메뉴 건너뛰기




Volumn 347, Issue 1, 2005, Pages 81-93

Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20

Author keywords

Hidden Markov models; Import receptors; Mitochondria; Protein import; Protein targeting sequences

Indexed keywords

AMINO ACID; FUNGAL PROTEIN; ISOPROTEIN; RECEPTOR SUBTYPE; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20;

EID: 20044392656     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.057     Document Type: Article
Times cited : (47)

References (72)
  • 1
    • 0041401720 scopus 로고    scopus 로고
    • The dual origin of the yeast mitochondrial proteome
    • O. Karlberg, B. Canback, C.G. Kurland, and S.G. Andersson The dual origin of the yeast mitochondrial proteome Yeast 17 2000 170 187
    • (2000) Yeast , vol.17 , pp. 170-187
    • Karlberg, O.1    Canback, B.2    Kurland, C.G.3    Andersson, S.G.4
  • 4
    • 10744224439 scopus 로고    scopus 로고
    • Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria
    • V.K. Mootha, J. Bunkenborg, J.V. Olsen, M. Hjerrild, J.R. Wisniewski, and E. Stahl Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria Cell 115 2003 629 640
    • (2003) Cell , vol.115 , pp. 629-640
    • Mootha, V.K.1    Bunkenborg, J.2    Olsen, J.V.3    Hjerrild, M.4    Wisniewski, J.R.5    Stahl, E.6
  • 5
    • 0038637237 scopus 로고    scopus 로고
    • Mitochondrial proteomics. Undercover in the lipid bilayer
    • T.G. McDonald, and J.E. Van Eyk Mitochondrial proteomics. Undercover in the lipid bilayer Basic Res. Cardiol. 98 2003 219 227
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 219-227
    • McDonald, T.G.1    Van Eyk, J.E.2
  • 7
    • 3242875263 scopus 로고    scopus 로고
    • MITOPRED: A genome-scale method for prediction of nucleus-encoded mitochondrial proteins
    • C. Guda, E. Fahy, and S. Subramaniam MITOPRED: a genome-scale method for prediction of nucleus-encoded mitochondrial proteins Bioinformatics 20 2004 1785 1794
    • (2004) Bioinformatics , vol.20 , pp. 1785-1794
    • Guda, C.1    Fahy, E.2    Subramaniam, S.3
  • 8
    • 0022725788 scopus 로고
    • A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers
    • D. Roise, S.J. Horvath, J.M. Tomich, J.H. Richards, and G. Schatz A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers EMBO J. 5 1986 1327 1334
    • (1986) EMBO J. , vol.5 , pp. 1327-1334
    • Roise, D.1    Horvath, S.J.2    Tomich, J.M.3    Richards, J.H.4    Schatz, G.5
  • 9
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • G. von Heijne Mitochondrial targeting sequences may form amphiphilic helices EMBO J. 5 1986 1335 1342
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Von Heijne, G.1
  • 10
    • 0023916577 scopus 로고
    • Mitochondrial import of the ADP/ATP carrier protein in Saccharomyces cerevisiae. Sequences required for receptor binding and membrane translocation
    • C. Smagula, and M.G. Douglas Mitochondrial import of the ADP/ATP carrier protein in Saccharomyces cerevisiae. Sequences required for receptor binding and membrane translocation J. Biol. Chem. 263 1988 6783 6790
    • (1988) J. Biol. Chem. , vol.263 , pp. 6783-6790
    • Smagula, C.1    Douglas, M.G.2
  • 11
    • 0142242210 scopus 로고    scopus 로고
    • Signal-anchor domains of proteins of the outer membrane of mitochondria: Structural and functional characteristics
    • T. Waizenegger, T. Stan, W. Neupert, and D. Rapaport Signal-anchor domains of proteins of the outer membrane of mitochondria: structural and functional characteristics J. Biol. Chem. 278 2003 42064 42071
    • (2003) J. Biol. Chem. , vol.278 , pp. 42064-42071
    • Waizenegger, T.1    Stan, T.2    Neupert, W.3    Rapaport, D.4
  • 13
    • 0035153316 scopus 로고    scopus 로고
    • The alpha and the beta: Protein translocation across mitochondrial and plastid outer membranes
    • K. Gabriel, S.K. Buchanan, and T. Lithgow The alpha and the beta: protein translocation across mitochondrial and plastid outer membranes Trends Biochem. Sci. 26 2001 36 40
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 36-40
    • Gabriel, K.1    Buchanan, S.K.2    Lithgow, T.3
  • 14
    • 0037009087 scopus 로고    scopus 로고
    • Functions of outer membrane receptors in mitochondrial protein import
    • T. Endo, and D. Kohda Functions of outer membrane receptors in mitochondrial protein import Biochim. Biophys. Acta 1592 2002 3 14
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 3-14
    • Endo, T.1    Kohda, D.2
  • 15
    • 0142059893 scopus 로고    scopus 로고
    • Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space
    • A.E. Frazier, A. Chacinska, K.N. Truscott, B. Guiard, N. Pfanner, and P. Rehling Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space Mol. Cell. Biol. 23 2003 7818 7828
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7818-7828
    • Frazier, A.E.1    Chacinska, A.2    Truscott, K.N.3    Guiard, B.4    Pfanner, N.5    Rehling, P.6
  • 16
    • 0029096887 scopus 로고
    • Reconstitution of the initial steps of mitochondrial protein import
    • N. Hachiya, K. Mihara, K. Suda, M. Horst, G. Schatz, and T. Lithgow Reconstitution of the initial steps of mitochondrial protein import Nature 376 1995 705 709
    • (1995) Nature , vol.376 , pp. 705-709
    • Hachiya, N.1    Mihara, K.2    Suda, K.3    Horst, M.4    Schatz, G.5    Lithgow, T.6
  • 17
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex
    • P.J. Dekker, M.T. Ryan, J. Brix, H. Muller, A. Honlinger, and N. Pfanner Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex Mol. Cell. Biol. 18 1998 6515 6524
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.1    Ryan, M.T.2    Brix, J.3    Muller, H.4    Honlinger, A.5    Pfanner, N.6
  • 19
    • 0033619269 scopus 로고    scopus 로고
    • Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase
    • S. van Wilpe, M.T. Ryan, K. Hill, A.C. Maarse, C. Meisinger, and J. Brix Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase Nature 401 1999 485 489
    • (1999) Nature , vol.401 , pp. 485-489
    • Van Wilpe, S.1    Ryan, M.T.2    Hill, K.3    Maarse, A.C.4    Meisinger, C.5    Brix, J.6
  • 20
    • 0035931764 scopus 로고    scopus 로고
    • Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex
    • T. Krimmer, D. Rapaport, M.T. Ryan, C. Meisinger, C.K. Kassenbrock, and E. Blachly-Dyson Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex J. Cell. Biol. 152 2001 289 300
    • (2001) J. Cell. Biol. , vol.152 , pp. 289-300
    • Krimmer, T.1    Rapaport, D.2    Ryan, M.T.3    Meisinger, C.4    Kassenbrock, C.K.5    Blachly-Dyson, E.6
  • 21
    • 0024801086 scopus 로고
    • MOM19, an import receptor for mitochondrial precursor proteins
    • T. Sollner, G. Griffiths, R. Pfaller, N. Pfanner, and W. Neupert MOM19, an import receptor for mitochondrial precursor proteins Cell 59 1989 1061 1070
    • (1989) Cell , vol.59 , pp. 1061-1070
    • Sollner, T.1    Griffiths, G.2    Pfaller, R.3    Pfanner, N.4    Neupert, W.5
  • 22
    • 0027434076 scopus 로고
    • Functional cooperation of mitochondrial protein import receptors in yeast
    • L. Ramage, T. Junne, K. Hahne, T. Lithgow, and G. Schatz Functional cooperation of mitochondrial protein import receptors in yeast EMBO J. 12 1993 4115 4123
    • (1993) EMBO J. , vol.12 , pp. 4115-4123
    • Ramage, L.1    Junne, T.2    Hahne, K.3    Lithgow, T.4    Schatz, G.5
  • 24
    • 0032500553 scopus 로고    scopus 로고
    • Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria
    • M. Yano, M. Kanazawa, K. Terada, M. Takeya, N. Hoogenraad, and M. Mori Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria J. Biol. Chem. 273 1998 26844 26851
    • (1998) J. Biol. Chem. , vol.273 , pp. 26844-26851
    • Yano, M.1    Kanazawa, M.2    Terada, K.3    Takeya, M.4    Hoogenraad, N.5    Mori, M.6
  • 25
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Y. Abe, T. Shodai, T. Muto, K. Mihara, H. Torii, and S. Nishikawa Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20 Cell 100 2000 551 560
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.6
  • 26
    • 0029963554 scopus 로고    scopus 로고
    • The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: Evidence for a single hetero-oligomeric receptor
    • V. Haucke, M. Horst, G. Schatz, and T. Lithgow The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor EMBO J. 15 1996 1231 1237
    • (1996) EMBO J. , vol.15 , pp. 1231-1237
    • Haucke, V.1    Horst, M.2    Schatz, G.3    Lithgow, T.4
  • 27
    • 0029619088 scopus 로고
    • Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria
    • L. Bolliger, T. Junne, G. Schatz, and T. Lithgow Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria EMBO J. 14 1995 6318 6326
    • (1995) EMBO J. , vol.14 , pp. 6318-6326
    • Bolliger, L.1    Junne, T.2    Schatz, G.3    Lithgow, T.4
  • 28
    • 0034675885 scopus 로고    scopus 로고
    • Characterization of the signal that directs Tom20 to the mitochondrial outer membrane
    • S. Kanaji, J. Iwahashi, Y. Kida, M. Sakaguchi, and K. Mihara Characterization of the signal that directs Tom20 to the mitochondrial outer membrane J. Cell. Biol. 151 2000 277 288
    • (2000) J. Cell. Biol. , vol.151 , pp. 277-288
    • Kanaji, S.1    Iwahashi, J.2    Kida, Y.3    Sakaguchi, M.4    Mihara, K.5
  • 29
    • 0034189150 scopus 로고    scopus 로고
    • Sensitive protein comparisons with profiles and hidden Markov models
    • K. Hofmann Sensitive protein comparisons with profiles and hidden Markov models Brief Bioinform. 1 2000 167 178
    • (2000) Brief Bioinform. , vol.1 , pp. 167-178
    • Hofmann, K.1
  • 30
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • T.L. Bailey, and C. Elkan Fitting a mixture model by expectation maximization to discover motifs in biopolymers Proc. Int. Conf. Intell. Syst. Mol. Biol. 2 1994 28 36
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 31
    • 0032512801 scopus 로고    scopus 로고
    • A symmetric-iterated multiple alignment of protein sequences
    • L. Brocchieri, and S. Karlin A symmetric-iterated multiple alignment of protein sequences J. Mol. Biol. 276 1998 249 264
    • (1998) J. Mol. Biol. , vol.276 , pp. 249-264
    • Brocchieri, L.1    Karlin, S.2
  • 32
    • 0030788541 scopus 로고    scopus 로고
    • Extracting protein alignment models from the sequence database
    • A.F. Neuwald, J.S. Liu, D.J. Lipman, and C.E. Lawrence Extracting protein alignment models from the sequence database Nucl. Acids Res. 25 1997 1665 1677
    • (1997) Nucl. Acids Res. , vol.25 , pp. 1665-1677
    • Neuwald, A.F.1    Liu, J.S.2    Lipman, D.J.3    Lawrence, C.E.4
  • 33
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European molecular biology open software suite
    • P. Rice, I. Longden, and A. Bleasby EMBOSS: the European molecular biology open software suite Trends Genet. 16 2000 276 277
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 34
  • 36
    • 19244383139 scopus 로고    scopus 로고
    • Gene structure of the human mitochondrial outer membrane receptor Tom20 and evolutionary study of its family of processed pseudogenes
    • J.M. Hernandez, P. Giner, and J. Hernandez-Yago Gene structure of the human mitochondrial outer membrane receptor Tom20 and evolutionary study of its family of processed pseudogenes Gene 239 1999 283 291
    • (1999) Gene , vol.239 , pp. 283-291
    • Hernandez, J.M.1    Giner, P.2    Hernandez-Yago, J.3
  • 38
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • M.J. Sippl Recognition of errors in three-dimensional structures of proteins Proteins: Struct. Funct. Genet. 17 1993 355 362
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 39
    • 0035895431 scopus 로고    scopus 로고
    • NMR identification of the Tom20 binding segment in mitochondrial presequences
    • T. Muto, T. Obita, Y. Abe, T. Shodai, T. Endo, and D. Kohda NMR identification of the Tom20 binding segment in mitochondrial presequences J. Mol. Biol. 306 2001 137 143
    • (2001) J. Mol. Biol. , vol.306 , pp. 137-143
    • Muto, T.1    Obita, T.2    Abe, Y.3    Shodai, T.4    Endo, T.5    Kohda, D.6
  • 40
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • D. Eisenberg, E. Schwarz, M. Komaromy, and R. Wall Analysis of membrane and surface protein sequences with the hydrophobic moment plot J. Mol. Biol. 179 1984 125 142
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 41
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 42
    • 0033430312 scopus 로고    scopus 로고
    • The mitochondrial TIM22 preprotein translocase is highly conserved throughout the eukaryotic kingdom
    • M.F. Bauer, U. Rothbauer, N. Muhlenbein, R.J. Smith, K. Gerbitz, and W. Neupert The mitochondrial TIM22 preprotein translocase is highly conserved throughout the eukaryotic kingdom FEBS Letters 464 1999 41 47
    • (1999) FEBS Letters , vol.464 , pp. 41-47
    • Bauer, M.F.1    Rothbauer, U.2    Muhlenbein, N.3    Smith, R.J.4    Gerbitz, K.5    Neupert, W.6
  • 43
    • 0034518604 scopus 로고    scopus 로고
    • Gene discovery using computational and microarray analysis of transcription in the Drosophila melanogaster testis
    • J. Andrews, G.G. Bouffard, C. Cheadle, J. Lu, K.G. Becker, and B. Oliver Gene discovery using computational and microarray analysis of transcription in the Drosophila melanogaster testis Genome Res. 10 2000 2030 2043
    • (2000) Genome Res. , vol.10 , pp. 2030-2043
    • Andrews, J.1    Bouffard, G.G.2    Cheadle, C.3    Lu, J.4    Becker, K.G.5    Oliver, B.6
  • 44
    • 1842368473 scopus 로고    scopus 로고
    • Just follow the acid chain
    • G. Schatz Just follow the acid chain Nature 388 1997 121 122
    • (1997) Nature , vol.388 , pp. 121-122
    • Schatz, G.1
  • 45
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • W. Neupert Protein import into mitochondria Annu. Rev. Biochem. 66 1997 863 917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 46
    • 0036631379 scopus 로고    scopus 로고
    • How mitochondria import hydrophilic and hydrophobic proteins
    • A. Chacinska, N. Pfanner, and C. Meisinger How mitochondria import hydrophilic and hydrophobic proteins Trends Cell Biol. 12 2002 299 303
    • (2002) Trends Cell Biol. , vol.12 , pp. 299-303
    • Chacinska, A.1    Pfanner, N.2    Meisinger, C.3
  • 47
    • 3242761606 scopus 로고    scopus 로고
    • Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes
    • D. Macasev, J. Whelan, E. Newbigin, M.C. Silva-Filho, T.D. Mulhern, and T. Lithgow Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes Mol. Biol. Evol. 21 2004 1557 1564
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1557-1564
    • MacAsev, D.1    Whelan, J.2    Newbigin, E.3    Silva-Filho, M.C.4    Mulhern, T.D.5    Lithgow, T.6
  • 48
    • 0030160495 scopus 로고    scopus 로고
    • A receptor for protein import into potato mitochondria
    • L. Heins, and U.K. Schmitz A receptor for protein import into potato mitochondria Plant J. 9 1996 829 839
    • (1996) Plant J. , vol.9 , pp. 829-839
    • Heins, L.1    Schmitz, U.K.2
  • 49
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20
    • W. Werhahn, A. Niemeyer, L. Jansch, V. Kruft, U.K. Schmitz, and H. Braun Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20 Plant Physiol. 125 2001 943 954
    • (2001) Plant Physiol. , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jansch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.6
  • 50
    • 4143065974 scopus 로고    scopus 로고
    • Germ-line specific variants of components of the mitochondrial outer membrane import machinery in Drosophila
    • J.J. Hwa, A.J. Zhu, M.A. Hiller, C.Y. Kon, M.T. Fuller, and A. Santel Germ-line specific variants of components of the mitochondrial outer membrane import machinery in Drosophila FEBS Letters 572 2004 141 146
    • (2004) FEBS Letters , vol.572 , pp. 141-146
    • Hwa, J.J.1    Zhu, A.J.2    Hiller, M.A.3    Kon, C.Y.4    Fuller, M.T.5    Santel, A.6
  • 52
    • 0038790159 scopus 로고    scopus 로고
    • Gene expression profiles in different stages of mouse spermatogenic cells during spermatogenesis
    • Z. Yu, R. Guo, Y. Ge, J. Ma, J. Guan, and S. Li Gene expression profiles in different stages of mouse spermatogenic cells during spermatogenesis Biol. Reprod. 69 2003 37 47
    • (2003) Biol. Reprod. , vol.69 , pp. 37-47
    • Yu, Z.1    Guo, R.2    Ge, Y.3    Ma, J.4    Guan, J.5    Li, S.6
  • 53
    • 0032127981 scopus 로고    scopus 로고
    • Molecular mechanisms of male germ cell differentiation
    • N.B. Hecht Molecular mechanisms of male germ cell differentiation Bioessays 20 1998 555 561
    • (1998) Bioessays , vol.20 , pp. 555-561
    • Hecht, N.B.1
  • 54
    • 0037150676 scopus 로고    scopus 로고
    • Unique chromatin remodeling and transcriptional regulation in spermatogenesis
    • P. Sassone-Corsi Unique chromatin remodeling and transcriptional regulation in spermatogenesis Science 296 2002 2176 2178
    • (2002) Science , vol.296 , pp. 2176-2178
    • Sassone-Corsi, P.1
  • 55
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R. Eddy Profile hidden Markov models Bioinformatics 14 1998 755 763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 56
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 59
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 60
    • 0026069154 scopus 로고
    • Development of hydrophobicity parameters to analyze proteins which bear post- or cotranslational modifications
    • S.D. Black, and D.R. Mould Development of hydrophobicity parameters to analyze proteins which bear post- or cotranslational modifications Anal. Biochem. 193 1991 72 82
    • (1991) Anal. Biochem. , vol.193 , pp. 72-82
    • Black, S.D.1    Mould, D.R.2
  • 61
    • 0024278357 scopus 로고
    • Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds
    • M.A. Roseman Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds J. Mol. Biol. 200 1988 513 522
    • (1988) J. Mol. Biol. , vol.200 , pp. 513-522
    • Roseman, M.A.1
  • 64
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • S. Guindon, and O. Gascuel A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood Syst. Biol. 52 2003 696 704
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 65
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Z. Yang PAML: a program package for phylogenetic analysis by maximum likelihood Comput. Appl. Biosci. 13 1997 555 556
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 555-556
    • Yang, Z.1
  • 66
    • 0036139287 scopus 로고    scopus 로고
    • CONSEL: For assessing the confidence of phylogenetic tree selection
    • H. Shimodaira, and M. Hasegawa CONSEL: for assessing the confidence of phylogenetic tree selection Bioinformatics 17 2001 1246 1247
    • (2001) Bioinformatics , vol.17 , pp. 1246-1247
    • Shimodaira, H.1    Hasegawa, M.2
  • 67
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum-likelihood method for reconstructing tree topologies
    • K. Strimmer, and A. von Haeseler Quartet puzzling: a quartet maximum-likelihood method for reconstructing tree topologies Mol. Biol. Evol. 1996 964 969
    • (1996) Mol. Biol. Evol. , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 68
    • 0034079389 scopus 로고    scopus 로고
    • Statistical tests of gamma-distributed rate heterogeneity in models of sequence evolution in phylogenetics
    • N. Goldman, and S. Whelan Statistical tests of gamma-distributed rate heterogeneity in models of sequence evolution in phylogenetics Mol. Biol. Evol. 17 2000 975 978
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 975-978
    • Goldman, N.1    Whelan, S.2
  • 69
    • 0033984609 scopus 로고    scopus 로고
    • Weighted neighbor joining: A likelihood-based approach to distance-based phylogeny reconstruction
    • W.J. Bruno, N.D. Socci, and A.L. Halpern Weighted neighbor joining: a likelihood-based approach to distance-based phylogeny reconstruction Mol. Biol. Evol. 17 2000 189 197
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 189-197
    • Bruno, W.J.1    Socci, N.D.2    Halpern, A.L.3
  • 70
    • 0000182225 scopus 로고
    • The nematode Caenorhabditis elegans
    • W.B. Wood Cold Spring Harbor Laboratory Press Plainview, NY
    • J.E. Sulston, and J. Hodgkin The nematode Caenorhabditis elegans W.B. Wood Methods 1988 Cold Spring Harbor Laboratory Press Plainview, NY 587 606
    • (1988) Methods , pp. 587-606
    • Sulston, J.E.1    Hodgkin, J.2
  • 71
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • S. Brenner The genetics of Caenorhabditis elegans Genetics 77 1974 71 94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 72
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • L. Timmons, D.L. Court, and A. Fire Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans Gene 263 2001 103 112
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.