메뉴 건너뛰기




Volumn 3, Issue 3, 2011, Pages 271-282

A combinatorial method to enable detailed investigation of protein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

AB INITIO CALCULATION; ARTICLE; COMBINATORIAL CHEMISTRY; CONTROLLED STUDY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION;

EID: 79953240780     PISSN: 17568919     EISSN: None     Source Type: Journal    
DOI: 10.4155/fmc.10.289     Document Type: Article
Times cited : (5)

References (41)
  • 1
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • DOI 10.1126/science.1083653
    • Pawson T, Nash P. Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452 (2003). The core regions in protein-protein interaction are discrete and localized structures. (Pubitemid 36444318)
    • (2003) Science , vol.300 , Issue.5618 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 2
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009 (2007). Discussion of the potential benefits, obstacles to progression, and the state of the art in drugging protein-protein interfaces. (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 3
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sørensen HP, Mortensen KK. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell Fact. 4, 1-8 (2005).
    • (2005) Microb. Cell Fact. , vol.4 , pp. 1-8
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 4
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F, Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22, 1399-1408 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 6
    • 77949270274 scopus 로고    scopus 로고
    • A-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel
    • Bhushan S, Gartmann M, Halic M et al. a-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel. Nat. Struct. Mol. Biol. 17, 313-317 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 313-317
    • Bhushan, S.1    Gartmann, M.2    Halic, M.3
  • 7
    • 77950562866 scopus 로고    scopus 로고
    • A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes
    • Koplin A, Preissler S, Ilina Y et al. A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J. Cell Biol. 189, 57-68 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 57-68
    • Koplin, A.1    Preissler, S.2    Ilina, Y.3
  • 8
    • 38449092312 scopus 로고    scopus 로고
    • Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
    • De Marco A. Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat. Protocols 2, 2632-2629 (2007).
    • (2007) Nat. Protocols , vol.2 , pp. 2632-2629
    • De Marco, A.1
  • 9
    • 0030272553 scopus 로고    scopus 로고
    • Optimization of heterologous protein production in Escherichia coli
    • DOI 10.1016/S0958-1669(96)80051-6
    • Weickert MJ, Doherty DH, Best EA, Olins PO. Optimization of heterologous protein production in Escherichia coli. Curr. Opin. Biotechnol. 7, 494-499 (1996). (Pubitemid 26381750)
    • (1996) Current Opinion in Biotechnology , vol.7 , Issue.5 , pp. 494-499
    • Weickert, M.J.1    Doherty, D.H.2    Best, E.A.3    Olins, P.O.4
  • 10
    • 33645471817 scopus 로고    scopus 로고
    • An automatable screen for the rapid identification of proteins amenable to refolding
    • Cowieson NP, Wensley B, Listwan P, Hume DA, Kobe B, Martin JL. An automatable screen for the rapid identification of proteins amenable to refolding. Proteomics 6, 1750-1757 (2006).
    • (2006) Proteomics , vol.6 , pp. 1750-1757
    • Cowieson, N.P.1    Wensley, B.2    Listwan, P.3    Hume, D.A.4    Kobe, B.5    Martin, J.L.6
  • 11
    • 31344474305 scopus 로고    scopus 로고
    • Strategies for protein coexpression in Escherichia coli
    • DOI 10.1038/nmeth0106-55, PII N010655
    • Tolia NH, Joshua-Tor L. Strategies for protein coexpression in Escherichia coli. Nat. Methods 3, 55-64 (2006). (Pubitemid 43135350)
    • (2006) Nature Methods , vol.3 , Issue.1 , pp. 55-64
    • Tolia, N.H.1    Joshua-Tor, L.2
  • 12
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: From purified protein to diffraction-quality crystal
    • DOI 10.1038/nmeth.f.203, PII NMETH.F.203
    • Chayen NE, Saridakis E. Protein crystallization: From purified protein to diffraction-quality crystal. Nat. Methods 5, 147-153(2008). (Pubitemid 351181740)
    • (2008) Nature Methods , vol.5 , Issue.2 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 13
    • 33644874674 scopus 로고    scopus 로고
    • Entropy and surface engineering in protein crystallization
    • Derewenda ZS, Vekilov PG. Entropy and surface engineering in protein crystallization. Acta Crystallogr. D 62, 116-124 (2006).
    • (2006) Acta Crystallogr. D , Issue.62 , pp. 116-124
    • Derewenda, Z.S.1    Vekilov, P.G.2
  • 14
    • 41949099222 scopus 로고    scopus 로고
    • Towards atomic resolution structural determination by single-particle cryo-electron microscopy
    • Zhou ZH. Towards atomic resolution structural determination by single-particle cryo-electron microscopy. Curr. Opin. Struct. Biol. 18, 218-228 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 218-228
    • Zhou, Z.H.1
  • 15
    • 0034535525 scopus 로고    scopus 로고
    • Structure determination of biological macromolecules in solution using nuclear magnetic resonance spectroscopy
    • Wider G. Structure determination of biological macromolecules in solution using nuclear magnetic resonance spectroscopy. BioTechniques 29, 1278-1294 (2000). (Pubitemid 32002636)
    • (2000) BioTechniques , vol.29 , Issue.6 , pp. 1278-1294
    • Wider, G.1
  • 16
    • 33846285730 scopus 로고    scopus 로고
    • Solution NMR of large molecules and assemblies
    • DOI 10.1021/bi0621314
    • Foster MP, McElroy CA, Amero CD. Solution NMR of large molecules and assemblies. Biochemistry 46, 331-340 (2007). (Pubitemid 46115942)
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 331-340
    • Foster, M.P.1    McElroy, C.A.2    Amero, C.D.3
  • 18
    • 0028103565 scopus 로고
    • Improving protein solubility through rationally designed amino acid replacements
    • Dale GE, Broger C, Langen H, D'arcy A, Stuber D. Improving protein solubility through rationally designed amino acid replacements. Protein Eng. 7, 933-939 (1994).
    • (1994) Protein Eng. , vol.7 , pp. 933-939
    • Dale, G.E.1    Broger, C.2    Langen, H.3    D'arcy, A.4    Stuber, D.5
  • 20
    • 33746023965 scopus 로고    scopus 로고
    • Screening for soluble expression constructs using cell-free protein synthesis
    • DOI 10.1016/j.ijbiomac.2006.02.027, PII S0141813006000821
    • Lamla T, Hoerer S, Bauer MMT. Screening for soluble expression constructs using cell-free protein synthesis. Int. J. Biol. Macromol. 39, 111-121 (2006). (Pubitemid 44066545)
    • (2006) International Journal of Biological Macromolecules , vol.39 , Issue.1-3 , pp. 111-121
    • Lamla, T.1    Hoerer, S.2    Bauer, M.M.T.3
  • 22
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • DOI 10.1093/emboj/cdg359
    • Nooren IMA, Thornton JM. Diversity of protein-protein interactions. EMBO J. 22, 3486-3492 (2003). Useful primer for appreciating the different types of protein-protein interaction. (Pubitemid 36898326)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 23
    • 3543148406 scopus 로고    scopus 로고
    • Expression screening, protein purification and NMR analysis of human protein domains for structural genomics
    • DOI 10.1023/B:JSFG.0000029200.66197.0c
    • Folkers GE, van Buuren BNM, Kaptein R. Expression screening, protein purification and NMR analysis of human protein domains for structural genomics. J. Struct. Funct. Genom. 5, 119-131 (2004). (Pubitemid 39030628)
    • (2004) Journal of Structural and Functional Genomics , vol.5 , Issue.1-2 , pp. 119-131
    • Folkers, G.E.1    Van Buuren, B.N.M.2    Kaptein, R.3
  • 24
    • 77954819629 scopus 로고    scopus 로고
    • Combinatorial domain hunting: Solving problems in protein expression
    • Concise introduction to the benefits of empirical discovery of functional protein truncations in medically important classes of proteins
    • Littler E. Combinatorial domain hunting: Solving problems in protein expression. Drug Discov. Today 15, 461-467 (2010). Concise introduction to the benefits of empirical discovery of functional protein truncations in medically important classes of proteins.
    • (2010) Drug Discov. Today , vol.15 , pp. 461-467
    • Littler, E.1
  • 26
    • 44349116166 scopus 로고    scopus 로고
    • Identification of soluble protein fragments by gene fragmentation and genetic selection
    • Dyson MR, Perera RL, Shadbolt SP et al. Identification of soluble protein fragments by gene fragmentation and genetic selection. Nucl. Acids Res. 36, E51 (2008).
    • (2008) Nucl. Acids Res. , vol.36
    • Dyson, M.R.1    Perera, R.L.2    Shadbolt, S.P.3
  • 28
    • 23644442058 scopus 로고    scopus 로고
    • Colony filtration blot: A new screening method for soluble protein expression in Escherichia coli
    • Cornvik T, Dahlroth SL, Magnusdottir A et al. Colony filtration blot: A new screening method for soluble protein expression in Escherichia coli. Nat. Methods 2, 507-509 (2006).
    • (2006) Nat. Methods , vol.2 , pp. 507-509
    • Cornvik, T.1    Dahlroth, S.L.2    Magnusdottir, A.3
  • 29
    • 23644461031 scopus 로고    scopus 로고
    • Soluble domains of telomerase reverse transcriptase identified by high-throughput screening
    • DOI 10.1110/ps.051532105
    • Jacobs SA, Podell ER, Wuttke DS, Cech TR. Soluble domains of telomerase reverse transcriptase identified by high-throughput screening. Protein Sci. 14, 2051-2058 (2005). (Pubitemid 41132370)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2051-2058
    • Jacobs, S.A.1    Podell, E.R.2    Wuttke, D.S.3    Cech, T.R.4
  • 30
    • 0344983825 scopus 로고    scopus 로고
    • A system using convertible vectors for screening soluble recombinant proteins produced in Escherichia coli from randomly fragmented cDNAs
    • DOI 10.1016/j.bbrc.2003.10.193
    • Nakayama M, Ohara O. A system using convertible vectors for screening soluble recombinant proteins produced in Escherichia coli from randomly fragmented cDNAs. Biochem. Biophys. Res. Commun. 312, 825-830 (2003). (Pubitemid 37468246)
    • (2003) Biochemical and Biophysical Research Communications , vol.312 , Issue.3 , pp. 825-830
    • Nakayama, M.1    Ohara, O.2
  • 31
    • 0034816151 scopus 로고    scopus 로고
    • Random PCR-based screening for soluble domains using green fluorescent protein
    • DOI 10.1006/bbrc.2000.4229
    • Kawasaki M, Inagaki F. Random PCR-based screening for soluble domains using green fluorescent protein. Biochem. Biophys. Res. Commun. 280, 842-844 (2001). (Pubitemid 32924507)
    • (2001) Biochemical and Biophysical Research Communications , vol.280 , Issue.3 , pp. 842-844
    • Kawasaki, M.1    Inagaki, F.2
  • 32
    • 35748981146 scopus 로고    scopus 로고
    • DNA fragmentation-based combinatorial approaches to soluble protein expression. Part I. Generating DNA fragment libraries
    • DOI 10.1016/j.drudis.2007.08.012, PII S1359644607003546
    • Prodromou C, Savva R, Driscoll PC. DNA Fragmentation-based combinatorial approaches to soluble protein expression. Part I: Generating DNA fragment libraries. Drug Discov. Today 12, 931-938 (2007). Detailed review of alternative techniques for the empirical discovery of truncation mutants of proteins. (Pubitemid 350052674)
    • (2007) Drug Discovery Today , vol.12 , Issue.21-22 , pp. 931-938
    • Prodromou, C.1    Savva, R.2    Driscoll, P.C.3
  • 33
    • 33644874198 scopus 로고    scopus 로고
    • Combinatorial library approaches for improving soluble protein expression in Escherichia coli
    • Overview of the technologies available for discovering empirical truncation mutants of proteins
    • Hart DJ, Tarendeau F. Combinatorial library approaches for improving soluble protein expression in Escherichia coli. Acta. Crystallogr. D 62, 19-26 (2006). Overview of the technologies available for discovering empirical truncation mutants of proteins.
    • (2006) Acta. Crystallogr. D , vol.62 , pp. 19-26
    • Hart, D.J.1    Tarendeau, F.2
  • 34
    • 35748961085 scopus 로고    scopus 로고
    • DNA fragmentation based combinatorial approaches to soluble protein expression. Part II: Library expression, screening and scale-up
    • DOI 10.1016/j.drudis.2007.08.016, PII S1359644607003698
    • Savva R, Prodromou C, Driscoll PC. DNA fragmentation based combinatorial approaches to soluble protein expression Part II: Library expression, screening and scale-up. Drug Discov. Today, 12, 939-947 (2007). Detailed review analyzing truncation mutants of proteins discovered using various methods. (Pubitemid 350052675)
    • (2007) Drug Discovery Today , vol.12 , Issue.21-22 , pp. 939-947
    • Savva, R.1    Prodromou, C.2    Driscoll, P.C.3
  • 35
    • 79953243756 scopus 로고    scopus 로고
    • Tackling difficult-to-express proteins for structural studies: A case study of using library methods
    • Presented at: Germany, 6-7 October
    • Meier C. Tackling difficult-to-express proteins for structural studies: A case study of using library methods. Presented at: PEGS Europe. Hannover, Germany, 6-7 October 2009.
    • (2009) PEGS Europe. Hannover
    • Meier, C.1
  • 40
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier FW. Protein production by auto-induction in high-density shaking cultures. Protein Express. Purif. 41, 207-234 (2005).
    • (2005) Protein Express. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 41
    • 72149125851 scopus 로고    scopus 로고
    • Characterization of celastrol to inhibit Hsp90 and Cdc37 interaction
    • Zhang T, Li Y, Yu Y, Zou P, Jiang Y, Sun D. Characterization of celastrol to inhibit Hsp90 and Cdc37 interaction. J. Biol. Chem. 284, 35381-35389 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 35381-35389
    • Zhang, T.1    Li, Y.2    Yu, Y.3    Zou, P.4    Jiang, Y.5    Sun, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.