^“Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases”. The Journal of Biological Chemistry277 (7): 4999–5007. (Feb 2002). doi:10.1074/jbc.M107430200. PMID11741929.
^“The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr”. The Journal of Biological Chemistry272 (52): 33260–70. (Dec 1997). doi:10.1074/jbc.272.52.33260. PMID9407116.
^“Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites”. Genes & Development8 (7): 783–95. (Apr 1994). doi:10.1101/gad.8.7.783. PMID7926767.
^“Competitive binding assay of src homology domain 3 interactions between 5-lipoxygenase and growth factor receptor binding protein 2”. Analytical Biochemistry230 (1): 108–14. (Sep 1995). doi:10.1006/abio.1995.1444. PMID8585605.
^“5-Lipoxygenase contains a functional Src homology 3-binding motif that interacts with the Src homology 3 domain of Grb2 and cytoskeletal proteins”. The Journal of Biological Chemistry269 (39): 24163–8. (Sep 1994). doi:10.1016/S0021-9258(19)51063-8. PMID7929073.
^“Specific inhibition of FGF-induced MAPK activation by the receptor-like protein tyrosine phosphatase LAR”. Oncogene19 (19): 2346–53. (May 2000). doi:10.1038/sj.onc.1203558. PMID10822386.
^“Insulin stimulates sequestration of beta-adrenergic receptors and enhanced association of beta-adrenergic receptors with Grb2 via tyrosine 350”. The Journal of Biological Chemistry273 (49): 33035–41. (Dec 1998). doi:10.1074/jbc.273.49.33035. PMID9830057.
^“Specific uncoupling of GRB2 from the Met receptor. Differential effects on transformation and motility”. The Journal of Biological Chemistry271 (24): 14119–23. (Jun 1996). doi:10.1074/jbc.271.24.14119. PMID8662889.
^“Signaling by HGF and KGF in corneal epithelial cells: Ras/MAP kinase and Jak-STAT pathways”. Investigative Ophthalmology & Visual Science39 (8): 1329–38. (Jul 1998). PMID9660480.
^“The CBL-related protein CBLB participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells”. The Journal of Biological Chemistry273 (24): 14962–7. (Jun 1998). doi:10.1074/jbc.273.24.14962. PMID9614102.
^“Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation”. Oncogene18 (5): 1147–56. (Feb 1999). doi:10.1038/sj.onc.1202411. PMID10022120.
^ ab“Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway”. The Journal of Biological Chemistry271 (21): 12129–32. (May 1996). doi:10.1074/jbc.271.21.12129. PMID8647802.
^“CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux”. The Journal of Biological Chemistry275 (23): 17420–7. (Jun 2000). doi:10.1074/jbc.M001892200. PMID10748054.
^“CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1”. The Journal of Biological Chemistry276 (47): 44315–22. (Nov 2001). doi:10.1074/jbc.M105446200. PMID11551923.
^“Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction”. The Journal of Biological Chemistry273 (33): 21194–202. (Aug 1998). doi:10.1074/jbc.273.33.21194. PMID9694876.
^“Signal transduction by CD28 costimulatory receptor on T cells. B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules”. The Journal of Biological Chemistry271 (3): 1591–8. (Jan 1996). doi:10.1074/jbc.271.3.1591. PMID8576157.
^“Direct binding of the signal-transducing adaptor Grb2 facilitates down-regulation of the cyclin-dependent kinase inhibitor p27Kip1”. The Journal of Biological Chemistry276 (15): 12084–90. (Apr 2001). doi:10.1074/jbc.M010811200. PMID11278754.
^“Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins”. The Journal of Biological Chemistry271 (24): 14468–72. (Jun 1996). doi:10.1074/jbc.271.24.14468. PMID8662907.
^ ab“Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor”. The Journal of Biological Chemistry271 (41): 25533–8. (Oct 1996). doi:10.1074/jbc.271.41.25533. PMID8810325.
^ ab“Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages”. Journal of Leukocyte Biology65 (4): 523–34. (Apr 1999). doi:10.1002/jlb.65.4.523. PMID10204582.
^ abc“Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc”. Oncogene17 (24): 3073–82. (Dec 1998). doi:10.1038/sj.onc.1202337. PMID9872323.
^ abc“High affinity IgG receptor activation of Src family kinases is required for modulation of the Shc-Grb2-Sos complex and the downstream activation of the nicotinamide adenine dinucleotide phosphate (reduced) oxidase”. Journal of Immunology163 (11): 6023–34. (Dec 1999). doi:10.4049/jimmunol.163.11.6023. PMID10570290.
^“Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase”. Oncogene14 (18): 2217–28. (May 1997). doi:10.1038/sj.onc.1201049. PMID9174058.
^“A c-Cbl yeast two hybrid screen reveals interactions with 14-3-3 isoforms and cytoskeletal components”. Biochemical and Biophysical Research Communications240 (1): 46–50. (Nov 1997). doi:10.1006/bbrc.1997.7608. PMID9367879.
^“The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor”. The Journal of Biological Chemistry269 (37): 22921–4. (Sep 1994). doi:10.1016/S0021-9258(17)31595-8. PMID8083187.
^“Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells”. The Journal of Biological Chemistry273 (7): 3986–93. (Feb 1998). doi:10.1074/jbc.273.7.3986. PMID9461587.
^“CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2”. Oncogene14 (19): 2331–8. (May 1997). doi:10.1038/sj.onc.1201074. PMID9178909.
^“Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl”. Blood89 (8): 2745–56. (Apr 1997). doi:10.1182/blood.V89.8.2745. PMID9108392.
^“Identification of a second Grb2 binding site in the v-Fms tyrosine kinase”. Oncogene15 (13): 1565–72. (Sep 1997). doi:10.1038/sj.onc.1201518. PMID9380408.
^“Identification of a novel 135-kDa Grb2-binding protein in osteoclasts”. The Journal of Biological Chemistry271 (51): 33141–7. (Dec 1996). doi:10.1074/jbc.271.51.33141. PMID8955163.
^“Association of Ash/Grb-2 with dynamin through the Src homology 3 domain”. The Journal of Biological Chemistry269 (8): 5489–92. (Feb 1994). doi:10.1016/S0021-9258(17)37484-7. PMID8119878.
^“SH3 domain-mediated interaction of dystroglycan and Grb2”. The Journal of Biological Chemistry270 (20): 11711–4. (May 1995). doi:10.1074/jbc.270.20.11711. PMID7744812.
^“Activation of the EphA2 tyrosine kinase stimulates the MAP/ERK kinase signaling cascade”. Oncogene21 (50): 7690–9. (Oct 2002). doi:10.1038/sj.onc.1205758. PMID12400011.
^ abcd“UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug”. Oncogene21 (13): 2037–50. (Mar 2002). doi:10.1038/sj.onc.1205271. PMID11960376.
^“A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling”. The Journal of Biological Chemistry274 (13): 8900–9. (Mar 1999). doi:10.1074/jbc.274.13.8900. PMID10085134.
^“Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells”. The Journal of Biological Chemistry269 (49): 31310–4. (Dec 1994). doi:10.1016/S0021-9258(18)47424-8. hdl:20.500.14094/D2001922. PMID7527043.
^ ab“The RIalpha subunit of protein kinase A (PKA) binds to Grb2 and allows PKA interaction with the activated EGF-receptor”. Oncogene14 (8): 923–8. (Feb 1997). doi:10.1038/sj.onc.1200906. PMID9050991.
^“Cloning and characterization of GRB14, a novel member of the GRB7 gene family”. The Journal of Biological Chemistry271 (21): 12502–10. (May 1996). doi:10.1074/jbc.271.21.12502. PMID8647858.
^ ab“A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells”. The Journal of Biological Chemistry269 (12): 9019–23. (Mar 1994). doi:10.1016/S0021-9258(17)37070-9. PMID7510700.
^ ab“Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck”. The Journal of Biological Chemistry274 (9): 5542–9. (Feb 1999). doi:10.1074/jbc.274.9.5542. PMID10026169.
^“Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways”. The Journal of Biological Chemistry270 (10): 5631–5. (Mar 1995). doi:10.1074/jbc.270.10.5631. PMID7534299.
^“Suc1-associated neurotrophic factor target (SNT) protein is a major FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to the SH2 domain of GRB2”. Biochemical and Biophysical Research Communications225 (3): 1021–6. (Aug 1996). doi:10.1006/bbrc.1996.1288. PMID8780727.
^“The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation”. The Journal of Biological Chemistry274 (14): 9861–70. (Apr 1999). doi:10.1074/jbc.274.14.9861. PMID10092678.
^“A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway”. Cell89 (5): 693–702. (May 1997). doi:10.1016/s0092-8674(00)80252-4. PMID9182757.
^“Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)”. FEBS Letters519 (1–3): 50–8. (May 2002). doi:10.1016/s0014-5793(02)02709-6. PMID12023017.
^“Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor”. FEBS Letters509 (2): 255–62. (Dec 2001). doi:10.1016/s0014-5793(01)03174-x. PMID11741599.
^ ab“The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif”. Oncogene20 (9): 1052–62. (Mar 2001). doi:10.1038/sj.onc.1204202. PMID11314042.
^“Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1”. The Journal of Biological Chemistry274 (28): 19649–54. (Jul 1999). doi:10.1074/jbc.274.28.19649. PMID10391903.
^ ab“Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”. FEBS Letters401 (2–3): 133–7. (Jan 1997). doi:10.1016/s0014-5793(96)01456-1. PMID9013873.
^ ab“Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth”. The Journal of Biological Chemistry276 (52): 48679–92. (Dec 2001). doi:10.1074/jbc.M106759200. PMID11606575.
^“Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by poly(U) RNA”. The Journal of Biological Chemistry273 (13): 7776–81. (Mar 1998). doi:10.1074/jbc.273.13.7776. PMID9516488.
^“SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes”. The Journal of Biological Chemistry272 (13): 8121–4. (Mar 1997). doi:10.1074/jbc.272.13.8121. PMID9079622.
^“ETV6-NTRK3 transformation requires insulin-like growth factor 1 receptor signaling and is associated with constitutive IRS-1 tyrosine phosphorylation”. Oncogene21 (37): 5684–95. (Aug 2002). doi:10.1038/sj.onc.1205669. PMID12173038.
^“Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade”. The Journal of Biological Chemistry275 (3): 2219–30. (Jan 2000). doi:10.1074/jbc.275.3.2219. PMID10636929.
^“Through induction of juxtaposition and tyrosine kinase activity of Jak1, X-gene product of hepatitis B virus stimulates Ras and the transcriptional activation through AP-1, NF-kappaB, and SRE enhancers”. Biochemical and Biophysical Research Communications286 (5): 886–94. (Sep 2001). doi:10.1006/bbrc.2001.5496. PMID11527382.
^“Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src”. Oncogene18 (33): 4647–53. (Aug 1999). doi:10.1038/sj.onc.1203079. PMID10467411.
^“Phosphorylation of the linker for activation of T-cells by Itk promotes recruitment of Vav”. Biochemistry41 (34): 10732–40. (Aug 2002). doi:10.1021/bi025554o. PMID12186560.
^“SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells”. The Journal of Biological Chemistry272 (2): 1363–7. (Jan 1997). doi:10.1074/jbc.272.2.1363. PMID8995445.
^“Regulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding protein”. The Journal of Biological Chemistry275 (27): 20578–87. (Jul 2000). doi:10.1074/jbc.M001887200. PMID10781592.
^“Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2”. The Journal of Biological Chemistry276 (43): 39950–8. (Oct 2001). doi:10.1074/jbc.M107807200. PMID11546790.
^“Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor”. The Journal of Biological Chemistry273 (38): 24301–4. (Sep 1998). doi:10.1074/jbc.273.38.24301. PMID9733714.
^“The germinal center kinase (GCK)-related protein kinases HPK1 and KHS are candidates for highly selective signal transducers of Crk family adapter proteins”. Oncogene17 (15): 1893–901. (Oct 1998). doi:10.1038/sj.onc.1202108. PMID9788432.
^“SH2/SH3 adaptor proteins can link tyrosine kinases to a Ste20-related protein kinase, HPK1”. The Journal of Biological Chemistry272 (44): 27804–11. (Oct 1997). doi:10.1074/jbc.272.44.27804. PMID9346925.
^“Involvement of hematopoietic progenitor kinase 1 in T cell receptor signaling”. The Journal of Biological Chemistry276 (22): 18908–14. (Jun 2001). doi:10.1074/jbc.M101485200. PMID11279207.
^“Magicin, a novel cytoskeletal protein associates with the NF2 tumor suppressor merlin and Grb2”. Oncogene23 (54): 8815–25. (Nov 2004). doi:10.1038/sj.onc.1208110. PMID15467741.
^ ab“Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein”. Cancer Research55 (18): 4000–3. (Sep 1995). PMID7664271.
^“Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents”. Cell Growth & Differentiation6 (12): 1651–8. (Dec 1995). PMID9019171.
^“Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase”. The Journal of Biological Chemistry270 (32): 18871–4. (Aug 1995). doi:10.1074/jbc.270.32.18871. PMID7642542.
^“mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation”. The Journal of Biological Chemistry276 (42): 39290–4. (Oct 2001). doi:10.1074/jbc.M107026200. PMID11509578.
^ ab“Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor”. Oncogene15 (15): 1823–32. (Oct 1997). doi:10.1038/sj.onc.1201351. PMID9362449.
^“Monocyte colony-stimulating factor stimulates binding of phosphatidylinositol 3-kinase to Grb2.Sos complexes in human monocytes”. The Journal of Biological Chemistry270 (18): 10380–3. (May 1995). doi:10.1074/jbc.270.18.10380. PMID7737969.
^“Direct association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinase”. The Journal of Biological Chemistry270 (21): 12774–80. (May 1995). doi:10.1074/jbc.270.21.12774. PMID7759531.
^“A new function for phospholipase C-gamma1: coupling to the adaptor protein GRB2”. Archives of Biochemistry and Biophysics345 (1): 103–10. (Sep 1997). doi:10.1006/abbi.1997.0245. PMID9281317.
^ ab“Ligation of the T-cell antigen receptor (TCR) induces association of hSos1, ZAP-70, phospholipase C-gamma 1, and other phosphoproteins with Grb2 and the zeta-chain of the TCR”. The Journal of Biological Chemistry270 (31): 18428–36. (Aug 1995). doi:10.1074/jbc.270.31.18428. PMID7629168.
^ ab“Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells”. Journal of Leukocyte Biology65 (3): 372–80. (Mar 1999). doi:10.1002/jlb.65.3.372. PMID10080542.
^ abc“Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk”. The Journal of Biological Chemistry275 (23): 17263–8. (Jun 2000). doi:10.1074/jbc.M000689200. PMID10747947.
^“Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases”. The Journal of Biological Chemistry272 (2): 1032–7. (Jan 1997). doi:10.1074/jbc.272.2.1032. PMID8995399.
^“Fyn kinase-directed activation of SH2 domain-containing protein-tyrosine phosphatase SHP-2 by Gi protein-coupled receptors in Madin-Darby canine kidney cells”. The Journal of Biological Chemistry274 (18): 12401–7. (Apr 1999). doi:10.1074/jbc.274.18.12401. PMID10212213.
^“Epidermal growth factor induces coupling of protein-tyrosine phosphatase 1D to GRB2 via the COOH-terminal SH3 domain of GRB2”. The Journal of Biological Chemistry271 (35): 20981–4. (Aug 1996). doi:10.1074/jbc.271.35.20981. PMID8702859.
^“Coupling of the murine protein tyrosine phosphatase PEST to the epidermal growth factor (EGF) receptor through a Src homology 3 (SH3) domain-mediated association with Grb2”. Oncogene14 (14): 1643–51. (Apr 1997). doi:10.1038/sj.onc.1201008. PMID9135065.
^“Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein”. The Journal of Biological Chemistry275 (6): 4283–9. (Feb 2000). doi:10.1074/jbc.275.6.4283. PMID10660596.
^“Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)”. The Journal of Biological Chemistry271 (49): 31290–5. (Dec 1996). doi:10.1074/jbc.271.49.31290. PMID8940134.
^“The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells”. The Journal of Biological Chemistry271 (7): 3856–62. (Feb 1996). doi:10.1074/jbc.271.7.3856. PMID8632004.
^“Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors”. The Journal of Biological Chemistry271 (15): 8564–9. (Apr 1996). doi:10.1074/jbc.271.15.8564. PMID8621483.
^“The oncogenic versions of the Ret and Trk tyrosine kinases bind Shc and Grb2 adaptor proteins”. Oncogene9 (6): 1661–8. (Jun 1994). PMID8183561.
^“The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10”. The Journal of Biological Chemistry270 (37): 21461–3. (Sep 1995). doi:10.1074/jbc.270.37.21461. PMID7665556.
^“Identification and characterization of novel substrates of Trk receptors in developing neurons”. Neuron21 (5): 1017–29. (Nov 1998). doi:10.1016/s0896-6273(00)80620-0. PMID9856458.
^“SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins”. Cellular Signalling12 (11–12): 769–79. (Dec 2000). doi:10.1016/s0898-6568(00)00129-7. PMID11152963.
^ ab“Tyrosine phosphorylation of ACK in response to temperature shift-down, hyperosmotic shock, and epidermal growth factor stimulation”. FEBS Letters386 (2–3): 230–4. (May 1996). doi:10.1016/0014-5793(96)00449-8. PMID8647288.
^“Pathways downstream of Shc and Grb2 are required for cell transformation by the tpr-Met oncoprotein”. The Journal of Biological Chemistry271 (22): 13116–22. (May 1996). doi:10.1074/jbc.271.22.13116. PMID8662733.
^“Functional importance of Shc tyrosine 317 on insulin signaling in Rat1 fibroblasts expressing insulin receptors”. The Journal of Biological Chemistry272 (14): 9581–6. (Apr 1997). doi:10.1074/jbc.272.14.9581. PMID9083103.
^“Role of tyrosine residues and protein interaction domains of SHC adaptor in VEGF receptor 3 signaling”. Oncogene18 (2): 507–14. (Jan 1999). doi:10.1038/sj.onc.1202315. PMID9927207.
^“The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation”. The Journal of Biological Chemistry269 (3): 1599–602. (Jan 1994). doi:10.1016/S0021-9258(17)42066-7. PMID8294403.
^ ab“Role of Src in the modulation of multiple adaptor proteins in FcalphaRI oxidant signaling”. Blood94 (6): 2112–20. (Sep 1999). doi:10.1182/blood.V94.6.2112. PMID10477741.
^“Shc mediates ligand-induced internalization of epidermal growth factor receptors”. Biochemical and Biophysical Research Communications282 (5): 1154–60. (Apr 2001). doi:10.1006/bbrc.2001.4680. PMID11302736.
^“Inhibition of insulin-like growth factor-I signaling by ethanol in neuronal cells”. Alcoholism: Clinical and Experimental Research25 (7): 1058–64. (Jul 2001). doi:10.1111/j.1530-0277.2001.tb02317.x. PMID11505033.
^“Direct interaction between Shc and the platelet-derived growth factor beta-receptor”. The Journal of Biological Chemistry269 (21): 15337–43. (May 1994). doi:10.1016/S0021-9258(17)36611-5. PMID8195171.
^“Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2”. The Journal of Biological Chemistry270 (13): 7587–93. (Mar 1995). doi:10.1074/jbc.270.13.7587. PMID7535773.
^“Signal transduction pathway of human fibroblast growth factor receptor 3. Identification of a novel 66-kDa phosphoprotein”. The Journal of Biological Chemistry272 (10): 6621–8. (Mar 1997). doi:10.1074/jbc.272.10.6621. PMID9045692.
^ ab“Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells”. The Journal of Biological Chemistry269 (20): 14419–23. (May 1994). doi:10.1016/S0021-9258(17)36639-5. PMID7514169.
^“Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase”. Journal of Immunology158 (9): 4097–103. (May 1997). doi:10.4049/jimmunol.158.9.4097. PMID9126968.
^“SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases”. The Journal of Biological Chemistry269 (19): 14081–7. (May 1994). doi:10.1016/S0021-9258(17)36757-1. PMID8188688.
^“16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells”. Molecular Endocrinology13 (5): 692–704. (May 1999). doi:10.1210/mend.13.5.0280. PMID10319320.
^“Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells”. Biochemical and Biophysical Research Communications239 (2): 412–7. (Oct 1997). doi:10.1006/bbrc.1997.7480. PMID9344843.
^“The inhibitory gamma subunit of the type 6 retinal cGMP phosphodiesterase functions to link c-Src and G-protein-coupled receptor kinase 2 in a signaling unit that regulates p42/p44 mitogen-activated protein kinase by epidermal growth factor”. The Journal of Biological Chemistry278 (20): 18658–63. (May 2003). doi:10.1074/jbc.M212103200. PMID12624098.
^“Epidermal growth factor stimulation of the ACK1/Dbl pathway in a Cdc42 and Grb2-dependent manner”. Biochemical and Biophysical Research Communications284 (2): 470–7. (Jun 2001). doi:10.1006/bbrc.2001.5004. PMID11394904.
^“Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells”. The Journal of Biological Chemistry277 (8): 6703–7. (Feb 2002). doi:10.1074/jbc.M110338200. PMID11733534.
^“Direct binding of the signaling adapter protein Grb2 to the activation loop tyrosines on the nerve growth factor receptor tyrosine kinase, TrkA”. The Journal of Biological Chemistry275 (24): 18225–33. (Jun 2000). doi:10.1074/jbc.M001862200. PMID10748052.
^“Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex”. The Journal of Biological Chemistry271 (43): 26962–70. (Oct 1996). doi:10.1074/jbc.271.43.26962. PMID8900182.
“[Design of new anti-tumor agents interrupting deregulated signaling pathways induced by tyrosine kinase proteins. Inhibition of protein-protein interaction involving Grb2]”. Journal de la Société de Biologie198 (2): 133–7. (2004). doi:10.1051/jbio/2004198020133. PMID15368963.