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Volumn 109, Issue 34, 2012, Pages

Structural and functional analysis of phosphorylation-specific binders of the kinase ERK from designed ankyrin repeat protein libraries

Author keywords

Intrabodies; X ray crystallography

Indexed keywords

ANKYRIN; GREEN FLUORESCENT PROTEIN; LUCIFERASE; MITOGEN ACTIVATED PROTEIN KINASE 1;

EID: 84865302440     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205399109     Document Type: Article
Times cited : (86)

References (54)
  • 1
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometrybased proteomics
    • Choudhary C, Mann M (2010) Decoding signalling networks by mass spectrometrybased proteomics. Nat Rev Mol Cell Biol 11:427-439.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 2
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen ON (2006) Interpreting the protein language using proteomics. Nat Rev Mol Cell Biol 7:391-403.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 391-403
    • Jensen, O.N.1
  • 3
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • Witze ES, Old WM, Resing KA, Ahn NG (2007) Mapping protein post-translational modifications with mass spectrometry. Nat Methods 4:798-806.
    • (2007) Nat Methods , vol.4 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 4
    • 33845921119 scopus 로고    scopus 로고
    • ProteomeBinders: Planning a European resource of affinity reagents for analysis of the human proteome
    • Taussig MJ, et al. (2007) ProteomeBinders: Planning a European resource of affinity reagents for analysis of the human proteome. Nat Methods 4:13-17.
    • (2007) Nat Methods , vol.4 , pp. 13-17
    • Taussig, M.J.1
  • 5
    • 67651161904 scopus 로고    scopus 로고
    • Design of high-density antibody microarrays for disease proteomics: Key technological issues
    • Borrebaeck CA, Wingren C (2009) Design of high-density antibody microarrays for disease proteomics: Key technological issues. J Proteomics 72:928-935.
    • (2009) J Proteomics , vol.72 , pp. 928-935
    • Borrebaeck, C.A.1    Wingren, C.2
  • 6
    • 0036306954 scopus 로고    scopus 로고
    • Knowledge-based design of reagentless fluorescent biosensors from recombinant antibodies
    • RenardM, et al. (2002) Knowledge-based design of reagentless fluorescent biosensors from recombinant antibodies. J Mol Biol 318:429-442.
    • (2002) J Mol Biol , vol.318 , pp. 429-442
  • 7
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J, Plückthun A (1997) In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA 94:4937-4942.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 8
    • 63449121086 scopus 로고    scopus 로고
    • Generation and validation of affinity reagents on a proteome-wide level
    • Uhlén M, Hober S (2009) Generation and validation of affinity reagents on a proteome-wide level. J Mol Recognit 22:57-64.
    • (2009) J Mol Recognit , vol.22 , pp. 57-64
    • Uhlén, M.1    Hober, S.2
  • 9
    • 9344223986 scopus 로고    scopus 로고
    • Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library
    • Vaughan TJ, et al. (1996) Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library. Nat Biotechnol 14:309-314.
    • (1996) Nat Biotechnol , vol.14 , pp. 309-314
    • Vaughan, T.J.1
  • 10
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik A, et al. (2000) Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J Mol Biol 296:57-86.
    • (2000) J Mol Biol , vol.296 , pp. 57-86
    • Knappik, A.1
  • 11
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz HK, Amstutz P, Plückthun A (2005) Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 23:1257-1268.
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Plückthun, A.3
  • 12
    • 2342624119 scopus 로고    scopus 로고
    • High-affinity binders selected from designed ankyrin repeat protein libraries
    • Binz HK, et al. (2004) High-affinity binders selected from designed ankyrin repeat protein libraries. Nat Biotechnol 22:575-582.
    • (2004) Nat Biotechnol , vol.22 , pp. 575-582
    • Binz, H.K.1
  • 13
    • 80054856259 scopus 로고    scopus 로고
    • DARPins and other repeat protein scaffolds: Advances in engineering and applications
    • Boersma YL, Plückthun A (2011) DARPins and other repeat protein scaffolds: Advances in engineering and applications. Curr Opin Biotechnol 22:849-857.
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 849-857
    • Boersma, Y.L.1    Plückthun, A.2
  • 14
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz HK, Stumpp MT, Forrer P, Amstutz P, Plückthun A (2003) Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J Mol Biol 332:489-503.
    • (2003) J Mol Biol , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plückthun, A.5
  • 15
    • 38049063892 scopus 로고    scopus 로고
    • Folding and unfolding mechanismof highly stable full-consensus ankyrin repeat proteins
    • Wetzel SK, Settanni G, Kenig M, Binz HK, Plückthun A (2008) Folding and unfolding mechanismof highly stable full-consensus ankyrin repeat proteins. JMol Biol 376:241-257.
    • (2008) JMol Biol , vol.376 , pp. 241-257
    • Wetzel, S.K.1    Settanni, G.2    Kenig, M.3    Binz, H.K.4    Plückthun, A.5
  • 16
    • 34548445097 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB activation with designed ankyrin-repeat proteins targeting the ubiquitin-binding/oligomerization domain of NEMO
    • Wyler E, et al. (2007) Inhibition of NF-kappaB activation with designed ankyrin-repeat proteins targeting the ubiquitin-binding/oligomerization domain of NEMO. Protein Sci 16:2013-2022.
    • (2007) Protein Sci , vol.16 , pp. 2013-2022
    • Wyler, E.1
  • 17
    • 33845993299 scopus 로고    scopus 로고
    • Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening
    • Kawe M, Forrer P, Amstutz P, Plückthun A (2006) Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening. J Biol Chem 281:40252-40263.
    • (2006) J Biol Chem , vol.281 , pp. 40252-40263
    • Kawe, M.1    Forrer, P.2    Amstutz, P.3    Plückthun, A.4
  • 18
    • 21744440783 scopus 로고    scopus 로고
    • Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins
    • Amstutz P, et al. (2005) Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins. J Biol Chem 280:24715-24722.
    • (2005) J Biol Chem , vol.280 , pp. 24715-24722
    • Amstutz, P.1
  • 19
    • 33646267001 scopus 로고    scopus 로고
    • Rapid selection of specific MAP kinase-binders from designed ankyrin repeat protein libraries
    • Amstutz P, Koch H, Binz HK, Deuber SA, Plückthun A (2006) Rapid selection of specific MAP kinase-binders from designed ankyrin repeat protein libraries. Protein Eng Des Sel 19:219-229.
    • (2006) Protein Eng des Sel , vol.19 , pp. 219-229
    • Amstutz, P.1    Koch, H.2    Binz, H.K.3    Deuber, S.A.4    Plückthun, A.5
  • 20
    • 51349091340 scopus 로고    scopus 로고
    • Efficient selection of DARPins with subnanomolar affinities using SRP phage display
    • Steiner D, Forrer P, Plückthun A (2008) Efficient selection of DARPins with subnanomolar affinities using SRP phage display. J Mol Biol 382:1211-1227.
    • (2008) J Mol Biol , vol.382 , pp. 1211-1227
    • Steiner, D.1    Forrer, P.2    Plückthun, A.3
  • 21
    • 0035413618 scopus 로고    scopus 로고
    • MAP kinases
    • Chen Z, et al. (2001) MAP kinases. Chem Rev 101:2449-2476.
    • (2001) Chem Rev , vol.101 , pp. 2449-2476
    • Chen, Z.1
  • 22
    • 41849088475 scopus 로고    scopus 로고
    • The roles of MAPKs in disease
    • Lawrence MC, et al. (2008) The roles of MAPKs in disease. Cell Res 18:436-442.
    • (2008) Cell Res , vol.18 , pp. 436-442
    • Lawrence, M.C.1
  • 23
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, et al. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1
  • 24
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90:859-869.
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 25
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ (1994) Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367:704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 26
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 27
    • 33747050998 scopus 로고    scopus 로고
    • Novel, isotype-specific sensors for protein kinase A subunit interaction based on bioluminescence resonance energy transfer (BRET)
    • Prinz A, Diskar M, Erlbruch A, Herberg FW (2006) Novel, isotype-specific sensors for protein kinase A subunit interaction based on bioluminescence resonance energy transfer (BRET). Cell Signal 18:1616-1625.
    • (2006) Cell Signal , vol.18 , pp. 1616-1625
    • Prinz, A.1    Diskar, M.2    Erlbruch, A.3    Herberg, F.W.4
  • 28
    • 0031956424 scopus 로고    scopus 로고
    • PD98059 is an equipotent antagonist of the aryl hydrocarbon receptor and inhibitor of mitogen-activated protein kinase kinase
    • Reiners JJ, Jr., Lee JY, Clift RE, Dudley DT, Myrand SP (1998) PD98059 is an equipotent antagonist of the aryl hydrocarbon receptor and inhibitor of mitogen-activated protein kinase kinase. Mol Pharmacol 53:438-445.
    • (1998) Mol Pharmacol , vol.53 , pp. 438-445
    • Reiners Jr., J.J.1    Lee, J.Y.2    Clift, R.E.3    Dudley, D.T.4    Myrand, S.P.5
  • 29
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches
    • Seo J, Lee KJ (2004) Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches. J Biochem Mol Biol 37:35-44.
    • (2004) J Biochem Mol Biol , vol.37 , pp. 35-44
    • Seo, J.1    Lee, K.J.2
  • 30
    • 84862014201 scopus 로고    scopus 로고
    • Designed Ankyrin Repeat Proteins (DARPins) as novel isoformspecific intracellular inhibitors of c-Jun N-terminal kinases
    • 10.1021/cb3001167
    • Parizek P, et al. (2012) Designed Ankyrin Repeat Proteins (DARPins) as novel isoformspecific intracellular inhibitors of c-Jun N-terminal kinases. ACS Chem Biol, 10.1021/cb3001167.
    • (2012) ACS Chem Biol
    • Parizek, P.1
  • 31
    • 33750350832 scopus 로고    scopus 로고
    • Expression and characterization of MAP kinases in bacteria
    • Heise CJ, Cobb MH (2006) Expression and characterization of MAP kinases in bacteria. Methods 40:209-212.
    • (2006) Methods , vol.40 , pp. 209-212
    • Heise, C.J.1    Cobb, M.H.2
  • 32
    • 0035056375 scopus 로고    scopus 로고
    • Bacterial expression of activated mitogen-activated protein kinases
    • Wilsbacher JL, Cobb MH (2001) Bacterial expression of activated mitogen-activated protein kinases. Methods Enzymol 332:387-400.
    • (2001) Methods Enzymol , vol.332 , pp. 387-400
    • Wilsbacher, J.L.1    Cobb, M.H.2
  • 33
    • 0029998541 scopus 로고    scopus 로고
    • Crystal structure of p38 mitogen-activated protein kinase
    • Wilson KP, et al. (1996) Crystal structure of p38 mitogen-activated protein kinase. J Biol Chem 271:27696-27700.
    • (1996) J Biol Chem , vol.271 , pp. 27696-27700
    • Wilson, Kp.1
  • 34
    • 0032528998 scopus 로고    scopus 로고
    • Crystal structure of JNK3: A kinase implicated in neuronal apoptosis
    • Xie X, et al. (1998) Crystal structure of JNK3: A kinase implicated in neuronal apoptosis. Structure 6:983-991.
    • (1998) Structure , vol.6 , pp. 983-991
    • Xie, X.1
  • 35
    • 23444448571 scopus 로고    scopus 로고
    • Allosteric inhibition of aminoglycoside phosphotransferase by a designed ankyrin repeat protein
    • Kohl A, et al. (2005) Allosteric inhibition of aminoglycoside phosphotransferase by a designed ankyrin repeat protein. Structure 13:1131-1141.
    • (2005) Structure , vol.13 , pp. 1131-1141
    • Kohl, A.1
  • 36
    • 41949142073 scopus 로고    scopus 로고
    • Structure of wild-type Plk-1 kinase domain in complex with a selective DARPin
    • Bandeiras TM, et al. (2008) Structure of wild-type Plk-1 kinase domain in complex with a selective DARPin. Acta Crystallogr D Biol Crystallogr 64:339-353.
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , pp. 339-353
    • Bandeiras, T.M.1
  • 37
    • 34248549239 scopus 로고    scopus 로고
    • A designed ankyrin repeat protein evolved to picomolar affinity to Her2
    • Zahnd C, et al. (2007) A designed ankyrin repeat protein evolved to picomolar affinity to Her2. J Mol Biol 369:1015-1028.
    • (2007) J Mol Biol , vol.369 , pp. 1015-1028
    • Zahnd, C.1
  • 38
    • 33746683073 scopus 로고    scopus 로고
    • Applications of antibody array platforms
    • Haab BB (2006) Applications of antibody array platforms. Curr Opin Biotechnol 17:415-421.
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 415-421
    • Haab, B.B.1
  • 39
    • 34247853389 scopus 로고    scopus 로고
    • Inhibition of caspase-2 by a designed ankyrin repeat protein: Specificity, structure, and inhibition mechanism
    • Schweizer A, et al. (2007) Inhibition of caspase-2 by a designed ankyrin repeat protein: Specificity, structure, and inhibition mechanism. Structure 15:625-636.
    • (2007) Structure , vol.15 , pp. 625-636
    • Schweizer, A.1
  • 40
    • 0037177819 scopus 로고    scopus 로고
    • Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
    • Robinson FL, Whitehurst AW, Raman M, Cobb MH (2002) Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1. J Biol Chem 277:14844-14852.
    • (2002) J Biol Chem , vol.277 , pp. 14844-14852
    • Robinson, F.L.1    Whitehurst, A.W.2    Raman, M.3    Cobb, M.H.4
  • 41
    • 19444375104 scopus 로고    scopus 로고
    • DNA-based therapeutics and DNA delivery systems: A comprehensive review
    • Patil SD, Rhodes DG, Burgess DJ (2005) DNA-based therapeutics and DNA delivery systems: A comprehensive review. AAPS J 7:E61-E77.
    • (2005) AAPS J , vol.7
    • Patil, S.D.1    Rhodes, D.G.2    Burgess, D.J.3
  • 42
    • 79959379424 scopus 로고    scopus 로고
    • A biosensor generated via high-throughput screening quantifies cell edge Src dynamics
    • Gulyani A, et al. (2011) A biosensor generated via high-throughput screening quantifies cell edge Src dynamics. Nat Chem Biol 7:437-444.
    • (2011) Nat Chem Biol , vol.7 , pp. 437-444
    • Gulyani, A.1
  • 44
    • 0031669205 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay for measurement of JNK, ERK, and p38 kinase activities
    • Forrer P, Tamaskovic R, Jaussi R (1998) Enzyme-linked immunosorbent assay for measurement of JNK, ERK, and p38 kinase activities. Biol Chem 379:1101-1111.
    • (1998) Biol Chem , vol.379 , pp. 1101-1111
    • Forrer, P.1    Tamaskovic, R.2    Jaussi, R.3
  • 45
    • 77956292486 scopus 로고    scopus 로고
    • Designed ankyrin repeat proteins: A novel tool for testing epidermal growth factor receptor 2 expression in breast cancer
    • Theurillat JP, et al. (2010) Designed ankyrin repeat proteins: A novel tool for testing epidermal growth factor receptor 2 expression in breast cancer. Mod Pathol 23:1289-1297.
    • (2010) Mod Pathol , vol.23 , pp. 1289-1297
    • Theurillat, J.P.1
  • 46
    • 79952278990 scopus 로고    scopus 로고
    • Ribosome display: A technology for selecting and evolving proteins from large libraries
    • Dreier B, Plückthun A (2011) Ribosome display: A technology for selecting and evolving proteins from large libraries. Methods Mol Biol 687:283-306.
    • (2011) Methods Mol Biol , vol.687 , pp. 283-306
    • Dreier, B.1    Plückthun, A.2
  • 47
    • 33845939857 scopus 로고    scopus 로고
    • Selection and characterization of Her2 binding-designed ankyrin repeat proteins
    • Zahnd C, Pecorari F, Straumann N, Wyler E, Plückthun A (2006) Selection and characterization of Her2 binding-designed ankyrin repeat proteins. J Biol Chem 281:35167-35175.
    • (2006) J Biol Chem , vol.281 , pp. 35167-35175
    • Zahnd, C.1    Pecorari, F.2    Straumann, N.3    Wyler, E.4    Plückthun, A.5
  • 48
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26:795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 49
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40:658-674.
    • (2007) J Appl Cryst , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 50
    • 0037452697 scopus 로고    scopus 로고
    • Designed to be stable: Crystal structure of a consensus ankyrin repeat protein
    • Kohl A, et al. (2003) Designed to be stable: Crystal structure of a consensus ankyrin repeat protein. Proc Natl Acad Sci USA 100:1700-1705.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1700-1705
    • Kohl, A.1
  • 51
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58:1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 52
  • 53
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372:774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 54
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67:235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1


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