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Volumn 3, Issue 3, 2002, Pages 177-186

Phosphotyrosine-binding domains in signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; AMINO ACID; GROWTH FACTOR RECEPTOR; PHOSPHOTYROSINE; PROTEIN; PROTEIN TYROSINE KINASE; LIGAND;

EID: 0036518996     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm759     Document Type: Review
Times cited : (304)

References (148)
  • 1
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J. & Cowburn, D. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26, 259-288 (1997). A thorough and detailed review of the structural basis for peptide binding by SH2, SH3 and PTB domains.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 3
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T. & Scott, J. D. Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080 (1997). A classic summary of modular signalling domains. Much of the information has not been presented in later reviews.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 5
    • 0023497801 scopus 로고
    • A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell
    • DeClue, J. E., Sadowski, I., Martin, G. S. & Pawson, T. A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell. Proc. Natl Acad. Sci. USA 84, 9064-9068 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 9064-9068
    • DeClue, J.E.1    Sadowski, I.2    Martin, G.S.3    Pawson, T.4
  • 6
    • 0021849381 scopus 로고
    • N-terminal deletions in Rous sarcoma virus p60src: Effects on tyrosine kinase and biological activities and on recombination in tissue culture with the cellular src gene
    • Cross, F. R., Garber, E. A. & Hanafusa, H. N-terminal deletions in Rous sarcoma virus p60src: effects on tyrosine kinase and biological activities and on recombination in tissue culture with the cellular src gene. Mol. Cell. Biol. 5, 2789-2795 (1985).
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2789-2795
    • Cross, F.R.1    Garber, E.A.2    Hanafusa, H.3
  • 7
    • 0023433991 scopus 로고
    • Identification of an amino terminal domain required for the transforming activity of the Rous sarcoma virus src protein
    • Raymond, V. W. & Parsons, J. T. Identification of an amino terminal domain required for the transforming activity of the Rous sarcoma virus src protein. Virology 160, 400-410 (1987).
    • (1987) Virology , vol.160 , pp. 400-410
    • Raymond, V.W.1    Parsons, J.T.2
  • 8
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J. C. et al. The sequence of the human genome. Science 291, 1304-1351 (2001).
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 9
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase Cγ1, GAP, and Src to activated growth factor receptors
    • Anderson, D. et al. Binding of SH2 domains of phospholipase Cγ1, GAP, and Src to activated growth factor receptors. Science 250, 979-982 (1990).
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1
  • 10
    • 0025298967 scopus 로고
    • gag-crk, to a broad range of phosphotyrosine-containing proteins
    • gag-crk, to a broad range of phosphotyrosine-containing proteins. Science 248, 1537-1539 (1990).
    • (1990) Science , vol.248 , pp. 1537-1539
    • Matsuda, M.1    Mayer, B.J.2    Fukui, Y.3    Hanafusa, H.4
  • 11
    • 0025978644 scopus 로고
    • Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins
    • Matsuda, M., Mayer, B. J. & Hanafusa, H. Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins. Mol. Cell. Biol. 11, 1607-1613 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1607-1613
    • Matsuda, M.1    Mayer, B.J.2    Hanafusa, H.3
  • 12
    • 0026059615 scopus 로고
    • The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity
    • Mayer, B. J., Jackson, P. K. & Baltimore, D. The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc. Natl Acad. Sci. USA 88, 627-631 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 627-631
    • Mayer, B.J.1    Jackson, P.K.2    Baltimore, D.3
  • 13
    • 0025119824 scopus 로고
    • Src homology region 2 domains direct protein-protein interactions in signal transduction
    • Moran, M. F. et al. Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl Acad. Sci. USA 87, 8622-8626 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8622-8626
    • Moran, M.F.1
  • 14
    • 0026069474 scopus 로고
    • Oncogenes and signal transduction
    • Cantley, L. C. et al. Oncogenes and signal transduction. Cell 64, 281-302 (1991). A unified view of signal transduction involving protein-tyrosine-kinase and lipid-kinase signalling that was remarkably prescient and is still timely.
    • (1991) Cell , vol.64 , pp. 281-302
    • Cantley, L.C.1
  • 15
    • 0025630506 scopus 로고
    • The tyrosine phosphorylated carboxy-terminus of the EGF receptor is a binding site for GAP and PLC-γ
    • Margolis, B. et al. The tyrosine phosphorylated carboxy-terminus of the EGF receptor is a binding site for GAP and PLC-γ. EMBO J. 9, 4375-4380 (1990).
    • (1990) EMBO J. , vol.9 , pp. 4375-4380
    • Margolis, B.1
  • 16
    • 0026085468 scopus 로고
    • A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine
    • Escobedo, J. A., Kaplan, D. R., Kavanaugh, W. M., Turck, C. W. & Williams, L. T. A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine. Mol. Cell. Biol. 11, 1125-1132 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1125-1132
    • Escobedo, J.A.1    Kaplan, D.R.2    Kavanaugh, W.M.3    Turck, C.W.4    Williams, L.T.5
  • 17
    • 0026652899 scopus 로고
    • Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
    • Fantl, W. J. et al. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell 69, 413-423 (1992). This was one of the first studies that showed that distinct phosphotyrosine sites on receptor tyrosine kinases recruit different signalling molecules.
    • (1992) Cell , vol.69 , pp. 413-423
    • Fantl, W.J.1
  • 18
    • 0026664293 scopus 로고
    • GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor β subunit
    • Kazlauskas, A., Kashishian, A., Cooper, J. A. & Valius, M. GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor β subunit. Mol. Cell. Biol. 12, 2534-2544 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2534-2544
    • Kazlauskas, A.1    Kashishian, A.2    Cooper, J.A.3    Valius, M.4
  • 19
    • 0027506762 scopus 로고
    • Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β-subunit and are required for binding of phospholipase Cγ and a 64-kilodalton protein, respectively
    • Valius, M., Bazenet, C. & Kazlauskas, A. Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β-subunit and are required for binding of phospholipase Cγ and a 64-kilodalton protein, respectively. Mol. Cell. Biol. 13, 133-143 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 133-143
    • Valius, M.1    Bazenet, C.2    Kazlauskas, A.3
  • 20
    • 0027179869 scopus 로고
    • The 64-kDa protein that associates with the platelet-derived growth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp
    • Kazlauskas, A., Feng, G. S., Pawson, T. & Valius, M. The 64-kDa protein that associates with the platelet-derived growth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp. Proc. Natl Acad. Sci. USA 90, 6939-6943 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6939-6943
    • Kazlauskas, A.1    Feng, G.S.2    Pawson, T.3    Valius, M.4
  • 21
    • 0026674977 scopus 로고
    • Identification of two C-terminal autophosphorylation sites in the PDGF β-receptor: Involvement in the interaction with phospholipase C-γ
    • Ronnstrand, L. et al. Identification of two C-terminal autophosphorylation sites in the PDGF β-receptor: involvement in the interaction with phospholipase C-γ. EMBO J. 11, 3911-3919 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3911-3919
    • Ronnstrand, L.1
  • 22
    • 0026793557 scopus 로고
    • Interactions of polyomavirus middle T with the SH2 domains of the pp85 subunit of phosphatidylinositol-3-kinase
    • Yoakim, M, et al. Interactions of polyomavirus middle T with the SH2 domains of the pp85 subunit of phosphatidylinositol-3-kinase. J. Virol. 66, 5485-5491 (1992).
    • (1992) J. Virol. , vol.66 , pp. 5485-5491
    • Yoakim, M.1
  • 23
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z. et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778 (1993). The first description of the use of oriented peptide-library screening to deduce phosphotyrosine motifs that are recognized by different SH2 domains.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 24
    • 0028351583 scopus 로고
    • Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav
    • Songyang, Z. et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell. Biol. 14, 2777-2785 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2777-2785
    • Songyang, Z.1
  • 25
    • 0027409064 scopus 로고
    • Binding of a high affinity 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 affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790 (1993). A classic study of structural biology that shows how SH2 domains bind to phosphotyrosine-containing peptides.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 26
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
    • Lee, C. H. et al. Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2, 423-438 (1994).
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.H.1
  • 27
    • 0029878266 scopus 로고    scopus 로고
    • Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes
    • Nolte, R. T., Eck, M. J., Schlessinger J., Shoelson, S. E. & Harrison, S. C. Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nature Struct. Biol. 3, 364-374 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 364-374
    • Nolte, R.T.1    Eck, M.J.2    Schlessinger, J.3    Shoelson, S.E.4    Harrison, S.C.5
  • 28
    • 0029967679 scopus 로고    scopus 로고
    • Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 Å and 1.8 Å resolution
    • Tong, L. et al. Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 Å and 1.8 Å resolution. J. Mol. Biol. 256, 601-610 (1996).
    • (1996) J. Mol. Biol. , vol.256 , pp. 601-610
    • Tong, L.1
  • 29
    • 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
  • 30
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signaling pathways
    • Yaffe, M. B. et al. A motif-based profile scanning approach for genome-wide prediction of signaling pathways. Nature Biotechnol. 19, 348-353 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 348-353
    • Yaffe, M.B.1
  • 31
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. Protein modules and signalling networks. Nature 373, 573-580 (1995).
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 32
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson, T. & Nash, P. Protein-protein interactions define specificity in signal transduction. Genes Dev. 14, 1027-1047 (2000). An excellent and up-to-date review of many modular domains and their roles in cell signalling and development.
    • (2000) Genes Dev. , vol.14 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 33
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    • Waksman, G. et al. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358, 646-653 (1992).
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1
  • 35
    • 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
  • 36
    • 0033586726 scopus 로고    scopus 로고
    • Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: Dissection of the phosphopeptide sequence specificity and coupling energetics
    • Bradshaw, J. M. & Waksman, G. Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics. Biochemistry 38, 5147-5154 (1999).
    • (1999) Biochemistry , vol.38 , pp. 5147-5154
    • Bradshaw, J.M.1    Waksman, G.2
  • 37
    • 0033638441 scopus 로고    scopus 로고
    • Structural basis for specificity switching of the Src SH2 domain
    • Kimber, M.S. et al. Structural basis for specificity switching of the Src SH2 domain. Mol. Cell 5, 1043-1049 (2000).
    • (2000) Mol Cell , vol.5 , pp. 1043-1049
    • Kimber, M.S.1
  • 38
    • 0032190081 scopus 로고    scopus 로고
    • The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM
    • Sayos, J. et al. The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM. Nature 395, 462-469 (1998).
    • (1998) Nature , vol.395 , pp. 462-469
    • Sayos, J.1
  • 39
    • 0033588251 scopus 로고    scopus 로고
    • mGrb10 interacts with Nedd4
    • Morrione, A. et al. mGrb10 interacts with Nedd4. J. Biol. Chem. 274, 24094-24099 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24094-24099
    • Morrione, A.1
  • 40
    • 0033518296 scopus 로고    scopus 로고
    • Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A
    • Li, S. C. et al. Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A. Curr. Biol. 9, 1355-1362 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1355-1362
    • Li, S.C.1
  • 41
    • 0028346469 scopus 로고
    • SH2 domain specificity and activity modified by a single residue
    • Marengere, L. E. et al. SH2 domain specificity and activity modified by a single residue. Nature 369, 502-505 (1994).
    • (1994) Nature , vol.369 , pp. 502-505
    • Marengere, L.E.1
  • 42
    • 0027211693 scopus 로고
    • Phospholipase C-γ1 and phosphatidylinositol-3-kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • Valius, M. & Kazlauskas, A. Phospholipase C-γ1 and phosphatidylinositol-3-kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell 73, 321-334 (1993).
    • (1993) Cell , vol.73 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 43
    • 0031450917 scopus 로고    scopus 로고
    • The platelet-derived growth factor β receptor triggers multiple cytoplasmic signaling cascades that arrive at the nucleus as distinguishable inputs
    • Montmayeur, J. P., Valius, M., Vandenheede, J. & Kazlauskas, A. The platelet-derived growth factor β receptor triggers multiple cytoplasmic signaling cascades that arrive at the nucleus as distinguishable inputs. J. Biol. Chem. 272, 32670-32678 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 32670-32678
    • Montmayeur, J.P.1    Valius, M.2    Vandenheede, J.3    Kazlauskas, A.4
  • 44
    • 0034671968 scopus 로고    scopus 로고
    • Retention of PDGFR-β function in mice in the absence of phosphatidylinositol-3′-kinase and phospholipase Cγ signaling pathways
    • Tallquist, M. D. et al. Retention of PDGFR-β function in mice in the absence of phosphatidylinositol-3′-kinase and phospholipase Cγ signaling pathways. Genes Dev. 14, 3179-3190 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 3179-3190
    • Tallquist, M.D.1
  • 45
    • 0030907541 scopus 로고    scopus 로고
    • Positive and negative tissue-specific signaling by a nematode epidermal growth factor receptor
    • Lesa, G. M. & Sternberg, P. W. Positive and negative tissue-specific signaling by a nematode epidermal growth factor receptor. Mol. Biol. Cell 8, 779-793 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 779-793
    • Lesa, G.M.1    Sternberg, P.W.2
  • 46
    • 0028277954 scopus 로고
    • Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins
    • Soler, C., Beguinot, L. & Carpenter, G. Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins. J. Biol. Chem. 269, 12320-12324 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12320-12324
    • Soler, C.1    Beguinot, L.2    Carpenter, G.3
  • 47
    • 0027987263 scopus 로고
    • Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins
    • Li, N., Schlessinger, J. & Margolis, B. Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins. Oncogene 9, 3457-3465 (1994).
    • (1994) Oncogene , vol.9 , pp. 3457-3465
    • Li, N.1    Schlessinger, J.2    Margolis, B.3
  • 48
    • 0032189977 scopus 로고    scopus 로고
    • Developmental roles of HGF/SF and its receptor, the c-Met tyrosine kinase
    • Birchmeier, C. & Gherardi, E. Developmental roles of HGF/SF and its receptor, the c-Met tyrosine kinase. Trends Cell Biol. 8, 404-410 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 404-410
    • Birchmeier, C.1    Gherardi, E.2
  • 49
    • 0034969431 scopus 로고    scopus 로고
    • Coupling Met to specific pathways results in distinct developmental outcomes
    • Maina, F. et al. Coupling Met to specific pathways results in distinct developmental outcomes. Mol. Cell 7, 1293-1306 (2001).
    • (2001) Mol Cell , vol.7 , pp. 1293-1306
    • Maina, F.1
  • 50
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • Lowenstein, E. J. et al. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 70, 431-442 (1992). The first of several papers to describe Grb2 as a link between receptor tyrosine kinases and Raf (see also references 53-56).
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1
  • 51
    • 0026777369 scopus 로고
    • A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
    • Pelicci, G. et al. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70, 93-104 (1992). This report was the first identification of SHC.
    • (1992) Cell , vol.70 , pp. 93-104
    • Pelicci, G.1
  • 52
    • 0026644391 scopus 로고
    • High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains
    • Margolis, B. et al. High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains. Proc. Natl Acad. Sci. USA 89, 8894-8898 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8894-8898
    • Margolis, B.1
  • 53
    • 0027312272 scopus 로고
    • Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
    • Li, N. et al. Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363, 85-88 (1993).
    • (1993) Nature , vol.363 , pp. 85-88
    • Li, N.1
  • 54
    • 0027468233 scopus 로고
    • A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos
    • Olivier, J. P. et al. A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. Cell 73, 179-191 (1993).
    • (1993) Cell , vol.73 , pp. 179-191
    • Olivier, J.P.1
  • 55
    • 0027229556 scopus 로고
    • Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras
    • Gale, N. W., Kaplan, S., Lowenstein, E. J., Schlessinger, J. & Bar-Sagi, D. Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras. Nature 363, 88-92 (1993).
    • (1993) Nature , vol.363 , pp. 88-92
    • Gale, N.W.1    Kaplan, S.2    Lowenstein, E.J.3    Schlessinger, J.4    Bar-Sagi, D.5
  • 56
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E. et al. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 363, 45-51 (1993).
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1
  • 57
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor
    • Lechleider, R. J. et al. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J. Biol. Chem. 268, 21478-21481 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1
  • 58
    • 0029085194 scopus 로고
    • Identification of a putative Syp substrate, the PDGF β receptor
    • Klinghoffer, R. A. & Kazlauskas, A. Identification of a putative Syp substrate, the PDGF β receptor. J. Biol. Chem. 270, 22208-22217 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 22208-22217
    • Klinghoffer, R.A.1    Kazlauskas, A.2
  • 59
    • 0029930117 scopus 로고    scopus 로고
    • Drosophila terminal structure development is regulated by the compensatory activities of positive and negative phosphotyrosine signaling sites on the Torso RTK
    • Cleghon, V. et al. Drosophila terminal structure development is regulated by the compensatory activities of positive and negative phosphotyrosine signaling sites on the Torso RTK. Genes Dev. 10, 566-577 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 566-577
    • Cleghon, V.1
  • 60
    • 0032238275 scopus 로고    scopus 로고
    • Opposing actions of CSW and RasGAP modulate the strength of Torso RTK signaling in the Drosophila terminal pathway
    • Cleghon, V. et al. Opposing actions of CSW and RasGAP modulate the strength of Torso RTK signaling in the Drosophila terminal pathway. Mol. Cell 2, 719-727 (1998).
    • (1998) Mol Cell , vol.2 , pp. 719-727
    • Cleghon, V.1
  • 61
    • 0029094649 scopus 로고
    • Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation
    • Galisteo, M. L., Dikic, I., Batzer, A. G., Langdon, W. Y. & Schlessinger, J. Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation. J. Biol. Chem. 270, 20242-20245 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 20242-20245
    • Galisteo, M.L.1    Dikic, I.2    Batzer, A.G.3    Langdon, W.Y.4    Schlessinger, J.5
  • 62
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
    • Meng, W., Sawasdikosol, S., Burakoff, S. J. & Eck, M. J. Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 398, 84-90 (1999).
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 63
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro, C. A. et al. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 286, 309-312 (1999). Together with references 64-67, this paper elucidates the recognition of Cbl as a ubiquitin ligase.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1
  • 64
    • 0032217156 scopus 로고    scopus 로고
    • c-Cbl/Sli-l regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz, G. et al. c-Cbl/Sli-l regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12, 3663-3674 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3663-3674
    • Levkowitz, G.1
  • 65
    • 0034614652 scopus 로고    scopus 로고
    • The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor
    • Lill, N. L. et al. The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor. J. Biol. Chem. 275, 367-377 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 367-377
    • Lill, N.L.1
  • 66
    • 0032493444 scopus 로고    scopus 로고
    • The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor
    • Miyake, S., Lupher, M. L. Jr, Druker, B. & Band, H. The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor. Proc. Natl Acad. Sci. USA 95, 7927-7932 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7927-7932
    • Miyake, S.1    Lupher M.L., Jr.2    Druker, B.3    Band, H.4
  • 67
    • 0033529537 scopus 로고    scopus 로고
    • The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor
    • Waterman, H., Levkowitz, G., Alroy, I. & Yarden, Y. The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor. J. Biol. Chem. 274, 22151-22154 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22151-22154
    • Waterman, H.1    Levkowitz, G.2    Alroy, I.3    Yarden, Y.4
  • 68
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C. & Eck, M. J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602 (1997). Together with references 69-71, these papers defined the structure of Src-family tyrosine kinases and determined their mechanism of activation.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 69
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I. & Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609 (1997).
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 70
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu, W., Doshi, A., Lei, M., Eck, M. J. & Harrison, S. C. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell 3, 629-638 (1999).
    • (1999) Mol Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 71
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young, M. A., Gonfloni, S., Superti-Furga, G., Roux, B. & Kudyan, J. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105, 115-126 (2001).
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kudyan, J.5
  • 72
    • 0027288978 scopus 로고
    • Regulation of c-Src tyrosine kinase activity by the Src SH2 domain
    • Liu, X. et al. Regulation of c-Src tyrosine kinase activity by the Src SH2 domain. Oncogene 8, 1119-1126 (1993).
    • (1993) Oncogene , vol.8 , pp. 1119-1126
    • Liu, X.1
  • 73
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi, I. et al. Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653 (1997).
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1
  • 74
    • 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). Together with references 75 and 76, these papers show that the SH2 domains of Src-family kinases function to enhance processive phosphorylation.
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 75
    • 0032547071 scopus 로고    scopus 로고
    • Enhanced phosphorylation of Src family kinase substrates containing SH2 domain binding sites
    • Pellicena, P., Stowell, K. R. & Miller, W. T. Enhanced phosphorylation of Src family kinase substrates containing SH2 domain binding sites. J. Biol. Chem. 273, 15325-15328 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15325-15328
    • Pellicena, P.1    Stowell, K.R.2    Miller, W.T.3
  • 76
    • 0034727646 scopus 로고    scopus 로고
    • A peptide model system for processive phosphorylation by Src family kinases
    • Scott, M. P. & Miller, W. T. A peptide model system for processive phosphorylation by Src family kinases. Biochemistry 39, 14531-14537 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14531-14537
    • Scott, M.P.1    Miller, W.T.2
  • 77
    • 0030066325 scopus 로고    scopus 로고
    • Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
    • Eck, M. J., Pluskey, S., Trub, T., Harrison, S. C. & Shoelson, S. E. Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 379, 277-280 (1996).
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trub, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 78
    • 0031964602 scopus 로고    scopus 로고
    • Tandem SH2 domains confer high specificity in tyrosine kinase signaling
    • Ottinger, E. A., Botfield, M. C. & Shoelson, S. E. Tandem SH2 domains confer high specificity in tyrosine kinase signaling. J. Biol. Chem. 273, 729-735 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 729-735
    • Ottinger, E.A.1    Botfield, M.C.2    Shoelson, S.E.3
  • 79
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof, P., Pluskey, S., Dhe-Paganon, S., Eck, M. J. & Shoelson, S. E. Crystal structure of the tyrosine phosphatase SHP-2. Cell 92, 441-450 (1998).
    • (1998) Cell , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 80
    • 0032555744 scopus 로고    scopus 로고
    • Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide
    • Futterer, K., Wong, J., Grucza, R. A., Chan, A. C. & Waksman, G. Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J. Mol. Biol. 281, 523-537 (1998).
    • (1998) J. Mol. Biol. , vol.281 , pp. 523-537
    • Futterer, K.1    Wong, J.2    Grucza, R.A.3    Chan, A.C.4    Waksman, G.5
  • 81
    • 0028568639 scopus 로고
    • A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
    • Blaikie, P. et al. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269, 32031-32034 (1994). The first recognition of the PTB domain as an alternative phosphotyrosine-binding module.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32031-32034
    • Blaikie, P.1
  • 82
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh, W. M. & Williams, L. T. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266, 1862-1865 (1994).
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 83
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain
    • Gustafson, T. A., He, W., Craparo, A., Schaub, C. D. & O'Neill, T. J. Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15, 2500-2508 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 84
    • 0029420949 scopus 로고
    • Structure and function of the phosphotyrosine binding (PTB) domain
    • Zhou, M. M. & Fesik, S. W. Structure and function of the phosphotyrosine binding (PTB) domain. Prog. Biophys. Mol. Biol. 64, 221-235 (1995).
    • (1995) Prog. Biophys. Mol. Biol. , vol.64 , pp. 221-235
    • Zhou, M.M.1    Fesik, S.W.2
  • 85
    • 0031197193 scopus 로고    scopus 로고
    • SH2 and PTB domain interactions in tyrosine kinase signal transduction
    • Shoelson, S. E. SH2 and PTB domain interactions in tyrosine kinase signal transduction. Curr. Opin. Chem. Biol. 1, 227-234 (1997).
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 227-234
    • Shoelson, S.E.1
  • 86
    • 0032424250 scopus 로고    scopus 로고
    • How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains
    • Zhou, Y. & Abagyan, R. How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains. Fold. Des. 3, 513-522 (1998).
    • (1998) Fold. Des. , vol.3 , pp. 513-522
    • Zhou, Y.1    Abagyan, R.2
  • 87
    • 0032776320 scopus 로고    scopus 로고
    • Diversity in protein recognition by PTB domains
    • Forman-Kay, J. D. & Pawson, T. Diversity in protein recognition by PTB domains. Curr. Opin. Struct. Biol. 9, 690-695 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 690-695
    • Forman-Kay, J.D.1    Pawson, T.2
  • 89
    • 0029094991 scopus 로고
    • Specificity of the PTB domain of Shc for β turn-forming pentapeptide motifs amino-terminal to phosphotyrosine
    • Trub, T. et al. Specificity of the PTB domain of Shc for β turn-forming pentapeptide motifs amino-terminal to phosphotyrosine. J. Biol. Chem. 270, 18205-18208 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18205-18208
    • Trub, T.1
  • 90
    • 0029278769 scopus 로고
    • A conserved amino-terminal SHC domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides
    • Van der Geer, P. et al. A conserved amino-terminal SHC domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides. Curr. Biol. 5, 404-412 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 404-412
    • Van der Geer, P.1
  • 91
    • 0030032062 scopus 로고    scopus 로고
    • Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites
    • Van der Geer, P. et al. Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites. Proc. Natl Acad. Sci. USA 93, 963-968 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 963-968
    • Van der Geer, P.1
  • 92
    • 0028874953 scopus 로고
    • PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities
    • Wolf, G. et al. PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J. Biol. Chem. 270, 27407-27410 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 27407-27410
    • Wolf, G.1
  • 93
    • 0029010308 scopus 로고
    • The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif
    • Zhou, S., Margolis, B., Chaudhuri, M., Shoelson, S. E. & Cantley, L. C. The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif. J. Biol. Chem. 270, 14863-14866 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14863-14866
    • Zhou, S.1    Margolis, B.2    Chaudhuri, M.3    Shoelson, S.E.4    Cantley, L.C.5
  • 94
    • 0029731182 scopus 로고    scopus 로고
    • Characterization of the phosphotyrosine-binding domain of the Drosophila Shc protein
    • Li, S. C. et al. Characterization of the phosphotyrosine-binding domain of the Drosophila Shc protein. J. Biol. Chem. 271, 31855-31862 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31855-31862
    • Li, S.C.1
  • 95
    • 0030049298 scopus 로고    scopus 로고
    • Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors
    • Laminet, A. A., Apell, G., Conroy, L. & Kavanaugh, W. M. Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors. J. Biol. Chem. 271, 264-269 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 264-269
    • Laminet, A.A.1    Apell, G.2    Conroy, L.3    Kavanaugh, W.M.4
  • 96
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg, J. P., Ooi, J., Levy, E. & Margolis, B. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16, 6229-6241 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 97
    • 0030723614 scopus 로고    scopus 로고
    • Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain
    • Zhang, Z. et al. Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. EMBO J. 16, 6141-6150 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6141-6150
    • Zhang, Z.1
  • 98
    • 0032502726 scopus 로고    scopus 로고
    • The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX
    • Dho, S. E. et al. The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX. J. Biol. Chem. 273, 9179-9187 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 9179-9187
    • Dho, S.E.1
  • 99
    • 0031962189 scopus 로고    scopus 로고
    • Numb-associated kinase interacts with the phosphotyrosine binding domain of Numb and antagonizes the function of Numb in vivo
    • Chien, C. T., Wang, S., Rothenberg, M., Jan, L. Y. & Jan, Y. N. Numb-associated kinase interacts with the phosphotyrosine binding domain of Numb and antagonizes the function of Numb in vivo. Mol. Cell. Biol. 18, 598-607 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 598-607
    • Chien, C.T.1    Wang, S.2    Rothenberg, M.3    Jan, L.Y.4    Jan, Y.N.5
  • 100
    • 0031790608 scopus 로고    scopus 로고
    • Structure of a Numb PTB domain-peptide complex suggests a basis for diverse binding specificity
    • Li, S. C. et al. Structure of a Numb PTB domain-peptide complex suggests a basis for diverse binding specificity. Nature Struct. Biol. 5, 1075-1083 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1075-1083
    • Li, S.C.1
  • 101
    • 0033520918 scopus 로고    scopus 로고
    • Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons
    • Meyer, D., Liu, A. & Margolis, B. Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons. J. Biol. Chem. 274, 35113-35118 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 35113-35118
    • Meyer, D.1    Liu, A.2    Margolis, B.3
  • 102
    • 0029082202 scopus 로고
    • Deletion of a conserved juxtamembrane sequence in Trk abolishes NGF-promoted neuritogenesis
    • Peng, X., Greene, L. A., Kaplan, D. R. & Stephens, R. M. Deletion of a conserved juxtamembrane sequence in Trk abolishes NGF-promoted neuritogenesis. Neuron 15, 395-406 (1995).
    • (1995) Neuron , vol.15 , pp. 395-406
    • Peng, X.1    Greene, L.A.2    Kaplan, D.R.3    Stephens, R.M.4
  • 103
    • 0033515534 scopus 로고    scopus 로고
    • The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation
    • Meakin, S. O., MacDonald, J. I., Gryz, E. A., Kubu, C. J. & Verdi, J. M. The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation. J. Biol. Chem. 274, 9861-9870 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 9861-9870
    • Meakin, S.O.1    MacDonald, J.I.2    Gryz, E.A.3    Kubu, C.J.4    Verdi, J.M.5
  • 104
    • 0032540941 scopus 로고    scopus 로고
    • Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins
    • Xu, H., Lee, K. W. & Goldfarb, M. Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins. J. Biol. Chem. 273, 17987-17990 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 17987-17990
    • Xu, H.1    Lee, K.W.2    Goldfarb, M.3
  • 105
    • 0033974109 scopus 로고    scopus 로고
    • FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors
    • Ong, S. H. et al. FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. Mol. Cell. Biol. 20, 979-989 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 979-989
    • Ong, S.H.1
  • 106
    • 0028860968 scopus 로고
    • Structure and ligand recognition of the phosphotyrosine binding domain of Shc
    • Zhou, M. M. et al. Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378, 584-592 (1995). This study described the first PTB-domain structure that was solved by NMR.
    • (1995) Nature , vol.378 , pp. 584-592
    • Zhou, M.M.1
  • 107
    • 0030010590 scopus 로고    scopus 로고
    • Structure of the IRS-1 PTB domain bound to the juxtamembrene region of the insulin receptor
    • Eck, M. J., Dhe-Paganon, S., Trub, T., Nolte, R. T. & Shoelson, S. E. Structure of the IRS-1 PTB domain bound to the juxtamembrene region of the insulin receptor. Cell 85, 695-705 (1996). The first X-ray structure of a PTB domain, which showed how the divergent IRS-1 and SHC PTB domains have the same basic fold but use different residues to bind to phosphotyrosine-containing ligands.
    • (1996) Cell , vol.85 , pp. 695-705
    • Eck, M.J.1    Dhe-Paganon, S.2    Trub, T.3    Nolte, R.T.4    Shoelson, S.E.5
  • 108
    • 0029940882 scopus 로고    scopus 로고
    • Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain
    • Zhou, M. M. et al. Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain. Nature Struct. Biol. 3, 388-393 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 388-393
    • Zhou, M.M.1
  • 109
    • 0034599721 scopus 로고    scopus 로고
    • Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb
    • Zwahlen, C., Li, S. C., Kay, L. E., Pawson, T. & Forman-Kay, J. D. Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb. EMBO J. 19, 1505-1515 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1505-1515
    • Zwahlen, C.1    Li, S.C.2    Kay, L.E.3    Pawson, T.4    Forman-Kay, J.D.5
  • 110
    • 0033635195 scopus 로고    scopus 로고
    • Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors
    • Dhalluin, C. et al. Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors. Mol. Cell 6, 921-929 (2000).
    • (2000) Mol Cell , vol.6 , pp. 921-929
    • Dhalluin, C.1
  • 111
    • 0033553508 scopus 로고    scopus 로고
    • Structure of the enabled/VASP homology 1 domain-peptide complex: A key component in the spatial control of actin assembly
    • Prehoda, K. E., Lee, D. J. & Lim, W. A. Structure of the enabled/ VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Cell 97, 471-480 (1999).
    • (1999) Cell , vol.97 , pp. 471-480
    • Prehoda, K.E.1    Lee, D.J.2    Lim, W.A.3
  • 112
    • 0033031122 scopus 로고    scopus 로고
    • Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function
    • Fedorov, A. A., Fedorov, E., Gertler, F. & Almo, S. C. Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. Nature Struct. Biol. 6, 661-665 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 661-665
    • Fedorov, A.A.1    Fedorov, E.2    Gertler, F.3    Almo, S.C.4
  • 113
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A. & Ferguson, K. M. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1-18 (2000).
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 114
    • 0030848936 scopus 로고    scopus 로고
    • Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo
    • Ravichandran, K. S. et al. Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo. Mol. Cell. Biol. 17, 5540-5549 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5540-5549
    • Ravichandran, K.S.1
  • 115
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell, B. W., Lanier, L. M., Frank, R., Gertler, F. B. & Cooper, J. A. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19, 5179-5188 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A.5
  • 116
    • 0033525733 scopus 로고    scopus 로고
    • Phosphotyrosine binding domains of Shc and insulin receptor substrate 1 recognize the NPXpY motif in a thermodynamically distinct manner
    • Farooq, A., Plotnikova, O., Zeng, L. & Zhou, M. M. Phosphotyrosine binding domains of Shc and insulin receptor substrate 1 recognize the NPXpY motif in a thermodynamically distinct manner. J. Biol. Chem. 274, 6114-6121 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 6114-6121
    • Farooq, A.1    Plotnikova, O.2    Zeng, L.3    Zhou, M.M.4
  • 117
    • 0035474473 scopus 로고    scopus 로고
    • Signaling via Shc family adapter proteins
    • Ravichandran, K. S. Signaling via Shc family adapter proteins. Oncogene 20, 6322-6330 (2001).
    • (2001) Oncogene , vol.20 , pp. 6322-6330
    • Ravichandran, K.S.1
  • 118
    • 0031444245 scopus 로고    scopus 로고
    • Identification of the Abl- and RasGAP-associated 62 kDa protein as a docking protein
    • Yamanashi, Y. & Baltimore, D. Identification of the Abl- and RasGAP-associated 62 kDa protein as a docking protein. Dok. Cell 88, 205-211 (1997). Together with reference 119, this study described the first identification of p62dok as a membrane-associated RasGAP-binding molecule that is targeted by activated tyrosine kinases.
    • (1997) Dok. Cell , vol.88 , pp. 205-211
    • Yamanashi, Y.1    Baltimore, D.2
  • 119
    • 0031459864 scopus 로고    scopus 로고
    • p62(Dok): A constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells
    • Carpino, N. et al. p62(Dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 88, 197-204 (1997).
    • (1997) Cell , vol.88 , pp. 197-204
    • Carpino, N.1
  • 120
    • 0032480321 scopus 로고    scopus 로고
    • The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R
    • Jones, N. & Dumont, D. J. The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R. Oncogene 17, 1097-1108 (1998).
    • (1998) Oncogene , vol.17 , pp. 1097-1108
    • Jones, N.1    Dumont, D.J.2
  • 121
    • 0033598172 scopus 로고    scopus 로고
    • Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation
    • Jones, N. & Dumont, D. J. Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation. Curr. Biol. 9, 1057-1060 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1057-1060
    • Jones, N.1    Dumont, D.J.2
  • 122
    • 0035914308 scopus 로고    scopus 로고
    • Multiple ErbB-2/Neu phosphorylation sites mediate transformation through distinct effector proteins
    • Dankort, D., Jeybala, N., Jones, N., Dumont, D. J. & Muller, W. J. Multiple ErbB-2/Neu phosphorylation sites mediate transformation through distinct effector proteins. J. Biol. Chem. 276, 38921-38928 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 38921-38928
    • Dankort, D.1    Jeybala, N.2    Jones, N.3    Dumont, D.J.4    Muller, W.J.5
  • 123
    • 0035900720 scopus 로고    scopus 로고
    • Insulin receptor-mediated p62(superdok) tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GAP and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt
    • Wick, M. J., Dong, L. Q., Hu, D., Langlais, P. & Liu, P. Insulin receptor-mediated p62(superdok) tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GAP and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt. J. Biol. Chem. 276, 42843-42850 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42843-42850
    • Wick, M.J.1    Dong, L.Q.2    Hu, D.3    Langlais, P.4    Liu, P.5
  • 124
    • 0033979324 scopus 로고    scopus 로고
    • Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling
    • Yamanashi, Y. et al. Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling. Genes Dev. 14, 11-16 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 11-16
    • Yamanashi, Y.1
  • 125
    • 0034640062 scopus 로고    scopus 로고
    • Evidence that Lick-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signaling
    • Nemorin, J. G. & Duplay, P. Evidence that Lick-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signaling. J. Biol. Chem. 275, 14590-14597 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14590-14597
    • Nemorin, J.G.1    Duplay, P.2
  • 126
    • 0031001812 scopus 로고    scopus 로고
    • Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells
    • Holland, S. J. et al. Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells. EMBO J. 16, 3877-3888 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3877-3888
    • Holland, S.J.1
  • 127
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein
    • Trommsdorff, M., Borg, J. P., Margolis, B. & Herz, J. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 273, 33556-33560 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 128
    • 0033003134 scopus 로고    scopus 로고
    • Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2
    • Trommsdorff, M. et al. Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. Cell 97, 689-701 (1999).
    • (1999) Cell , vol.97 , pp. 689-701
    • Trommsdorff, M.1
  • 129
    • 0030281598 scopus 로고    scopus 로고
    • Scrambler, a new neurological mutation of the mouse with abnormalities of neuronal migration
    • Sweet, H. O., Bronson, R. T., Johnson, K. R., Cook, S. A. & Davisson, M. T. Scrambler, a new neurological mutation of the mouse with abnormalities of neuronal migration. Mamm. Genome 7, 798-802 (1996).
    • (1996) Mamm. Genome , vol.7 , pp. 798-802
    • Sweet, H.O.1    Bronson, R.T.2    Johnson, K.R.3    Cook, S.A.4    Davisson, M.T.5
  • 130
    • 0030717493 scopus 로고    scopus 로고
    • Scrambler and yotari disrupt the disabled gene and produce a reeler-like phenotype in mice
    • Sheldon, M. et al. Scrambler and yotari disrupt the disabled gene and produce a reeler-like phenotype in mice. Nature 389, 730-733 (1997).
    • (1997) Nature , vol.389 , pp. 730-733
    • Sheldon, M.1
  • 131
    • 0030868450 scopus 로고    scopus 로고
    • Aberrant splicing of a mouse disabled homolog, mdab 1, in the scrambler mouse
    • Ware, M. L. et al. Aberrant splicing of a mouse disabled homolog, mdab1, in the scrambler mouse. Neuron 19, 239-249 (1997).
    • (1997) Neuron , vol.19 , pp. 239-249
    • Ware, M.L.1
  • 132
    • 0030704354 scopus 로고    scopus 로고
    • Neuronal position in the developing brain is regulated by mouse disabled-1
    • Howell, B. W., Hawkes, R., Soriano, P. & Cooper, J. A. Neuronal position in the developing brain is regulated by mouse disabled-1. Nature 389, 733-737 (1997).
    • (1997) Nature , vol.389 , pp. 733-737
    • Howell, B.W.1    Hawkes, R.2    Soriano, P.3    Cooper, J.A.4
  • 133
    • 0031658384 scopus 로고    scopus 로고
    • Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain
    • Rice, D. S. et al. Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain. Development 125, 3719-3729 (1998).
    • (1998) Development , vol.125 , pp. 3719-3729
    • Rice, D.S.1
  • 134
    • 0035906961 scopus 로고    scopus 로고
    • Autosomal recessive hypercholesterolemia caused by mutations in a putative LDL receptor adaptor protein
    • Garcia, C. K. et al. Autosomal recessive hypercholesterolemia caused by mutations in a putative LDL receptor adaptor protein. Science 292, 1394-1398 (2001). This study showed that a form of autosomal recessive hypercholesterolaemia is caused by mutations in the ARH protein, which contains a PTB domain that might bind to the LDL receptor.
    • (2001) Science , vol.292 , pp. 1394-1398
    • Garcia, C.K.1
  • 135
    • 0030199973 scopus 로고    scopus 로고
    • Control of daughter cell fates during asymmetric division: Interaction of Numb and Notch
    • Guo, M., Jan, L. Y. & Jan, Y. N. Control of daughter cell fates during asymmetric division: interaction of Numb and Notch. Neuron 17, 27-41 (1996).
    • (1996) Neuron , vol.17 , pp. 27-41
    • Guo, M.1    Jan, L.Y.2    Jan, Y.N.3
  • 136
    • 0032562567 scopus 로고    scopus 로고
    • Functional analysis of the Numb phosphotyrosine-binding domain using site-directed mutagenesis
    • Yaich, L. et al. Functional analysis of the Numb phosphotyrosine-binding domain using site-directed mutagenesis. J. Biol. Chem. 273, 10381-10388 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10381-10388
    • Yaich, L.1
  • 137
    • 15844398102 scopus 로고    scopus 로고
    • Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode
    • Rahuel, J. et al. Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode. Nature Struct. Biol. 3, 586-589 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 586-589
    • Rahuel, J.1
  • 138
    • 0033546119 scopus 로고    scopus 로고
    • Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide
    • Ogura, K. et al. Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide. J. Mol. Biol. 289, 439-445 (1999).
    • (1999) J. Mol. Biol. , vol.289 , pp. 439-445
    • Ogura, K.1
  • 139
    • 0028359598 scopus 로고
    • Brief report: A point mutation in the SH2 domain of Bruton's tyrosine kinase in atypical X-linked agammaglobulinemia
    • Saffran, D. C. et al. Brief report: a point mutation in the SH2 domain of Bruton's tyrosine kinase in atypical X-linked agammaglobulinemia. N. Engl. J. Med. 330, 1488-1491 (1994).
    • (1994) N. Engl. J. Med. , vol.330 , pp. 1488-1491
    • Saffran, D.C.1
  • 140
    • 17344372694 scopus 로고    scopus 로고
    • Host response to EBV infection in X-linked lymphoproliferative disease results from mutations in an SH2-domain encoding gene
    • Coffey, A. J. et al. Host response to EBV infection in X-linked lymphoproliferative disease results from mutations in an SH2-domain encoding gene. Nature Genet. 20, 129-135 (1998).
    • (1998) Nature Genet. , vol.20 , pp. 129-135
    • Coffey, A.J.1
  • 141
    • 13144278345 scopus 로고    scopus 로고
    • Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome
    • Nichols, K. E. et al. Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome. Proc. Natl Acad. Sci. USA 95, 13765-13770 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13765-13770
    • Nichols, K.E.1
  • 142
    • 18344385476 scopus 로고    scopus 로고
    • Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
    • Tartaglia, M. et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nature Genet. 29, 465-468 (2001). An elegant example of how mutations in the SHP-2 amino-SH2 domain are associated with a human disease.
    • (2001) Nature Genet. , vol.29 , pp. 465-468
    • Tartaglia, M.1
  • 143
    • 0034773599 scopus 로고    scopus 로고
    • SH2 and SH3 domains as targets for anti-proliferative agents
    • Vidal, M., Gigoux, V. & Garbay, C. SH2 and SH3 domains as targets for anti-proliferative agents. Crit. Rev. Oncol. Hematol. 40, 175-186 (2001).
    • (2001) Crit. Rev. Oncol. Hematol. , vol.40 , pp. 175-186
    • Vidal, M.1    Gigoux, V.2    Garbay, C.3
  • 144
    • 12944281813 scopus 로고    scopus 로고
    • Structure-based design of an osteoclast-selective, nonpeptide src homology 2 inhibitor with in vivo antiresorptive activity
    • Shakespeare, W. et al. Structure-based design of an osteoclast-selective, nonpeptide src homology 2 inhibitor with in vivo antiresorptive activity. Proc. Natl Acad. Sci. USA 97, 9373-9378 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9373-9378
    • Shakespeare, W.1
  • 145
    • 0033741651 scopus 로고    scopus 로고
    • Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries
    • Yaffe, M. B. & Cantley, L. C. Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries. Methods Enzymol. 328, 157-170 (2000).
    • (2000) Methods Enzymol. , vol.328 , pp. 157-170
    • Yaffe, M.B.1    Cantley, L.C.2
  • 146
    • 0037059461 scopus 로고    scopus 로고
    • A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules
    • Tong, A. H. et al. A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295, 321-324 (2002).
    • (2002) Science , vol.295 , pp. 321-324
    • Tong, A.H.1
  • 147
    • 0034724569 scopus 로고    scopus 로고
    • SH3-SPOT: An algorithm to predict preferred ligands to different members of the SH3 gene family
    • Brannetti, B., Via, A., Cestra, G., Cesareni, G. & Helmer-Citterich, M. SH3-SPOT: an algorithm to predict preferred ligands to different members of the SH3 gene family. J. Mol. Biol. 298, 313-328 (2000).
    • (2000) J. Mol. Biol. , vol.298 , pp. 313-328
    • Brannetti, B.1    Via, A.2    Cestra, G.3    Cesareni, G.4    Helmer-Citterich, M.5
  • 148
    • 0032568655 scopus 로고    scopus 로고
    • SMART a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P. & Ponting, C. P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl Acad. Sci. USA 95, 5857-5864 (1998). This study described a classic bioinformatics tool for the study of modular protein domains.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4


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