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Volumn 12, Issue 9, 2015, Pages 859-865

ProteoPlex: Stability optimization of macromolecular complexes by sparse-matrix screening of chemical space

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; MULTIPROTEIN COMPLEX; PROTEIN BINDING;

EID: 84940608127     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.3493     Document Type: Article
Times cited : (81)

References (27)
  • 1
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17. 1030-1032 (1999
    • (1999) Nat. Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1
  • 2
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger, I., Fitzgerald, D.J., & Richmond, T.J. Baculovirus expression system for heterologous multiprotein complexes. Nat. Biotechnol. 22. 1583-1587 (2004
    • (2004) Nat. Biotechnol , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 3
    • 0037227959 scopus 로고    scopus 로고
    • An efficient protein complex purification method for functional proteomics in higher eukaryotes
    • Forler, D., et al. An efficient protein complex purification method for functional proteomics in higher eukaryotes. Nat. Biotechnol. 21. 89-92 (2003
    • (2003) Nat. Biotechnol , vol.21 , pp. 89-92
    • Forler, D.1
  • 4
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin, A.C., et al. Proteome survey reveals modularity of the yeast cell machinery. Nature. 440. 631-636 (2006
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1
  • 5
    • 79960027830 scopus 로고    scopus 로고
    • Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells
    • Vijayachandran, L.S., et al. Robots, pipelines, polyproteins: enabling multiprotein expression in prokaryotic and eukaryotic cells. J. Struct. Biol. 175. 198-208 (2011
    • (2011) J. Struct. Biol , vol.175 , pp. 198-208
    • Vijayachandran, L.S.1
  • 6
    • 40549086568 scopus 로고    scopus 로고
    • Automated technologies and novel techniques to accelerate protein crystallography for structural genomics
    • Manjasetty, B.A., Turnbull, A.P., Panjikar, S., Bussow, K., & Chance, M.R. Automated technologies and novel techniques to accelerate protein crystallography for structural genomics. Proteomics. 8. 612-625 (2008
    • (2008) Proteomics , vol.8 , pp. 612-625
    • Manjasetty, B.A.1    Turnbull, A.P.2    Panjikar, S.3    Bussow, K.4    Chance, M.R.5
  • 8
    • 84928400353 scopus 로고    scopus 로고
    • Single-particle cryo-EM at crystallographic resolution
    • Cheng, Y. Single-particle cryo-EM at crystallographic resolution. Cell. 161. 450-457 (2015
    • (2015) Cell , vol.161 , pp. 450-457
    • Cheng, Y.1
  • 9
    • 35548958606 scopus 로고    scopus 로고
    • Strategies for crystallization and structure determination of very large macromolecular assemblies
    • Mueller, M., Jenni, S., & Ban, N. Strategies for crystallization and structure determination of very large macromolecular assemblies. Curr. Opin. Struct. Biol. 17. 572-579 (2007
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 572-579
    • Mueller, M.1    Jenni, S.2    Ban, N.3
  • 10
    • 84883894803 scopus 로고    scopus 로고
    • Optimization of protein purification and characterization using Thermofluor screens
    • Boivin, S., Kozak, S., & Meijers, R. Optimization of protein purification and characterization using Thermofluor screens. Protein Expr. Purif. 91. 192-206 (2013
    • (2013) Protein Expr. Purif , vol.91 , pp. 192-206
    • Boivin, S.1    Kozak, S.2    Meijers, R.3
  • 11
    • 79960001045 scopus 로고    scopus 로고
    • Comparison of fluorescence and light scattering based methods to assess formation and stability of protein-protein complexes
    • Kopec, J., & Schneider, G. Comparison of fluorescence and light scattering based methods to assess formation and stability of protein-protein complexes. J. Struct. Biol. 175. 216-223 (2011
    • (2011) J. Struct. Biol , vol.175 , pp. 216-223
    • Kopec, J.1    Schneider, G.2
  • 12
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F.H., Berglund, H., & Vedadi, M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2. 2212-2221 (2007
    • (2007) Nat. Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 14
    • 0014800814 scopus 로고
    • Comparison of molecular structures of proteins: Helix content; Distribution of apolar residues
    • Klotz, I.M. Comparison of molecular structures of proteins: helix content; distribution of apolar residues. Arch. Biochem. Biophys. 138. 704-706 (1970
    • (1970) Arch. Biochem. Biophys , vol.138 , pp. 704-706
    • Klotz, I.M.1
  • 16
    • 33750356686 scopus 로고    scopus 로고
    • Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 Å resolution
    • Chandrasekhar, K., et al. Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 62. 1382-1386 (2006
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 1382-1386
    • Chandrasekhar, K.1
  • 17
    • 0017403869 scopus 로고
    • Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Bates, D.L., Danson, M.J., Hale, G., Hooper, E.A., & Perham, R.N. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Nature. 268. 313-316 (1977
    • (1977) Nature , vol.268 , pp. 313-316
    • Bates, D.L.1    Danson, M.J.2    Hale, G.3    Hooper, E.A.4    Perham, R.N.5
  • 18
    • 54549102220 scopus 로고    scopus 로고
    • An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs
    • Chari, A., et al. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell. 135. 497-509 (2008
    • (2008) Cell , vol.135 , pp. 497-509
    • Chari, A.1
  • 20
    • 33747080785 scopus 로고    scopus 로고
    • Red blood with blue-blood ancestry: Intriguing structure of a snail hemoglobin
    • Lieb, B., et al. Red blood with blue-blood ancestry: intriguing structure of a snail hemoglobin. Proc. Natl. Acad. Sci. USA. 103. 12011-12016 (2006
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12011-12016
    • Lieb, B.1
  • 21
    • 84880171038 scopus 로고    scopus 로고
    • Electron microscopy structure of human APC/CCDH-1-EMI1 reveals multimodal mechanism of E3 ligase shutdown
    • Frye, J.J., et al. Electron microscopy structure of human APC/CCDH-1-EMI1 reveals multimodal mechanism of E3 ligase shutdown. Nat. Struct. Mol. Biol. 20. 827-835 (2013
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 827-835
    • Frye, J.J.1
  • 22
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Gao, Y.G., et al. The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science. 326. 694-699 (2009
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1
  • 23
    • 42949164124 scopus 로고    scopus 로고
    • Improved structures of full-length p97, an AAA ATPase: Implications for mechanisms of nucleotide-dependent conformational change
    • Davies, J.M., Brunger, A.T., & Weis, W.I. Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. Structure. 16. 715-726 (2008
    • (2008) Structure , vol.16 , pp. 715-726
    • Davies, J.M.1    Brunger, A.T.2    Weis, W.I.3
  • 24
    • 79961137129 scopus 로고    scopus 로고
    • Structure of a key intermediate of the SMN complex reveals Gemin2s crucial function in snRNP assembly
    • Zhang, R., et al. Structure of a key intermediate of the SMN complex reveals Gemin2s crucial function in snRNP assembly. Cell. 146. 384-395 (2011
    • (2011) Cell , vol.146 , pp. 384-395
    • Zhang, R.1
  • 25
    • 84874256850 scopus 로고    scopus 로고
    • Structural basis of assembly chaperone- mediated snRNP formation
    • Grimm, C., et al. Structural basis of assembly chaperone- mediated snRNP formation. Mol. Cell. 49. 692-703 (2013
    • (2013) Mol. Cell , vol.49 , pp. 692-703
    • Grimm, C.1
  • 26
    • 66249108600 scopus 로고    scopus 로고
    • Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP
    • Monecke, T., et al. Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP. Science. 324. 1087-1091 (2009
    • (2009) Science , vol.324 , pp. 1087-1091
    • Monecke, T.1
  • 27
    • 84876265995 scopus 로고    scopus 로고
    • Alternating sites reactivity is a common feature of thiamin diphosphate-dependent enzymes as evidenced by isothermal titration calorimetry studies of substrate binding
    • Schröder-Tittmann, K., et al. Alternating sites reactivity is a common feature of thiamin diphosphate-dependent enzymes as evidenced by isothermal titration calorimetry studies of substrate binding. Biochemistry. 52. 2505-2507 (2013
    • (2013) Biochemistry , vol.52 , pp. 2505-2507
    • Schröder-Tittmann, K.1


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