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Volumn 48, Issue 4, 2013, Pages 373-396

Molecular paleontology and complexity in the last eukaryotic common ancestor

Author keywords

Cellular structure; Cytoskeleton; Endomembrane system; Eukaryogenesis; Evolution; LECA; Metabolomics

Indexed keywords

ACTIN; ESCRT PROTEIN; KINESIN; MYOSIN; NUCLEOPORIN; TUBULIN;

EID: 84880916121     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2013.821444     Document Type: Review
Times cited : (157)

References (295)
  • 3
    • 48749118215 scopus 로고    scopus 로고
    • Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins
    • Allen JW, Ferguson SJ, Ginger ML. (2008). Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins. FEBS Lett 582:2817-25.
    • (2008) FEBS Lett , vol.582 , pp. 2817-2825
    • Allen, J.W.1    Ferguson, S.J.2    Ginger, M.L.3
  • 5
    • 33846194528 scopus 로고    scopus 로고
    • A sirtuin in the African trypanosome is involved in both DNA repair and telomeric gene silencing but is not required for antigenic variation
    • Alsford S, Kawahara T, Isamah C, Horn D. (2007). A sirtuin in the African trypanosome is involved in both DNA repair and telomeric gene silencing but is not required for antigenic variation. Mol Microbiol 63:724-7.
    • (2007) Mol Microbiol , vol.63 , pp. 724-727
    • Alsford, S.1    Kawahara, T.2    Isamah, C.3    Horn, D.4
  • 6
    • 6344251034 scopus 로고    scopus 로고
    • Mitochondrial histone-like DNA-binding proteins are essential for normal cell growth and mitochondrial function in Crithidia fasciculata
    • DOI 10.1128/EC.3.2.518-526.2004
    • Avliyakulov NK, Lukes J, Ray DS. (2004). Mitochondrial histone-like DNA-binding proteins are essential for normal cell growth and mitochondrial function in Crithidia fasciculata. Eukaryot Cell 3: 518-26. (Pubitemid 38497989)
    • (2004) Eukaryotic Cell , vol.3 , Issue.2 , pp. 518-526
    • Avliyakulov, N.K.1    Lukes, J.2    Ray, D.S.3
  • 8
    • 79954416607 scopus 로고    scopus 로고
    • Ancient and essential: The assembly of ironsulfur clusters in plants
    • Balk J, Pilon M. (2011). Ancient and essential: the assembly of ironsulfur clusters in plants. Trends Plant Sci 16:218-26.
    • (2011) Trends Plant Sci , vol.16 , pp. 218-226
    • Balk, J.1    Pilon, M.2
  • 9
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • DOI 10.1038/sj.emboj.7600216
    • Balk J, Pierik AJ, Netz DJ, et al. (2004). The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J 23:2105-15. (Pubitemid 38737737)
    • (2004) EMBO Journal , vol.23 , Issue.10 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Aguilar Netz, D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 12
    • 84873116001 scopus 로고    scopus 로고
    • Divergence of Erv1-associated mitochondrial import and export pathways in trypanosomes and anaerobic protists
    • Basu S, Leonard JC, desai N, et al. (2013). Divergence of Erv1-associated mitochondrial import and export pathways in trypanosomes and anaerobic protists. Eukaryot Cell 12:343-55.
    • (2013) Eukaryot Cell , vol.12 , pp. 343-355
    • Basu, S.1    Leonard, J.C.2    Desai, N.3
  • 13
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • DOI 10.1128/JB.01322-07
    • Bendezu FO, de Boer PA. (2008). Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J Bacteriol 190:1792-811. (Pubitemid 351304035)
    • (2008) Journal of Bacteriology , vol.190 , Issue.5 , pp. 1792-1811
    • Bendezu, F.O.1    De Boer, P.A.J.2
  • 14
    • 78649686001 scopus 로고    scopus 로고
    • FtsZ-less cell division in archaea and bacteria
    • Bernander R, Ettema TJ. (2010). FtsZ-less cell division in archaea and bacteria. Curr Opin Microbiol 13:747-52.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 747-752
    • Bernander, R.1    Ettema, T.J.2
  • 16
    • 79954779971 scopus 로고    scopus 로고
    • Making new out of old: Recycling and modification of an ancient protein translocation system during eukaryotic evolution. Mechanistic comparison and phylogenetic analysis of ERAD, SELMA and the peroxisomal importomer
    • Bolte K, Gruenheit N, Felsner G, et al. (2011). Making new out of old: recycling and modification of an ancient protein translocation system during eukaryotic evolution. Mechanistic comparison and phylogenetic analysis of ERAD, SELMA and the peroxisomal importomer. Bioessays 33:368-76.
    • (2011) Bioessays , vol.33 , pp. 368-376
    • Bolte, K.1    Gruenheit, N.2    Felsner, G.3
  • 17
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P, Sander C, Valencia A. (1992). An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A 89:7290-4.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 18
    • 62649149894 scopus 로고    scopus 로고
    • Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins
    • Boyd JM, Drevland RM, Downs DM, Graham DE. (2009). Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins. J Bacteriol 191:1490-7.
    • (2009) J Bacteriol , vol.191 , pp. 1490-1497
    • Boyd, J.M.1    Drevland, R.M.2    Downs, D.M.3    Graham, D.E.4
  • 19
    • 84869434856 scopus 로고    scopus 로고
    • Structure and function of bacterial dynamin-like proteins
    • Bramkamp M. (2012). Structure and function of bacterial dynamin-like proteins. Biol Chem 393:1203-14.
    • (2012) Biol Chem , vol.393 , pp. 1203-1214
    • Bramkamp, M.1
  • 20
    • 79953845468 scopus 로고    scopus 로고
    • Autophagy in parasitic protists: Unique features and drug targets
    • Brennand A, Gualdrón-López M, Coppens I, et al. (2011). Autophagy in parasitic protists: unique features and drug targets. Mol Biochem Parasitol 177:83-99.
    • (2011) Mol Biochem Parasitol , vol.177 , pp. 83-99
    • Brennand, A.1    Gualdrón-López, M.2    Coppens, I.3
  • 21
    • 4143126756 scopus 로고    scopus 로고
    • More than one way to build a flagellum: Comparative genomics of parasitic protozoa [2]
    • DOI 10.1016/j.cub.2004.07.041, PII S0960982204005457
    • Briggs LJ, Davidge JA, Wickstead B, et al. (2004). More than one way to build a flagellum: comparative genomics of parasitic protozoa. Curr Biol 14:R611-12. (Pubitemid 39081651)
    • (2004) Current Biology , vol.14 , Issue.15
    • Briggs, L.J.1    Davidge, J.A.2    Wickstead, B.3    Ginger, M.L.4    Gull, K.5
  • 22
    • 78149306025 scopus 로고    scopus 로고
    • Multisubunit tethering complexes and their role in membrane fusion
    • Bröcker C, Engelbrecht-VandréS, Ungermann C. (2010). Multisubunit tethering complexes and their role in membrane fusion. Curr Biol 20: R943-52.
    • (2010) Curr Biol , vol.20
    • Bröcker, C.1    Engelbrecht-Vandré, S.2    Ungermann, C.3
  • 23
    • 6444230733 scopus 로고    scopus 로고
    • Devescovinid features, a remarkable surface cytoskeleton, and epibiotic bacteria revisited in Mixotricha paradoxa, a parabasalid flagellate
    • DOI 10.1007/s00709-004-0052-8
    • Brugerolle G. (2004). Devescovinid features, a remarkable surface cytoskeleton, and epibiotic bacteria revisited in Mixotricha paradoxa, a parabasalid flagellate. Protoplasma 224:49-59. (Pubitemid 39403885)
    • (2004) Protoplasma , vol.224 , Issue.1-2 , pp. 49-59
    • Brugerolle, G.1
  • 24
    • 4644299619 scopus 로고    scopus 로고
    • Evolution of the mitochondrial genome: Protist connections to animals, fungi and plants
    • DOI 10.1016/j.mib.2004.08.008, PII S136952740400102X
    • Bullerwell CE, Gray MW. (2004). Evolution of the mitochondrial genome: protist connections to animals, fungi and plants. Curr Opin Microbiol 7:528-34. (Pubitemid 39297134)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.5 , pp. 528-534
    • Bullerwell, C.E.1    Gray, M.W.2
  • 26
    • 79951783943 scopus 로고    scopus 로고
    • A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion
    • Burmann F, Ebert N, van Baarle S, Bramkamp M. (2011). A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion. Mol Microbiol 79:1294-304.
    • (2011) Mol Microbiol , vol.79 , pp. 1294-1304
    • Burmann, F.1    Ebert, N.2    Van Baarle, S.3    Bramkamp, M.4
  • 27
    • 77951527421 scopus 로고    scopus 로고
    • Pupylation versus ubiquitylation: Tagging for proteasome-dependent degradation
    • Burns KE, Darwin KH. (2010). Pupylation versus ubiquitylation: tagging for proteasome-dependent degradation. Cell Microbiol 12:424-31.
    • (2010) Cell Microbiol , vol.12 , pp. 424-431
    • Burns, K.E.1    Darwin, K.H.2
  • 29
    • 80054833492 scopus 로고    scopus 로고
    • Split decision: A thaumarchaeon encoding both FtsZ and Cdv cell division proteins chooses Cdv for cytokinesis
    • Busiek KK, Margolin W. (2011). Split decision: a thaumarchaeon encoding both FtsZ and Cdv cell division proteins chooses Cdv for cytokinesis. Mol Microbiol 82:535-8.
    • (2011) Mol Microbiol , vol.82 , pp. 535-538
    • Busiek, K.K.1    Margolin, W.2
  • 30
    • 33846063713 scopus 로고    scopus 로고
    • Macroevolution and macroecology through deep time
    • DOI 10.1111/j.1475-4983.2006.00613.x
    • Butterfield NJ. (2007). Macroevolution and macroecology through deep time. Palaeontology 50:41-55. (Pubitemid 46055989)
    • (2007) Palaeontology , vol.50 , Issue.1 , pp. 41-55
    • Butterfield, N.J.1
  • 31
    • 0023823452 scopus 로고
    • Exceptional preservation of fossils in an Upper Proterozoic shale
    • Butterfield NJ, Knoll AH, Swett K. (1988). Exceptional preservation of fossils in an Upper Proterozoic shale. Nature 334:424-7.
    • (1988) Nature , vol.334 , pp. 424-427
    • Butterfield, N.J.1    Knoll, A.H.2    Swett, K.3
  • 32
    • 0025573969 scopus 로고
    • A bangiophyte red alga from the Proterozoic of arctic Canada
    • Butterfield NJ, Knoll AH, Swett K. (1990). A bangiophyte red alga from the Proterozoic of arctic Canada. Science 250:104-7.
    • (1990) Science , vol.250 , pp. 104-107
    • Butterfield, N.J.1    Knoll, A.H.2    Swett, K.3
  • 33
    • 84864795131 scopus 로고    scopus 로고
    • Nuclear inheritance and genetic exchange without meiosis in the binucleate parasite Giardia intestinalis
    • Carpenter ML, Assaf ZJ, Gourguechon S, Cande WZ. (2012). Nuclear inheritance and genetic exchange without meiosis in the binucleate parasite Giardia intestinalis. J Cell Sci 125:2523-32.
    • (2012) J Cell Sci , vol.125 , pp. 2523-2532
    • Carpenter, M.L.1    Assaf, Z.J.2    Gourguechon, S.3    Cande, W.Z.4
  • 34
    • 79952254224 scopus 로고    scopus 로고
    • Crystal structure of the dynein motor domain
    • Carter AP, Cho C, Jin L, Vale RD. (2011). Crystal structure of the dynein motor domain. Science 331:1159-65.
    • (2011) Science , vol.331 , pp. 1159-1165
    • Carter, A.P.1    Cho, C.2    Jin, L.3    Vale, R.D.4
  • 36
    • 78149389123 scopus 로고    scopus 로고
    • Fission yeast cells undergo nuclear division in the absence of spindle microtubules
    • Castagnetti S, Oliferenko S, Nurse P. (2010). Fission yeast cells undergo nuclear division in the absence of spindle microtubules. PLoS Biol 8: e1000512.
    • (2010) PLoS Biol , vol.8
    • Castagnetti, S.1    Oliferenko, S.2    Nurse, P.3
  • 37
    • 0017960705 scopus 로고
    • The evolutionary origin and phylogeny of microtubules, mitotic spindles and eukaryote flagella
    • Cavalier-Smith T. (1978). The evolutionary origin and phylogeny of microtubules, mitotic spindles and eukaryote flagella. Biosystems 10: 93-114.
    • (1978) Biosystems , vol.10 , pp. 93-114
    • Cavalier-Smith, T.1
  • 38
    • 0023665552 scopus 로고
    • Eukaryotes with no mitochondria
    • Cavalier-Smith T. (1987). Eukaryotes with no mitochondria. Nature 326: 332-3.
    • (1987) Nature , vol.326 , pp. 332-333
    • Cavalier-Smith, T.1
  • 39
    • 0842345488 scopus 로고    scopus 로고
    • Protist phylogeny and the high-level classification of Protozoa
    • DOI 10.1078/0932-4739-00002
    • Cavalier-Smith T. (2003). Protist phylogeny and the high-level classification of Protozoa. Eur J Protistology 39:338-48. (Pubitemid 38171058)
    • (2003) European Journal of Protistology , vol.39 , Issue.4 , pp. 338-348
    • Cavalier-Smith, T.1
  • 41
    • 84864288673 scopus 로고    scopus 로고
    • Orchestrating vesicle transport, ESCRTs and kinase surveillance during abscission
    • Chen CT, Hehnly H, Doxsey SJ. (2012). Orchestrating vesicle transport, ESCRTs and kinase surveillance during abscission. Nat Rev Mol Cell Biol 13:483-8.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 483-488
    • Chen, C.T.1    Hehnly, H.2    Doxsey, S.J.3
  • 42
    • 79956030187 scopus 로고    scopus 로고
    • A late origin of the extant eukaryotic diversity: Divergence time estimates using rare genomic changes
    • Chernikova D, Motamedi S, Csürös M, et al. (2011). A late origin of the extant eukaryotic diversity: divergence time estimates using rare genomic changes. Biol Direct 19:26.
    • (2011) Biol Direct , vol.19 , pp. 26
    • Chernikova, D.1    Motamedi, S.2    Csürös, M.3
  • 43
    • 72849118873 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis thaliana exocyst complex gene families by phylogenetic., expression profiling, and subcellular localization studies
    • Chong YT, Gidda SK, Sanford C, et al. (2010). Characterization of the Arabidopsis thaliana exocyst complex gene families by phylogenetic., expression profiling, and subcellular localization studies. New Phytol 185:401-19.
    • (2010) New Phytol , vol.185 , pp. 401-419
    • Chong, Y.T.1    Gidda, S.K.2    Sanford, C.3
  • 44
    • 70349459932 scopus 로고    scopus 로고
    • The reducible complexity of a mitochondrial molecular machine
    • Clements A, Bursac D, Gatsos X, et al. (2009). The reducible complexity of a mitochondrial molecular machine. Proc Nat Acad Sci 106: 15791-5.
    • (2009) Proc Nat Acad Sci , vol.106 , pp. 15791-15795
    • Clements, A.1    Bursac, D.2    Gatsos, X.3
  • 46
    • 0033062611 scopus 로고    scopus 로고
    • The first sexual lineage and the relevance of facultative sex
    • DOI 10.1007/PL00013156
    • Dacks J, Roger AJ. (1999). The first sexual lineage and the relevance of facultative sex. J Mol Evol 48:779-83. (Pubitemid 29287968)
    • (1999) Journal of Molecular Evolution , vol.48 , Issue.6 , pp. 779-783
    • Dacks, J.1    Roger, A.J.2
  • 47
    • 0035900653 scopus 로고    scopus 로고
    • Reconstructing/deconstructing the earliest eukaryotes: How comparative genomics can help
    • DOI 10.1016/S0092-8674(01)00584-0
    • Dacks JB, Doolittle WF. (2001). Reconstructing/deconstructing the earliest eukaryotes: how comparative genomics can help. Cell 107: 419-25. (Pubitemid 33152778)
    • (2001) Cell , vol.107 , Issue.4 , pp. 419-425
    • Dacks, J.B.1    Doolittle W.Ford2
  • 48
    • 0037089090 scopus 로고    scopus 로고
    • Novel syntaxin gene sequences from Giardia, trypanosoma and algae: Implications for the ancient evolution of the eukaryotic endomembrane system
    • Dacks JB, Doolittle WF. (2002). Novel syntaxin gene sequences from Giardia, Trypanosoma and algae: implications for the ancient evolution of the eukaryotic endomembrane system. J Cell Sci 115:1635-42. (Pubitemid 34520593)
    • (2002) Journal of Cell Science , vol.115 , Issue.8 , pp. 1635-1642
    • Dacks, J.B.1    Doolittle, W.F.2
  • 49
    • 2942527445 scopus 로고    scopus 로고
    • Molecular and phylogenetic characterization of syntaxin genes from parasitic protozoa
    • DOI 10.1016/j.molbiopara.2004.02.014, PII S0166685104000696
    • Dacks JB, Doolittle WF. (2004). Molecular and phylogenetic characterization of syntaxin genes from parasitic protozoa. Mol Biochem Parasitol 136:123-36. (Pubitemid 38757981)
    • (2004) Molecular and Biochemical Parasitology , vol.136 , Issue.2 , pp. 123-136
    • Dacks, J.B.1    Doolittle, W.F.2
  • 50
    • 34948835726 scopus 로고    scopus 로고
    • Evolution of the eukaryotic membrane-trafficking system: Origins, tempo and mode
    • DOI 10.1242/jcs.013250
    • Dacks JB, Field MC. (2007). Evolution of the eukaryotic membranetrafficking system: origin., tempo and mode. J Cell Sci 120:2977-85. (Pubitemid 47517081)
    • (2007) Journal of Cell Science , vol.120 , Issue.17 , pp. 2977-2985
    • Dacks, J.B.1    Field, M.C.2
  • 51
    • 84880883622 scopus 로고    scopus 로고
    • Evidence for Golgi bodies in proposed 'Golgi-lacking' lineages
    • Dacks JB, Davis LA, Sjögren AM, et al. (2003). Evidence for Golgi bodies in proposed 'Golgi-lacking' lineages. Proc Biol Sci 7:270.
    • (2003) Proc Biol Sci , vol.7 , pp. 270
    • Dacks, J.B.1    Davis, L.A.2    Sjögren, A.M.3
  • 53
    • 68949210493 scopus 로고    scopus 로고
    • The protein import channel in the outer mitosomal membrane of Giardia intestinalis
    • Dagley MJ, Dolezal P, Likic VA, et al. (2009). The protein import channel in the outer mitosomal membrane of Giardia intestinalis. Mol Biol Evol 26:1941-7.
    • (2009) Mol Biol Evol , vol.26 , pp. 1941-1947
    • Dagley, M.J.1    Dolezal, P.2    Likic, V.A.3
  • 55
    • 0026705484 scopus 로고
    • The essential bacterial celldivision protein FtsZ is a GTPase
    • de Boer P, Crossley R, Rothfield L. (1992). The essential bacterial celldivision protein FtsZ is a GTPase. Nature 359:254-6.
    • (1992) Nature , vol.359 , pp. 254-256
    • De Boer, P.1    Crossley, R.2    Rothfield, L.3
  • 57
    • 71049191352 scopus 로고    scopus 로고
    • Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor
    • deGrasse JA, DuBois KN, Devos D, et al. (2009). Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor. Mol Cell Proteomics 8:2119-30.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2119-2130
    • Degrasse, J.A.1    Dubois, K.N.2    Devos, D.3
  • 58
    • 70350141267 scopus 로고    scopus 로고
    • Phylogenetic analysis identifies many uncharacterized actin-like proteins Alps in bacteria: Regulated polymerization, dynamic instability and treadmilling in Alp7A
    • Derman AI, Becker EC, Truong BD, et al. (2009). Phylogenetic analysis identifies many uncharacterized actin-like proteins Alps in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A. Mol Microbiol 73:534-52.
    • (2009) Mol Microbiol , vol.73 , pp. 534-552
    • Derman, A.I.1    Becker, E.C.2    Truong, B.D.3
  • 59
    • 77949881304 scopus 로고    scopus 로고
    • Phylogenomics of sterol synthesis: Insights into the origin, evolution, and diversity of a key eukaryotic feature
    • Desmond E, Gribaldo S. (2009). Phylogenomics of sterol synthesis: insights into the origin, evolution, and diversity of a key eukaryotic feature. Genome Biol Evol 1:364-81.
    • (2009) Genome Biol Evol , vol.1 , pp. 364-381
    • Desmond, E.1    Gribaldo, S.2
  • 60
    • 83555177274 scopus 로고    scopus 로고
    • Regarding the presence of membrane coat proteins in bacteria: Confusion? What confusion?
    • Devos DP. (2012). Regarding the presence of membrane coat proteins in bacteria: confusion? What confusion? Bioessays 34:38-9.
    • (2012) Bioessays , vol.34 , pp. 38-39
    • Devos, D.P.1
  • 61
    • 9444273167 scopus 로고    scopus 로고
    • Components of coated vesicles and nuclear pore complexes share a common molecular architecture
    • Devos D, Dokudovskaya S, Alber F, et al. (2004). Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol 2:e380.
    • (2004) PLoS Biol , vol.2
    • Devos, D.1    Dokudovskaya, S.2    Alber, F.3
  • 62
    • 80055078598 scopus 로고    scopus 로고
    • Thousands of rab GTPases for the cell biologist
    • Diekmann Y, Seixas E, Gouw M, et al. (2011). Thousands of rab GTPases for the cell biologist. PLoS Comput Biol 7:e1002217.
    • (2011) PLoS Comput Biol , vol.7
    • Diekmann, Y.1    Seixas, E.2    Gouw, M.3
  • 63
    • 35748984432 scopus 로고    scopus 로고
    • LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis thaliana
    • DOI 10.1105/tpc.107.053231
    • Dittmer TA, Stacey NJ, Sugimoto-Shirasu K, Richards EJ. (2007). LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis thaliana. Plant Cell 19:2793-803. (Pubitemid 350046229)
    • (2007) Plant Cell , vol.19 , Issue.9 , pp. 2793-2803
    • Dittmer, T.A.1    Stacey, N.J.2    Sugimoto-Shirasu, K.3    Richards, E.J.4
  • 64
    • 84880883715 scopus 로고    scopus 로고
    • Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggest spiraling filaments are involved in membrane scission
    • in press
    • Dobro MJ, Samson RY, Yu Z, et al. (2013). Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggest spiraling filaments are involved in membrane scission. Mol Biol Cell in press.
    • (2013) Mol Biol Cell
    • Dobro, M.J.1    Samson, R.Y.2    Yu, Z.3
  • 65
    • 79957971892 scopus 로고    scopus 로고
    • A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae
    • M110.006478
    • Dokudovskaya S, Waharte F, Schlessinger A, et al. (2011). A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae. Mol Cell Proteomics 10:M110.006478.
    • (2011) Mol Cell Proteomics , vol.10
    • Dokudovskaya, S.1    Waharte, F.2    Schlessinger, A.3
  • 66
    • 77950428640 scopus 로고    scopus 로고
    • The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica
    • Dolezal P, Dagley MJ, Kono M, et al. (2010). The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica. PLoS Pathog 6:e1000812.
    • (2010) PLoS Pathog , vol.6
    • Dolezal, P.1    Dagley, M.J.2    Kono, M.3
  • 67
    • 34249282745 scopus 로고    scopus 로고
    • Homologs of eukaryotic Ras superfamily proteins in prokaryotes and their novel phylogenetic correlation with their eukaryotic analogs
    • Dong JH, Wen JF, Tian HF. (2007). Homologs of eukaryotic Ras superfamily proteins in prokaryotes and their novel phylogenetic correlation with their eukaryotic analogs. Gene 396:116-24.
    • (2007) Gene , vol.396 , pp. 116-124
    • Dong, J.H.1    Wen, J.F.2    Tian, H.F.3
  • 68
    • 0032404453 scopus 로고    scopus 로고
    • You are what you eat: A gene transfer ratchet could account for bacterial genes in eukaryotic nuclear genomes
    • Doolittle WF. (1998). You are what you eat: a gene transfer ratchet could account for bacterial genes in eukaryotic nuclear genomes. Trends Genet 14:307-11.
    • (1998) Trends Genet , vol.14 , pp. 307-311
    • Doolittle, W.F.1
  • 69
    • 84858966521 scopus 로고    scopus 로고
    • NUP-1 Is a large coiled-coil nucleoskeletal protein in trypanosomes with lamin-like functions
    • DuBois KN, Alsford S, Holden JM, et al. (2012). NUP-1 Is a large coiled-coil nucleoskeletal protein in trypanosomes with lamin-like functions. PLoS Biol 10:e1001287.
    • (2012) PLoS Biol , vol.10
    • Dubois, K.N.1    Alsford, S.2    Holden, J.M.3
  • 71
    • 84873851187 scopus 로고    scopus 로고
    • Divergent molecular evolution of the mitochondrial sulfhydryl:Cytochrome C oxidoreductase Erv in opisthokonts and parasitic protists
    • Eckers E, Petrungaro C, Gross D, et al. (2013). Divergent molecular evolution of the mitochondrial sulfhydryl:cytochrome C oxidoreductase Erv in opisthokonts and parasitic protists. J Biol Chem 288: 2676-88.
    • (2013) J Biol Chem , vol.288 , pp. 2676-2688
    • Eckers, E.1    Petrungaro, C.2    Gross, D.3
  • 72
    • 84864805551 scopus 로고    scopus 로고
    • Sculpting the endomembrane system in deep time: High resolution phylogenetics of Rab GTPases
    • Elias M, Brighouse A, Gabernet-Castello C, et al. (2012). Sculpting the endomembrane system in deep time: high resolution phylogenetics of Rab GTPases. J Cell Sci 125:2500-8.
    • (2012) J Cell Sci , vol.125 , pp. 2500-2508
    • Elias, M.1    Brighouse, A.2    Gabernet-Castello, C.3
  • 74
    • 77749309281 scopus 로고    scopus 로고
    • Virulence and immunomodulatory roles of bacterial outer membrane vesicles
    • Ellis TN, Kuehn MJ. (2010). Virulence and immunomodulatory roles of bacterial outer membrane vesicles. Microbiol Mol Biol Rev 74:81-94.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 81-94
    • Ellis, T.N.1    Kuehn, M.J.2
  • 75
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • Embley TM, Martin W. (2006). Eukaryotic evolution, changes and challenges. Nature 440:623-30.
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 76
    • 15944426129 scopus 로고    scopus 로고
    • Requirement of sterols in the life cycle of the nematode Caenorhabditis elegans
    • DOI 10.1016/j.semcdb.2005.01.004, Cellular Cholesterol Metabolism and Trafficking and Apoptosis in Development
    • Entchev EV, Kurzchalia TV. (2005). Requirements of sterols in the life cycle of the nematode Caenorhabditis elegans. Semin. Cell Dev Biol 16:175-82. (Pubitemid 40432119)
    • (2005) Seminars in Cell and Developmental Biology , vol.16 , Issue.2 , pp. 175-182
    • Entchev, E.V.1    Kurzchalia, T.V.2
  • 77
    • 0032432844 scopus 로고    scopus 로고
    • Molecular phylogeny of metazoan intermediate filament proteins
    • DOI 10.1007/PL00006434
    • Erber A, Riemer D, Bovenschulte M, Weber K. (1998). Molecular phylogeny of metazoan intermediate filament proteins. J Mol Evol 47: 751-62. (Pubitemid 29008778)
    • (1998) Journal of Molecular Evolution , vol.47 , Issue.6 , pp. 751-762
    • Erber, A.1    Riemer, D.2    Bovenschulte, M.3    Weber, K.4
  • 78
    • 78649343842 scopus 로고    scopus 로고
    • Cell division without FtsZ-A variety of redundant mechanisms
    • Erickson HP, Osawa M. (2010). Cell division without FtsZ-a variety of redundant mechanisms. Mol Microbiol 78:267-70.
    • (2010) Mol Microbiol , vol.78 , pp. 267-270
    • Erickson, H.P.1    Osawa, M.2
  • 81
    • 61349170303 scopus 로고    scopus 로고
    • First and last ancestors: Reconstructing evolution of the endomembrane system with ESCRTs., vesicle coat proteins., and nuclear pore complexes
    • Field MC, Dacks JB. (2009). First and last ancestors: reconstructing evolution of the endomembrane system with ESCRTs., vesicle coat proteins., and nuclear pore complexes. Curr Opin Cell Biol 21:4-13.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 4-13
    • Field, M.C.1    Dacks, J.B.2
  • 82
    • 84934441798 scopus 로고    scopus 로고
    • Reconstructing the evolution of the endocytic system: Insights from genomics and molecular cell biology
    • Field MC, Gabernet-Castello C, Dacks JB. (2007). Reconstructing the evolution of the endocytic system: insights from genomics and molecular cell biology. Adv Exp Med Biol 607:84-96.
    • (2007) Adv Exp Med Biol , vol.607 , pp. 84-96
    • Field, M.C.1    Gabernet-Castello, C.2    Dacks, J.B.3
  • 83
    • 79959413234 scopus 로고    scopus 로고
    • Evolution: On a bender-BARs, ESCRTs, COPs, and finally getting your coat
    • Field MC, Sali A, Rout MP. (2011). Evolution: On a bender-BARs, ESCRTs, COPs, and finally getting your coat. J Cell Biol 193:963-72.
    • (2011) J Cell Biol , vol.193 , pp. 963-972
    • Field, M.C.1    Sali, A.2    Rout, M.P.3
  • 84
    • 77649088404 scopus 로고    scopus 로고
    • Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein
    • Field MC, Sergeenko T, Wang YN, et al. (2010). Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein. PLoS One 5:e8468.
    • (2010) PLoS One , vol.5
    • Field, M.C.1    Sergeenko, T.2    Wang, Y.N.3
  • 85
    • 67649397588 scopus 로고    scopus 로고
    • Epigenetic regulation in African trypanosomes: A new kid on the block
    • Figueiredo LM, Cross GA, Janzen CJ. (2009). Epigenetic regulation in African trypanosomes: a new kid on the block. Nat Rev Microbiol 7: 504-13.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 504-513
    • Figueiredo, L.M.1    Cross, G.A.2    Janzen, C.J.3
  • 87
    • 78751584657 scopus 로고    scopus 로고
    • A new fusion hypothesis for the origin of Eukarya: Better than previous ones, but probably also wrong
    • Forterre P. (2011). A new fusion hypothesis for the origin of Eukarya: better than previous ones, but probably also wrong. Res Microbiol 162:77-91.
    • (2011) Res Microbiol , vol.162 , pp. 77-91
    • Forterre, P.1
  • 89
    • 84861430732 scopus 로고    scopus 로고
    • Cryptic peroxisomal targeting via alternative splicing and stop codon read-through in fungi
    • Freitag J, Ast J, Bölker M. (2012). Cryptic peroxisomal targeting via alternative splicing and stop codon read-through in fungi. Nature 485: 522-5.
    • (2012) Nature , vol.485 , pp. 522-525
    • Freitag, J.1    Ast, J.2    Bölker, M.3
  • 90
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • Fuchs E, Weber K. (1994). Intermediate filaments: structure, dynamics, function, and disease. Annu Rev Biochem 63:345-82.
    • (1994) Annu Rev Biochem , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 91
    • 27144551296 scopus 로고    scopus 로고
    • Intracellular compartmentation in planctomycetes
    • DOI 10.1146/annurev.micro.59.030804.121258
    • Fuerst JA. (2005). Intracellular compartmentation in planctomycetes. Annu Rev Microbiol 59:299-328. (Pubitemid 41507434)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 299-328
    • Fuerst, J.A.1
  • 92
    • 79956136196 scopus 로고    scopus 로고
    • Beyond the bacterium: Planctomycetes challenge our concepts of microbial structure and function
    • Fuerst JA, Sagulenko E. (2011). Beyond the bacterium: Planctomycetes challenge our concepts of microbial structure and function. Nat Rev Microbiol 9:403-13.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 403-413
    • Fuerst, J.A.1    Sagulenko, E.2
  • 93
    • 84875761914 scopus 로고    scopus 로고
    • Keys to eukaryality: Planctomycetes and ancestral evolution of cellular complexity
    • Fuerst JA, Sagulenko E. (2012). Keys to eukaryality: planctomycetes and ancestral evolution of cellular complexity. Front Microbiol 3:167.
    • (2012) Front Microbiol , vol.3 , pp. 167
    • Fuerst, J.A.1    Sagulenko, E.2
  • 95
    • 77955576219 scopus 로고    scopus 로고
    • Lack of phylogenetic support for a supposed actinobacterial origin of peroxisomes
    • Gabaldón T, Capella-Gutiérrez S. (2010). Lack of phylogenetic support for a supposed actinobacterial origin of peroxisomes. Gene 461:61-5.
    • (2010) Gene , vol.461 , pp. 61-65
    • Gabaldón, T.1    Capella-Gutiérrez, S.2
  • 96
    • 33747893546 scopus 로고    scopus 로고
    • Origin and evolution of the peroxisome proteome
    • Gabaldón T, Snel B, van Zimmeren F, et al. (2006). Origin and evolution of the peroxisome proteome. Biol Direct 1:8.
    • (2006) Biol Direct , vol.1 , pp. 8
    • Gabaldón, T.1    Snel, B.2    Van Zimmeren, F.3
  • 98
    • 0005073263 scopus 로고    scopus 로고
    • Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein
    • Garbarino JE, Gibbons IR. (2002). Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein. BMC Genomics 3:18.
    • (2002) BMC Genomics , vol.3 , pp. 18
    • Garbarino, J.E.1    Gibbons, I.R.2
  • 99
    • 0029084610 scopus 로고
    • Dynein family of motor proteins: Present status and future questions
    • Gibbons IR. (1995). Dynein family of motor proteins: present status and future questions. Cell Motil Cytoskeleton 32:136-44.
    • (1995) Cell Motil Cytoskeleton , vol.32 , pp. 136-144
    • Gibbons, I.R.1
  • 100
    • 78649635768 scopus 로고    scopus 로고
    • Intermediary metabolism in protists: A sequence-based view of facultative anaerobic metabolism in evolutionarily diverse eukaryotes
    • Ginger ML, Fritz-Laylin LK, Fulton C, et al. (2010). Intermediary metabolism in protists: a sequence-based view of facultative anaerobic metabolism in evolutionarily diverse eukaryotes. Protist 161:642-71.
    • (2010) Protist , vol.161 , pp. 642-671
    • Ginger, M.L.1    Fritz-Laylin, L.K.2    Fulton, C.3
  • 102
    • 10944243685 scopus 로고    scopus 로고
    • Mitochondria of protists
    • DOI 10.1146/annurev.genet.37.110801.142526
    • Gray MW, Lang BF, Burger GE. (2004). Mitochondria of protists. Annu Rev Genet 38:477-524. (Pubitemid 40013736)
    • (2004) Annual Review of Genetics , vol.38 , pp. 477-524
    • Gray, M.W.1    Lang, B.F.2    Burger, G.3
  • 103
    • 77957134043 scopus 로고    scopus 로고
    • The origin of eukaryotes and their relationship with the Archaea: Are we at a phylogenomic impasse?
    • Gribaldo S, Poole AM, Daubin V, et al. (2010). The origin of eukaryotes and their relationship with the Archaea: are we at a phylogenomic impasse? Nat Rev Microbiol 8:743-52.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 743-752
    • Gribaldo, S.1    Poole, A.M.2    Daubin, V.3
  • 104
    • 84861384878 scopus 로고    scopus 로고
    • Functional architecture of the nuclear pore complex
    • Grossman E, Medalia O, Zwerger M. (2012). Functional architecture of the nuclear pore complex. Annu Rev Biophys 41:557-84.
    • (2012) Annu Rev Biophys , vol.41 , pp. 557-584
    • Grossman, E.1    Medalia, O.2    Zwerger, M.3
  • 105
    • 84855192934 scopus 로고    scopus 로고
    • When, how and why glycolysis became compartmentalised in the Kinetoplastea. A new look at an ancient organelle
    • Gualdrón-López M, Brennand A, Hannaert V, et al. (2012). When, how and why glycolysis became compartmentalised in the Kinetoplastea. A new look at an ancient organelle. Int J Parasitol 42:1-20.
    • (2012) Int J Parasitol , vol.42 , pp. 1-20
    • Gualdrón-López, M.1    Brennand, A.2    Hannaert, V.3
  • 106
    • 84255209035 scopus 로고    scopus 로고
    • Amino acids biosynthesis and nitrogen assimilation pathways: A great genomic deletion during eukaryotes evolution
    • Guedes RL, Prosdocimi F, Fernandes GR, et al. (2011). Amino acids biosynthesis and nitrogen assimilation pathways: a great genomic deletion during eukaryotes evolution. BMC Genomics 12:S2.
    • (2011) BMC Genomics , vol.12
    • Guedes, R.L.1    Prosdocimi, F.2    Fernandes, G.R.3
  • 107
    • 0015218669 scopus 로고
    • Role for ferredoxins in the origin of life and biological evolution
    • Hall DO, Cammack R, Rao KK. (1971). Role for ferredoxins in the origin of life and biological evolution. Nature 233:136-8.
    • (1971) Nature , vol.233 , pp. 136-138
    • Hall, D.O.1    Cammack, R.2    Rao, K.K.3
  • 108
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • DOI 10.1083/jcb.200707031
    • Hanson PI, Roth R, Lin Y, Heuser JE. (2008). Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J Cell Biol 180:389-402. (Pubitemid 351185923)
    • (2008) Journal of Cell Biology , vol.180 , Issue.2 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 109
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase-an energy sensor that regulates all aspects of cell function
    • Hardie DG. (2011). AMP-activated protein kinase-an energy sensor that regulates all aspects of cell function. Genes Dev 25:1895-908.
    • (2011) Genes Dev , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 110
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie DG, Ross FA, Hawley SA. (2012). AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nature Rev Mol Cell Biol 13:251-62.
    • (2012) Nature Rev Mol Cell Biol , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 111
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • DOI 10.1016/S0014-5793(03)00560-X
    • Hardie DG, Scott JW, Pan DA, Hudson ER. (2003). Management of cellular energy by the AMP-activated protein kinase system. FEBS Lett 546:113-20. (Pubitemid 36782291)
    • (2003) FEBS Letters , vol.546 , Issue.1 , pp. 113-120
    • Hardie, D.G.1    Scott, J.W.2    Pan, D.A.3    Hudson, E.R.4
  • 112
    • 63849158685 scopus 로고    scopus 로고
    • The evolution of the cilium and the eukaryotic cell
    • Hartman H, Smith TF. (2009). The evolution of the cilium and the eukaryotic cell. Cell Motil Cytoskeleton 66:215-19.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 215-219
    • Hartman, H.1    Smith, T.F.2
  • 114
    • 78651393562 scopus 로고    scopus 로고
    • Selective sorting of cargo proteins into bacterial membrane vesicles
    • Haurat MF, Aduse-Opoku J, Rangarajan M, et al. (2011). Selective sorting of cargo proteins into bacterial membrane vesicles. J Biol Chem 286:1269-76.
    • (2011) J Biol Chem , vol.286 , pp. 1269-1276
    • Haurat, M.F.1    Aduse-Opoku, J.2    Rangarajan, M.3
  • 115
    • 41449083862 scopus 로고    scopus 로고
    • Turnover of glycosomes during life-cycle differentiation of Trypanosoma brucei
    • Herman M, Pérez-Morga D, Schtickzelle N, Michels PAM. (2008). Turnover of glycosomes during life-cycle differentiation of Trypanosoma brucei. Autophagy 4:294-308. (Pubitemid 351458090)
    • (2008) Autophagy , vol.4 , Issue.3 , pp. 294-308
    • Herman, M.1    Perez-Morga, D.2    Schtickzelle, N.3    Michels, P.A.M.4
  • 116
    • 79851512902 scopus 로고    scopus 로고
    • Minor modifications and major adaptations: The evolution of molecular machines driving mitochondrial protein import
    • Hewitt V, Alcock F, Lithgow T. (2011). Minor modifications and major adaptations: The evolution of molecular machines driving mitochondrial protein import. Biochim Biophys Acta (BBA)-Biomembranes 1808:947-54.
    • (2011) Biochim Biophys Acta (BBA)-Biomembranes , vol.1808 , pp. 947-954
    • Hewitt, V.1    Alcock, F.2    Lithgow, T.3
  • 118
    • 77951743346 scopus 로고    scopus 로고
    • Reconstructing the evolutionary history of the centriole from protein components
    • Hodges ME, Scheumann N, Wickstead B, et al. (2010). Reconstructing the evolutionary history of the centriole from protein components. J Cell Sci 123:1407-13.
    • (2010) J Cell Sci , vol.123 , pp. 1407-1413
    • Hodges, M.E.1    Scheumann, N.2    Wickstead, B.3
  • 119
    • 22144465170 scopus 로고    scopus 로고
    • Contribution of the endoplasmic reticulum to peroxisome formation
    • DOI 10.1016/j.cell.2005.04.025, PII S0092867405004058
    • Hoepfner D, Schildknegt D, Braakman I, et al. (2005). Contribution of the endoplasmic reticulum to peroxisome formation. Cell 122:85-95. (Pubitemid 40977942)
    • (2005) Cell , vol.122 , Issue.1 , pp. 85-95
    • Hoepfner, D.1    Schildknegt, D.2    Braakman, I.3    Philippsen, P.4    Tabak, H.F.5
  • 120
    • 0036495241 scopus 로고    scopus 로고
    • Iron hydrogenases - Ancient enzymes in modern eukaryotes
    • DOI 10.1016/S0968-0004(01)02053-9, PII S0968000401020539
    • Horner DS, Heil B, Happe T, Embley TM. (2002). Iron hydrogenases-ancient enzymes in modern eukaryotes. Trends Biochem Sci 27: 148-53. (Pubitemid 34219325)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 148-153
    • Horner, D.S.1    Heil, B.2    Happe, T.3    Embley T.Martin4
  • 121
    • 74549210085 scopus 로고    scopus 로고
    • Phylogenetic distributions and histories of proteins involved in anaerobic pyruvate metabolism in eukaryotes
    • Hug LA, Stechmann A, Roger AJ. (2010). Phylogenetic distributions and histories of proteins involved in anaerobic pyruvate metabolism in eukaryotes. Mol Biol Evol 27:311-24.
    • (2010) Mol Biol Evol , vol.27 , pp. 311-324
    • Hug, L.A.1    Stechmann, A.2    Roger, A.J.3
  • 122
    • 73849149089 scopus 로고    scopus 로고
    • Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii
    • Humbard MA, Miranda HV, Lim JM, et al. (2010). Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii. Nature 463:54-60.
    • (2010) Nature , vol.463 , pp. 54-60
    • Humbard, M.A.1    Miranda, H.V.2    Lim, J.M.3
  • 123
    • 49749120551 scopus 로고    scopus 로고
    • Cilium evolution: Identification of a novel protein, nematocilin, in the mechanosensory cilium of Hydra nematocytes
    • Hwang JS, Takaku Y, Chapman J, et al. (2008). Cilium evolution: identification of a novel protein, nematocilin, in the mechanosensory cilium of Hydra nematocytes. Mol Biol Evol 25:2009-17.
    • (2008) Mol Biol Evol , vol.25 , pp. 2009-2017
    • Hwang, J.S.1    Takaku, Y.2    Chapman, J.3
  • 124
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • DOI 10.1016/j.jsb.2003.10.010, PII S1047847703002235
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. (2004). Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol 146: 11-31. (Pubitemid 38369015)
    • (2004) Journal of Structural Biology , vol.146 , Issue.1-2 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 126
    • 80455131023 scopus 로고    scopus 로고
    • The long journey: Actin on the road to pro-and eukaryotic cells
    • Jockusch BM, Graumann PL. (2012). The long journey: actin on the road to pro-and eukaryotic cells. Rev Physiol Biochem Pharmacol 161: 67-85.
    • (2012) Rev Physiol Biochem Pharmacol , vol.161 , pp. 67-85
    • Jockusch, B.M.1    Graumann, P.L.2
  • 127
    • 0028337335 scopus 로고
    • Protein translocation: Common themes from bacteria to man
    • DOI 10.1016/0014-5793(94)00367-X
    • Jungnickel B, Rapoport TA, Hartmann E. (1994). Protein translocation: common themes from bacteria to man. FEBS Lett 346:73-7. (Pubitemid 24183831)
    • (1994) FEBS Letters , vol.346 , Issue.1 , pp. 73-77
    • Jungnickel, B.1
  • 128
  • 130
    • 84856090681 scopus 로고    scopus 로고
    • Connecting threads: Epigenetics and metabolism
    • Katada S, Imhof A, Sassone-Corsi P. (2012). Connecting Threads: epigenetics and metabolism. Cell 148:24-8.
    • (2012) Cell , vol.148 , pp. 24-28
    • Katada, S.1    Imhof, A.2    Sassone-Corsi, P.3
  • 134
    • 0034597558 scopus 로고    scopus 로고
    • Dynein light chains of the Roadblock/LC7 group belong to an ancient protein superfamily implicated in NTPase regulation
    • Koonin EV, Aravind L. (2000). Dynein light chains of the Roadblock/LC7 group belong to an ancient protein superfamily implicated in NTPase regulation. Curr Biol 10:R774-6.
    • (2000) Curr Biol , vol.10
    • Koonin, E.V.1    Aravind, L.2
  • 135
    • 33847648364 scopus 로고    scopus 로고
    • Control systems for membrane fusion in the ancestral eukaryote; Evolution of tethering complexes and SM proteins
    • Koumandou VL, Dacks JB, Coulson RM, Field MC. (2007). Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins. BMC Evol Biol 7:29.
    • (2007) BMC Evol Biol , vol.7 , pp. 29
    • Koumandou, V.L.1    Dacks, J.B.2    Coulson, R.M.3    Field, M.C.4
  • 136
    • 84880872695 scopus 로고    scopus 로고
    • The emergence of cellular complexity at the dawn of the eukaryotes: Reconstructing the endomembrane system with in silico and functional analyses
    • Pontarotti P, ed. Berlin and Heidelberg: Springer Verlag, Chapter 10
    • Koumandou VL, Field MC. (2011). The emergence of cellular complexity at the dawn of the eukaryotes: reconstructing the endomembrane system with in silico and functional analyses. In: Pontarotti P, ed. Evolutionary biology concepts, biodiversity, macroevolution and genome evolution. Berlin and Heidelberg: Springer Verlag, Chapter 10, 153-67.
    • (2011) Evolutionary Biology Concepts, Biodiversity, Macroevolution and Genome Evolution , pp. 153-167
    • Koumandou, V.L.1    Field, M.C.2
  • 137
    • 77951827772 scopus 로고    scopus 로고
    • Genome-wide in silico screen for CCCH-type zinc finger proteins of Trypanosoma brucei, Trypanosoma cruzi and Leishmania major
    • Kramer S, Kimblin NC, Carrington M. (2010). Genome-wide in silico screen for CCCH-type zinc finger proteins of Trypanosoma brucei, Trypanosoma cruzi and Leishmania major. BMC Genomics 11:283.
    • (2010) BMC Genomics , vol.11 , pp. 283
    • Kramer, S.1    Kimblin, N.C.2    Carrington, M.3
  • 138
    • 84855874844 scopus 로고    scopus 로고
    • Characterization of NE81, the first lamin-like nucleoskeleton protein in a unicellular organism
    • Krüger A, Batsios P, Baumann O, et al. (2012). Characterization of NE81, the first lamin-like nucleoskeleton protein in a unicellular organism. Mol Biol Cell 23:360-70.
    • (2012) Mol Biol Cell , vol.23 , pp. 360-370
    • Krüger, A.1    Batsios, P.2    Baumann, O.3
  • 139
    • 0032410805 scopus 로고    scopus 로고
    • The case for a common ancestor: Kinesin and myosin motor proteins and G proteins
    • DOI 10.1023/A:1005489907021
    • Kull FJ, Vale RD, Fletterick RJ. (1998). The case for a common ancestor: kinesin and myosin motor proteins and G proteins. J Muscle Res Cell Motil 19:877-86. (Pubitemid 29054483)
    • (1998) Journal of Muscle Research and Cell Motility , vol.19 , Issue.8 , pp. 877-886
    • Kull, F.J.1    Vale, R.D.2    Fletterick, R.J.3
  • 140
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • DOI 10.1038/380550a0
    • Kull FJ, Sablin EP, Lau R, et al. (1996). Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380: 550-5. (Pubitemid 26110647)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 141
    • 0043198069 scopus 로고    scopus 로고
    • Why do worms need cholesterol?
    • DOI 10.1038/ncb0803-684
    • Kurzchalia TV, Ward S. (2003). Why do worms need cholesterol? Nature Cell Biol 5:684-8. (Pubitemid 36986768)
    • (2003) Nature Cell Biology , vol.5 , Issue.8 , pp. 684-688
    • Kurzchalia, T.V.1    Ward, S.2
  • 142
    • 79959629502 scopus 로고    scopus 로고
    • Energetics and genetics across the prokaryote-eukaryote divide
    • Lane N. (2011). Energetics and genetics across the prokaryote-eukaryote divide. Biology Direct 6:35.
    • (2011) Biology Direct , vol.6 , pp. 35
    • Lane, N.1
  • 143
    • 77950456083 scopus 로고    scopus 로고
    • How did LUCA make a living? Chemiosmosis in the origin of life
    • Lane N, Allen JF, Martin W. (2010). How did LUCA make a living? Chemiosmosis in the origin of life. BioEssays 32:271-80.
    • (2010) BioEssays , vol.32 , pp. 271-280
    • Lane, N.1    Allen, J.F.2    Martin, W.3
  • 144
    • 84988044805 scopus 로고    scopus 로고
    • The energetics of genome complexity
    • Lane N, Martin W. (2010). The energetics of genome complexity. Nature 467:929-34.
    • (2010) Nature , vol.467 , pp. 929-934
    • Lane, N.1    Martin, W.2
  • 145
    • 0035009107 scopus 로고    scopus 로고
    • Dyneins have run their course in plant lineage
    • DOI 10.1034/j.1600-0854.2001.25020508.x
    • Lawrence CJ, Morris NR, Meagher RB, Dawe RK. (2001). Dyneins have run their course in plant lineage. Traffic 2:362-3. (Pubitemid 32487566)
    • (2001) Traffic , vol.2 , Issue.5 , pp. 362-363
    • Lawrence, C.J.1    Morris, N.R.2    Meagher, R.B.3    Dawe, R.K.4
  • 146
    • 60149089263 scopus 로고    scopus 로고
    • Life without a wall or division machine in Bacillus subtilis
    • Leaver M, Dominguez-Cuevas P, Coxhead JM, et al. (2009). Life without a wall or division machine in Bacillus subtilis. Nature 457:849-53.
    • (2009) Nature , vol.457 , pp. 849-853
    • Leaver, M.1    Dominguez-Cuevas, P.2    Coxhead, J.M.3
  • 147
    • 73149088617 scopus 로고    scopus 로고
    • Gram-positive bacteria produce membrane vesicles: Proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles
    • Lee EY, Choi DY, Kim DK, et al. (2009). Gram-positive bacteria produce membrane vesicles: proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles. Proteomics 9: 5425-36.
    • (2009) Proteomics , vol.9 , pp. 5425-5436
    • Lee, E.Y.1    Choi, D.Y.2    Kim, D.K.3
  • 148
    • 0026502684 scopus 로고
    • Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin
    • Lees-Miller JP, Henry G, Helfman DM. (1992). Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin. Proc Natl Acad Sci U S A 89:80-3.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 80-83
    • Lees-Miller, J.P.1    Henry, G.2    Helfman, D.M.3
  • 149
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • Leipe DD, Wolf YI, Koonin EV, Aravind L. (2002). Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317: 41-72. (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 150
    • 0024317055 scopus 로고
    • The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity
    • Lemire BD, Fankhauser C, Baker A, Schatz G. (1989). The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity. J Biol Chem 264: 20206-15. (Pubitemid 20009197)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.34 , pp. 20206-20215
    • Lemire, B.D.1    Fankhauser, C.2    Baker, A.3    Schatz, G.4
  • 151
    • 77954874614 scopus 로고    scopus 로고
    • Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP
    • Leonardy S, Miertzschke M, Bulyha I, et al. (2010). Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP. EMBO J 29:2276-89.
    • (2010) EMBO J , vol.29 , pp. 2276-2289
    • Leonardy, S.1    Miertzschke, M.2    Bulyha, I.3
  • 152
    • 47149100894 scopus 로고    scopus 로고
    • Evolution of the multivesicular body ESCRT machinery; Retention across the eukaryotic lineage
    • Leung KF, Dacks JB, Field MC. (2008). Evolution of the multivesicular body ESCRT machinery; retention across the eukaryotic lineage. Traffic 9:1698-716.
    • (2008) Traffic , vol.9 , pp. 1698-1716
    • Leung, K.F.1    Dacks, J.B.2    Field, M.C.3
  • 153
    • 10044297008 scopus 로고    scopus 로고
    • Functional genomic analysis of the ADP-ribosylation factor family of GTPases: Phylogeny among diverse eukaryotes and function in C. elegans
    • DOI 10.1096/fj.04-2273com
    • Li Y, Kelly WG, Logsdon JM, et al. (2004). Functional genomic analysis of the ADP-ribosylation factor family of GTPases: phylogeny among diverse eukaryotes and function in C. elegans. FASEB J 18: 1834-50. (Pubitemid 39610507)
    • (2004) FASEB Journal , vol.18 , Issue.15 , pp. 1834-1850
    • Li, Y.1    Kelly, W.G.2    Logsdon Jr., J.M.3    Schurko, A.M.4    Harfe, B.D.5    Hill-Harfe, K.L.6    Kahn, R.A.7
  • 154
    • 33845679477 scopus 로고    scopus 로고
    • Reconstructing the mosaic glycolytic pathway of the anaerobic eukaryote Monocercomonoides
    • DOI 10.1128/EC.00258-06
    • Liapounova NA, Hampl V, Gordon PMK, et al. (2006). Reconstructing the mosaic glycolytic pathway of the anaerobic eukaryote Monocercomonoides. Eukaryot Cell 5:2138-46. (Pubitemid 44956825)
    • (2006) Eukaryotic Cell , vol.5 , Issue.12 , pp. 2138-2146
    • Liapounova, N.A.1    Hampl, V.2    Gordon, P.M.K.3    Sensen, C.W.4    Gedamu, L.5    Dacks, J.B.6
  • 155
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. (2009). Function and biogenesis of iron-sulphur proteins. Nature 460:831-8.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 156
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • DOI 10.1016/S0968-0004(00)01589-9, PII S0968000400015899
    • Lill R, Kispal G. (2000). Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem. Sci 25:352-6. (Pubitemid 30497238)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.8 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 157
    • 84864296714 scopus 로고    scopus 로고
    • The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
    • Lill R, Hoffmann B, Molik S, et al. (2012). The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism. Biochim Biophys Acta 1823:1491-508.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 1491-1508
    • Lill, R.1    Hoffmann, B.2    Molik, S.3
  • 159
    • 77954743125 scopus 로고    scopus 로고
    • Endocytosis-like protein uptake in the bacterium Gemmata obscuriglobus
    • Lonhienne TG, Sagulenko E, Webb RI, et al. (2010). Endocytosis-like protein uptake in the bacterium Gemmata obscuriglobus. Proc Natl Acad Sci U S A 107:12883-8.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12883-12888
    • Lonhienne, T.G.1    Sagulenko, E.2    Webb, R.I.3
  • 160
    • 0345299175 scopus 로고    scopus 로고
    • Metabolic symbiosis at the origin of eukaryotes
    • DOI 10.1016/S0968-0004(98)01342-5, PII S0968000498013425
    • López-Garćia P, Moreira D. (1999). Metabolic symbiosis at the origin of eukaryotes. Trends Biochem Sci 24:88-93. (Pubitemid 29225240)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.3 , pp. 88-93
    • Lopez-Garcia, P.1    Moreira, D.2
  • 161
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • Lopez D, Kolter R. (2010). Functional microdomains in bacterial membranes. Genes Dev 24:1893-902.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • Lopez, D.1    Kolter, R.2
  • 162
    • 59649113268 scopus 로고    scopus 로고
    • Fossil steroids record the appearance of Demospongiae during the Cryogenian period
    • Love GD, Grosjean E, Stalvies C, et al. (2009). Fossil steroids record the appearance of Demospongiae during the Cryogenian period. Nature 457:718-21.
    • (2009) Nature , vol.457 , pp. 718-721
    • Love, G.D.1    Grosjean, E.2    Stalvies, C.3
  • 163
    • 33845672530 scopus 로고    scopus 로고
    • A bacterial dynamin-like protein
    • DOI 10.1038/nature05312, PII NATURE05312
    • Low HH, Lowe J. (2006). A bacterial dynamin-like protein. Nature 444: 766-9. (Pubitemid 44949606)
    • (2006) Nature , vol.444 , Issue.7120 , pp. 766-769
    • Low, H.H.1    Lowe, J.2
  • 164
    • 72249102216 scopus 로고    scopus 로고
    • Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving
    • Low HH, Sachse C, Amos LA, Lowe J. (2009). Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. Cell 139:1342-52.
    • (2009) Cell , vol.139 , pp. 1342-1352
    • Low, H.H.1    Sachse, C.2    Amos, L.A.3    Lowe, J.4
  • 165
    • 84870700689 scopus 로고    scopus 로고
    • The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster assembly pathway to maintain nuclear genome integrity in Arabidopsis
    • Luo D, Bernard DG, Balk J, et al. (2012). The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster assembly pathway to maintain nuclear genome integrity in Arabidopsis. Plant Cell 24:4135-48.
    • (2012) Plant Cell , vol.24 , pp. 4135-4148
    • Luo, D.1    Bernard, D.G.2    Balk, J.3
  • 167
    • 77957130448 scopus 로고    scopus 로고
    • Evolution of diverse cell division and vesicle formation systems in Archaea
    • Makarova KS, Yutin N, Bell SD, Koonin EV. (2010). Evolution of diverse cell division and vesicle formation systems in Archaea. Nat Rev Microbiol 8:731-41.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 731-741
    • Makarova, K.S.1    Yutin, N.2    Bell, S.D.3    Koonin, E.V.4
  • 168
    • 51449085783 scopus 로고    scopus 로고
    • An expanded inventory of conserved meiotic genes provides evidence for sex in Trichomonas vaginalis
    • Malik SB, Pightling AW, Stefaniak LM, et al. (2007a). An expanded inventory of conserved meiotic genes provides evidence for sex in Trichomonas vaginalis. PLoS One 3:e2879.
    • (2007) PLoS One , vol.3
    • Malik, S.B.1    Pightling, A.W.2    Stefaniak, L.M.3
  • 169
    • 37549056250 scopus 로고    scopus 로고
    • Protist homologs of the meiotic Spo11 gene and topoisomerase VI reveal an evolutionary history of gene duplication and lineage-specific loss
    • Malik SB, Ramesh MA, Hulstrand AM, Logsdon Jr JM. (2007b). Protist homologs of the meiotic Spo11 gene and topoisomerase VI reveal an evolutionary history of gene duplication and lineage-specific loss. Mol Biol Evol 24:2827-41.
    • (2007) Mol Biol Evol , vol.24 , pp. 2827-2841
    • Malik, S.B.1    Ramesh, M.A.2    Hulstrand, A.M.3    Logsdon Jr., J.M.4
  • 170
  • 171
    • 84873443433 scopus 로고    scopus 로고
    • Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids
    • Manna PT, Kelly S, Field MC. (2013). Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids. Mol Phylogenet Evol 67:123-8.
    • (2013) Mol Phylogenet Evol , vol.67 , pp. 123-128
    • Manna, P.T.1    Kelly, S.2    Field, M.C.3
  • 172
    • 17144404877 scopus 로고    scopus 로고
    • Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex
    • Mans BJ, Anantharaman V, Aravind L, Koonin EV. (2004). Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Cell Cycle 3:1612-37. (Pubitemid 40521416)
    • (2004) Cell Cycle , vol.3 , Issue.12 , pp. 1612-1637
    • Mans, B.J.1    Anantharaman, V.2    Aravind, L.3    Koonin, E.V.4
  • 173
    • 82955193292 scopus 로고    scopus 로고
    • The puzzling origin of the autophagosomal membrane
    • Mari M, Tooze SA, Reggiori F. (2011). The puzzling origin of the autophagosomal membrane. F1000 Biol Rep 3:25.
    • (2011) F1000 Biol Rep , vol.3 , pp. 25
    • Mari, M.1    Tooze, S.A.2    Reggiori, F.3
  • 174
    • 84882460141 scopus 로고    scopus 로고
    • Eukaryote and mitochondrial origins: Two sides of the same coin and too much ado about oxygen
    • Falkowski P, Knoll AH, eds. New York: Academic Press
    • Martin W. (2007). Eukaryote and mitochondrial origins: two sides of the same coin and too much ado about oxygen. In: Falkowski P, Knoll AH, eds. Primary Producers of the Sea. New York: Academic Press.
    • (2007) Primary Producers of the Sea
    • Martin, W.1
  • 175
    • 33644783626 scopus 로고    scopus 로고
    • Introns and the origin of nucleus-cytosol compartmentalization
    • DOI 10.1038/nature04531, PII N04531
    • Martin W, Koonin EV. (2006). Introns and the origin of nucleus-cytosol compartmentalization. Nature 440:41-5. (Pubitemid 43336261)
    • (2006) Nature , vol.440 , Issue.7080 , pp. 41-45
    • Martin, W.1    Koonin, E.V.2
  • 176
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis for the first eukaryote
    • DOI 10.1038/32096
    • Martin W, Müller M. (1998). The hydrogen hypothesis for the first eukaryote. Nature 392:37-41. (Pubitemid 28150580)
    • (1998) Nature , vol.392 , Issue.6671 , pp. 37-41
    • Martin, W.1    Muller, M.2
  • 178
    • 25144456544 scopus 로고    scopus 로고
    • Membrane vesicles traffic signals and facilitate group activities in a prokaryote
    • DOI 10.1038/nature03925, PII N03925
    • Mashburn LM, Whiteley M. (2005). Membrane vesicles traffic signals and facilitate group activities in a prokaryote. Nature 437:422-5. (Pubitemid 41613505)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 422-425
    • Mashburn, L.M.1    Whiteley, M.2
  • 179
    • 64949154995 scopus 로고    scopus 로고
    • Evolution of the metazoanspecific importin alpha gene family
    • Mason DA, Stage DE, Goldfarb DS. (2009). Evolution of the metazoanspecific importin alpha gene family. J Mol Evol 68:351-65.
    • (2009) J Mol Evol , vol.68 , pp. 351-365
    • Mason, D.A.1    Stage, D.E.2    Goldfarb, D.S.3
  • 180
    • 75049084936 scopus 로고    scopus 로고
    • Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA
    • Mauriello EM, Mouhamar F, Nan B, et al. (2010). Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA. EMBO J 29:315-26.
    • (2010) EMBO J , vol.29 , pp. 315-326
    • Mauriello, E.M.1    Mouhamar, F.2    Nan, B.3
  • 182
    • 84860388895 scopus 로고    scopus 로고
    • Planctomycetes and eukaryotes: A case of analogy not homology
    • McInerney JO, Martin WF, Koonin EV, et al. (2011). Planctomycetes and eukaryotes: a case of analogy not homology. Bioessays 33:810-7.
    • (2011) Bioessays , vol.33 , pp. 810-817
    • McInerney, J.O.1    Martin, W.F.2    Koonin, E.V.3
  • 183
    • 0015575834 scopus 로고
    • The axostyle of saccinobaculus. II. Motion of the microtubule bundle and a structural comparison of straight and bent axostyles
    • McIntosh JR. (1973). The axostyle of Saccinobaculus. II. Motion of the microtubule bundle and a structural comparison of straight and bent axostyles. J Cell Biol 56:324-39.
    • (1973) J Cell Biol , vol.56 , pp. 324-339
    • McIntosh, J.R.1
  • 184
    • 0015581274 scopus 로고
    • The axostyle of saccinobaculus. I. Structure of the organism and its microtubule bundle
    • McIntosh JR, Ogata ES, Landis SC. (1973). The axostyle of Saccinobaculus. I. Structure of the organism and its microtubule bundle. J Cell Biol 56:304-23.
    • (1973) J Cell Biol , vol.56 , pp. 304-323
    • McIntosh, J.R.1    Ogata, E.S.2    Landis, S.C.3
  • 185
    • 33845899112 scopus 로고    scopus 로고
    • Composition of the plant nuclear envelope: Theme and variations
    • DOI 10.1093/jxb/erl009
    • Meier I. (2007). Composition of the plant nuclear envelope: theme and variations. J Exp Bot 58:27-34. (Pubitemid 46026246)
    • (2007) Journal of Experimental Botany , vol.58 , Issue.1 , pp. 27-34
    • Meier, I.1
  • 186
    • 4444252876 scopus 로고    scopus 로고
    • Speculations on the evolution of 9+2 organelles and the role of central pair microtubules
    • DOI 10.1016/j.biolcel.2004.07.004, PII S0248490004001662
    • Mitchell DR. (2004). Speculations on the evolution of 9+2 organelles and the role of central pair microtubules. Biol Cell 96:691-6. (Pubitemid 39618876)
    • (2004) Biology of the Cell , vol.96 , Issue.9 , pp. 691-696
    • Mitchell, D.R.1
  • 187
    • 84934439875 scopus 로고    scopus 로고
    • The evolution of eukaryotic cilia and flagella as motile and sensory organelles
    • Mitchell DR. (2007). The evolution of eukaryotic cilia and flagella as motile and sensory organelles. Adv Exp Med Biol 607:130-40.
    • (2007) Adv Exp Med Biol , vol.607 , pp. 130-140
    • Mitchell, D.R.1
  • 188
    • 0000411385 scopus 로고
    • A case of maternal inheritance in Neurospora crassa
    • Mitchell M, Mitchell H. (1952). A case of maternal inheritance in Neurospora crassa. Proc Natl Acad Sci USA 38:442.
    • (1952) Proc Natl Acad Sci USA , vol.38 , pp. 442
    • Mitchell, M.1    Mitchell, H.2
  • 189
    • 84863270815 scopus 로고    scopus 로고
    • Acinetobacter baumannii outer membrane protein a modulates the biogenesis of outer membrane vesicles
    • Moon DC, Choi CH, Lee JH, et al. (2012). Acinetobacter baumannii outer membrane protein a modulates the biogenesis of outer membrane vesicles. J Microbiol 50:155-60.
    • (2012) J Microbiol , vol.50 , pp. 155-160
    • Moon, D.C.1    Choi, C.H.2    Lee, J.H.3
  • 190
    • 84856996622 scopus 로고    scopus 로고
    • Clustered organization, polycistronic transcription, and evolution of modification-guide snoRNA genes in Euglena gracilis
    • Moore AN, Russell AG. (2012). Clustered organization, polycistronic transcription, and evolution of modification-guide snoRNA genes in Euglena gracilis. Mol Genet Genomics 287:55-66.
    • (2012) Mol Genet Genomics , vol.287 , pp. 55-66
    • Moore, A.N.1    Russell, A.G.2
  • 194
    • 70450224864 scopus 로고    scopus 로고
    • Evolution and diversity of the Golgi body
    • Mowbrey K, Dacks JB. (2009). Evolution and diversity of the Golgi body. FEBS Lett 583:3738-45.
    • (2009) FEBS Lett , vol.583 , pp. 3738-3745
    • Mowbrey, K.1    Dacks, J.B.2
  • 196
    • 84862556334 scopus 로고    scopus 로고
    • Biochemistry and evolution of anaerobic energy metabolism in eukaryotes
    • Müller M, Mentel M, Van Hellemond JJ, et al. (2012). Biochemistry and evolution of anaerobic energy metabolism in eukaryotes. Microbiol Mol Biol Rev 76:444-95.
    • (2012) Microbiol Mol Biol Rev , vol.76 , pp. 444-495
    • Müller, M.1    Mentel, M.2    Van Hellemond, J.J.3
  • 197
    • 78651128209 scopus 로고
    • Intramitochondrial fibers with DNA characteristics. I. Fixation and electron staining reactions
    • Nass MM, Nass S. (1963). Intramitochondrial fibers with DNA characteristics. I. Fixation and electron staining reactions. J Cell Biol 19:593-611.
    • (1963) J Cell Biol , vol.19 , pp. 593-611
    • Nass, M.M.1    Nass, S.2
  • 198
    • 84863345834 scopus 로고    scopus 로고
    • Novel sterol metabolic network of Trypanosoma brucei procyclic and bloodstream forms
    • Nes CR, Singha UK, Liu J, et al. (2012). Novel sterol metabolic network of Trypanosoma brucei procyclic and bloodstream forms. Biochem. J 443:267-77.
    • (2012) Biochem. J , vol.443 , pp. 267-277
    • Nes, C.R.1    Singha, U.K.2    Liu, J.3
  • 199
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W, Herrmann JM. (2007). Translocation of proteins into mitochondria. Annu Rev Biochem 76:723-49.
    • (2007) Annu Rev Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 200
    • 59449093322 scopus 로고    scopus 로고
    • Repeated secondary loss of adaptin complex genes in the Apicomplexa
    • Nevin WD, Dacks JB. (2009). Repeated secondary loss of adaptin complex genes in the Apicomplexa. Parasitol Int 58:86-94.
    • (2009) Parasitol Int , vol.58 , pp. 86-94
    • Nevin, W.D.1    Dacks, J.B.2
  • 201
    • 79955598535 scopus 로고    scopus 로고
    • Insights into the evolution of Archaea and eukaryotic protein modifier systems revealed by the genome of a novel archaeal group
    • Nunoura T, Takaki Y, Kakuta J, et al. (2011). Insights into the evolution of Archaea and eukaryotic protein modifier systems revealed by the genome of a novel archaeal group. Nucleic Acids Res 39:3204-23.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3204-3223
    • Nunoura, T.1    Takaki, Y.2    Kakuta, J.3
  • 202
    • 77957749413 scopus 로고    scopus 로고
    • The first eukaryote cell: An unfinished history of contestation
    • O'Malley MA. (2010). The first eukaryote cell: an unfinished history of contestation. Stud Hist Philos Biol Biomed Sci 41:212-24.
    • (2010) Stud Hist Philos Biol Biomed Sci , vol.41 , pp. 212-224
    • O'Malley, M.A.1
  • 203
    • 79955679956 scopus 로고    scopus 로고
    • Evolution of the karyopherinβ family of nucleocytoplasmic transport factors; Ancient origins and continued specialization
    • O'Reilly AJ, Dacks JB, Field MC. (2011). Evolution of the karyopherinβ family of nucleocytoplasmic transport factors; ancient origins and continued specialization. PLoS One 6:e19308.
    • (2011) PLoS One , vol.6
    • O'Reilly, A.J.1    Dacks, J.B.2    Field, M.C.3
  • 204
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species
    • Odronitz F, Kollmar M. (2007). Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species. Genome Biol 8:R196.
    • (2007) Genome Biol , vol.8
    • Odronitz, F.1    Kollmar, M.2
  • 205
    • 84860450204 scopus 로고    scopus 로고
    • To the pore and through the pore: A story of mRNA export kinetics
    • Oeffinger M, Zenklusen D. (2012). To the pore and through the pore: a story of mRNA export kinetics. Biochim Biophys Acta 1819:494-506.
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 494-506
    • Oeffinger, M.1    Zenklusen, D.2
  • 206
    • 84856866968 scopus 로고    scopus 로고
    • The roles of flotillin microdomains-endocytosis and beyond
    • Otto GP, Nichols BJ. (2011). The roles of flotillin microdomains- endocytosis and beyond. J Cell Sci 124:3933-40.
    • (2011) J Cell Sci , vol.124 , pp. 3933-3940
    • Otto, G.P.1    Nichols, B.J.2
  • 207
    • 0028936690 scopus 로고
    • Biochemical and physiological effects of sterol alterations in yeast-A review
    • Parks LW, Smith SJ, Crowley JH. (1995). Biochemical and physiological effects of sterol alterations in yeast-a review. Lipids 30:227-30.
    • (1995) Lipids , vol.30 , pp. 227-230
    • Parks, L.W.1    Smith, S.J.2    Crowley, J.H.3
  • 208
    • 80052019696 scopus 로고    scopus 로고
    • Estimating the timing of early eukaryotic diversification with multigene molecular clocks
    • Parfrey LW, Lahr DJ, Knoll AH, Katz LA. (2011). Estimating the timing of early eukaryotic diversification with multigene molecular clocks. Proc Natl Acad Sci U S A 108:13624-9.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 13624-13629
    • Parfrey, L.W.1    Lahr, D.J.2    Knoll, A.H.3    Katz, L.A.4
  • 209
    • 33646490975 scopus 로고    scopus 로고
    • YfhJ, a molecular adaptor in iron-sulfur cluster formation or a Frataxin-like protein?
    • Pastore C, Adinolfi S, Huynen MA, et al. (2006). YfhJ, a molecular adaptor in iron-sulfur cluster formation or a Frataxin-like protein? Structure 14:857-67.
    • (2006) Structure , vol.14 , pp. 857-867
    • Pastore, C.1    Adinolfi, S.2    Huynen, M.A.3
  • 210
    • 32944463126 scopus 로고    scopus 로고
    • Retention and loss of amino acid biosynthetic pathways based on analysis of whole-genome sequences
    • DOI 10.1128/EC.5.2.272-276.2006
    • Payne SH, Loomis WF. (2006). Retention and loss of amino acid biosynthetic pathways based on the analysis of whole-genome sequences. Eukaryot Cell 5:272-6. (Pubitemid 43262014)
    • (2006) Eukaryotic Cell , vol.5 , Issue.2 , pp. 272-276
    • Payne, S.H.1    Loomis, W.F.2
  • 211
    • 79952744463 scopus 로고    scopus 로고
    • Identification of the meiotic life cycle stage of Trypanosoma brucei in the tsetse fly
    • Peacock L, Ferris V, Sharma R, et al. (2011). Identification of the meiotic life cycle stage of Trypanosoma brucei in the tsetse fly. Proc Natl Acad Sci U S A 108:3671-6.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3671-3676
    • Peacock, L.1    Ferris, V.2    Sharma, R.3
  • 212
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce MJ, Mintseris J, Ferreyra J, et al. (2008). Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 322:1104-7.
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3
  • 213
    • 80054845081 scopus 로고    scopus 로고
    • Cdv-based cell division and cell cycle organization in the thaumarchaeon Nitrosopumilus maritimus
    • Pelve EA, Lindas AC, Martens-Habbena W, et al. (2011). Cdv-based cell division and cell cycle organization in the thaumarchaeon Nitrosopumilus maritimus. Mol Microbiol 82:555-66.
    • (2011) Mol Microbiol , vol.82 , pp. 555-566
    • Pelve, E.A.1    Lindas, A.C.2    Martens-Habbena, W.3
  • 214
    • 37249063075 scopus 로고    scopus 로고
    • The Ypt/Rab family and the evolution of trafficking in fungi
    • DOI 10.1111/j.1600-0854.2007.00667.x
    • Pereira-Leal JB. (2008). The Ypt/Rab family and the evolution of trafficking in fungi. Traffic 9:27-38. (Pubitemid 350263461)
    • (2008) Traffic , vol.9 , Issue.1 , pp. 27-38
    • Pereira-Leal, J.B.1
  • 216
    • 0016077677 scopus 로고
    • The evolution of mitosis and the eukaryotic condition
    • Pickett-Heaps J. (1974). The evolution of mitosis and the eukaryotic condition. Biosystems 6:37-48.
    • (1974) Biosystems , vol.6 , pp. 37-48
    • Pickett-Heaps, J.1
  • 217
    • 36749101927 scopus 로고    scopus 로고
    • Characterization of bacterial operons consisting of two tubulins and a kinesin-like gene by the novel Two-Step Gene Walking method
    • Pilhofer M, Bauer AP, Schrallhammer M, et al. (2007). Characterization of bacterial operons consisting of two tubulins and a kinesin-like gene by the novel Two-Step Gene Walking method. Nucleic Acids Res 35:e135.
    • (2007) Nucleic Acids Res , vol.35
    • Pilhofer, M.1    Bauer, A.P.2    Schrallhammer, M.3
  • 218
    • 84855170213 scopus 로고    scopus 로고
    • Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton
    • Pilhofer M, Ladinsky MS, McDowall AW, et al. (2011). Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton. PLoS Biol 9:e1001213.
    • (2011) PLoS Biol , vol.9
    • Pilhofer, M.1    Ladinsky, M.S.2    McDowall, A.W.3
  • 219
    • 34547751897 scopus 로고    scopus 로고
    • Supertrees disentangle the chimerical origin of eukaryotic genomes
    • DOI 10.1093/molbev/msm095
    • Pisani D, Cotton JA, Mcinerney JO. (2007). Supertrees disentangle the chimerical origin of eukaryotic genomes. Mol Biol Evol 24:1752-60. (Pubitemid 47236695)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1752-1760
    • Pisani, D.1    Cotton, J.A.2    McInerney, J.O.3
  • 220
    • 39749142690 scopus 로고    scopus 로고
    • The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
    • Podar M, Wall MA, Makarova KS, Koonin EV. (2008). The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system. Biol Direct 3:2.
    • (2008) Biol Direct , vol.3 , pp. 2
    • Podar, M.1    Wall, M.A.2    Makarova, K.S.3    Koonin, E.V.4
  • 221
    • 0037402596 scopus 로고    scopus 로고
    • Prokaryote and eukaryote evolvability
    • DOI 10.1016/S0303-2647(02)00131-4, PII S0303264702001314
    • Poole AM, Phillips MJ, Penny D. (2003). Prokaryote and eukaryote evolvability. Biosystems 69:163-85. (Pubitemid 36411742)
    • (2003) BioSystems , vol.69 , Issue.2-3 , pp. 163-185
    • Poole, A.M.1    Phillips, M.J.2    Penny, D.3
  • 222
    • 12544259704 scopus 로고    scopus 로고
    • A phylogenomic inventory of meiotic genes; Evidence for sex in Giardia and an early eukaryotic origin of meiosis
    • Ramesh MA, Malik SB, Logsdon JM. (2005). A phylogenomic inventory of meiotic genes; evidence for sex in Giardia and an early eukaryotic origin of meiosis. Curr Biol 15:185-91.
    • (2005) Curr Biol , vol.15 , pp. 185-191
    • Ramesh, M.A.1    Malik, S.B.2    Logsdon, J.M.3
  • 223
    • 0026778964 scopus 로고
    • Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein
    • Ray Chaudhuri D, Park JT. (1992). Escherichia coli cell-division gene fts Z encodes a novel GTP-binding protein. Nature 359:251-4.
    • (1992) Nature , vol.359 , pp. 251-254
    • Raychaudhuri, D.1    Park, J.T.2
  • 224
    • 79955025448 scopus 로고    scopus 로고
    • Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes
    • Renner LD, Weibel DB. (2011). Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes. Proc Natl Acad Sci U S A 108:6264-9.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6264-6269
    • Renner, L.D.1    Weibel, D.B.2
  • 225
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single α- proteobacterial endosymbiosis for all eukaryotes
    • DOI 10.1093/molbev/msl001
    • Richards TA, Van Der Giezen M. (2006). Evolution of the Isd11/IscS complex reveals a single a-proteobacterial endosymbiosis for all eukaryotes. Mol Biol Evol 23:1341-4. (Pubitemid 43992334)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.7 , pp. 1341-1344
    • Richards, T.A.1    Van Der Giezen, M.2
  • 226
    • 24144503755 scopus 로고    scopus 로고
    • Myosin domain evolution and the primary divergence of eukaryotes
    • DOI 10.1038/nature03949
    • Richards TA, Cavalier-Smith T. (2005). Myosin domain evolution and the primary divergence of eukaryotes. Nature 436:1113-18. (Pubitemid 41232283)
    • (2005) Nature , vol.436 , Issue.7054 , pp. 1113-1118
    • Richards, T.A.1    Cavalier-Smith, T.2
  • 227
    • 69449083833 scopus 로고    scopus 로고
    • Autophagy in protists. Examples of secondary loss, lineage-specific innovations, and the conundrum of remodelling a single mitochondrion
    • Rigden DJ, Michels PAM., Ginger ML. (2009). Autophagy in protists. Examples of secondary loss, lineage-specific innovations, and the conundrum of remodelling a single mitochondrion. Autophagy 5: 784-94.
    • (2009) Autophagy , vol.5 , pp. 784-794
    • Rigden, D.J.1    Michels, P.A.M.2    Ginger, M.L.3
  • 229
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • DOI 10.1016/j.tcb.2004.02.002, PII S0962892404000492
    • Robinson MS. (2004). Adaptable adaptors for coated vesicles. Trends Cell Biol 4:167-74. (Pubitemid 38447116)
    • (2004) Trends in Cell Biology , vol.14 , Issue.4 , pp. 167-174
    • Robinson, M.S.1
  • 230
    • 0032702602 scopus 로고    scopus 로고
    • Reconstructing early events in eukaryotic evolution
    • Roger AJ. (1999). Reconstructing early events in eukaryotic evolution. Am Nat 154:S146-S163.
    • (1999) Am Nat , vol.154
    • Roger, A.J.1
  • 231
    • 34250016257 scopus 로고    scopus 로고
    • Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli
    • DOI 10.1111/j.1365-2958.2007.05727.x
    • Romantsov T, Helbig S, Culham DE, et al. (2007). Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli. Mol Microbiol 64:1455-65. (Pubitemid 46889896)
    • (2007) Molecular Microbiology , vol.64 , Issue.6 , pp. 1455-1465
    • Romantsov, T.1    Helbig, S.2    Culham, D.E.3    Gill, C.4    Stalker, L.5    Wood, J.M.6
  • 233
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout MP, Aitchison JD, Suprapto A, et al. (2000). The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148:635-51.
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3
  • 234
    • 0014070709 scopus 로고
    • On the origin of mitosing cells
    • Sagan L. (1967). On the origin of mitosing cells. J Theoret Biol 14: 225-74.
    • (1967) J Theoret Biol , vol.14 , pp. 225-274
    • Sagan, L.1
  • 236
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • Samson RY, Obita T, Freund SM, et al. (2008). A role for the ESCRT system in cell division in archaea. Science 322:1710-13.
    • (2008) Science , vol.322 , pp. 1710-1713
    • Samson, R.Y.1    Obita, T.2    Freund, S.M.3
  • 237
    • 78651468723 scopus 로고    scopus 로고
    • Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division
    • Samson RY, Obita T, Hodgson B, et al. (2011). Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division. Mol Cell 41:186-96.
    • (2011) Mol Cell , vol.41 , pp. 186-196
    • Samson, R.Y.1    Obita, T.2    Hodgson, B.3
  • 238
    • 27844543263 scopus 로고    scopus 로고
    • Archaeal chromatin proteins: Different structures but common function?
    • DOI 10.1016/j.mib.2005.10.007, PII S1369527405001633, Growth Development
    • Sandman K, Reeve JN. (2005). Archaeal chromatin proteins: different structures but common function? Curr Opin Microbiol 8:656-61. (Pubitemid 41643033)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 656-661
    • Sandman, K.1    Reeve, J.N.2
  • 240
    • 75749127849 scopus 로고    scopus 로고
    • The compartmentalized bacteria of the planctomycetes- verrucomicrobiachlamydiae superphylum have membrane coat-like proteins
    • Santarella-Mellwig R, Franke J, Jaedicke A, et al. (2010). The compartmentalized bacteria of the planctomycetes-verrucomicrobiachlamydiae superphylum have membrane coat-like proteins. PLoS Biol 19:e1000281.
    • (2010) PLoS Biol , vol.19
    • Santarella-Mellwig, R.1    Franke, J.2    Jaedicke, A.3
  • 242
    • 79959310042 scopus 로고    scopus 로고
    • Novel metabolic pathways in Archaea
    • Sato T, Atomi H. (2011). Novel metabolic pathways in Archaea. Curr Opin Microbiol 14:307-14.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 307-314
    • Sato, T.1    Atomi, H.2
  • 243
    • 84857159902 scopus 로고    scopus 로고
    • Cystinosin, MPDU1, SWEETs and KDELR belong to a well-defined protein family with putative function of cargo receptors involved in vesicle trafficking
    • Saudek V. (2012). Cystinosin, MPDU1, SWEETs and KDELR belong to a well-defined protein family with putative function of cargo receptors involved in vesicle trafficking. PLoS One 7:e30876.
    • (2012) PLoS One , vol.7
    • Saudek, V.1
  • 244
    • 0037730405 scopus 로고    scopus 로고
    • Essential role of the C. Elegans Arp2/3 complex in cell migration during ventral enclosure
    • DOI 10.1242/jcs.00362
    • Sawa M, Suetsugu S, Sugimoto A, et al. (2003). Essential role of the C. elegans Arp2/3 complex in cell migration during ventral enclosure. J Cell Sci 116:1505-18. (Pubitemid 36527497)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1505-1518
    • Sawa, M.1    Suetsugu, S.2    Sugimoto, A.3    Miki, H.4    Yamamoto, M.5    Takenawa, T.6
  • 246
    • 84860503869 scopus 로고    scopus 로고
    • A bilayer-couple model of bacterial outer membrane vesicle biogenesis
    • Schertzer JW, Whiteley M. (2012). A bilayer-couple model of bacterial outer membrane vesicle biogenesis. Mbio 3:e00297-11.
    • (2012) Mbio , vol.3
    • Schertzer, J.W.1    Whiteley, M.2
  • 248
    • 45549094609 scopus 로고    scopus 로고
    • Using a meiosis detection toolkit to investigate ancient asexual "scandals" and the evolution of sex
    • DOI 10.1002/bies.20764
    • Schurko AM, Logsdon Jr JM. (2008). Using a meiosis detection toolkit to investigate ancient asexual "scandals" and the evolution of sex. Bioessays 30:579-89. (Pubitemid 351859414)
    • (2008) BioEssays , vol.30 , Issue.6 , pp. 579-589
    • Schurko, A.M.1    Logsdon Jr., J.M.2
  • 249
    • 0026571486 scopus 로고
    • New yeast actin-like gene required late in the cell cycle
    • Schwob E, Martin RP. (1992). New yeast actin-like gene required late in the cell cycle. Nature 355:179-82.
    • (1992) Nature , vol.355 , pp. 179-182
    • Schwob, E.1    Martin, R.P.2
  • 250
    • 34247250312 scopus 로고    scopus 로고
    • The actin multigene family of Paramecium tetraurelia
    • Sehring IM, Mansfeld J, Reiner C, et al. (2007). The actin multigene family of Paramecium tetraurelia. BMC Genomics 8:82.
    • (2007) BMC Genomics , vol.8 , pp. 82
    • Sehring, I.M.1    Mansfeld, J.2    Reiner, C.3
  • 251
    • 84860719904 scopus 로고    scopus 로고
    • Discovery of an archetypal protein transport system in bacterial outer membranes
    • Selkrig J, Mosbahi K, Webb CT, et al. (2012). Discovery of an archetypal protein transport system in bacterial outer membranes. Nat Struct Mol Biol 19:506-10.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 506-510
    • Selkrig, J.1    Mosbahi, K.2    Webb, C.T.3
  • 252
    • 78651090509 scopus 로고    scopus 로고
    • Comparative genomics of proteins involved in RNA nucleocytoplasmic export
    • Serpeloni M, Vidal NM, Goldenberg S, et al. (2011). Comparative genomics of proteins involved in RNA nucleocytoplasmic export. BMC Evol Biol 11:7.
    • (2011) BMC Evol Biol , vol.11 , pp. 7
    • Serpeloni, M.1    Vidal, N.M.2    Goldenberg, S.3
  • 253
    • 70849086538 scopus 로고    scopus 로고
    • Why and how bacteria localize proteins
    • Shapiro L, McAdams HH, Losick R. (2009). Why and how bacteria localize proteins. Science 326:1225-8.
    • (2009) Science , vol.326 , pp. 1225-1228
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 254
    • 23044446243 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters
    • DOI 10.1002/prot.20481
    • Shimomura Y, Takahashi Y, Kakuta Y, Fukuyama K. (2005). Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters. Proteins 60: 566-9. (Pubitemid 41061649)
    • (2005) Proteins: Structure, Function and Genetics , vol.60 , Issue.3 , pp. 566-569
    • Shimomura, Y.1    Takahashi, Y.2    Kakuta, Y.3    Fukuyama, K.4
  • 255
    • 27844507018 scopus 로고    scopus 로고
    • Unusual pathways and enzymes of central carbohydrate metabolism in Archaea
    • DOI 10.1016/j.mib.2005.10.014, PII S1369527405001700, Growth Development
    • Siebers B, Schönheit P. (2005). Unusual pathways and enzymes of central carbohydrate metabolism in Archaea. Curr. Opin. Microbiol 8: 695-705. (Pubitemid 41643038)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 695-705
    • Siebers, B.1    Schonheit, P.2
  • 256
    • 80054902318 scopus 로고    scopus 로고
    • The nucleoskeleton as a genomeassociated dynamic network of networks
    • Simon DN, Wilson KL. (2011). The nucleoskeleton as a genomeassociated dynamic network of networks. Nat Rev Mol Cell Biol 12: 695-708.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 695-708
    • Simon, D.N.1    Wilson, K.L.2
  • 257
    • 33749337533 scopus 로고    scopus 로고
    • MoxR AAA+ ATPases: A novel family of molecular chaperones?
    • DOI 10.1016/j.jsb.2006.02.009, PII S1047847706000657, AAA + Proteins
    • Snider J, Houry WA. (2006). MoxR AAA+ ATPases: a novel family of molecular chaperones? J Struct Biol 156:200-9. (Pubitemid 44488671)
    • (2006) Journal of Structural Biology , vol.156 , Issue.1 , pp. 200-209
    • Snider, J.1    Houry, W.A.2
  • 258
    • 79955547953 scopus 로고    scopus 로고
    • Mouse knock-out of IOP1 protein reveals its essential role in mammalian cytosolic iron-sulfur protein biogenesis
    • Song D, Lee FS. (2011). Mouse knock-out of IOP1 protein reveals its essential role in mammalian cytosolic iron-sulfur protein biogenesis. J Biol Chem 286:15797-805.
    • (2011) J Biol Chem , vol.286 , pp. 15797-15805
    • Song, D.1    Lee, F.S.2
  • 259
    • 84862241805 scopus 로고    scopus 로고
    • The DSL1 Complex: The smallest but not the least CATCHR
    • Spang A. (2012). The DSL1 Complex: The smallest but not the least CATCHR. Traffic 13:908-13.
    • (2012) Traffic , vol.13 , pp. 908-913
    • Spang, A.1
  • 260
    • 53749093685 scopus 로고    scopus 로고
    • Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography
    • DOI 10.1104/pp.108.120618
    • Staehelin LA, Kang BH. (2008). Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography. Plant Physiol 147:1454-68. (Pubitemid 352844193)
    • (2008) Plant Physiology , vol.147 , Issue.4 , pp. 1454-1468
    • Staehelin, L.A.1    Kang, B.-H.2
  • 261
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • Starr DA, Fridolfsson HN. (2010). Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu Rev Cell Dev Biol 26:421-44.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 262
  • 263
    • 84863747679 scopus 로고    scopus 로고
    • MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity
    • Stehling O, Vashisht AA, Mascarenhas J, et al. (2012). MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity. Science 337:195-9.
    • (2012) Science , vol.337 , pp. 195-199
    • Stehling, O.1    Vashisht, A.A.2    Mascarenhas, J.3
  • 264
    • 84858296065 scopus 로고    scopus 로고
    • The yeast Golgi apparatus
    • Suda Y, Nakano A. (2011). The yeast Golgi apparatus. Traffic 13: 505-10.
    • (2011) Traffic , vol.13 , pp. 505-510
    • Suda, Y.1    Nakano, A.2
  • 266
    • 79956308305 scopus 로고    scopus 로고
    • Motor-driven intracellular transport powers bacterial gliding motility
    • Sun M, Wartel M, Cascales E, et al. (2011). Motor-driven intracellular transport powers bacterial gliding motility. Proc Natl Acad Sci USA 108:7559-64.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7559-7564
    • Sun, M.1    Wartel, M.2    Cascales, E.3
  • 268
    • 79551629546 scopus 로고    scopus 로고
    • Identification and characterization of nuclear pore complex components in Arabidopsis thaliana
    • Tamura K, Fukao Y, Iwamoto M, et al. (2010). Identification and characterization of nuclear pore complex components in Arabidopsis thaliana. Plant Cell 22:4084-97.
    • (2010) Plant Cell , vol.22 , pp. 4084-4097
    • Tamura, K.1    Fukao, Y.2    Iwamoto, M.3
  • 269
    • 80052410893 scopus 로고    scopus 로고
    • The mechanism of nucleocytoplasmic transport through the nuclear pore complex
    • Tetenbaum-Novatt J, Rout MP. (2010). The mechanism of nucleocytoplasmic transport through the nuclear pore complex. Cold Spring Harb Symp Quant Biol 75:567-84.
    • (2010) Cold Spring Harb Symp Quant Biol , vol.75 , pp. 567-584
    • Tetenbaum-Novatt, J.1    Rout, M.P.2
  • 270
    • 2442611708 scopus 로고    scopus 로고
    • Snf1-related protein kinase 1 is needed for growth in a normal day-night light cycle
    • DOI 10.1038/sj.emboj.7600182
    • Thelander M, Olsson T, Ronne H. (2004). Snf1-related protein kinase 1 is needed for growth in a normal day-night light cycle. EMBO J 23: 1900-10. (Pubitemid 38649652)
    • (2004) EMBO Journal , vol.23 , Issue.8 , pp. 1900-1910
    • Thelander, M.1    Olsson, T.2    Ronne, H.3
  • 271
    • 84862562185 scopus 로고    scopus 로고
    • An evolutionary network of genes present in the eukaryote common ancestor polls genomes on eukaryotic and mitochondrial origin
    • Thiergart T, Landan G, Schenk M, et al. (2012). An evolutionary network of genes present in the eukaryote common ancestor polls genomes on eukaryotic and mitochondrial origin. Genome Biol Evol 4:466-85.
    • (2012) Genome Biol Evol , vol.4 , pp. 466-485
    • Thiergart, T.1    Landan, G.2    Schenk, M.3
  • 272
    • 84863001148 scopus 로고    scopus 로고
    • Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis
    • Tsaousis AD, Choudens SOD, Gentekaki E, et al. (2012). Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis. Proc Natl Acad Sci U S A 109:10426-31.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10426-10431
    • Tsaousis, A.D.1    Choudens, S.O.D.2    Gentekaki, E.3
  • 273
    • 44349083493 scopus 로고    scopus 로고
    • A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi
    • Tsaousis AD, Kunji ER, Goldberg AV, et al. (2008). A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi. Nature 453:533-6.
    • (2008) Nature , vol.453 , pp. 533-536
    • Tsaousis, A.D.1    Kunji, E.R.2    Goldberg, A.V.3
  • 274
    • 65849420352 scopus 로고    scopus 로고
    • Hydrogenosomes and mitosomes: Conservation and evolution of functions
    • Van Der Giezen M. (2009). Hydrogenosomes and mitosomes: conservation and evolution of functions. J Euk Microbiol 56: 221-31.
    • (2009) J Euk Microbiol , vol.56 , pp. 221-231
    • Van Der Giezen, M.1
  • 275
    • 84876854722 scopus 로고    scopus 로고
    • Evolution of modular intraflagellar transport from a coatomer-like progenitor
    • van Dam TPJ, Townsend MJ, Turk M, et al. (2013). Evolution of modular intraflagellar transport from a coatomer-like progenitor. Proc Natl Acad Sci U S A 110:6943-8.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6943-6948
    • Van Dam, T.P.J.1    Townsend, M.J.2    Turk, M.3
  • 277
    • 1642462396 scopus 로고    scopus 로고
    • Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota
    • Vaughan S, Wickstead B, Gull K, Addinall SG. (2004). Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota. J Mol Evol 58:19-29.
    • (2004) J Mol Evol , vol.58 , pp. 19-29
    • Vaughan, S.1    Wickstead, B.2    Gull, K.3    Addinall, S.G.4
  • 278
    • 70749093076 scopus 로고    scopus 로고
    • Comparative analysis of plant genomes allows the definition of the "Phytolongins": A novel non-SNARE longin domain protein family
    • Vedovato M, Rossi V, Dacks JB, Filippini F. (2009). Comparative analysis of plant genomes allows the definition of the "Phytolongins": a novel non-SNARE longin domain protein family. BMC Genomics 10:510.
    • (2009) BMC Genomics , vol.10 , pp. 510
    • Vedovato, M.1    Rossi, V.2    Dacks, J.B.3    Filippini, F.4
  • 281
    • 0024447881 scopus 로고
    • Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode
    • Weber K, Plessmann U, Ulrich W. (1989). Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode. EMBO J 8:3221-7. (Pubitemid 19273547)
    • (1989) EMBO Journal , vol.8 , Issue.11 , pp. 3221-3227
    • Weber, K.1    Plessmann, U.2    Ulrich, W.3
  • 283
    • 35948979262 scopus 로고    scopus 로고
    • Dyneins across eukaryotes: A comparative genomic analysis
    • DOI 10.1111/j.1600-0854.2007.00646.x
    • Wickstead B, Gull K. (2007). Dyneins across eukaryotes: a comparative genomic analysis. Traffic 8:1708-21. (Pubitemid 350066684)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1708-1721
    • Wickstead, B.1    Gull, K.2
  • 284
    • 80052614055 scopus 로고    scopus 로고
    • The evolution of the cytoskeleton
    • Wickstead B, Gull K. (2011a). The evolution of the cytoskeleton. J Cell Biol 194:513-25.
    • (2011) J Cell Biol , vol.194 , pp. 513-525
    • Wickstead, B.1    Gull, K.2
  • 285
    • 84882384008 scopus 로고    scopus 로고
    • The evolutionary biology of dyneins
    • King S, ed. Waltham (MA): Academic Press
    • Wickstead B, Gull K. (2011b). The evolutionary biology of dyneins. In: King S, ed. Dyneins: structure, biology and disease. Waltham (MA): Academic Press, 88-121.
    • (2011) Dyneins: Structure, Biology and Disease , pp. 88-121
    • Wickstead, B.1    Gull, K.2
  • 286
    • 77951244793 scopus 로고    scopus 로고
    • Patterns of kinesin evolution reveal a complex ancestral eukaryote with a multifunctional cytoskeleton
    • Wickstead B, Gull K, Richards TA. (2010). Patterns of kinesin evolution reveal a complex ancestral eukaryote with a multifunctional cytoskeleton. BMC Evol Biol 10:110.
    • (2010) BMC Evol Biol , vol.10 , pp. 110
    • Wickstead, B.1    Gull, K.2    Richards, T.A.3
  • 287
    • 41449086954 scopus 로고    scopus 로고
    • Twenty-five dyneins in Tetrahymena: A re-examination of the multidynein hypothesis
    • DOI 10.1002/cm.20264
    • Wilkes DE, Watson HE, Mitchell DR, Asai DJ. (2008). Twenty-five dyneins in Tetrahymena: A re-examination of the multidynein hypothesis. Cell Motil Cytoskeleton 65:342-51. (Pubitemid 351458147)
    • (2008) Cell Motility and the Cytoskeleton , vol.65 , Issue.4 , pp. 342-351
    • Wilkes, D.E.1    Watson, H.E.2    Mitchell, D.R.3    Asai, D.J.4
  • 288
    • 0142104375 scopus 로고    scopus 로고
    • Cell motility: Deaf drosophila keep the beat
    • DOI 10.1016/j.cub.2003.09.047
    • Witman GB. (2003). Cell motility: deaf Drosophila keep the beat. Curr Biol 13:R796-8. (Pubitemid 37269108)
    • (2003) Current Biology , vol.13 , Issue.20
    • Witman, G.B.1
  • 290
    • 79954595431 scopus 로고    scopus 로고
    • Iron sulfur clusters: Biogenesis, molecular mechanisms, and their functional significance
    • Xu XM, Møller SG. (2011). Iron Sulfur Clusters: Biogenesis, Molecular Mechanisms, and Their Functional Significance. Antioxidants Redox Signal 15:271-307.
    • (2011) Antioxidants Redox Signal , vol.15 , pp. 271-307
    • Xu, X.M.1    Møller, S.G.2
  • 291
    • 34250857058 scopus 로고    scopus 로고
    • Anchorage of plant ranGAP to the nuclear envelope involves novel nuclear-pore-associated proteins
    • DOI 10.1016/j.cub.2007.05.076, PII S0960982207015102
    • Xu XM, Meulia T, Meier I. (2007). Anchorage of plant RanGAP to the nuclear envelope involves novel nuclear-pore-associated proteins. Curr Biol 17:1157-63. (Pubitemid 46990889)
    • (2007) Current Biology , vol.17 , Issue.13 , pp. 1157-1163
    • Xu, X.M.1    Meulia, T.2    Meier, I.3
  • 292
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: A history of macroautophagy
    • Yang Z, Klionsky DJ. (2010). Eaten alive: a history of macroautophagy. Nature Cell Biol 12:814-22.
    • (2010) Nature Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 293
    • 33745761913 scopus 로고    scopus 로고
    • Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic
    • Yoshizawa AC, Kawashima S, Okuda S, et al. (2006). Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic. Traffic 7:1104-18.
    • (2006) Traffic , vol.7 , pp. 1104-1118
    • Yoshizawa, A.C.1    Kawashima, S.2    Okuda, S.3
  • 295
    • 77955015657 scopus 로고    scopus 로고
    • Abacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility
    • Zhang Y, Franco M, Ducret A, Mignot T. (2010). Abacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility. PLoS Biol 8:e1000430.
    • (2010) PLoS Biol , vol.8
    • Zhang, Y.1    Franco, M.2    Ducret, A.3    Mignot, T.4


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