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Volumn 17, Issue 4, 2010, Pages 519-527

A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; PROTEIN SH2; STAT5 PROTEIN;

EID: 77950502609     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1793     Document Type: Article
Times cited : (133)

References (58)
  • 1
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T. & Nash, P. Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452 (2003).
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 2
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • Rual, J.F. et al. Towards a proteome-scale map of the human protein-protein interaction network. Nature 437, 1173-1178 (2005).
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1
  • 3
    • 35848955168 scopus 로고    scopus 로고
    • Mass spectrometry-based functional proteomics: From molecular machines to protein networks
    • Kocher, T. & Superti-Furga, G. Mass spectrometry-based functional proteomics: from molecular machines to protein networks. Nat. Methods 4, 807-815 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 807-815
    • Kocher, T.1    Superti-Furga, G.2
  • 4
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • DOI 10.1038/nature04177, PII NATURE04177
    • Jones, R.B., Gordus, A., Krall, J.A. & MacBeath, G. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439, 168-174 (2006). (Pubitemid 43083134)
    • (2006) Nature , vol.439 , Issue.7073 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 5
    • 36249031068 scopus 로고    scopus 로고
    • Recognizing and exploiting differences between RNAi and small-molecule inhibitors
    • Weiss, W.A., Taylor, S.S. & Shokat, K.M. Recognizing and exploiting differences between RNAi and small-molecule inhibitors. Nat. Chem. Biol. 3, 739-744 (2007).
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 739-744
    • Weiss, W.A.1    Taylor, S.S.2    Shokat, K.M.3
  • 6
    • 43049088156 scopus 로고    scopus 로고
    • In vivo selection of intrabodies specifcally targeting protein-protein interactions: A general platform for an "undruggable" class of disease targets
    • Visintin, M., Melchionna, T., Cannistraci, I. & Cattaneo, A. In vivo selection of intrabodies specifcally targeting protein-protein interactions: a general platform for an "undruggable" class of disease targets. J. Biotechnol. 135, 1-15 (2008).
    • (2008) J. Biotechnol. , vol.135 , pp. 1-15
    • Visintin, M.1    Melchionna, T.2    Cannistraci, I.3    Cattaneo, A.4
  • 7
    • 0037693805 scopus 로고    scopus 로고
    • Diversity in the SH2 domain family phosphotyrosyl peptide binding site
    • Campbell, S.J. & Jackson, R.M. Diversity in the SH2 domain family phosphotyrosyl peptide binding site. Protein Eng. 16, 217-227 (2003).
    • (2003) Protein Eng. , vol.16 , pp. 217-227
    • Campbell, S.J.1    Jackson, R.M.2
  • 8
    • 0033527682 scopus 로고    scopus 로고
    • Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
    • Bradshaw, J.M., Mitaxov, V. & Waksman, G. Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase. J. Mol. Biol. 293, 971-985 (1999).
    • (1999) J. Mol. Biol. , vol.293 , pp. 971-985
    • Bradshaw, J.M.1    Mitaxov, V.2    Waksman, G.3
  • 9
    • 0034008847 scopus 로고    scopus 로고
    • Searching for specifcity in SH domains
    • Ladbury, J.E. & Arold, S. Searching for specifcity in SH domains. Chem. Biol. 7, R3-R8 (2000).
    • (2000) Chem. Biol. , vol.7
    • Ladbury, J.E.1    Arold, S.2
  • 10
    • 58149293958 scopus 로고    scopus 로고
    • Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: Implications for drug design
    • Taylor, J.D. et al. Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: implications for drug design. Proteins 73, 929-940 (2008).
    • (2008) Proteins , vol.73 , pp. 929-940
    • Taylor, J.D.1
  • 11
    • 61449194210 scopus 로고    scopus 로고
    • Binding specifcity of SH2 domains: Insight from free energy simulations
    • Gan, W. & Roux, B. Binding specifcity of SH2 domains: insight from free energy simulations. Proteins 74, 996-1007 (2009).
    • (2009) Proteins , vol.74 , pp. 996-1007
    • Gan, W.1    Roux, B.2
  • 12
    • 0035415663 scopus 로고    scopus 로고
    • SH2 domain inhibition: A problem solved?
    • Shakespeare, W.C. SH2 domain inhibition: a problem solved? Curr. Opin. Chem. Biol. 5, 409-415 (2001).
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 409-415
    • Shakespeare, W.C.1
  • 13
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • Machida, K. & Mayer, B.J. The SH2 domain: versatile signaling module and pharmaceutical target. Biochim. Biophys. Acta 1747, 1-25 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 1-25
    • MacHida, K.1    Mayer, B.J.2
  • 14
    • 0036408418 scopus 로고    scopus 로고
    • High-affnity Src-SH2 ligands which do not activate Tyr(527)- phosphorylated Src in an experimental in vivo system
    • Mandine, E. et al. High-affnity Src-SH2 ligands which do not activate Tyr(527)-phosphorylated Src in an experimental in vivo system. Biochem. Biophys. Res. Commun. 298, 185-192 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 185-192
    • Mandine, E.1
  • 15
    • 0035172977 scopus 로고    scopus 로고
    • Antagonists of the Src homology 2 (SH2) domains of Grb2, Src, Lck and ZAP-70
    • Garcia-Echeverria, C. Antagonists of the Src homology 2 (SH2) domains of Grb2, Src, Lck and ZAP-70. Curr. Med. Chem. 8, 1589-1604 (2001).
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1589-1604
    • Garcia-Echeverria, C.1
  • 17
    • 0032509129 scopus 로고    scopus 로고
    • The fbronectin type III domain as a scaffold for novel binding proteins
    • Koide, A., Bailey, C.W., Huang, X. & Koide, S. The fbronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 284, 1141-1151 (1998).
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 18
    • 0037022351 scopus 로고    scopus 로고
    • Probing protein conformational changes in living cells by using designer binding proteins: Application to the estrogen receptor
    • Koide, A., Abbatiello, S., Rothgery, L. & Koide, S. Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor. Proc. Natl. Acad. Sci. USA 99, 1253-1258 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1253-1258
    • Koide, A.1    Abbatiello, S.2    Rothgery, L.3    Koide, S.4
  • 19
    • 47049105753 scopus 로고    scopus 로고
    • A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces
    • Gilbreth, R.N., Esaki, K., Koide, A., Sidhu, S.S. & Koide, S. A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces. J. Mol. Biol. 381, 407-418 (2008).
    • (2008) J. Mol. Biol. , vol.381 , pp. 407-418
    • Gilbreth, R.N.1    Esaki, K.2    Koide, A.3    Sidhu, S.S.4    Koide, S.5
  • 20
    • 0025117392 scopus 로고
    • Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome
    • Daley, G.Q., Van Etten, R.A. & Baltimore, D. Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247, 824-830 (1990).
    • (1990) Science , vol.247 , pp. 824-830
    • Daley, G.Q.1    Van Etten, R.A.2    Baltimore, D.3
  • 21
    • 33644871166 scopus 로고    scopus 로고
    • Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase
    • Nagar, B. et al. Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase. Mol. Cell 21, 787-798 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 787-798
    • Nagar, B.1
  • 22
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr-Abl tyrosine kinases
    • DOI 10.1038/nrm1280
    • Hantschel, O. & Superti-Furga, G. Regulation of the c-Abl and Bcr-Abl tyrosine kinases. Nat. Rev. Mol. Cell Biol. 5, 33-44 (2004). (Pubitemid 38089839)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.1 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 23
    • 50249132542 scopus 로고    scopus 로고
    • Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation
    • Filippakopoulos, P. et al. Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation. Cell 134, 793-803 (2008).
    • (2008) Cell , vol.134 , pp. 793-803
    • Filippakopoulos, P.1
  • 24
    • 48749101428 scopus 로고    scopus 로고
    • Picomolar affnity fbronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffing
    • Hackel, B.J., Kapila, A. & Wittrup, K.D. Picomolar affnity fbronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffing. J. Mol. Biol. 381, 1238-1252 (2008).
    • (2008) J. Mol. Biol. , vol.381 , pp. 1238-1252
    • Hackel, B.J.1    Kapila, A.2    Wittrup, K.D.3
  • 26
    • 37449002863 scopus 로고    scopus 로고
    • Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation
    • Porter, C.J. et al. Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation. BMC Struct. Biol. 7, 58 (2007).
    • (2007) BMC Struct. Biol. , vol.7 , pp. 58
    • Porter, C.J.1
  • 27
    • 33751211249 scopus 로고    scopus 로고
    • An effcient tandem affnity purifcation procedure for interaction proteomics in mammalian cells
    • Burckstummer, T. et al. An effcient tandem affnity purifcation procedure for interaction proteomics in mammalian cells. Nat. Methods 3, 1013-1019 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 1013-1019
    • Burckstummer, T.1
  • 28
    • 66149095910 scopus 로고    scopus 로고
    • Charting the molecular network of the drug target Bcr-Abl
    • Brehme, M. et al. Charting the molecular network of the drug target Bcr-Abl. Proc. Natl. Acad. Sci. USA 106, 7414-7419 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7414-7419
    • Brehme, M.1
  • 29
    • 4644303503 scopus 로고    scopus 로고
    • Interchangeable functions of Arabidopsis PIROGI and the human WAVE complex subunit SRA1 during leaf epidermal development
    • Basu, D., El-Assal Sel, D., Le, J., Mallery, E.L. & Szymanski, D.B. Interchangeable functions of Arabidopsis PIROGI and the human WAVE complex subunit SRA1 during leaf epidermal development. Development 131, 4345-4355 (2004).
    • (2004) Development , vol.131 , pp. 4345-4355
    • Basu, D.1    El-Assal Sel Le D, J.2    Mallery, E.L.3    Szymanski, D.B.4
  • 30
    • 33947219266 scopus 로고    scopus 로고
    • Large-scale mapping of human protein-protein interactions by mass spectrometry
    • Ewing, R.M. et al. Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol. Syst. Biol. 3, 89 (2007).
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 89
    • Ewing, R.M.1
  • 31
    • 34250379613 scopus 로고    scopus 로고
    • Systematic identifcation of SH3 domain-mediated human protein-protein interactions by peptide array target screening
    • Wu, C. et al. Systematic identifcation of SH3 domain-mediated human protein-protein interactions by peptide array target screening. Proteomics 7, 1775-1785 (2007).
    • (2007) Proteomics , vol.7 , pp. 1775-1785
    • Wu, C.1
  • 32
    • 47549101393 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is not essential for Bcr-Abl-mediated transformation of lymphoid or myeloid cells
    • MacPartlin, M., Smith, A.M., Druker, B.J., Honigberg, L.A. & Deininger, M.W. Bruton's tyrosine kinase is not essential for Bcr-Abl-mediated transformation of lymphoid or myeloid cells. Leukemia 22, 1354-1360 (2008).
    • (2008) Leukemia , vol.22 , pp. 1354-1360
    • MacPartlin, M.1    Smith, A.M.2    Druker, B.J.3    Honigberg, L.A.4    Deininger, M.W.5
  • 33
    • 0027368352 scopus 로고
    • BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein
    • Pendergast, A.M. et al. BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Cell 75, 175-185 (1993).
    • (1993) Cell , vol.75 , pp. 175-185
    • Pendergast, A.M.1
  • 34
    • 51249099557 scopus 로고    scopus 로고
    • The chemokine interleukin-8 and the surface activation protein CD69 are markers for Bcr-Abl activity in chronic myeloid leukemia
    • Hantschel, O. et al. The chemokine interleukin-8 and the surface activation protein CD69 are markers for Bcr-Abl activity in chronic myeloid leukemia. Mol. Oncol. 2, 272-281 (2008).
    • (2008) Mol. Oncol. , vol.2 , pp. 272-281
    • Hantschel, O.1
  • 35
    • 27944452734 scopus 로고    scopus 로고
    • HCaRG increases renal cell migration by a TGF-α autocrine loop mechanism
    • El Hader, C. et al. HCaRG increases renal cell migration by a TGF-α autocrine loop mechanism. Am. J. Physiol. Renal Physiol. 289, F1273-F1280 (2005).
    • (2005) Am. J. Physiol. Renal Physiol. , vol.289
    • El Hader, C.1
  • 36
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar, B. et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112, 859-871 (2003).
    • (2003) Cell , vol.112 , pp. 859-871
    • Nagar, B.1
  • 37
    • 0026669472 scopus 로고
    • Three-dimensional solution structure of the src homology 2 domain of c-abl
    • Overduin, M., Rios, C.B., Mayer, B.J., Baltimore, D. & Cowburn, D. Three-dimensional solution structure of the src homology 2 domain of c-abl. Cell 70, 697-704 (1992).
    • (1992) Cell , vol.70 , pp. 697-704
    • Overduin, M.1    Rios, C.B.2    Mayer, B.J.3    Baltimore, D.4    Cowburn, D.5
  • 38
    • 0027409064 scopus 로고
    • Binding of a high affnity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D. & Kuriyan, J. Binding of a high affnity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790 (1993).
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 39
    • 0027502504 scopus 로고
    • Recognition of a high-affnity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
    • Eck, M.J., Shoelson, S.E. & Harrison, S.C. Recognition of a high-affnity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature 362, 87-91 (1993).
    • (1993) Nature , vol.362 , pp. 87-91
    • Eck, M.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 40
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M.C. & Colman, P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 41
    • 0344626925 scopus 로고    scopus 로고
    • A myristoyl/phosphotyrosine switch regulates c-Abl
    • Hantschel, O. et al. A myristoyl/phosphotyrosine switch regulates c-Abl. Cell 112, 845-857 (2003).
    • (2003) Cell , vol.112 , pp. 845-857
    • Hantschel, O.1
  • 42
    • 34548379387 scopus 로고    scopus 로고
    • Processive phosphorylation: Mechanism and biological importance
    • Patwardhan, P. & Miller, W.T. Processive phosphorylation: mechanism and biological importance. Cell. Signal. 19, 2218-2226 (2007).
    • (2007) Cell. Signal. , vol.19 , pp. 2218-2226
    • Patwardhan, P.1    Miller, W.T.2
  • 43
    • 0035890917 scopus 로고    scopus 로고
    • Multiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillin
    • Schaller, M.D. & Schaefer, E.M. Multiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillin. Biochem. J. 360, 57-66 (2001).
    • (2001) Biochem. J. , vol.360 , pp. 57-66
    • Schaller, M.D.1    Schaefer, E.M.2
  • 44
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer, B.J., Hirai, H. & Sakai, R. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr. Biol. 5, 296-305 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 45
    • 33745057158 scopus 로고    scopus 로고
    • STAT5 signaling is required for the effcient induction and maintenance of CML in mice
    • Ye, D., Wolff, N., Li, L., Zhang, S. & Ilaria, R.L. Jr. STAT5 signaling is required for the effcient induction and maintenance of CML in mice. Blood 107, 4917-4925 (2006).
    • (2006) Blood , vol.107 , pp. 4917-4925
    • Ye, D.1    Wolff, N.2    Li, L.3    Zhang, S.4    Ilaria Jr., R.L.5
  • 46
    • 0033583530 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription (STAT)5 activation by BCR/ABL is dependent on intact Src homology (SH)3 and SH2 domains of BCR/ABL and is required for leukemogenesis
    • Nieborowska-Skorska, M. et al. Signal transducer and activator of transcription (STAT)5 activation by BCR/ABL is dependent on intact Src homology (SH)3 and SH2 domains of BCR/ABL and is required for leukemogenesis. J. Exp. Med. 189, 1229-1242 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1229-1242
    • Nieborowska-Skorska, M.1
  • 47
    • 0033579856 scopus 로고    scopus 로고
    • Highly potent inhibitors of the Grb2-SH2 domain
    • Schoepfer, J. et al. Highly potent inhibitors of the Grb2-SH2 domain. Bioorg. Med. Chem. Lett. 9, 221-226 (1999).
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 221-226
    • Schoepfer, J.1
  • 48
    • 0033212986 scopus 로고    scopus 로고
    • Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition
    • Poy, F. et al. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol. Cell 4, 555-561 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 555-561
    • Poy, F.1
  • 49
    • 68049110634 scopus 로고    scopus 로고
    • The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site
    • Bae, J.H. et al. The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell 138, 514-524 (2009).
    • (2009) Cell , vol.138 , pp. 514-524
    • Bae, J.H.1
  • 50
    • 34848848421 scopus 로고    scopus 로고
    • High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries
    • Fellouse, F.A. et al. High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries. J. Mol. Biol. 373, 924-940 (2007).
    • (2007) J. Mol. Biol. , vol.373 , pp. 924-940
    • Fellouse, F.A.1
  • 52
    • 18044377989 scopus 로고    scopus 로고
    • Molecular recognition by a binary code
    • Fellouse, F.A. et al. Molecular recognition by a binary code. J. Mol. Biol. 348, 1153-1162 (2005).
    • (2005) J. Mol. Biol. , vol.348 , pp. 1153-1162
    • Fellouse, F.A.1
  • 53
    • 33644783935 scopus 로고    scopus 로고
    • Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code
    • Fellouse, F.A., Barthelemy, P.A., Kelley, R.F. & Sidhu, S.S. Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code. J. Mol. Biol. 357, 100-114 (2006).
    • (2006) J. Mol. Biol. , vol.357 , pp. 100-114
    • Fellouse, F.A.1    Barthelemy, P.A.2    Kelley, R.F.3    Sidhu, S.S.4
  • 54
  • 55
    • 0026601293 scopus 로고
    • Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo
    • Mayer, B.J., Jackson, P.K., Van Etten, R.A. & Baltimore, D. Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol. Cell. Biol. 12, 609-618 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    Van Etten, R.A.3    Baltimore, D.4
  • 57
    • 34547457742 scopus 로고    scopus 로고
    • Antibody mimics based on the scaffold of the fbronectin type III domain
    • Koide, A. & Koide, S. Monobodies: antibody mimics based on the scaffold of the fbronectin type III domain. Methods Mol. Biol. 352, 95-109 (2007).
    • (2007) Methods Mol. Biol. , vol.352 , pp. 95-109
    • Koide, A.1    Monobodies, K.S.2
  • 58
    • 34250641161 scopus 로고    scopus 로고
    • High-throughput phosphotyrosine profling using SH2 domains
    • Machida, K. et al. High-throughput phosphotyrosine profling using SH2 domains. Mol. Cell 26, 899-915 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 899-915
    • MacHida, K.1


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