메뉴 건너뛰기




Volumn 23, Issue 9, 2015, Pages 1715-1724

A YidC-like Protein in the Archaeal Plasma Membrane

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; UNCLASSIFIED DRUG; YIDC LIKE PROTEIN; ARCHAEAL PROTEIN; CARRIER PROTEIN;

EID: 84946714921     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.06.025     Document Type: Article
Times cited : (57)

References (66)
  • 2
    • 84878941023 scopus 로고    scopus 로고
    • Signal recognition particle: An essential protein-targeting machine
    • D. Akopian, K. Shen, X. Zhang, and S.O. Shan Signal recognition particle: an essential protein-targeting machine Annu. Rev. Biochem. 82 2013 693 721
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 693-721
    • Akopian, D.1    Shen, K.2    Zhang, X.3    Shan, S.O.4
  • 3
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • H.D. Bernstein, M.A. Poritz, K. Strub, P.J. Hoben, S. Brenner, and P. Walter Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle Nature 340 1989 482 486
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 4
    • 77954378286 scopus 로고    scopus 로고
    • Remote origins of tail-anchored proteins
    • N. Borgese, and M. Righi Remote origins of tail-anchored proteins Traffic 11 2010 877 885
    • (2010) Traffic , vol.11 , pp. 877-885
    • Borgese, N.1    Righi, M.2
  • 5
    • 67650757433 scopus 로고    scopus 로고
    • TrimAl: A tool for automated alignment trimming in large-scale phylogenetic analyses
    • S. Capella-Gutierrez, J.M. Silla-Martinez, and T. Gabaldon trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses Bioinformatics 25 2009 1972 1973
    • (2009) Bioinformatics , vol.25 , pp. 1972-1973
    • Capella-Gutierrez, S.1    Silla-Martinez, J.M.2    Gabaldon, T.3
  • 6
    • 84861774091 scopus 로고    scopus 로고
    • The complex process of GETting tail-anchored membrane proteins to the ER
    • J.W. Chartron, W.M. Clemons Jr., and C.J. Suloway The complex process of GETting tail-anchored membrane proteins to the ER Curr. Opin. Struct. Biol. 22 2012 217 224
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 217-224
    • Chartron, J.W.1    Clemons, W.M.2    Suloway, C.J.3
  • 7
    • 84919484766 scopus 로고    scopus 로고
    • The role of the strictly conserved positively charged residue differs among the gram-positive, gram-negative, and chloroplast YidC homologs
    • Y. Chen, R. Soman, S.K. Shanmugam, A. Kuhn, and R.E. Dalbey The role of the strictly conserved positively charged residue differs among the gram-positive, gram-negative, and chloroplast YidC homologs J. Biol. Chem. 289 2014 35656 35667
    • (2014) J. Biol. Chem. , vol.289 , pp. 35656-35667
    • Chen, Y.1    Soman, R.2    Shanmugam, S.K.3    Kuhn, A.4    Dalbey, R.E.5
  • 8
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
    • J.W. Chin, A.B. Martin, D.S. King, L. Wang, and P.G. Schultz Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli Proc. Natl. Acad. Sci. USA 99 2002 11020 11024
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 10
    • 79954529507 scopus 로고    scopus 로고
    • ProtTest 3: Fast selection of best-fit models of protein evolution
    • D. Darriba, G.L. Taboada, R. Doallo, and D. Posada ProtTest 3: fast selection of best-fit models of protein evolution Bioinformatics 27 2011 1164 1165
    • (2011) Bioinformatics , vol.27 , pp. 1164-1165
    • Darriba, D.1    Taboada, G.L.2    Doallo, R.3    Posada, D.4
  • 11
    • 84866595263 scopus 로고    scopus 로고
    • A portrait of the GET pathway as a surprisingly complicated young man
    • V. Denic A portrait of the GET pathway as a surprisingly complicated young man Trends Biochem. Sci. 37 2012 411 417
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 411-417
    • Denic, V.1
  • 12
    • 84939999765 scopus 로고    scopus 로고
    • Phage display selections for affinity reagents to membrane proteins in nanodiscs
    • P.K. Dominik, and A.A. Kossiakoff Phage display selections for affinity reagents to membrane proteins in nanodiscs Methods Enzymol. 557 2015 219 245
    • (2015) Methods Enzymol. , vol.557 , pp. 219-245
    • Dominik, P.K.1    Kossiakoff, A.A.2
  • 15
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • R.D. Gietz, and R.A. Woods Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method Methods Enzymol. 350 2002 87 96
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 16
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • F. Glaser, T. Pupko, I. Paz, R.E. Bell, D. Bechor-Shental, E. Martz, and N. Ben-Tal ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information Bioinformatics 19 2003 163 164
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 17
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • S. Guindon, J.F. Dufayard, V. Lefort, M. Anisimova, W. Hordijk, and O. Gascuel New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0 Syst. Biol. 59 2010 307 321
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 19
    • 81855184492 scopus 로고    scopus 로고
    • Tail-anchored membrane protein insertion into the endoplasmic reticulum
    • R.S. Hegde, and R.J. Keenan Tail-anchored membrane protein insertion into the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 12 2011 787 798
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 787-798
    • Hegde, R.S.1    Keenan, R.J.2
  • 20
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • L. Holm, and J. Park DaliLite workbench for protein structure comparison Bioinformatics 16 2000 566 567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 22
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal region of Oxa1
    • L. Jia, M. Dienhart, M. Schramp, M. McCauley, K. Hell, and R.A. Stuart Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1 EMBO J. 22 2003 6438 6447
    • (2003) EMBO J. , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 23
    • 34248138912 scopus 로고    scopus 로고
    • Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex
    • L. Jia, M.K. Dienhart, and R.A. Stuart Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex Mol. Biol. Cell 18 2007 1897 1908
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1897-1908
    • Jia, L.1    Dienhart, M.K.2    Stuart, R.A.3
  • 26
    • 84856719849 scopus 로고    scopus 로고
    • Dynamic disulfide scanning of the membrane-inserting Pf3 coat protein reveals multiple YidC substrate contacts
    • C. Klenner, and A. Kuhn Dynamic disulfide scanning of the membrane-inserting Pf3 coat protein reveals multiple YidC substrate contacts J. Biol. Chem. 287 2012 3769 3776
    • (2012) J. Biol. Chem. , vol.287 , pp. 3769-3776
    • Klenner, C.1    Kuhn, A.2
  • 27
    • 0037115768 scopus 로고    scopus 로고
    • The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana
    • E. Klostermann, I. Droste Gen Helling, J.P. Carde, and D. Schunemann The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana Biochem. J. 368 2002 777 781
    • (2002) Biochem. J. , vol.368 , pp. 777-781
    • Klostermann, E.1    Droste Gen Helling, I.2    Carde, J.P.3    Schunemann, D.4
  • 30
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Y. Liu, and D. Eisenberg 3D domain swapping: as domains continue to swap Protein Sci. 11 2002 1285 1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 31
    • 0035854694 scopus 로고    scopus 로고
    • YidC/Oxa1p/Alb3: Evolutionarily conserved mediators of membrane protein assembly
    • J. Luirink, T. Samuelsson, and J.W. de Gier YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly FEBS Lett. 501 2001 1 5
    • (2001) FEBS Lett. , vol.501 , pp. 1-5
    • Luirink, J.1    Samuelsson, T.2    De Gier, J.W.3
  • 32
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • A. Lupas, M. Van Dyke, and J. Stock Predicting coiled coils from protein sequences Science 252 1991 1162 1164
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 33
    • 84924406953 scopus 로고    scopus 로고
    • Comparative genomic analysis of evolutionarily conserved but functionally uncharacterized membrane proteins in archaea: Prediction of novel components of secretion, membrane remodeling and glycosylation systems
    • K.S. Makarova, M.Y. Galperin, and E.V. Koonin Comparative genomic analysis of evolutionarily conserved but functionally uncharacterized membrane proteins in archaea: prediction of novel components of secretion, membrane remodeling and glycosylation systems Biochimie 2015 10.1016/j.biochi.2015.01.004
    • (2015) Biochimie
    • Makarova, K.S.1    Galperin, M.Y.2    Koonin, E.V.3
  • 34
    • 80052407064 scopus 로고    scopus 로고
    • The mechanism of membrane-associated steps in tail-anchored protein insertion
    • M. Mariappan, A. Mateja, M. Dobosz, E. Bove, R.S. Hegde, and R.J. Keenan The mechanism of membrane-associated steps in tail-anchored protein insertion Nature 477 2011 61 66
    • (2011) Nature , vol.477 , pp. 61-66
    • Mariappan, M.1    Mateja, A.2    Dobosz, M.3    Bove, E.4    Hegde, R.S.5    Keenan, R.J.6
  • 35
    • 84924362921 scopus 로고    scopus 로고
    • Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo
    • A. Mateja, M. Paduch, H.Y. Chang, A. Szydlowska, A.A. Kossiakoff, R.S. Hegde, and R.J. Keenan Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo Science 347 2015 1152 1155
    • (2015) Science , vol.347 , pp. 1152-1155
    • Mateja, A.1    Paduch, M.2    Chang, H.Y.3    Szydlowska, A.4    Kossiakoff, A.A.5    Hegde, R.S.6    Keenan, R.J.7
  • 38
    • 2442585126 scopus 로고    scopus 로고
    • Role of YidC in folding of polytopic membrane proteins
    • S. Nagamori, I.N. Smirnova, and H.R. Kaback Role of YidC in folding of polytopic membrane proteins J. Cell Biol. 165 2004 53 62
    • (2004) J. Cell Biol. , vol.165 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 39
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: a novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 40
    • 16844375031 scopus 로고    scopus 로고
    • Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery
    • M. Preuss, M. Ott, S. Funes, J. Luirink, and J.M. Herrmann Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery J. Biol. Chem. 280 2005 13004 13011
    • (2005) J. Biol. Chem. , vol.280 , pp. 13004-13011
    • Preuss, M.1    Ott, M.2    Funes, S.3    Luirink, J.4    Herrmann, J.M.5
  • 43
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli
    • A. Saaf, M. Monne, J.W. de Gier, and G. von Heijne Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli J. Biol. Chem. 273 1998 30415 30418
    • (1998) J. Biol. Chem. , vol.273 , pp. 30415-30418
    • Saaf, A.1    Monne, M.2    De Gier, J.W.3    Von Heijne, G.4
  • 44
    • 84869389750 scopus 로고    scopus 로고
    • The YidC/Oxa1/Alb3 protein family: Common principles and distinct features
    • M.J. Saller, Z.C. Wu, J. de Keyzer, and A.J. Driessen The YidC/Oxa1/Alb3 protein family: common principles and distinct features Biol. Chem. 393 2012 1279 1290
    • (2012) Biol. Chem. , vol.393 , pp. 1279-1290
    • Saller, M.J.1    Wu, Z.C.2    De Keyzer, J.3    Driessen, A.J.4
  • 46
    • 34248583785 scopus 로고    scopus 로고
    • Generation of ribosome nascent chain complexes for structural and functional studies
    • C. Schaffitzel, and N. Ban Generation of ribosome nascent chain complexes for structural and functional studies J. Struct. Biol. 158 2007 463 471
    • (2007) J. Struct. Biol. , vol.158 , pp. 463-471
    • Schaffitzel, C.1    Ban, N.2
  • 49
    • 84891946539 scopus 로고    scopus 로고
    • The C-terminal regions of YidC from Rhodopirellula baltica and Oceanicaulis alexandrii bind to ribosomes and partially substitute for SRP receptor function in Escherichia coli
    • I. Seitl, S. Wickles, R. Beckmann, A. Kuhn, and D. Kiefer The C-terminal regions of YidC from Rhodopirellula baltica and Oceanicaulis alexandrii bind to ribosomes and partially substitute for SRP receptor function in Escherichia coli Mol. Microbiol. 91 2014 408 421
    • (2014) Mol. Microbiol. , vol.91 , pp. 408-421
    • Seitl, I.1    Wickles, S.2    Beckmann, R.3    Kuhn, A.4    Kiefer, D.5
  • 50
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • S. Shao, and R.S. Hegde Membrane protein insertion at the endoplasmic reticulum Annu. Rev. Cell Dev. Biol. 27 2011 25 56
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 51
    • 80051672009 scopus 로고    scopus 로고
    • A conserved archaeal pathway for tail-anchored membrane protein insertion
    • J. Sherrill, M. Mariappan, P. Dominik, R.S. Hegde, and R.J. Keenan A conserved archaeal pathway for tail-anchored membrane protein insertion Traffic 12 2011 1119 1123
    • (2011) Traffic , vol.12 , pp. 1119-1123
    • Sherrill, J.1    Mariappan, M.2    Dominik, P.3    Hegde, R.S.4    Keenan, R.J.5
  • 52
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • M. Strong, M.R. Sawaya, S. Wang, M. Phillips, D. Cascio, and D. Eisenberg Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis Proc. Natl. Acad. Sci. USA 103 2006 8060 8065
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 53
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 54
    • 84856413908 scopus 로고    scopus 로고
    • Tail-anchor targeting by a Get3 tetramer: The structure of an archaeal homologue
    • C.J. Suloway, M.E. Rome, and W.M. Clemons Jr. Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue EMBO J. 31 2012 707 719
    • (2012) EMBO J. , vol.31 , pp. 707-719
    • Suloway, C.J.1    Rome, M.E.2    Clemons, W.M.3
  • 55
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • G. Szyrach, M. Ott, N. Bonnefoy, W. Neupert, and J.M. Herrmann Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria EMBO J. 22 2003 6448 6457
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 57
    • 4944248085 scopus 로고    scopus 로고
    • F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. Coli inner membrane
    • E. van Bloois, G. Jan Haan, J.W. de Gier, B. Oudega, and J. Luirink F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane FEBS Lett. 576 2004 97 100
    • (2004) FEBS Lett. , vol.576 , pp. 97-100
    • Van Bloois, E.1    Jan Haan, G.2    De Gier, J.W.3    Oudega, B.4    Luirink, J.5
  • 59
    • 2142705713 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
    • M. van der Laan, P. Bechtluft, S. Kol, N. Nouwen, and A.J. Driessen F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis J. Cell Biol. 165 2004 213 222
    • (2004) J. Cell Biol. , vol.165 , pp. 213-222
    • Van Der Laan, M.1    Bechtluft, P.2    Kol, S.3    Nouwen, N.4    Driessen, A.J.5
  • 60
    • 79953137111 scopus 로고    scopus 로고
    • WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored proteins into the ER membrane
    • F. Vilardi, H. Lorenz, and B. Dobberstein WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored proteins into the ER membrane J. Cell Sci. 124 2011 1301 1307
    • (2011) J. Cell Sci. , vol.124 , pp. 1301-1307
    • Vilardi, F.1    Lorenz, H.2    Dobberstein, B.3
  • 61
    • 80052271259 scopus 로고    scopus 로고
    • The mechanism of tail-anchored protein insertion into the ER membrane
    • F. Wang, A. Whynot, M. Tung, and V. Denic The mechanism of tail-anchored protein insertion into the ER membrane Mol. Cell 43 2011 738 750
    • (2011) Mol. Cell , vol.43 , pp. 738-750
    • Wang, F.1    Whynot, A.2    Tung, M.3    Denic, V.4
  • 62
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • G. Winter Xia2: an expert system for macromolecular crystallography data reduction J. Appl. Crystallogr. 43 2010 186 190
    • (2010) J. Appl. Crystallogr. , vol.43 , pp. 186-190
    • Winter, G.1
  • 63
    • 84885436747 scopus 로고    scopus 로고
    • Interaction of Streptococcus mutans YidC1 and YidC2 with translating and nontranslating ribosomes
    • Z.C. Wu, J. de Keyzer, G.A. Berrelkamp-Lahpor, and A.J. Driessen Interaction of Streptococcus mutans YidC1 and YidC2 with translating and nontranslating ribosomes J. Bacteriol. 195 2013 4545 4551
    • (2013) J. Bacteriol. , vol.195 , pp. 4545-4551
    • Wu, Z.C.1    De Keyzer, J.2    Berrelkamp-Lahpor, G.A.3    Driessen, A.J.4
  • 64
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxa1 family of protein translocases
    • M.R. Yen, K.T. Harley, Y.H. Tseng, and M.H. Saier Jr. Phylogenetic and structural analyses of the oxa1 family of protein translocases FEMS Microbiol. Lett. 204 2001 223 231
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier, M.H.4
  • 65
    • 58049216329 scopus 로고    scopus 로고
    • The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins
    • Z. Yu, G. Koningstein, A. Pop, and J. Luirink The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins J. Biol. Chem. 283 2008 34635 34642
    • (2008) J. Biol. Chem. , vol.283 , pp. 34635-34642
    • Yu, Z.1    Koningstein, G.2    Pop, A.3    Luirink, J.4
  • 66
    • 67650280920 scopus 로고    scopus 로고
    • The evolution of YidC/Oxa/Alb3 family in the three domains of life: A phylogenomic analysis
    • Y.J. Zhang, H.F. Tian, and J.F. Wen The evolution of YidC/Oxa/Alb3 family in the three domains of life: a phylogenomic analysis BMC Evol. Biol. 9 2009 137
    • (2009) BMC Evol. Biol. , vol.9 , pp. 137
    • Zhang, Y.J.1    Tian, H.F.2    Wen, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.