert, W.6
  • 12
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun H.P., Emmermann M., Kruft V., Schmitz U.K. The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J. 1992, 11:3219-3227.
    • (1992) EMBO J. , vol.11 , pp. 3219-3227
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 13
    • 0028177426 scopus 로고
    • Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and protein processing
    • Glaser E., Eriksson A., Sjoling S. Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and protein processing. FEBS Lett. 1994, 346:83-87.
    • (1994) FEBS Lett. , vol.346 , pp. 83-87
    • Glaser, E.1    Eriksson, A.2    Sjoling, S.3
  • 15
    • 84864293849 scopus 로고    scopus 로고
    • Processing of mitochondrial presequences
    • [Electronic publication ahead of print, Dec 7]
    • Mossmann D., Meisinger C., Vogtle F.N. Processing of mitochondrial presequences. Biochim. Biophys. Acta 2012, [Electronic publication ahead of print, Dec 7]. 10.1016/j.bbagrm.2011.11.007.
    • (2012) Biochim. Biophys. Acta
    • Mossmann, D.1    Meisinger, C.2    Vogtle, F.N.3
  • 16
    • 71049136017 scopus 로고    scopus 로고
    • Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55
    • Naamati A., Regev-Rudzki N., Galperin S., Lill R., Pines O. Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J. Biol. Chem. 2009, 284:30200-30208.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30200-30208
    • Naamati, A.1    Regev-Rudzki, N.2    Galperin, S.3    Lill, R.4    Pines, O.5
  • 17
    • 0023663892 scopus 로고
    • Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide
    • Hartl F.U., Ostermann J., Guiard B., Neupert W. Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell 1987, 51:1027-1037.
    • (1987) Cell , vol.51 , pp. 1027-1037
    • Hartl, F.U.1    Ostermann, J.2    Guiard, B.3    Neupert, W.4
  • 18
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari J., Fox T.D., Walter P. A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 1993, 262:1997-2004.
    • (1993) Science , vol.262 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 19
    • 63649088506 scopus 로고    scopus 로고
    • Structure and mechanism of intramembrane protease
    • Ha Y. Structure and mechanism of intramembrane protease. Semin. Cell Dev. Biol. 2009, 20:240-250.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 240-250
    • Ha, Y.1
  • 20
    • 84855240784 scopus 로고    scopus 로고
    • Mitochondrial AAA proteases - Towards a molecular understanding of membrane-bound proteolytic machines
    • Gerdes F., Tatsuta T., Langer T. Mitochondrial AAA proteases - Towards a molecular understanding of membrane-bound proteolytic machines. Biochim. Biophys. Acta 2012, 1823:49-55.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 49-55
    • Gerdes, F.1    Tatsuta, T.2    Langer, T.3
  • 21
    • 33846826875 scopus 로고    scopus 로고
    • Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase
    • Osman C., Wilmes C., Tatsuta T., Langer T. Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase. Mol. Biol. Cell 2007, 18:627-635.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 627-635
    • Osman, C.1    Wilmes, C.2    Tatsuta, T.3    Langer, T.4
  • 22
    • 33846813499 scopus 로고    scopus 로고
    • The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase
    • Zeng X., Neupert W., Tzagoloff A. The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase. Mol. Biol. Cell 2007, 18:617-626.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 617-626
    • Zeng, X.1    Neupert, W.2    Tzagoloff, A.3
  • 23
    • 11144321346 scopus 로고    scopus 로고
    • Mechanisms of protein import and routing in chloroplasts
    • Jarvis P., Robinson C. Mechanisms of protein import and routing in chloroplasts. Curr. Biol. 2004, 14:R1064-R1077.
    • (2004) Curr. Biol. , vol.14
    • Jarvis, P.1    Robinson, C.2
  • 24
    • 78650517733 scopus 로고    scopus 로고
    • Common ground for protein translocation: access control for mitochondria and chloroplasts
    • Schleiff E., Becker T. Common ground for protein translocation: access control for mitochondria and chloroplasts. Nat. Rev. Mol. Cell Biol. 2011, 12:48-59.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 48-59
    • Schleiff, E.1    Becker, T.2
  • 25
    • 79851508389 scopus 로고    scopus 로고
    • Protein import into chloroplasts - how chaperones feature into the game
    • Schwenkert S., Soll J., Bolter B. Protein import into chloroplasts - how chaperones feature into the game. Biochim. Biophys. Acta 2011, 1808:901-911.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 901-911
    • Schwenkert, S.1    Soll, J.2    Bolter, B.3
  • 27
    • 0141994866 scopus 로고    scopus 로고
    • Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal
    • Richter S., Lamppa G.K. Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal. J. Biol. Chem. 2003, 278:39497-39502.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39497-39502
    • Richter, S.1    Lamppa, G.K.2
  • 28
    • 0023646043 scopus 로고
    • Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis
    • Kirwin P.M., Elderfield P.D., Robinson C. Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis. J. Biol. Chem. 1987, 262:16386-16390.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16386-16390
    • Kirwin, P.M.1    Elderfield, P.D.2    Robinson, C.3
  • 29
    • 0024279608 scopus 로고
    • Transport of proteins into chloroplasts. Organization, orientation, and lateral distribution of the plastocyanin processing peptidase in the thylakoid network
    • Kirwin P.M., Elderfield P.D., Williams R.S., Robinson C. Transport of proteins into chloroplasts. Organization, orientation, and lateral distribution of the plastocyanin processing peptidase in the thylakoid network. J. Biol. Chem. 1988, 263:18128-18132.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18128-18132
    • Kirwin, P.M.1    Elderfield, P.D.2    Williams, R.S.3    Robinson, C.4
  • 30
    • 82755193828 scopus 로고    scopus 로고
    • The roles of chloroplast proteases in the biogenesis and maintenance of photosystem II
    • Chi W., Sun X., Zhang L. The roles of chloroplast proteases in the biogenesis and maintenance of photosystem II. Biochim. Biophys. Acta 2012, 1817:239-246.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 239-246
    • Chi, W.1    Sun, X.2    Zhang, L.3
  • 32
    • 33646543361 scopus 로고    scopus 로고
    • The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis
    • Johnson K.A., Bhushan S., Stahl A., Hallberg B.M., Frohn A., Glaser E., Eneqvist T. The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis. EMBO J. 2006, 25:1977-1986.
    • (2006) EMBO J. , vol.25 , pp. 1977-1986
    • Johnson, K.A.1    Bhushan, S.2    Stahl, A.3    Hallberg, B.M.4    Frohn, A.5    Glaser, E.6    Eneqvist, T.7
  • 33
    • 0036828801 scopus 로고    scopus 로고
    • Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants
    • Stahl A., Moberg P., Ytterberg J., Panfilov O., Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E. Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants. J. Biol. Chem. 2002, 277:41931-41939.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41931-41939
    • Stahl, A.1    Moberg, P.2    Ytterberg, J.3    Panfilov, O.4    Brockenhuus Von Lowenhielm, H.5    Nilsson, F.6    Glaser, E.7
  • 35
    • 67650156863 scopus 로고    scopus 로고
    • Refining the definition of plant mitochondrial presequences through analysis of sorting signals, N-terminal modifications, and cleavage motifs
    • Huang S., Taylor N.L., Whelan J., Millar A.H. Refining the definition of plant mitochondrial presequences through analysis of sorting signals, N-terminal modifications, and cleavage motifs. Plant Physiol. 2009, 150:1272-1285.
    • (2009) Plant Physiol. , vol.150 , pp. 1272-1285
    • Huang, S.1    Taylor, N.L.2    Whelan, J.3    Millar, A.H.4
  • 36
    • 0031964126 scopus 로고    scopus 로고
    • Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides
    • Schneider G., Sjoling S., Wallin E., Wrede P., Glaser E., von Heijne G. Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides. Proteins 1998, 30:49-60.
    • (1998) Proteins , vol.30 , pp. 49-60
    • Schneider, G.1    Sjoling, S.2    Wallin, E.3    Wrede, P.4    Glaser, E.5    von Heijne, G.6
  • 37
    • 33745411089 scopus 로고    scopus 로고
    • The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting
    • Bhushan S., Kuhn C., Berglund A.K., Roth C., Glaser E. The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting. FEBS Lett. 2006, 580:3966-3972.
    • (2006) FEBS Lett. , vol.580 , pp. 3966-3972
    • Bhushan, S.1    Kuhn, C.2    Berglund, A.K.3    Roth, C.4    Glaser, E.5
  • 38
    • 0036007390 scopus 로고    scopus 로고
    • Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone
    • Zhang X.P., Glaser E. Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone. Trends Plant Sci. 2002, 7:14-21.
    • (2002) Trends Plant Sci. , vol.7 , pp. 14-21
    • Zhang, X.P.1    Glaser, E.2
  • 39
    • 57749094259 scopus 로고    scopus 로고
    • Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs
    • Lee D.W., Kim J.K., Lee S., Choi S., Kim S., Hwang I. Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs. Plant Cell 2008, 20:1603-1622.
    • (2008) Plant Cell , vol.20 , pp. 1603-1622
    • Lee, D.W.1    Kim, J.K.2    Lee, S.3    Choi, S.4    Kim, S.5    Hwang, I.6
  • 40
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S., Endo T., Kohda D. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell 2000, 100:551-560.
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.6    Endo, T.7    Kohda, D.8
  • 41
    • 1242317038 scopus 로고    scopus 로고
    • NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia
    • Moberg P., Nilsson S., Stahl A., Eriksson A.C., Glaser E., Maler L. NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia. J. Mol. Biol. 2004, 336:1129-1140.
    • (2004) J. Mol. Biol. , vol.336 , pp. 1129-1140
    • Moberg, P.1    Nilsson, S.2    Stahl, A.3    Eriksson, A.C.4    Glaser, E.5    Maler, L.6
  • 43
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • von Heijne G. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 1986, 5:1335-1342.
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • von Heijne, G.1
  • 44
    • 0035852227 scopus 로고    scopus 로고
    • The paradox of plastid transit peptides: conservation of function despite divergence in primary structure
    • Bruce B.D. The paradox of plastid transit peptides: conservation of function despite divergence in primary structure. Biochim. Biophys. Acta 2001, 1541:2-21.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 2-21
    • Bruce, B.D.1
  • 45
    • 0033215007 scopus 로고    scopus 로고
    • A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii
    • Krimm I., Gans P., Hernandez J.F., Arlaud G.J., Lancelin J.M. A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii. Eur. J. Biochem. 1999, 265:171-180.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 171-180
    • Krimm, I.1    Gans, P.2    Hernandez, J.F.3    Arlaud, G.J.4    Lancelin, J.M.5
  • 46
    • 0028281852 scopus 로고
    • NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution
    • Lancelin J.M., Bally I., Arlaud G.J., Blackledge M., Gans P., Stein M., Jacquot J.P. NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett. 1994, 343:261-266.
    • (1994) FEBS Lett. , vol.343 , pp. 261-266
    • Lancelin, J.M.1    Bally, I.2    Arlaud, G.J.3    Blackledge, M.4    Gans, P.5    Stein, M.6    Jacquot, J.P.7
  • 47
    • 0026097503 scopus 로고
    • Chloroplast transit peptides. The perfect random coil?
    • von Heijne G., Nishikawa K. Chloroplast transit peptides. The perfect random coil?. FEBS Lett. 1991, 278:1-3.
    • (1991) FEBS Lett. , vol.278 , pp. 1-3
    • von Heijne, G.1    Nishikawa, K.2
  • 48
    • 70349804290 scopus 로고    scopus 로고
    • Defining the determinants for dual targeting of amino acyl-tRNA synthetases to mitochondria and chloroplasts
    • Berglund A.K., Pujol C., Duchene A.M., Glaser E. Defining the determinants for dual targeting of amino acyl-tRNA synthetases to mitochondria and chloroplasts. J. Mol. Biol. 2009, 393:803-814.
    • (2009) J. Mol. Biol. , vol.393 , pp. 803-814
    • Berglund, A.K.1    Pujol, C.2    Duchene, A.M.3    Glaser, E.4
  • 49
    • 60349127044 scopus 로고    scopus 로고
    • Protein transport in organelles: Dual targeting of proteins to mitochondria and chloroplasts
    • Carrie C., Giraud E., Whelan J. Protein transport in organelles: Dual targeting of proteins to mitochondria and chloroplasts. FEBS J. 2009, 276:1187-1195.
    • (2009) FEBS J. , vol.276 , pp. 1187-1195
    • Carrie, C.1    Giraud, E.2    Whelan, J.3
  • 50
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • Peeters N., Small I. Dual targeting to mitochondria and chloroplasts. Biochim. Biophys. Acta 2001, 1541:54-63.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 52
    • 0034330546 scopus 로고    scopus 로고
    • One RNA polymerase serving two genomes
    • Hedtke B., Borner T., Weihe A. One RNA polymerase serving two genomes. EMBO Rep. 2000, 1:435-440.
    • (2000) EMBO Rep. , vol.1 , pp. 435-440
    • Hedtke, B.1    Borner, T.2    Weihe, A.3
  • 53
    • 0036926941 scopus 로고    scopus 로고
    • N-terminal domain of the dual-targeted pea glutathione reductase signal peptide controls organellar targeting efficiency
    • Rudhe C., Clifton R., Whelan J., Glaser E. N-terminal domain of the dual-targeted pea glutathione reductase signal peptide controls organellar targeting efficiency. J. Mol. Biol. 2002, 324:577-585.
    • (2002) J. Mol. Biol. , vol.324 , pp. 577-585
    • Rudhe, C.1    Clifton, R.2    Whelan, J.3    Glaser, E.4
  • 54
    • 0032169540 scopus 로고    scopus 로고
    • Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation
    • Glaser E., Sjoling S., Tanudji M., Whelan J. Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation. Plant Mol. Biol. 1998, 38:311-338.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 311-338
    • Glaser, E.1    Sjoling, S.2    Tanudji, M.3    Whelan, J.4
  • 55
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou W.J., Ito A., Okazaki H., Omura T. Purification and characterization of a processing protease from rat liver mitochondria. EMBO J. 1989, 8:2605-2612.
    • (1989) EMBO J. , vol.8 , pp. 2605-2612
    • Ou, W.J.1    Ito, A.2    Okazaki, H.3    Omura, T.4
  • 57
    • 0029066902 scopus 로고
    • Are the 'core' proteins of the mitochondrial bc1 complex evolutionary relics of a processing protease?
    • Braun H.P., Schmitz U.K. Are the 'core' proteins of the mitochondrial bc1 complex evolutionary relics of a processing protease?. Trends Biochem. Sci. 1995, 20:171-175.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 171-175
    • Braun, H.P.1    Schmitz, U.K.2
  • 58
    • 0027225845 scopus 로고
    • Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria
    • Emmermann M., Braun H.P., Arretz M., Schmitz U.K. Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria. J. Biol. Chem. 1993, 268:18936-18942.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18936-18942
    • Emmermann, M.1    Braun, H.P.2    Arretz, M.3    Schmitz, U.K.4
  • 59
    • 0028072873 scopus 로고
    • The mitochondrial processing peptidase from potato: a self-processing enzyme encoded by two differentially expressed genes
    • Emmermann M., Braun H.P., Schmitz U.K. The mitochondrial processing peptidase from potato: a self-processing enzyme encoded by two differentially expressed genes. Mol. Gen. Genet. 1994, 245:237-245.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 237-245
    • Emmermann, M.1    Braun, H.P.2    Schmitz, U.K.3
  • 60
    • 0026440343 scopus 로고
    • Mitochondrial processing proteinase: a general processing proteinase of spinach leaf mitochondria is a membrane-bound enzyme
    • Eriksson A.C., Glaser E. Mitochondrial processing proteinase: a general processing proteinase of spinach leaf mitochondria is a membrane-bound enzyme. Biochim. Biophys. Acta 1992, 1140:208-214.
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 208-214
    • Eriksson, A.C.1    Glaser, E.2
  • 61
    • 0028075242 scopus 로고
    • The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing
    • Eriksson A.C., Sjoling S., Glaser E. The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing. Biochim. Biophys. Acta 1994, 1186:221-231.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 221-231
    • Eriksson, A.C.1    Sjoling, S.2    Glaser, E.3
  • 62
    • 0029901654 scopus 로고    scopus 로고
    • Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc1 complex in Spinacia oleracea
    • Eriksson A.C., Sjoling S., Glaser E. Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc1 complex in Spinacia oleracea. J. Bioenerg. Biomembr. 1996, 28:285-292.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 285-292
    • Eriksson, A.C.1    Sjoling, S.2    Glaser, E.3
  • 63
    • 0029953066 scopus 로고    scopus 로고
    • Evidence for a link between translocation and processing during protein import into soybean mitochondria
    • Whelan J., Tanudji M.R., Smith M.K., Day D.A. Evidence for a link between translocation and processing during protein import into soybean mitochondria. Biochim. Biophys. Acta 1996, 1312:48-54.
    • (1996) Biochim. Biophys. Acta , vol.1312 , pp. 48-54
    • Whelan, J.1    Tanudji, M.R.2    Smith, M.K.3    Day, D.A.4
  • 64
    • 0034520360 scopus 로고    scopus 로고
    • Studies on the topology of the protein import channel in relation to the plant mitochondrial processing peptidase integrated into the cytochrome bc1 complex
    • Dessi P., Rudhe C., Glaser E. Studies on the topology of the protein import channel in relation to the plant mitochondrial processing peptidase integrated into the cytochrome bc1 complex. Plant J. 2000, 24:637-644.
    • (2000) Plant J. , vol.24 , pp. 637-644
    • Dessi, P.1    Rudhe, C.2    Glaser, E.3
  • 65
    • 0025053384 scopus 로고
    • Cleavage-site motifs in mitochondrial targeting peptides
    • Gavel Y., von Heijne G. Cleavage-site motifs in mitochondrial targeting peptides. Protein Eng. 1990, 4:33-37.
    • (1990) Protein Eng. , vol.4 , pp. 33-37
    • Gavel, Y.1    von Heijne, G.2
  • 66
    • 0034794778 scopus 로고    scopus 로고
    • Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase
    • Zhang X.P., Sjoling S., Tanudji M., Somogyi L., Andreu D., Eriksson L.E., Graslund A., Whelan J., Glaser E. Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase. Plant J. 2001, 27:427-438.
    • (2001) Plant J. , vol.27 , pp. 427-438
    • Zhang, X.P.1    Sjoling, S.2    Tanudji, M.3    Somogyi, L.4    Andreu, D.5    Eriksson, L.E.6    Graslund, A.7    Whelan, J.8    Glaser, E.9
  • 67
    • 0032055781 scopus 로고    scopus 로고
    • Mitochondrial targeting peptides in plants
    • Sjoling S., Glaser E. Mitochondrial targeting peptides in plants. Trends Plant Sci. 1998, 3:136-140.
    • (1998) Trends Plant Sci. , vol.3 , pp. 136-140
    • Sjoling, S.1    Glaser, E.2
  • 68
    • 0034796437 scopus 로고    scopus 로고
    • Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import
    • Duby G., Oufattole M., Boutry M. Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import. Plant J. 2001, 27:539-549.
    • (2001) Plant J. , vol.27 , pp. 539-549
    • Duby, G.1    Oufattole, M.2    Boutry, M.3
  • 69
    • 4744359136 scopus 로고    scopus 로고
    • Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts
    • Rudhe C., Clifton R., Chew O., Zemam K., Richter S., Lamppa G., Whelan J., Glaser E. Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts. J. Mol. Biol. 2004, 343:639-647.
    • (2004) J. Mol. Biol. , vol.343 , pp. 639-647
    • Rudhe, C.1    Clifton, R.2    Chew, O.3    Zemam, K.4    Richter, S.5    Lamppa, G.6    Whelan, J.7    Glaser, E.8
  • 70
    • 0038832853 scopus 로고    scopus 로고
    • Signals required for the import and processing of the alternative oxidase into mitochondria
    • Tanudji M., Sjoling S., Glaser E., Whelan J. Signals required for the import and processing of the alternative oxidase into mitochondria. J. Biol. Chem. 1999, 274:1286-1293.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1286-1293
    • Tanudji, M.1    Sjoling, S.2    Glaser, E.3    Whelan, J.4
  • 71
    • 0028787643 scopus 로고
    • Conversion of a nonprocessed mitochondrial precursor protein into one that is processed by the mitochondrial processing peptidase
    • Waltner M., Weiner H. Conversion of a nonprocessed mitochondrial precursor protein into one that is processed by the mitochondrial processing peptidase. J. Biol. Chem. 1995, 270:26311-26317.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26311-26317
    • Waltner, M.1    Weiner, H.2
  • 72
    • 0034940401 scopus 로고    scopus 로고
    • Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
    • Taylor A.B., Smith B.S., Kitada S., Kojima K., Miyaura H., Otwinowski Z., Ito A., Deisenhofer J. Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Structure 2001, 9:615-625.
    • (2001) Structure , vol.9 , pp. 615-625
    • Taylor, A.B.1    Smith, B.S.2    Kitada, S.3    Kojima, K.4    Miyaura, H.5    Otwinowski, Z.6    Ito, A.7    Deisenhofer, J.8
  • 73
    • 0025821619 scopus 로고
    • Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
    • Isaya G., Kalousek F., Fenton W.A., Rosenberg L.E. Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide. J. Cell Biol. 1991, 113:65-76.
    • (1991) J. Cell Biol. , vol.113 , pp. 65-76
    • Isaya, G.1    Kalousek, F.2    Fenton, W.A.3    Rosenberg, L.E.4
  • 74
    • 0026639993 scopus 로고
    • Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue
    • Isaya G., Kalousek F., Rosenberg L.E. Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:8317-8321.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8317-8321
    • Isaya, G.1    Kalousek, F.2    Rosenberg, L.E.3
  • 75
    • 0026657150 scopus 로고
    • Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase
    • Isaya G., Kalousek F., Rosenberg L.E. Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase. J. Biol. Chem. 1992, 267:7904-7910.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7904-7910
    • Isaya, G.1    Kalousek, F.2    Rosenberg, L.E.3
  • 76
    • 0026638856 scopus 로고
    • Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization
    • Kalousek F., Isaya G., Rosenberg L.E. Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization. EMBO J. 1992, 11:2803-2809.
    • (1992) EMBO J. , vol.11 , pp. 2803-2809
    • Kalousek, F.1    Isaya, G.2    Rosenberg, L.E.3
  • 77
    • 0028049547 scopus 로고
    • MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae
    • Isaya G., Miklos D., Rollins R.A. MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae. Mol. Cell. Biol. 1994, 14:5603-5616.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5603-5616
    • Isaya, G.1    Miklos, D.2    Rollins, R.A.3
  • 78
    • 0028866991 scopus 로고
    • Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase
    • Branda S.S., Isaya G. Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase. J. Biol. Chem. 1995, 270:27366-27373.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27366-27373
    • Branda, S.S.1    Isaya, G.2
  • 79
    • 79959871792 scopus 로고    scopus 로고
    • Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization
    • Vogtle F.N., Prinz C., Kellermann J., Lottspeich F., Pfanner N., Meisinger C. Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization. Mol. Biol. Cell 2011, 22:2135-2143.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2135-2143
    • Vogtle, F.N.1    Prinz, C.2    Kellermann, J.3    Lottspeich, F.4    Pfanner, N.5    Meisinger, C.6
  • 80
    • 0024688488 scopus 로고
    • Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • Hendrick J.P., Hodges P.E., Rosenberg L.E. Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc. Natl. Acad. Sci. U.S.A. 1989, 86:4056-4060.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 81
    • 84859863110 scopus 로고    scopus 로고
    • Proteolytic system of plant mitochondria
    • [Electronic publication ahead of print, Nov 15.]
    • Kwasniak M., Pogorzelec L., Migdal I., Smakowska E., Janska H. Proteolytic system of plant mitochondria. Physiol. Plant. 2012, [Electronic publication ahead of print, Nov 15.]. 10.1111/j.1399-3054.2011.01542.x.
    • (2012) Physiol. Plant.
    • Kwasniak, M.1    Pogorzelec, L.2    Migdal, I.3    Smakowska, E.4    Janska, H.5
  • 84
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 1986, 234:179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 85
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Sci. 2011, 8:1298-1345.
    • (2011) Protein Sci. , vol.8 , pp. 1298-1345
    • Varshavsky, A.1
  • 86
    • 77951567636 scopus 로고    scopus 로고
    • The bacterial N-end rule pathway: expect the unexpected
    • Dougan D.A., Truscott K.N., Zeth K. The bacterial N-end rule pathway: expect the unexpected. Mol. Microbiol. 2010, 76:545-558.
    • (2010) Mol. Microbiol. , vol.76 , pp. 545-558
    • Dougan, D.A.1    Truscott, K.N.2    Zeth, K.3
  • 87
    • 80054958053 scopus 로고    scopus 로고
    • The N-end rule pathway: emerging functions and molecular principles of substrate recognition
    • Sriram S.M., Kim B.Y., Kwon Y.T. The N-end rule pathway: emerging functions and molecular principles of substrate recognition. Nat. Rev. Mol. Cell Biol. 2011, 12:735-747.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 735-747
    • Sriram, S.M.1    Kim, B.Y.2    Kwon, Y.T.3
  • 88
    • 76649093912 scopus 로고    scopus 로고
    • Degradation of an intramitochondrial protein by the cytosolic proteasome
    • Azzu V., Brand M.D. Degradation of an intramitochondrial protein by the cytosolic proteasome. J. Cell Sci. 2010, 123:578-585.
    • (2010) J. Cell Sci. , vol.123 , pp. 578-585
    • Azzu, V.1    Brand, M.D.2
  • 90
    • 84859844774 scopus 로고    scopus 로고
    • A novel mitochondrial and chloroplast peptidasome, PreP
    • [Electronic publication ahead of print, Oct 13]
    • Kmiec B., Glaser E. A novel mitochondrial and chloroplast peptidasome, PreP. Physiol. Plant. 2011, [Electronic publication ahead of print, Oct 13]. 10.1111/j.1399-3054.2011.01531.x.
    • (2011) Physiol. Plant.
    • Kmiec, B.1    Glaser, E.2
  • 91
    • 0028157227 scopus 로고
    • Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15)
    • Buchler M., Tisljar U., Wolf D.H. Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur. J. Biochem. 1994, 219:627-639.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 627-639
    • Buchler, M.1    Tisljar, U.2    Wolf, D.H.3
  • 92
    • 21244505013 scopus 로고    scopus 로고
    • Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria
    • Kambacheld M., Augustin S., Tatsuta T., Muller S., Langer T. Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J. Biol. Chem. 2005, 280:20132-20139.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20132-20139
    • Kambacheld, M.1    Augustin, S.2    Tatsuta, T.3    Muller, S.4    Langer, T.5
  • 94
    • 0033804253 scopus 로고    scopus 로고
    • Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2
    • Jan P.S., Esser K., Pratje E., Michaelis G. Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2. Mol. Gen. Genet. 2000, 263:483-491.
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 483-491
    • Jan, P.S.1    Esser, K.2    Pratje, E.3    Michaelis, G.4
  • 95
    • 0033621457 scopus 로고    scopus 로고
    • Signal peptides having standard and nonstandard cleavage sites can be processed by Imp1p of the mitochondrial inner membrane protease
    • Chen X., Van Valkenburgh C., Fang H., Green N. Signal peptides having standard and nonstandard cleavage sites can be processed by Imp1p of the mitochondrial inner membrane protease. J. Biol. Chem. 1999, 274:37750-37754.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37750-37754
    • Chen, X.1    Van Valkenburgh, C.2    Fang, H.3    Green, N.4
  • 96
    • 3142712428 scopus 로고    scopus 로고
    • The mitochondrial IMP peptidase of yeast: functional analysis of domains and identification of Gut2 as a new natural substrate
    • Esser K., Jan P.S., Pratje E., Michaelis G. The mitochondrial IMP peptidase of yeast: functional analysis of domains and identification of Gut2 as a new natural substrate. Mol. Genet. Genomics 2004, 271:616-626.
    • (2004) Mol. Genet. Genomics , vol.271 , pp. 616-626
    • Esser, K.1    Jan, P.S.2    Pratje, E.3    Michaelis, G.4
  • 98
    • 33646554209 scopus 로고    scopus 로고
    • Substrate specificity of inner membrane peptidase in yeast mitochondria
    • Luo W., Fang H., Green N. Substrate specificity of inner membrane peptidase in yeast mitochondria. Mol. Genet. Genomics 2006, 275:431-436.
    • (2006) Mol. Genet. Genomics , vol.275 , pp. 431-436
    • Luo, W.1    Fang, H.2    Green, N.3
  • 100
    • 77956391459 scopus 로고    scopus 로고
    • Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35
    • Potting C., Wilmes C., Engmann T., Osman C., Langer T. Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J. 2010, 29:2888-2898.
    • (2010) EMBO J. , vol.29 , pp. 2888-2898
    • Potting, C.1    Wilmes, C.2    Engmann, T.3    Osman, C.4    Langer, T.5
  • 101
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases
    • Koppen M., Langer T. Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Crit. Rev. Biochem. Mol. Biol. 2007, 42:221-242.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 221-242
    • Koppen, M.1    Langer, T.2
  • 102
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • Arlt H., Tauer R., Feldmann H., Neupert W., Langer T. The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 1996, 85:875-885.
    • (1996) Cell , vol.85 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 103
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • Nolden M., Ehses S., Koppen M., Bernacchia A., Rugarli E.I., Langer T. The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 2005, 123:277-289.
    • (2005) Cell , vol.123 , pp. 277-289
    • Nolden, M.1    Ehses, S.2    Koppen, M.3    Bernacchia, A.4    Rugarli, E.I.5    Langer, T.6
  • 104
    • 79960047807 scopus 로고    scopus 로고
    • Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria
    • Bonn F., Tatsuta T., Petrungaro C., Riemer J., Langer T. Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria. EMBO J. 2011, 30:2545-2556.
    • (2011) EMBO J. , vol.30 , pp. 2545-2556
    • Bonn, F.1    Tatsuta, T.2    Petrungaro, C.3    Riemer, J.4    Langer, T.5
  • 107
    • 70350230142 scopus 로고    scopus 로고
    • Autocatalytic processing of m-AAA protease subunits in mitochondria
    • Koppen M., Bonn F., Ehses S., Langer T. Autocatalytic processing of m-AAA protease subunits in mitochondria. Mol. Biol. Cell 2009, 20:4216-4224.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4216-4224
    • Koppen, M.1    Bonn, F.2    Ehses, S.3    Langer, T.4
  • 108
    • 77951246247 scopus 로고    scopus 로고
    • Identification and characterization of high molecular weight complexes formed by matrix AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana
    • Piechota J., Kolodziejczak M., Juszczak I., Sakamoto W., Janska H. Identification and characterization of high molecular weight complexes formed by matrix AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana. J. Biol. Chem. 2010, 285:12512-12521.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12512-12521
    • Piechota, J.1    Kolodziejczak, M.2    Juszczak, I.3    Sakamoto, W.4    Janska, H.5
  • 109
    • 74349127184 scopus 로고    scopus 로고
    • Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis
    • Urban S. Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis. Biochem. J. 2010, 425:501-512.
    • (2010) Biochem. J. , vol.425 , pp. 501-512
    • Urban, S.1
  • 110
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban G.A., Saurya S., Freeman M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 2003, 423:537-541.
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 111
    • 0037604567 scopus 로고    scopus 로고
    • A mitochondrial rhomboid protease
    • van der Bliek A.M., Koehler C.M. A mitochondrial rhomboid protease. Dev. Cell 2003, 4:769-770.
    • (2003) Dev. Cell , vol.4 , pp. 769-770
    • van der Bliek, A.M.1    Koehler, C.M.2
  • 112
    • 0036424840 scopus 로고    scopus 로고
    • A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1
    • Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E. A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J. Mol. Biol. 2002, 323:835-843.
    • (2002) J. Mol. Biol. , vol.323 , pp. 835-843
    • Esser, K.1    Tursun, B.2    Ingenhoven, M.3    Michaelis, G.4    Pratje, E.5
  • 113
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan M., Vogel F., Bornhovd C., Neupert W., Reichert A.S. Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 2003, 278:27781-27788.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 114
    • 77955085749 scopus 로고    scopus 로고
    • Intramembrane proteolysis of Mgm1 by the mitochondrial rhomboid protease is highly promiscuous regarding the sequence of the cleaved hydrophobic segment
    • Schafer A., Zick M., Kief J., Steger M., Heide H., Duvezin-Caubet S., Neupert W., Reichert A.S. Intramembrane proteolysis of Mgm1 by the mitochondrial rhomboid protease is highly promiscuous regarding the sequence of the cleaved hydrophobic segment. J. Mol. Biol. 2010, 401:182-193.
    • (2010) J. Mol. Biol. , vol.401 , pp. 182-193
    • Schafer, A.1    Zick, M.2    Kief, J.3    Steger, M.4    Heide, H.5    Duvezin-Caubet, S.6    Neupert, W.7    Reichert, A.S.8
  • 115
    • 48149115851 scopus 로고    scopus 로고
    • Plant mitochondrial rhomboid, AtRBL12, has different substrate specificity from its yeast counterpart
    • Kmiec-Wisniewska B., Krumpe K., Urantowka A., Sakamoto W., Pratje E., Janska H. Plant mitochondrial rhomboid, AtRBL12, has different substrate specificity from its yeast counterpart. Plant Mol. Biol. 2008, 68:159-171.
    • (2008) Plant Mol. Biol. , vol.68 , pp. 159-171
    • Kmiec-Wisniewska, B.1    Krumpe, K.2    Urantowka, A.3    Sakamoto, W.4    Pratje, E.5    Janska, H.6
  • 116
    • 77955280924 scopus 로고    scopus 로고
    • The PARL family of mitochondrial rhomboid proteases
    • Hill R.B., Pellegrini L. The PARL family of mitochondrial rhomboid proteases. Semin. Cell Dev. Biol. 2010, 21:582-592.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 582-592
    • Hill, R.B.1    Pellegrini, L.2
  • 117
    • 80052418295 scopus 로고    scopus 로고
    • Cytosolic HSP90 cochaperones HOP and FKBP interact with freshly synthesized chloroplast preproteins of Arabidopsis
    • Fellerer C., Schweiger R., Schongruber K., Soll J., Schwenkert S. Cytosolic HSP90 cochaperones HOP and FKBP interact with freshly synthesized chloroplast preproteins of Arabidopsis. Mol. Plant 2010, 4:1133-1145.
    • (2010) Mol. Plant , vol.4 , pp. 1133-1145
    • Fellerer, C.1    Schweiger, R.2    Schongruber, K.3    Soll, J.4    Schwenkert, S.5
  • 119
    • 84856658975 scopus 로고    scopus 로고
    • The phosphorylation state of chloroplast transit peptides regulates preprotein import
    • Lamberti G., Drurey C., Soll J., Schwenkert S. The phosphorylation state of chloroplast transit peptides regulates preprotein import. Plant Signal. Behav. 2010, 6.
    • (2010) Plant Signal. Behav. , vol.6
    • Lamberti, G.1    Drurey, C.2    Soll, J.3    Schwenkert, S.4
  • 120
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants
    • May T., Soll J. 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell 2000, 12:53-64.
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soll, J.2
  • 121
    • 0026495086 scopus 로고
    • Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast
    • Oblong J.E., Lamppa G.K. Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast. EMBO J. 1992, 11:4401-4409.
    • (1992) EMBO J. , vol.11 , pp. 4401-4409
    • Oblong, J.E.1    Lamppa, G.K.2
  • 122
    • 0032560485 scopus 로고    scopus 로고
    • A chloroplast processing enzyme functions as the general stromal processing peptidase
    • Richter S., Lamppa G.K. A chloroplast processing enzyme functions as the general stromal processing peptidase. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:7463-7468.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7463-7468
    • Richter, S.1    Lamppa, G.K.2
  • 123
    • 0345611654 scopus 로고
    • A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases
    • VanderVere P.S., Bennett T.M., Oblong J.E., Lamppa G.K. A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:7177-7181.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7177-7181
    • VanderVere, P.S.1    Bennett, T.M.2    Oblong, J.E.3    Lamppa, G.K.4
  • 124
    • 0033523765 scopus 로고    scopus 로고
    • Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts
    • Richter S., Lamppa G.K. Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts. J. Cell Biol. 1999, 147:33-44.
    • (1999) J. Cell Biol. , vol.147 , pp. 33-44
    • Richter, S.1    Lamppa, G.K.2
  • 125
    • 0037113996 scopus 로고    scopus 로고
    • Determinants for removal and degradation of transit peptides of chloroplast precursor proteins
    • Richter S., Lamppa G.K. Determinants for removal and degradation of transit peptides of chloroplast precursor proteins. J. Biol. Chem. 2002, 277:43888-43894.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43888-43894
    • Richter, S.1    Lamppa, G.K.2
  • 126
    • 0344668824 scopus 로고    scopus 로고
    • Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts
    • Moberg P., Stahl A., Bhushan S., Wright S.J., Eriksson A., Bruce B.D., Glaser E. Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts. Plant J. 2003, 36:616-628.
    • (2003) Plant J. , vol.36 , pp. 616-628
    • Moberg, P.1    Stahl, A.2    Bhushan, S.3    Wright, S.J.4    Eriksson, A.5    Bruce, B.D.6    Glaser, E.7
  • 127
    • 70350242932 scopus 로고    scopus 로고
    • Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana
    • Nilsson Cederholm S., Backman H.G., Pesaresi P., Leister D., Glaser E. Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana. Plant Mol. Biol. 2009, 71:497-508.
    • (2009) Plant Mol. Biol. , vol.71 , pp. 497-508
    • Nilsson Cederholm, S.1    Backman, H.G.2    Pesaresi, P.3    Leister, D.4    Glaser, E.5
  • 128
    • 0037742342 scopus 로고    scopus 로고
    • A pea antisense gene for the chloroplast stromal processing peptidase yields seedling lethals in Arabidopsis: survivors show defective GFP import in vivo
    • Zhong R., Wan J., Jin R., Lamppa G. A pea antisense gene for the chloroplast stromal processing peptidase yields seedling lethals in Arabidopsis: survivors show defective GFP import in vivo. Plant J. 2003, 34:802-812.
    • (2003) Plant J. , vol.34 , pp. 802-812
    • Zhong, R.1    Wan, J.2    Jin, R.3    Lamppa, G.4
  • 129
    • 77949376178 scopus 로고    scopus 로고
    • A rice stromal processing peptidase regulates chloroplast and root development
    • Yue R., Wang X., Chen J., Ma X., Zhang H., Mao C., Wu P. A rice stromal processing peptidase regulates chloroplast and root development. Plant Cell Physiol. 2010, 51:475-485.
    • (2010) Plant Cell Physiol. , vol.51 , pp. 475-485
    • Yue, R.1    Wang, X.2    Chen, J.3    Ma, X.4    Zhang, H.5    Mao, C.6    Wu, P.7
  • 130
    • 80051684816 scopus 로고    scopus 로고
    • The stromal processing peptidase of chloroplasts is essential in Arabidopsis, with knockout mutations causing embryo arrest after the 16-cell stage
    • Trosch R., Jarvis P. The stromal processing peptidase of chloroplasts is essential in Arabidopsis, with knockout mutations causing embryo arrest after the 16-cell stage. PLoS One 2011, 6:e23039.
    • (2011) PLoS One , vol.6
    • Trosch, R.1    Jarvis, P.2
  • 131
    • 0025830411 scopus 로고
    • Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions
    • Shackleton J.B., Robinson C. Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. J. Biol. Chem. 1991, 266:12152-12156.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12152-12156
    • Shackleton, J.B.1    Robinson, C.2
  • 132
    • 0022763140 scopus 로고
    • The role of the transit peptide in the routing of precursors toward different chloroplast compartments
    • Smeekens S., Bauerle C., Hageman J., Keegstra K., Weisbeek P. The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell 1986, 46:365-375.
    • (1986) Cell , vol.46 , pp. 365-375
    • Smeekens, S.1    Bauerle, C.2    Hageman, J.3    Keegstra, K.4    Weisbeek, P.5
  • 133
    • 18844442890 scopus 로고    scopus 로고
    • The Tat pathway in bacteria and chloroplasts (review)
    • Muller M., Klosgen R.B. The Tat pathway in bacteria and chloroplasts (review). Mol. Membr. Biol. 2005, 22:113-121.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 113-121
    • Muller, M.1    Klosgen, R.B.2
  • 134
    • 0028519276 scopus 로고
    • Targeting of proteins into and across the thylakoid membrane-a multitude of mechanisms
    • Robinson C., Klosgen R.B. Targeting of proteins into and across the thylakoid membrane-a multitude of mechanisms. Plant Mol. Biol. 1994, 26:15-24.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 15-24
    • Robinson, C.1    Klosgen, R.B.2
  • 136
    • 84866912780 scopus 로고    scopus 로고
    • Protein Traffic in Gram-negative bacteria - How exported and secreted proteins find their way
    • [Electronic publication ahead of print, Jan 17]
    • Dalbey R.E., Kuhn A. Protein Traffic in Gram-negative bacteria - How exported and secreted proteins find their way. FEMS Microbiol. Rev. 2012, [Electronic publication ahead of print, Jan 17]. 10.1111/j.1574-6976.2012.00327.x.
    • (2012) FEMS Microbiol. Rev.
    • Dalbey, R.E.1    Kuhn, A.2
  • 137
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey R.E., Lively M.O., Bron S., van Dijl J.M. The chemistry and enzymology of the type I signal peptidases. Protein Sci. 1997, 6:1129-1138.
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    van Dijl, J.M.4
  • 138
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes-a new protease family
    • Dalbey R.E., Von Heijne G. Signal peptidases in prokaryotes and eukaryotes-a new protease family. Trends Biochem. Sci. 1992, 17:474-478.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 139
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G., Steppuhn J., Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 1989, 180:535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 140
    • 0026316318 scopus 로고
    • Transport of proteins into chloroplasts. Delineation of envelope "transit" and thylakoid "transfer" signals within the pre-sequences of three imported thylakoid lumen proteins
    • Bassham D.C., Bartling D., Mould R.M., Dunbar B., Weisbeek P., Herrmann R.G., Robinson C. Transport of proteins into chloroplasts. Delineation of envelope "transit" and thylakoid "transfer" signals within the pre-sequences of three imported thylakoid lumen proteins. J. Biol. Chem. 1991, 266:23606-23610.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23606-23610
    • Bassham, D.C.1    Bartling, D.2    Mould, R.M.3    Dunbar, B.4    Weisbeek, P.5    Herrmann, R.G.6    Robinson, C.7
  • 141
    • 84860180844 scopus 로고    scopus 로고
    • Keep the balloon deflated: the significance of protein maturation for thylakoid flattening
    • Endow J.K., Ruppel N.J., Inoue K. Keep the balloon deflated: the significance of protein maturation for thylakoid flattening. Plant Signal. Behav. 2010, 5:721-723.
    • (2010) Plant Signal. Behav. , vol.5 , pp. 721-723
    • Endow, J.K.1    Ruppel, N.J.2    Inoue, K.3
  • 142
    • 27744459930 scopus 로고    scopus 로고
    • Complete maturation of the plastid protein translocation channel requires a type I signal peptidase
    • Inoue K., Baldwin A.J., Shipman R.L., Matsui K., Theg S.M., Ohme-Takagi M. Complete maturation of the plastid protein translocation channel requires a type I signal peptidase. J. Cell Biol. 2005, 171:425-430.
    • (2005) J. Cell Biol. , vol.171 , pp. 425-430
    • Inoue, K.1    Baldwin, A.J.2    Shipman, R.L.3    Matsui, K.4    Theg, S.M.5    Ohme-Takagi, M.6
  • 143
    • 80455174456 scopus 로고    scopus 로고
    • Functional diversification of thylakoidal processing peptidases in Arabidopsis thaliana
    • Hsu S.C., Endow J.K., Ruppel N.J., Roston R.L., Baldwin A.J., Inoue K. Functional diversification of thylakoidal processing peptidases in Arabidopsis thaliana. PLoS One 2011, 6:e27258.
    • (2011) PLoS One , vol.6
    • Hsu, S.C.1    Endow, J.K.2    Ruppel, N.J.3    Roston, R.L.4    Baldwin, A.J.5    Inoue, K.6
  • 144
    • 0024296902 scopus 로고
    • COOH-terminal processing of polypeptide D1 of the photosystem II reaction center of Scenedesmus obliquus is necessary for the assembly of the oxygen-evolving complex
    • Diner B.A., Ries D.F., Cohen B.N., Metz J.G. COOH-terminal processing of polypeptide D1 of the photosystem II reaction center of Scenedesmus obliquus is necessary for the assembly of the oxygen-evolving complex. J. Biol. Chem. 1988, 263:8972-8980.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8972-8980
    • Diner, B.A.1    Ries, D.F.2    Cohen, B.N.3    Metz, J.G.4
  • 145
    • 0029786970 scopus 로고    scopus 로고
    • Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants
    • Oelmuller R., Herrmann R.G., Pakrasi H.B. Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants. J. Biol. Chem. 1996, 271:21848-21852.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21848-21852
    • Oelmuller, R.1    Herrmann, R.G.2    Pakrasi, H.B.3
  • 146
    • 0026513218 scopus 로고
    • Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini
    • Silber K.R., Keiler K.C., Sauer R.T. Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:295-299.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 295-299
    • Silber, K.R.1    Keiler, K.C.2    Sauer, R.T.3
  • 147
  • 148
    • 0035831546 scopus 로고    scopus 로고
    • Overexpression and characterization of carboxyl-terminal processing protease for precursor D1 protein: regulation of enzyme-substrate interaction by molecular environments
    • Yamamoto Y., Inagaki N., Satoh K. Overexpression and characterization of carboxyl-terminal processing protease for precursor D1 protein: regulation of enzyme-substrate interaction by molecular environments. J. Biol. Chem. 2001, 276:7518-7525.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7518-7525
    • Yamamoto, Y.1    Inagaki, N.2    Satoh, K.3
  • 150
    • 0027978980 scopus 로고
    • Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import
    • Hugosson M., Andreu D., Boman H.G., Glaser E. Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import. Eur. J. Biochem. 1994, 223:1027-1033.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1027-1033
    • Hugosson, M.1    Andreu, D.2    Boman, H.G.3    Glaser, E.4
  • 151
    • 0028238446 scopus 로고
    • Effects of amphipathic peptides, including presequences, on the functional integrity of rat liver mitochondrial membranes
    • Nicolay K., Laterveer F.D., van Heerde W.L. Effects of amphipathic peptides, including presequences, on the functional integrity of rat liver mitochondrial membranes. J. Bioenerg. Biomembr. 1994, 26:327-334.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 327-334
    • Nicolay, K.1    Laterveer, F.D.2    van Heerde, W.L.3
  • 152
    • 0026042255 scopus 로고
    • Lipid-peptide interactions between fragments of the transit peptide of ribulose-1,5-bisphosphate carboxylase/oxygenase and chloroplast membrane lipids
    • Van't Hof R., Demel R.A., Keegstra K., de Kruijff B. Lipid-peptide interactions between fragments of the transit peptide of ribulose-1,5-bisphosphate carboxylase/oxygenase and chloroplast membrane lipids. FEBS Lett. 1991, 291:350-354.
    • (1991) FEBS Lett. , vol.291 , pp. 350-354
    • Van't Hof, R.1    Demel, R.A.2    Keegstra, K.3    de Kruijff, B.4
  • 153
    • 0026487057 scopus 로고
    • Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence
    • Zardeneta G., Horowitz P.M. Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence. J. Biol. Chem. 1992, 267:24193-24198.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24193-24198
    • Zardeneta, G.1    Horowitz, P.M.2
  • 154
    • 33846700429 scopus 로고    scopus 로고
    • Intracellular peptide transporters in human-compartmentalization of the "peptidome"
    • Herget M., Tampe R. Intracellular peptide transporters in human-compartmentalization of the "peptidome". Pflugers Arch. 2007, 453:591-600.
    • (2007) Pflugers Arch. , vol.453 , pp. 591-600
    • Herget, M.1    Tampe, R.2
  • 155
    • 0035896360 scopus 로고    scopus 로고
    • Role of the ABC transporter Mdl1 in peptide export from mitochondria
    • Young L., Leonhard K., Tatsuta T., Trowsdale J., Langer T. Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 2001, 291:2135-2138.
    • (2001) Science , vol.291 , pp. 2135-2138
    • Young, L.1    Leonhard, K.2    Tatsuta, T.3    Trowsdale, J.4    Langer, T.5
  • 156
    • 77953772172 scopus 로고    scopus 로고
    • The organellar peptidasome, PreP: A journey from Arabidopsis to Alzheimer's disease
    • Glaser E., Alikhani N. The organellar peptidasome, PreP: A journey from Arabidopsis to Alzheimer's disease. Biochim. Biophys. Acta 2010, 1797:1076-1080.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1076-1080
    • Glaser, E.1    Alikhani, N.2
  • 157
    • 0032994294 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases
    • Mzhavia N., Berman Y.L., Qian Y., Yan L., Devi L.A. Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases. DNA Cell Biol. 1999, 18:369-380.
    • (1999) DNA Cell Biol. , vol.18 , pp. 369-380
    • Mzhavia, N.1    Berman, Y.L.2    Qian, Y.3    Yan, L.4    Devi, L.A.5
  • 161
    • 0025735353 scopus 로고
    • The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein
    • Yang M.J., Geli V., Oppliger W., Suda K., James P., Schatz G. The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein. J. Biol. Chem. 1991, 266:6416-6423.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6416-6423
    • Yang, M.J.1    Geli, V.2    Oppliger, W.3    Suda, K.4    James, P.5    Schatz, G.6
  • 162
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 2005, 39:359-407.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 163
    • 0032970156 scopus 로고    scopus 로고
    • Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiae
    • Branda S.S., Yang Z.Y., Chew A., Isaya G. Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiae. Hum. Mol. Genet. 1999, 8:1099-1110.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1099-1110
    • Branda, S.S.1    Yang, Z.Y.2    Chew, A.3    Isaya, G.4
  • 164
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates
    • Cavadini P., Adamec J., Taroni F., Gakh O., Isaya G. Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates. J. Biol. Chem. 2000, 275:41469-41475.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41469-41475
    • Cavadini, P.1    Adamec, J.2    Taroni, F.3    Gakh, O.4    Isaya, G.5
  • 165
    • 0034969491 scopus 로고    scopus 로고
    • Friedreich ataxia: from GAA triplet-repeat expansion to frataxin deficiency
    • Patel P.I., Isaya G. Friedreich ataxia: from GAA triplet-repeat expansion to frataxin deficiency. Am. J. Hum. Genet. 2001, 69:15-24.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 15-24
    • Patel, P.I.1    Isaya, G.2
  • 166
    • 79956304666 scopus 로고    scopus 로고
    • Translocation breakpoint at 7q31 associated with tics: further evidence for IMMP2L as a candidate gene for Tourette syndrome
    • Patel C., Cooper-Charles L., McMullan D.J., Walker J.M., Davison V., Morton J. Translocation breakpoint at 7q31 associated with tics: further evidence for IMMP2L as a candidate gene for Tourette syndrome. Eur. J. Hum. Genet. 2011, 19:634-639.
    • (2011) Eur. J. Hum. Genet. , vol.19 , pp. 634-639
    • Patel, C.1    Cooper-Charles, L.2    McMullan, D.J.3    Walker, J.M.4    Davison, V.5    Morton, J.6
  • 167
    • 79960014270 scopus 로고    scopus 로고
    • The PARLance of Parkinson disease
    • McQuibban G.A., Bulman D.E. The PARLance of Parkinson disease. Autophagy 2011, 7:790-792.
    • (2011) Autophagy , vol.7 , pp. 790-792
    • McQuibban, G.A.1    Bulman, D.E.2
  • 168
    • 80155167229 scopus 로고    scopus 로고
    • Decreased proteolytic activity of the mitochondrial amyloid-beta degrading enzyme, PreP peptidasome, in Alzheimer's disease brain mitochondria
    • Alikhani N., Guo L., Yan S., Du H., Pinho C.M., Chen J.X., Glaser E., Yan S.S. Decreased proteolytic activity of the mitochondrial amyloid-beta degrading enzyme, PreP peptidasome, in Alzheimer's disease brain mitochondria. J. Alzheimers Dis. 2011, 27:75-87.
    • (2011) J. Alzheimers Dis. , vol.27 , pp. 75-87
    • Alikhani, N.1    Guo, L.2    Yan, S.3    Du, H.4    Pinho, C.M.5    Chen, J.X.6    Glaser, E.7    Yan, S.S.8
  • 169
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield D.A. Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic. Res. 2002, 36:1307-1313.
    • (2002) Free Radic. Res. , vol.36 , pp. 1307-1313
    • Butterfield, D.A.1
  • 171
    • 78649983748 scopus 로고    scopus 로고
    • Alzheimer's disease: effects of beta-amyloid on mitochondria
    • Tillement L., Lecanu L., Papadopoulos V. Alzheimer's disease: effects of beta-amyloid on mitochondria. Mitochondrion 2011, 11:13-21.
    • (2011) Mitochondrion , vol.11 , pp. 13-21
    • Tillement, L.1    Lecanu, L.2    Papadopoulos, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.