메뉴 건너뛰기




Volumn 174, Issue 1, 2011, Pages 124-136

Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies

Author keywords

Kinetoplastid; Nanobodies; OB fold proteins; RNA editing; VHH domain

Indexed keywords

ANTIBODY; PROTEIN KREPA6; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 79952451439     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.10.007     Document Type: Article
Times cited : (29)

References (92)
  • 2
    • 0032544662 scopus 로고    scopus 로고
    • SSB protein controls RecBCD enzyme nuclease activity during unwinding: a new role for looped intermediates
    • Anderson D.G., Kowalczykowski S.C. SSB protein controls RecBCD enzyme nuclease activity during unwinding: a new role for looped intermediates. J. Mol. Biol. 1998, 282:275-285.
    • (1998) J. Mol. Biol. , vol.282 , pp. 275-285
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 3
    • 0037450771 scopus 로고    scopus 로고
    • Isolation of a U-insertion/deletion editing complex from Leishmania tarentolae mitochondria
    • Aphasizhev R., Aphasizheva I., Nelson R.E., Gao G., Simpson A.M., et al. Isolation of a U-insertion/deletion editing complex from Leishmania tarentolae mitochondria. EMBO J. 2003, 22:913-924.
    • (2003) EMBO J. , vol.22 , pp. 913-924
    • Aphasizhev, R.1    Aphasizheva, I.2    Nelson, R.E.3    Gao, G.4    Simpson, A.M.5
  • 4
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: a snapshot of the evolution of sequence, structure and function
    • Arcus V. OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr. Opin. Struct. Biol. 2002, 12:794-801.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 794-801
    • Arcus, V.1
  • 5
    • 1342302794 scopus 로고    scopus 로고
    • From RPA to BRCA2: lessons from single-stranded DNA binding by the OB-fold
    • Bochkarev A., Bochkareva E. From RPA to BRCA2: lessons from single-stranded DNA binding by the OB-fold. Curr. Opin. Struct. Biol. 2004, 14:36-42.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 36-42
    • Bochkarev, A.1    Bochkareva, E.2
  • 6
    • 0037007223 scopus 로고    scopus 로고
    • Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA
    • Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A. Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. EMBO J. 2002, 21:1855-1863.
    • (2002) EMBO J. , vol.21 , pp. 1855-1863
    • Bochkareva, E.1    Korolev, S.2    Lees-Miller, S.P.3    Bochkarev, A.4
  • 7
    • 14644397311 scopus 로고    scopus 로고
    • TbMP42, a protein component of the RNA editing complex in African trypanosomes, has endo-exoribonuclease activity
    • Brecht M., Niemann M., Schluter E., Muller U.F., Stuart K., et al. TbMP42, a protein component of the RNA editing complex in African trypanosomes, has endo-exoribonuclease activity. Mol. Cell 2005, 17:621-630.
    • (2005) Mol. Cell , vol.17 , pp. 621-630
    • Brecht, M.1    Niemann, M.2    Schluter, E.3    Muller, U.F.4    Stuart, K.5
  • 8
    • 0037053286 scopus 로고    scopus 로고
    • Analysis of a multicomponent thermostable DNA polymerase III replicase from an extreme thermophile
    • Bruck I., Yuzhakov A., Yurieva O., Jeruzalmi D., Skangalis M., et al. Analysis of a multicomponent thermostable DNA polymerase III replicase from an extreme thermophile. J. Biol. Chem. 2002, 277:17334-17348.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17334-17348
    • Bruck, I.1    Yuzhakov, A.2    Yurieva, O.3    Jeruzalmi, D.4    Skangalis, M.5
  • 9
    • 0037036364 scopus 로고    scopus 로고
    • Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution
    • Bubb M.R., Govindasamy L., Yarmola E.G., Vorobiev S.M., Almo S.C., et al. Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution. J. Biol. Chem. 2002, 277:20999-21006.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20999-21006
    • Bubb, M.R.1    Govindasamy, L.2    Yarmola, E.G.3    Vorobiev, S.M.4    Almo, S.C.5
  • 11
    • 37549054714 scopus 로고    scopus 로고
    • RNA editing in Trypanosoma brucei requires three different editosomes
    • Carnes J., Trotter J.R., Peltan A., Fleck M., Stuart K. RNA editing in Trypanosoma brucei requires three different editosomes. Mol. Cell Biol. 2008, 28:122-130.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 122-130
    • Carnes, J.1    Trotter, J.R.2    Peltan, A.3    Fleck, M.4    Stuart, K.5
  • 12
    • 64649099756 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein complex from Helicobacter pylori suggests an ssDNA-binding surface
    • Chan K.W., Lee Y.J., Wang C.H., Huang H., Sun Y.J. Single-stranded DNA-binding protein complex from Helicobacter pylori suggests an ssDNA-binding surface. J. Mol. Biol. 2009, 388:508-519.
    • (2009) J. Mol. Biol. , vol.388 , pp. 508-519
    • Chan, K.W.1    Lee, Y.J.2    Wang, C.H.3    Huang, H.4    Sun, Y.J.5
  • 13
    • 0022555837 scopus 로고
    • Single-stranded DNA binding proteins required for DNA replication
    • Chase J.W., Williams K.R. Single-stranded DNA binding proteins required for DNA replication. Annu. Rev. Biochem. 1986, 55:103-136.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 103-136
    • Chase, J.W.1    Williams, K.R.2
  • 15
    • 1442280871 scopus 로고    scopus 로고
    • From the cell biology to the development of new chemotherapeutic approaches against trypanosomatids: dreams and reality
    • e-publication
    • De Souza W. From the cell biology to the development of new chemotherapeutic approaches against trypanosomatids: dreams and reality. Kinetoplastid Biol. Dis. 2002, 1:1-21. e-publication.
    • (2002) Kinetoplastid Biol. Dis. , vol.1 , pp. 1-21
    • De Souza, W.1
  • 16
    • 4744374004 scopus 로고    scopus 로고
    • High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei: RNA editing ligase 1
    • Deng J., Schnaufer A., Salavati R., Stuart K.D., Hol W.G. High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei: RNA editing ligase 1. J. Mol. Biol. 2004, 343:601-613.
    • (2004) J. Mol. Biol. , vol.343 , pp. 601-613
    • Deng, J.1    Schnaufer, A.2    Salavati, R.3    Stuart, K.D.4    Hol, W.G.5
  • 17
    • 28644431836 scopus 로고    scopus 로고
    • Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei
    • Deng J., Ernst N.L., Turley S., Stuart K.D., Hol W.G. Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. EMBO J. 2005, 24:4007-4017.
    • (2005) EMBO J. , vol.24 , pp. 4007-4017
    • Deng, J.1    Ernst, N.L.2    Turley, S.3    Stuart, K.D.4    Hol, W.G.5
  • 18
    • 0037189507 scopus 로고    scopus 로고
    • Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology
    • Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., et al. Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. J. Biol. Chem. 2002, 277:23645-23650.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23645-23650
    • Desmyter, A.1    Spinelli, S.2    Payan, F.3    Lauwereys, M.4    Wyns, L.5
  • 19
    • 33645034034 scopus 로고    scopus 로고
    • Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60A resolution
    • DiDonato M., Krishna S.S., Schwarzenbacher R., McMullan D., Jaroszewski L., et al. Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60A resolution. Proteins 2006, 63:256-260.
    • (2006) Proteins , vol.63 , pp. 256-260
    • DiDonato, M.1    Krishna, S.S.2    Schwarzenbacher, R.3    McMullan, D.4    Jaroszewski, L.5
  • 21
    • 2942642109 scopus 로고    scopus 로고
    • The single-stranded DNA-binding protein of Deinococcus radiodurans
    • e-publication
    • Eggington J.M., Haruta N., Wood E.A., Cox M.M. The single-stranded DNA-binding protein of Deinococcus radiodurans. BMC Microbiol. 2004, 4:1-12. e-publication.
    • (2004) BMC Microbiol. , vol.4 , pp. 1-12
    • Eggington, J.M.1    Haruta, N.2    Wood, E.A.3    Cox, M.M.4
  • 23
    • 65249140056 scopus 로고    scopus 로고
    • Differential functions of two editosome exoUases in Trypanosoma brucei
    • Ernst N.L., Panicucci B., Carnes J., Stuart K. Differential functions of two editosome exoUases in Trypanosoma brucei. RNA 2009, 15:947-957.
    • (2009) RNA , vol.15 , pp. 947-957
    • Ernst, N.L.1    Panicucci, B.2    Carnes, J.3    Stuart, K.4
  • 24
    • 0142258170 scopus 로고    scopus 로고
    • Chemotherapy of human African trypanosomiasis: current and future prospects
    • Fairlamb A.H. Chemotherapy of human African trypanosomiasis: current and future prospects. Trends Parasitol. 2003, 19:488-494.
    • (2003) Trends Parasitol. , vol.19 , pp. 488-494
    • Fairlamb, A.H.1
  • 25
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease
    • Genschel J., Curth U., Urbanke C. Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease. Biol. Chem. 2000, 381:183-192.
    • (2000) Biol. Chem. , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 26
    • 0032483511 scopus 로고    scopus 로고
    • The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template
    • Glover B.P., McHenry C.S. The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template. J. Biol. Chem. 1998, 273:23476-23484.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 27
    • 62649115927 scopus 로고    scopus 로고
    • Snapshots of the RNA editing machine in trypanosomes captured at different assembly stages in vivo
    • Golas M.M., Bohm C., Sander B., Effenberger K., Brecht M., et al. Snapshots of the RNA editing machine in trypanosomes captured at different assembly stages in vivo. EMBO J. 2009, 28:766-778.
    • (2009) EMBO J. , vol.28 , pp. 766-778
    • Golas, M.M.1    Bohm, C.2    Sander, B.3    Effenberger, K.4    Brecht, M.5
  • 28
    • 33845516882 scopus 로고    scopus 로고
    • Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library
    • Goldman E.R., Anderson G.P., Liu J.L., Delehanty J.B., Sherwood L.J., et al. Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library. Anal. Chem. 2006, 78:8245-8255.
    • (2006) Anal. Chem. , vol.78 , pp. 8245-8255
    • Goldman, E.R.1    Anderson, G.P.2    Liu, J.L.3    Delehanty, J.B.4    Sherwood, L.J.5
  • 29
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999, 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 30
    • 34047109097 scopus 로고    scopus 로고
    • Cell cycle regulation in Trypanosoma brucei
    • Hammarton T.C. Cell cycle regulation in Trypanosoma brucei. Mol. Biochem. Parasitol. 2007, 153:1-8.
    • (2007) Mol. Biochem. Parasitol. , vol.153 , pp. 1-8
    • Hammarton, T.C.1
  • 31
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases
    • Handa P., Acharya N., Varshney U. Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases. J. Biol. Chem. 2001, 276:16992-16997.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 32
    • 0032431057 scopus 로고    scopus 로고
    • Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA
    • Horvath M.P., Schweiker V.L., Bevilacqua J.M., Ruggles J.A., Schultz S.C. Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA. Cell 1998, 95:963-974.
    • (1998) Cell , vol.95 , pp. 963-974
    • Horvath, M.P.1    Schweiker, V.L.2    Bevilacqua, J.M.3    Ruggles, J.A.4    Schultz, S.C.5
  • 35
    • 1042278183 scopus 로고    scopus 로고
    • Disruption of the zinc finger motifs in the Leishmania tarentolae LC-4 (=TbMP63) L-complex editing protein affects the stability of the L-complex
    • Kang X., Falick A.M., Nelson R.E., Gao G., Rogers K., et al. Disruption of the zinc finger motifs in the Leishmania tarentolae LC-4 (=TbMP63) L-complex editing protein affects the stability of the L-complex. J. Biol. Chem. 2004, 279:3893-3899.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3893-3899
    • Kang, X.1    Falick, A.M.2    Nelson, R.E.3    Gao, G.4    Rogers, K.5
  • 36
    • 0037180443 scopus 로고    scopus 로고
    • Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: a common step in genetic recombination
    • Kantake N., Madiraju M.V., Sugiyama T., Kowalczykowski S.C. Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: a common step in genetic recombination. Proc. Natl. Acad. Sci. USA 2002, 99:15327-15332.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15327-15332
    • Kantake, N.1    Madiraju, M.V.2    Sugiyama, T.3    Kowalczykowski, S.C.4
  • 37
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman Z., Yuzhakov A., Andjelkovic J., O'Donnell M. Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J. 1998, 17:2436-2449.
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 38
    • 0037526104 scopus 로고    scopus 로고
    • Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein
    • Kerr I.D., Wadsworth R.I., Cubeddu L., Blankenfeldt W., Naismith J.H., et al. Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein. EMBO J. 2003, 22:2561-2570.
    • (2003) EMBO J. , vol.22 , pp. 2561-2570
    • Kerr, I.D.1    Wadsworth, R.I.2    Cubeddu, L.3    Blankenfeldt, W.4    Naismith, J.H.5
  • 40
    • 69249107262 scopus 로고    scopus 로고
    • Engineering of recombinant crystallization chaperones
    • Koide S. Engineering of recombinant crystallization chaperones. Curr. Opin. Struct. Biol. 2009, 19:449-457.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 449-457
    • Koide, S.1
  • 41
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov K.V., Pardon E., Steyaert J., Hol W.G. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 2009, 17:255-265.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 42
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 43
    • 60949108827 scopus 로고    scopus 로고
    • Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus
    • Lam A.Y., Pardon E., Korotkov K.V., Hol W.G., Steyaert J. Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus. J. Struct. Biol. 2009, 166:8-15.
    • (2009) J. Struct. Biol. , vol.166 , pp. 8-15
    • Lam, A.Y.1    Pardon, E.2    Korotkov, K.V.3    Hol, W.G.4    Steyaert, J.5
  • 44
    • 33846164078 scopus 로고    scopus 로고
    • In Trypanosoma brucei RNA editing, TbMP18 (band VII) is critical for editosome integrity and for both insertional and deletional cleavages
    • Law J.A., O'Hearn S., Sollner-Webb B. In Trypanosoma brucei RNA editing, TbMP18 (band VII) is critical for editosome integrity and for both insertional and deletional cleavages. Mol. Cell Biol. 2007, 27:777-787.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 777-787
    • Law, J.A.1    O'Hearn, S.2    Sollner-Webb, B.3
  • 45
    • 44149103662 scopus 로고    scopus 로고
    • Trypanosoma brucei RNA editing protein TbMP42 (band VI) is crucial for the endonucleolytic cleavages but not the subsequent steps of U-deletion and U-insertion
    • Law J.A., O'Hearn S.F., Sollner-Webb B. Trypanosoma brucei RNA editing protein TbMP42 (band VI) is crucial for the endonucleolytic cleavages but not the subsequent steps of U-deletion and U-insertion. RNA 2008, 14:1187-1200.
    • (2008) RNA , vol.14 , pp. 1187-1200
    • Law, J.A.1    O'Hearn, S.F.2    Sollner-Webb, B.3
  • 46
    • 33845711540 scopus 로고    scopus 로고
    • IMGT, the international ImMunoGeneTics information system: a standardized approach for immunogenetics and immunoinformatics
    • Lefranc M.P. IMGT, the international ImMunoGeneTics information system: a standardized approach for immunogenetics and immunoinformatics. Immunome Res. 2005, 1:3.
    • (2005) Immunome Res. , vol.1 , pp. 3
    • Lefranc, M.P.1
  • 47
    • 68149089810 scopus 로고    scopus 로고
    • Structure of the core editing complex (L-complex) involved in uridine insertion/deletion RNA editing in trypanosomatid mitochondria
    • Li F., Ge P., Hui W.H., Atanasov I., Rogers K., et al. Structure of the core editing complex (L-complex) involved in uridine insertion/deletion RNA editing in trypanosomatid mitochondria. Proc. Natl. Acad. Sci. USA 2009, 106:12306-12310.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 12306-12310
    • Li, F.1    Ge, P.2    Hui, W.H.3    Atanasov, I.4    Rogers, K.5
  • 48
    • 9644264027 scopus 로고    scopus 로고
    • Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli
    • Liu J.H., Chang T.W., Huang C.Y., Chen S.U., Wu H.N., et al. Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli. J. Biol. Chem. 2004, 279:50465-50471.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50465-50471
    • Liu, J.H.1    Chang, T.W.2    Huang, C.Y.3    Chen, S.U.4    Wu, H.N.5
  • 49
    • 0024039462 scopus 로고
    • E. coli single strand binding protein: a new look at helix-destabilizing proteins
    • Lohman T.M., Bujalowski W., Overman L.B. E. coli single strand binding protein: a new look at helix-destabilizing proteins. Trends Biochem. Sci. 1988, 13:250-255.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 250-255
    • Lohman, T.M.1    Bujalowski, W.2    Overman, L.B.3
  • 50
    • 7944229709 scopus 로고    scopus 로고
    • Crystal structure of PriB, a component of the Escherichia coli replication restart primosome
    • Lopper M., Holton J.M., Keck J.L. Crystal structure of PriB, a component of the Escherichia coli replication restart primosome. Structure 2004, 12:1967-1975.
    • (2004) Structure , vol.12 , pp. 1967-1975
    • Lopper, M.1    Holton, J.M.2    Keck, J.L.3
  • 51
  • 52
    • 28044460265 scopus 로고    scopus 로고
    • Unexplained complexity of the mitochondrial genome and transcriptome in kinetoplastid flagellates
    • Lukes J., Hashimi H., Zikova A. Unexplained complexity of the mitochondrial genome and transcriptome in kinetoplastid flagellates. Curr. Genet. 2005, 48:277-299.
    • (2005) Curr. Genet. , vol.48 , pp. 277-299
    • Lukes, J.1    Hashimi, H.2    Zikova, A.3
  • 53
    • 0034092927 scopus 로고    scopus 로고
    • Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-ray structure analysis
    • Matsumoto T., Morimoto Y., Shibata N., Kinebuchi T., Shimamoto N., et al. Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-ray structure analysis. J. Biochem. 2000, 127:329-335.
    • (2000) J. Biochem. , vol.127 , pp. 329-335
    • Matsumoto, T.1    Morimoto, Y.2    Shibata, N.3    Kinebuchi, T.4    Shimamoto, N.5
  • 55
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer R.R., Laine P.S. The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 1990, 54:342-380.
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 56
    • 7944224890 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target
    • Moyersoen J., Choe J., Fan E., Hol W.G., Michels P.A. Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target. FEMS Microbiol. Rev. 2004, 28:603-643.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 603-643
    • Moyersoen, J.1    Choe, J.2    Fan, E.3    Hol, W.G.4    Michels, P.A.5
  • 58
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences
    • Murzin A.G. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 1993, 12:861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 59
    • 0035715877 scopus 로고    scopus 로고
    • Single domain camel antibodies: current status
    • Muyldermans S. Single domain camel antibodies: current status. J. Biotechnol. 2001, 74:277-302.
    • (2001) J. Biotechnol. , vol.74 , pp. 277-302
    • Muyldermans, S.1
  • 60
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
    • Muyldermans S., Cambillau C., Wyns L. Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. Trends Biochem. Sci. 2001, 26:230-235.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 62
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Academic Press, New York
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 1997, vol. 276:307-326. Academic Press, New York.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 63
    • 33646870148 scopus 로고    scopus 로고
    • Compositionally and functionally distinct editosomes in Trypanosoma brucei
    • Panigrahi A.K., Ernst N.L., Domingo G.J., Fleck M., Salavati R., et al. Compositionally and functionally distinct editosomes in Trypanosoma brucei. RNA 2006, 12:1038-1049.
    • (2006) RNA , vol.12 , pp. 1038-1049
    • Panigrahi, A.K.1    Ernst, N.L.2    Domingo, G.J.3    Fleck, M.4    Salavati, R.5
  • 64
    • 0037379043 scopus 로고    scopus 로고
    • Identification of novel components of Trypanosoma brucei editosomes
    • Panigrahi A.K., Schnaufer A., Ernst N.L., Wang B., Carmean N., et al. Identification of novel components of Trypanosoma brucei editosomes. RNA 2003, 9:484-492.
    • (2003) RNA , vol.9 , pp. 484-492
    • Panigrahi, A.K.1    Schnaufer, A.2    Ernst, N.L.3    Wang, B.4    Carmean, N.5
  • 65
  • 66
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength X-ray diffraction on the selenomethionyl protein at 2.9-A resolution
    • Raghunathan S., Ricard C.S., Lohman T.M., Waksman G. Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength X-ray diffraction on the selenomethionyl protein at 2.9-A resolution. Proc. Natl. Acad. Sci. USA 1997, 94:6652-6657.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 68
    • 0030928201 scopus 로고    scopus 로고
    • Purification of a functional enzymatic editing complex from Trypanosoma brucei mitochondria
    • Rusche L.N., Cruz-Reyes J., Piller K.J., Sollner-Webb B. Purification of a functional enzymatic editing complex from Trypanosoma brucei mitochondria. EMBO J. 1997, 16:4069-4081.
    • (1997) EMBO J. , vol.16 , pp. 4069-4081
    • Rusche, L.N.1    Cruz-Reyes, J.2    Piller, K.J.3    Sollner-Webb, B.4
  • 69
    • 0041347886 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications
    • Saikrishnan K., Jeyakanthan J., Venkatesh J., Acharya N., Sekar K., et al. Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications. J. Mol. Biol. 2003, 331:385-393.
    • (2003) J. Mol. Biol. , vol.331 , pp. 385-393
    • Saikrishnan, K.1    Jeyakanthan, J.2    Venkatesh, J.3    Acharya, N.4    Sekar, K.5
  • 70
    • 25144522675 scopus 로고    scopus 로고
    • Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologous SSBs: biological implications of structural plasticity and variability in quaternary association
    • Saikrishnan K., Manjunath G.P., Singh P., Jeyakanthan J., Dauter Z., et al. Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologous SSBs: biological implications of structural plasticity and variability in quaternary association. Acta Crystallogr. D: Biol. Crystallogr. 2005, 61:1140-1148.
    • (2005) Acta Crystallogr. D: Biol. Crystallogr. , vol.61 , pp. 1140-1148
    • Saikrishnan, K.1    Manjunath, G.P.2    Singh, P.3    Jeyakanthan, J.4    Dauter, Z.5
  • 71
    • 33646189413 scopus 로고    scopus 로고
    • KREPA4, an RNA binding protein essential for editosome integrity and survival of Trypanosoma brucei
    • Salavati R., Ernst N.L., O'Rear J., Gilliam T., Tarun S., et al. KREPA4, an RNA binding protein essential for editosome integrity and survival of Trypanosoma brucei. RNA 2006, 12:819-831.
    • (2006) RNA , vol.12 , pp. 819-831
    • Salavati, R.1    Ernst, N.L.2    O'Rear, J.3    Gilliam, T.4    Tarun, S.5
  • 72
    • 3042625942 scopus 로고    scopus 로고
    • The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA
    • Savvides S.N., Raghunathan S., Futterer K., Kozlov A.G., Lohman T.M., et al. The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA. Protein Sci. 2004, 13:1942-1947.
    • (2004) Protein Sci. , vol.13 , pp. 1942-1947
    • Savvides, S.N.1    Raghunathan, S.2    Futterer, K.3    Kozlov, A.G.4    Lohman, T.M.5
  • 73
    • 0141922994 scopus 로고    scopus 로고
    • Separate insertion and deletion subcomplexes of the Trypanosoma brucei RNA editing complex
    • Schnaufer A., Ernst N.L., Palazzo S.S., O'Rear J., Salavati R., et al. Separate insertion and deletion subcomplexes of the Trypanosoma brucei RNA editing complex. Mol. Cell 2003, 12:307-319.
    • (2003) Mol. Cell , vol.12 , pp. 307-319
    • Schnaufer, A.1    Ernst, N.L.2    Palazzo, S.S.3    O'Rear, J.4    Salavati, R.5
  • 74
    • 77949327311 scopus 로고    scopus 로고
    • A protein-protein interaction map of trypanosome 20S editosomes
    • Schnaufer A., Wu M., Park Y.J., Nakai T., Deng J., et al. A protein-protein interaction map of trypanosome 20S editosomes. J. Biol. Chem. 2010, 285:5282-5295.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5282-5295
    • Schnaufer, A.1    Wu, M.2    Park, Y.J.3    Nakai, T.4    Deng, J.5
  • 76
    • 10644282271 scopus 로고    scopus 로고
    • Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site
    • Shioi S., Ose T., Maenaka K., Shiroishi M., Abe Y., et al. Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site. Biochem. Biophys. Res. Commun. 2005, 326:766-776.
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 766-776
    • Shioi, S.1    Ose, T.2    Maenaka, K.3    Shiroishi, M.4    Abe, Y.5
  • 77
    • 1642580825 scopus 로고    scopus 로고
    • Mitochondrial proteins and complexes in Leishmania and Trypanosoma involved in U-insertion/deletion RNA editing
    • Simpson L., Aphasizhev R., Gao G., Kang X. Mitochondrial proteins and complexes in Leishmania and Trypanosoma involved in U-insertion/deletion RNA editing. RNA 2004, 10:159-170.
    • (2004) RNA , vol.10 , pp. 159-170
    • Simpson, L.1    Aphasizhev, R.2    Gao, G.3    Kang, X.4
  • 80
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • Stein A., Weber G., Wahl M.C., Jahn R. Helical extension of the neuronal SNARE complex into the membrane. Nature 2009, 460:525-528.
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 83
    • 38649125860 scopus 로고    scopus 로고
    • KREPA6 is an RNA-binding protein essential for editosome integrity and survival of Trypanosoma brucei
    • Tarun S.Z., Schnaufer A., Ernst N.L., Proff R., Deng J., et al. KREPA6 is an RNA-binding protein essential for editosome integrity and survival of Trypanosoma brucei. RNA 2008, 14:347-358.
    • (2008) RNA , vol.14 , pp. 347-358
    • Tarun, S.Z.1    Schnaufer, A.2    Ernst, N.L.3    Proff, R.4    Deng, J.5
  • 84
    • 46449122768 scopus 로고    scopus 로고
    • Toward chaperone-assisted crystallography: protein engineering enhancement of crystal packing and X-ray phasing capabilities of a camelid single-domain antibody (VHH) scaffold
    • Tereshko V., Uysal S., Koide A., Margalef K., Koide S., et al. Toward chaperone-assisted crystallography: protein engineering enhancement of crystal packing and X-ray phasing capabilities of a camelid single-domain antibody (VHH) scaffold. Protein Sci. 2008, 17:1175-1187.
    • (2008) Protein Sci. , vol.17 , pp. 1175-1187
    • Tereshko, V.1    Uysal, S.2    Koide, A.3    Margalef, K.4    Koide, S.5
  • 86
    • 0028034452 scopus 로고
    • Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein
    • Umezu K., Kolodner R.D. Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein. J. Biol. Chem. 1994, 269:30005-30013.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30005-30013
    • Umezu, K.1    Kolodner, R.D.2
  • 87
    • 53949111444 scopus 로고    scopus 로고
    • Guide RNA-binding complex from mitochondria of trypanosomatids
    • Weng J., Aphasizheva I., Etheridge R.D., Huang L., Wang X., et al. Guide RNA-binding complex from mitochondria of trypanosomatids. Mol. Cell 2008, 32:198-209.
    • (2008) Mol. Cell , vol.32 , pp. 198-209
    • Weng, J.1    Aphasizheva, I.2    Etheridge, R.D.3    Huang, L.4    Wang, X.5
  • 88
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D: Biol. Crystallogr. 2001, 57:122-133.
    • (2001) Acta Crystallogr. D: Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 89
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery
    • Witte G., Urbanke C., Curth U. DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery. Nucleic Acids Res. 2003, 31:4434-4440.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 91
    • 0031023811 scopus 로고    scopus 로고
    • Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4A resolution
    • Yang C., Curth U., Urbanke C., Kang C. Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4A resolution. Nat. Struct. Biol. 1997, 4:153-157.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 153-157
    • Yang, C.1    Curth, U.2    Urbanke, C.3    Kang, C.4
  • 92
    • 18544372595 scopus 로고    scopus 로고
    • BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure
    • Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., et al. BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. Science 2002, 297:1837-1848.
    • (2002) Science , vol.297 , pp. 1837-1848
    • Yang, H.1    Jeffrey, P.D.2    Miller, J.3    Kinnucan, E.4    Sun, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.