메뉴 건너뛰기




Volumn 473, Issue 13, 2016, Pages 1941-1952

EssC: Domain structures inform on the elusive translocation channel in the Type VII secretion system

Author keywords

ATPase; ESX 1; Forkhead associated domain; Membrane bound protein; P loop containing domain; Secretion system

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CARRIER PROTEIN; DNA TRANSLOCASE FTSK; ESSC C PROTEIN; ESSC N PROTEIN; ESSC PROTEIN; MEMBRANE PROTEIN; POLYMER; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; PROTEIN BINDING; TYPE VII SECRETION SYSTEM;

EID: 85009383615     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BCJ20160257     Document Type: Article
Times cited : (42)

References (53)
  • 2
    • 12844288619 scopus 로고    scopus 로고
    • EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections
    • CrossRef PubMed
    • Burts, M. L., Williams, W. A., DeBord, K. And Missiakas, D. M. (2005) EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections. Proc. Natl. Acad. Sci. U. S. A. 102, 1169-1174 CrossRef PubMed
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1169-1174
    • Burts, M.L.1    Williams, W.A.2    DeBord, K.3    Missiakas, D.M.4
  • 3
    • 84906934249 scopus 로고    scopus 로고
    • Heterogeneity in ess transcriptional organization and variable contribution of the Ess/Type VII protein secretion system to virulence across closely related Staphylocccus aureus strains
    • CrossRef PubMed
    • Kneuper, H., Cao, Z. P., Twomey, K. B., Zoltner, M., Jaeger, F., Cargill, J. S., Chalmers, J., van der Kooi-Pol, M. M., van Dijl, J. M., Ryan, R. P., Hunter, W. N. And Palmer, T. (2014) Heterogeneity in ess transcriptional organization and variable contribution of the Ess/Type VII protein secretion system to virulence across closely related Staphylocccus aureus strains. Mol. Microbiol. 93, 928-943 CrossRef PubMed
    • (2014) Mol. Microbiol. , vol.93 , pp. 928-943
    • Kneuper, H.1    Cao, Z.P.2    Twomey, K.B.3    Zoltner, M.4    Jaeger, F.5    Cargill, J.S.6    Chalmers, J.7    Van Der Kooi-Pol, M.M.8    Van Dijl, J.M.9    Ryan, R.P.10    Hunter, W.N.11    Palmer, T.12
  • 4
    • 0028839886 scopus 로고
    • A new Escherichia coli cell division gene, ftsK
    • PubMed
    • Begg, K. J., Dewar, S. J. And Donachie, W. D. (1995) A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177, 6211-6222 PubMed
    • (1995) J. Bacteriol. , vol.177 , pp. 6211-6222
    • Begg, K.J.1    Dewar, S.J.2    Donachie, W.D.3
  • 5
    • 0028179987 scopus 로고
    • Bacillus subtilis SpoIIIE protein required for DNA segregation during asymmetric cell division
    • CrossRef PubMed
    • Wu, L. J. And Errington, J. (1994) Bacillus subtilis SpoIIIE protein required for DNA segregation during asymmetric cell division. Science 264, 572-575 CrossRef PubMed
    • (1994) Science , vol.264 , pp. 572-575
    • Wu, L.J.1    Errington, J.2
  • 7
    • 35448942364 scopus 로고    scopus 로고
    • Crystal structure analysis reveals a novel forkhead-associated domain of ESAT-6 secretion system C protein in Staphylococcus aureus
    • CrossRef PubMed
    • Tanaka, Y., Kuroda, M., Yasutake, Y., Yao, M., Tsumoto, K., Watanabe, N., Ohta, T. And Tanaka, I. (2007) Crystal structure analysis reveals a novel forkhead-associated domain of ESAT-6 secretion system C protein in Staphylococcus aureus. Proteins 69, 659-664 CrossRef PubMed
    • (2007) Proteins , vol.69 , pp. 659-664
    • Tanaka, Y.1    Kuroda, M.2    Yasutake, Y.3    Yao, M.4    Tsumoto, K.5    Watanabe, N.6    Ohta, T.7    Tanaka, I.8
  • 9
    • 58849136154 scopus 로고    scopus 로고
    • An improved tetracycline-inducible expression vector for Staphylococcus aureus
    • CrossRef PubMed
    • Corrigan, R. M. And Foster, T. J. (2009) An improved tetracycline-inducible expression vector for Staphylococcus aureus. Plasmid 61, 126-129 CrossRef PubMed
    • (2009) Plasmid , vol.61 , pp. 126-129
    • Corrigan, R.M.1    Foster, T.J.2
  • 10
    • 82555181642 scopus 로고    scopus 로고
    • Vectors for improved Tet repressor-dependent gradual gene induction or silencing in Staphylococcus aureus
    • CrossRef PubMed
    • Helle, L., Kull, M., Mayer, S., Marincola, G., Zelder, M.-E., Goerke, C., Wolz, C. And Bertram, R. (2011) Vectors for improved Tet repressor-dependent gradual gene induction or silencing in Staphylococcus aureus. Microbiology 157, 3314-3323 CrossRef PubMed
    • (2011) Microbiology , vol.157 , pp. 3314-3323
    • Helle, L.1    Kull, M.2    Mayer, S.3    Marincola, G.4    Zelder, M.-E.5    Goerke, C.6    Wolz, C.7    Bertram, R.8
  • 11
    • 84871446545 scopus 로고    scopus 로고
    • Characterization of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system: Atomic resolution crystal structure of the cytoplasmic segment
    • CrossRef PubMed
    • Zoltner, M., Fyfe, P. K., Palmer, T. And Hunter, W. N. (2013) Characterization of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system: Atomic resolution crystal structure of the cytoplasmic segment. Biochem. J. 449, 469-477 CrossRef PubMed
    • (2013) Biochem. J. , vol.449 , pp. 469-477
    • Zoltner, M.1    Fyfe, P.K.2    Palmer, T.3    Hunter, W.N.4
  • 12
    • 84875903606 scopus 로고    scopus 로고
    • The architecture of EssB, an integral membrane component of the type VII secretion system
    • CrossRef PubMed
    • Zoltner, M., Norman, D. G., Fyfe, P. K., El Mkami, H., Palmer, T. And Hunter, W. N. (2013) The architecture of EssB, an integral membrane component of the type VII secretion system. Structure 21, 595-603 CrossRef PubMed
    • (2013) Structure , vol.21 , pp. 595-603
    • Zoltner, M.1    Norman, D.G.2    Fyfe, P.K.3    El Mkami, H.4    Palmer, T.5    Hunter, W.N.6
  • 13
    • 76449099287 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • CrossRef PubMed
    • Kabsch, W. (2010) Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 125-132 CrossRef PubMed
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 14
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • CrossRef PubMed
    • Evans, P. (2006) Scaling and assessment of data quality. Acta Crystallogr. D Biol. Crystallogr. 62, 72-82 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 72-82
    • Evans, P.1
  • 15
    • 23844492576 scopus 로고    scopus 로고
    • Auto-Rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • CrossRef PubMed
    • Panjikar, S., Parthasarathy, V., Lamzin, V. S., Weiss, M. S. And Tucker, P. A. (2005) Auto-Rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr. D Biol. Crystallogr. 61, 449-457 CrossRef PubMed
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 16
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • CrossRef PubMed
    • Langer, G., Cohen, S. X., Lamzin, V. S. And Perrakis, A. (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179 CrossRef PubMed
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 17
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • CrossRef PubMed
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485 CrossRef PubMed
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 19
    • 13844301139 scopus 로고    scopus 로고
    • Direct incorporation of experimental phase information in model refinement
    • CrossRef PubMed
    • Skubák, P., Murshudov, G. N. And Pannu, N. S. (2004) Direct incorporation of experimental phase information in model refinement. Acta Crystallogr. D Biol. Crystallogr. 60, 2196-2201 CrossRef PubMed
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2196-2201
    • Skubák, P.1    Murshudov, G.N.2    Pannu, N.S.3
  • 20
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • CrossRef PubMed
    • Terwilliger, T. C. (2000) Maximum-likelihood density modification. Acta Crystallogr. D Biol. Crystallogr. 56, 965-972 CrossRef PubMed
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 21
    • 33748337934 scopus 로고    scopus 로고
    • The buccaneer software for automated model building
    • CrossRef PubMed
    • Cowtan, K. (2006) The Buccaneer software for automated model building. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 23
    • 13244281317 scopus 로고    scopus 로고
    • Coot : Model-building tools for molecular graphics
    • CrossRef PubMed
    • Emsley, P. And Cowtan, K. (2004) Coot : model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132 CrossRef PubMed
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 25
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • CrossRef PubMed
    • Painter, J. And Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 28
    • 77950798648 scopus 로고    scopus 로고
    • Recent developments in classical density modification
    • CrossRef PubMed
    • Cowtan, K. (2010) Recent developments in classical density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 470-478 CrossRef PubMed
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 470-478
    • Cowtan, K.1
  • 30
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • CrossRef PubMed
    • Holm, L. And Park, J. (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16, 566-567 CrossRef PubMed
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 32
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • CrossRef PubMed
    • Bond, C. And Schüttelkopf, A. W. (2009) ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr. D Biol. Crystallogr. 65, 510-512 CrossRef PubMed
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 510-512
    • Bond, C.1    Schüttelkopf, A.W.2
  • 33
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • CrossRef PubMed
    • Krissinel, E. And Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 CrossRef PubMed
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • CrossRef PubMed
    • Krogh, A., Larsson, B., von Heijne, G. And Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305, 567-580 CrossRef PubMed
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 35
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • CrossRef PubMed
    • Kelley, L. A. And Sternberg, M. J. E. (2009) Protein structure prediction on the Web: A case study using the Phyre server. Nat. Protoc. 4, 363-371 CrossRef PubMed
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 36
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: Structure and mechanism of hexameric FtsK
    • CrossRef PubMed
    • Massey, T. H., Mercogliano, C. P., Yates, J., Sherratt, D. J. And Löwe, J. (2006) Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol. Cell 23, 457-469 CrossRef PubMed
    • (2006) Mol. Cell , vol.23 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Löwe, J.5
  • 37
    • 84975780661 scopus 로고    scopus 로고
    • Membrane interactions and self-association of components of the Ess/Type VII secretion system of Staphylococcus aureus
    • CrossRef PubMed
    • Jaeger, F., Zoltner, M., Kneuper, H., Hunter, W. N. And Palmer, T. (2016) Membrane interactions and self-association of components of the Ess/Type VII secretion system of Staphylococcus aureus. FEBS Lett. 590, 349-357 CrossRef PubMed
    • (2016) FEBS Lett. , vol.590 , pp. 349-357
    • Jaeger, F.1    Zoltner, M.2    Kneuper, H.3    Hunter, W.N.4    Palmer, T.5
  • 38
    • 33645011914 scopus 로고    scopus 로고
    • Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67
    • CrossRef PubMed
    • Byeon, I. J., Li, H., Song, H., Gronenborn, A. M. And Tsai, M. D. (2005) Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. Nat. Struct. Mol. Biol. 12, 987-993 CrossRef PubMed
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 987-993
    • Byeon, I.J.1    Li, H.2    Song, H.3    Gronenborn, A.M.4    Tsai, M.D.5
  • 39
    • 84871977937 scopus 로고    scopus 로고
    • Function and evolution of ubiquitous bacterial signaling adapter phosphopeptide recognition domain FHA
    • CrossRef PubMed
    • Weiling, H., Xiaowen, Y., Chunmei, L. And Jianping, X. (2013) Function and evolution of ubiquitous bacterial signaling adapter phosphopeptide recognition domain FHA. Cell. Signal. 25, 660-665 CrossRef PubMed
    • (2013) Cell. Signal. , vol.25 , pp. 660-665
    • Weiling, H.1    Xiaowen, Y.2    Chunmei, L.3    Jianping, X.4
  • 40
    • 5144223072 scopus 로고    scopus 로고
    • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: Implications for the origins of chromosome segregation, cell division and viral capsid packaging
    • CrossRef PubMed
    • Iyer, L. M., Makarova, K. S., Koonin, E. V. And Aravind, L. (2004) Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Res. 32, 5260-5279 CrossRef PubMed
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 41
    • 33847668562 scopus 로고    scopus 로고
    • Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility
    • CrossRef PubMed
    • Satyshur, K. A., Worzalla, G. A., Meyer, L. S., Heiniger, E. K., Aukema, K. G., Misic, A. M. And Forest, K. T. (2007) Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Structure 15, 363-376 CrossRef PubMed
    • (2007) Structure , vol.15 , pp. 363-376
    • Satyshur, K.A.1    Worzalla, G.A.2    Meyer, L.S.3    Heiniger, E.K.4    Aukema, K.G.5    Misic, A.M.6    Forest, K.T.7
  • 42
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • PubMed
    • Walker, J. E., Saraste, M., Runswick, M. J. And Gay, N. J. (1982) Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951 PubMed
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 43
    • 0025048136 scopus 로고
    • The P-loop-A common motif in ATP-and GTP-binding proteins
    • CrossRef PubMed
    • Saraste, M., Sibbald, P. R. And Wittinghofer, A. (1990) The P-loop-a common motif in ATP-and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434 CrossRef PubMed
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 44
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • CrossRef PubMed
    • Story, R. M. And Steitz, T. A. (1992) Structure of the recA protein-ADP complex. Nature 355, 374-376 CrossRef PubMed
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 45
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • CrossRef PubMed
    • Babst, M., Wendland, B., Estepa, E. J. And Emr, S. D. (1998) The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982-2993 CrossRef PubMed
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 46
    • 21744446127 scopus 로고    scopus 로고
    • AAA+ proteins: Have engine, will work
    • CrossRef PubMed
    • Hanson, P. I. And Whiteheart, S. W. (2005) AAA+ proteins: have engine, will work. Nat. Rev. Mol. Cell Biol. 6, 519-529 CrossRef PubMed
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 519-529
    • Hanson, P.I.1    Whiteheart, S.W.2
  • 48
    • 84923074901 scopus 로고    scopus 로고
    • Linked domain architectures allow for specialization of function in the FtsK/SpoIIIE ATPases of ESX secretion systems
    • CrossRef PubMed
    • Ramsdell, T. L., Huppert, L. A., Sysoeva, T. A., Fortune, S. M. And Burton, B. M. (2015) Linked domain architectures allow for specialization of function in the FtsK/SpoIIIE ATPases of ESX secretion systems. J. Mol. Biol. 427, 1119-1132 CrossRef PubMed
    • (2015) J. Mol. Biol. , vol.427 , pp. 1119-1132
    • Ramsdell, T.L.1    Huppert, L.A.2    Sysoeva, T.A.3    Fortune, S.M.4    Burton, B.M.5
  • 49
    • 52949152375 scopus 로고    scopus 로고
    • Structure of Staphylococcus aureus EsxA suggests a contribution to virulence by action as a transport chaperone and/or adaptor protein
    • CrossRef PubMed
    • Sundaramoorthy, R., Fyfe, P. K. And Hunter, W. N. (2008) Structure of Staphylococcus aureus EsxA suggests a contribution to virulence by action as a transport chaperone and/or adaptor protein. J. Mol. Biol. 383, 603-614 CrossRef PubMed
    • (2008) J. Mol. Biol. , vol.383 , pp. 603-614
    • Sundaramoorthy, R.1    Fyfe, P.K.2    Hunter, W.N.3
  • 51
    • 4344596222 scopus 로고    scopus 로고
    • The RD1 virulence locus of Mycobacterium tuberculosis regulates DNA transfer in Mycobacterium smegmatis
    • CrossRef PubMed
    • Flint, J. L., Kowalski, J. C., Karnati, P. K. And Derbyshire, K. M. (2004) The RD1 virulence locus of Mycobacterium tuberculosis regulates DNA transfer in Mycobacterium smegmatis. Proc. Natl. Acad. Sci. U. S. A. 101, 12598-12603 CrossRef PubMed
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 12598-12603
    • Flint, J.L.1    Kowalski, J.C.2    Karnati, P.K.3    Derbyshire, K.M.4
  • 52
    • 47749109112 scopus 로고    scopus 로고
    • The specialized secretory apparatus ESX-1 is essential for DNA transfer in Mycobacterium smegmatis
    • PubMed
    • Coros, A., Callahan, B., Battaglioli, E. And Derbyshire, K. M. (2008) The specialized secretory apparatus ESX-1 is essential for DNA transfer in Mycobacterium smegmatis. Mol. Microbiol. 69, 794-808 PubMed
    • (2008) Mol. Microbiol. , vol.69 , pp. 794-808
    • Coros, A.1    Callahan, B.2    Battaglioli, E.3    Derbyshire, K.M.4
  • 53
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • CrossRef PubMed
    • Erzberger, J. P. And Berger, J. M. (2006) Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35, 93-114 CrossRef PubMed
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.